feature_id int64 0 16.4k | description stringlengths 43 3.53k | summary stringlengths 10 1.2k | activation_pattern stringlengths 0 1.23k | category stringclasses 14
values | exemplar_protein_families stringlengths 0 2.38k | uniref90_frequency int64 1.4M 208M | uniref90_idf float32 0 5 | uniref90_max_activation float32 7.8 50.7 | top_100_uniref_ids listlengths 100 100 | top_swissprot_activations listlengths 20 20 | decoder_nearest_neighbors listlengths 10 10 | threshold float64 0 1.22 ⌀ |
|---|---|---|---|---|---|---|---|---|---|---|---|---|
200 | Summary: Alpha-helical scaffolding segments of α/β enzyme cores, especially the outer helices of TIM-barrel or partial TIM-barrel folds, with preference for well-ordered, charged helical faces adjacent to but not comprising catalytic motifs
Activation pattern: Regional activation across multiple discrete α-helical segm... | Alpha-helical scaffolding segments of α/β enzyme cores, especially the outer helices of TIM-barrel or partial TIM-barrel folds, with preference for well-ordered, charged helical faces adjacent to but not comprising catalytic motifs | Regional activation across multiple discrete α-helical segments within the catalytic domain; strong structure dependence (high-confidence helices), sparse in loops, β-strands, and disordered tails; residue-level peaks often at charged residues (Glu, Asp, Arg); typically avoids annotated catalytic residues and metal/clu... | Domain | Fructose-bisphosphate aldolase (class I TIM-barrel): activation on specific barrel helices (e.g., E161–K172), not on catalytic Lys/Tyr; L-2-keto-3-deoxyarabonate dehydratase (enolase/TIM-barrel-like lyase): punctate activation on several helices, excluding the annotated active-site Lys; Homocitrate synthase (N-terminal... | 72,037,365 | 1.06038 | 15.390625 | [
{
"activation": 15.390625,
"uniref_id": "UPI00064D781C"
},
{
"activation": 14.9453125,
"uniref_id": "UPI001FE681AC"
},
{
"activation": 14.875,
"uniref_id": "A0A158BMY9"
},
{
"activation": 14.7890625,
"uniref_id": "A0A846NBA4"
},
{
"activation": 14.765625,
"uni... | [
{
"activation": 13.71765422821045,
"uniprot_id": "P0A991"
},
{
"activation": 13.357583045959473,
"uniprot_id": "Q58980"
},
{
"activation": 13.334098815917969,
"uniprot_id": "P0A6L4"
},
{
"activation": 13.290730476379395,
"uniprot_id": "Q57843"
},
{
"activation": 1... | [
15796,
11098,
14922,
11314,
2341,
6720,
4251,
13993,
4176,
10548
] | 0.376247 |
201 | Summary: Short, solvent‑exposed secondary‑structure boundary/capping segments — acidic/polar, Gly/Ser/Thr‑enriched loops and edge elements (helix caps, β‑strand starts/edges, loop–strand/loop–helix transitions) that are often flexible/disordered and form generic surface patches across diverse proteins and taxa.
Activat... | Short, solvent‑exposed secondary‑structure boundary/capping segments — acidic/polar, Gly/Ser/Thr‑enriched loops and edge elements (helix caps, β‑strand starts/edges, loop–strand/loop–helix transitions) that are often flexible/disordered and form generic surface patches across diverse proteins and taxa. | Regional activation with residue‑level peaks: contiguous 10–20 aa windows, often multiple per protein; strongest in coils/turns and at the beginnings/ends of helices or strands; enriched for G, S, T, D, E and Gly‑rich motifs; occurs both in low‑pLDDT disordered loops and in well‑structured loop–strand–loop or short hel... | Structural motif | - Type VI secretion spike (VgrG): activates on unstructured coil segments connecting β‑strands and extended disordered loops.
- Sulfate adenylyltransferase/PAPS synthase: activates across a surface α‑helix and flanking loop (helix‑capping acidic/polar segment).
- Respiratory molybdoenzymes (e.g., nitrate reductase): ac... | 25,179,760 | 2.111525 | 14.25 | [
{
"activation": 14.25,
"uniref_id": "A0A649VSQ6"
},
{
"activation": 14.1796875,
"uniref_id": "A0A0P9PBR8"
},
{
"activation": 14.1328125,
"uniref_id": "UPI000F5719B5"
},
{
"activation": 14.09375,
"uniref_id": "UPI002F4001AB"
},
{
"activation": 14.0859375,
"unir... | [
{
"activation": 12.856740951538086,
"uniprot_id": "P04331"
},
{
"activation": 11.486940383911133,
"uniprot_id": "Q0PDK6"
},
{
"activation": 11.245674133300781,
"uniprot_id": "Q9HUK7"
},
{
"activation": 10.984090805053711,
"uniprot_id": "P33973"
},
{
"activation": ... | [
9286,
9895,
12669,
14060,
1870,
10214,
12493,
2967,
1120,
9784
] | 0.154366 |
202 | Summary: Macromolecular interaction modules: the feature highlights segments that mediate assembly or partner binding (protein–protein/conjugation surfaces), frequently residing in terminal, flexible, or long helical regions; when a compact interaction domain is present it spans that domain (e.g., SWIB/MDM2, SCP/CAP), ... | Macromolecular interaction modules: the feature highlights segments that mediate assembly or partner binding (protein–protein/conjugation surfaces), frequently residing in terminal, flexible, or long helical regions; when a compact interaction domain is present it spans that domain (e.g., SWIB/MDM2, SCP/CAP), rather th... | Primarily regional/domain-level activation, typically one contiguous block. Two common modes: (1) entire structured interaction domains with high pLDDT; (2) charge-rich, low-complexity terminal segments with low pLDDT. Often biased toward C-terminal regions; residue-level peaks occur in surface loops and amphipathic he... | Interaction site | - SWI/SNF chromatin-remodeling subunit (SMARCD1/BAF60): strong activation across the C-terminal interaction region including the SWIB/MDM2 domain that binds SMARCC1/2; disordered N-terminus not selected.
- CAP/CRISP/antigen 5 family (SCP/CAP domain proteins): activation concentrated within the SCP/CAP core, especially ... | 4,795,333 | 3.769922 | 17.421875 | [
{
"activation": 17.421875,
"uniref_id": "A0A1F2WRR6"
},
{
"activation": 17.390625,
"uniref_id": "A0A1F2WUH3"
},
{
"activation": 17.34375,
"uniref_id": "A0A7V4MZ09"
},
{
"activation": 17.328125,
"uniref_id": "A0A7V4MXV9"
},
{
"activation": 17.28125,
"uniref_id"... | [
{
"activation": 14.225947380065918,
"uniprot_id": "A0A2I2F2J6"
},
{
"activation": 14.008065223693848,
"uniprot_id": "A0A1J0HSQ1"
},
{
"activation": 13.616530418395996,
"uniprot_id": "P0DOB3"
},
{
"activation": 13.563603401184082,
"uniprot_id": "I1RF59"
},
{
"activ... | [
3677,
7376,
14452,
12918,
12576,
7214,
9949,
286,
3000,
2117
] | 0.284737 |
203 | Summary: Transmembrane helix and adjacent juxtamembrane “hinge” segments in multi-pass inner-membrane proteins, especially membrane glycosylation machinery (lipid carrier–linked sugar transferases and O‑antigen/capsule enzymes); the feature favors hydrophobic helices with small-residue kinks/caps (often Gly, sometimes ... | Transmembrane helix and adjacent juxtamembrane “hinge” segments in multi-pass inner-membrane proteins, especially membrane glycosylation machinery (lipid carrier–linked sugar transferases and O‑antigen/capsule enzymes); the feature favors hydrophobic helices with small-residue kinks/caps (often Gly, sometimes with PG c... | Primarily regional activation across a single, long hydrophobic transmembrane helix (often mid-sequence), tapering into the adjoining loop; secondarily sharp, residue-level peaks at glycine helix-cap/hinge positions in short coils adjacent to helices or within a TM helix. Non-glycosylation transporters typically show o... | Membrane-associated | - Undecaprenyl-phosphate N-acetylgalactosamine phosphotransferase (WecA-like): strong, contiguous activation spanning a specific transmembrane helix and its flanking regions.
- O-antigen ligase (WaaL): activation on the loop immediately preceding a transmembrane helix (juxtamembrane linker).
- Lipopolysaccharide 1,2-N-... | 5,120,240 | 3.704364 | 22.984375 | [
{
"activation": 22.984375,
"uniref_id": "A0A245ZKZ5"
},
{
"activation": 22.90625,
"uniref_id": "T1B7M5"
},
{
"activation": 22.828125,
"uniref_id": "A0A351BGH8"
},
{
"activation": 22.828125,
"uniref_id": "UPI002365C665"
},
{
"activation": 22.78125,
"uniref_id":... | [
{
"activation": 21.9733829498291,
"uniprot_id": "Q56770"
},
{
"activation": 21.31674575805664,
"uniprot_id": "P26406"
},
{
"activation": 20.77698516845703,
"uniprot_id": "B3FN88"
},
{
"activation": 20.739931106567383,
"uniprot_id": "Q9ABR0"
},
{
"activation": 19.5... | [
12089,
12243,
7374,
14771,
4942,
2427,
11381,
7934,
5228,
6087
] | 0.176559 |
204 | Summary: A short, well-ordered alpha-helix in the C-terminal region of glycosyltransferases—a conserved, often charge-rich “terminal cap” helix that occurs within the last ~10–30 residues (or just upstream of a terminal transmembrane segment in membrane GTs) across diverse soluble and membrane-associated sugar-transfer... | A short, well-ordered alpha-helix in the C-terminal region of glycosyltransferases—a conserved, often charge-rich “terminal cap” helix that occurs within the last ~10–30 residues (or just upstream of a terminal transmembrane segment in membrane GTs) across diverse soluble and membrane-associated sugar-transfer enzymes. | Regional activation of a single contiguous C‑terminal alpha-helix (~10–20 aa), with strong, compact signal and occasional residue-level peaks on Lys/Arg/Glu/Asp; minimal activation elsewhere and sometimes weak spillover to adjacent helices. | Structural motif | - LPS core glucosyltransferase WaaG: strong activation on a single C-terminal alpha-helix.
- Bacterial glycosyltransferase (uncharacterized family): dominant activation on a 15-residue C-terminal helix.
- Alg2 alpha-1,3/1,6-mannosyltransferase (Dol-PP-linked mannosyltransferase): basic C-terminal helix immediately upst... | 9,940,459 | 3.040952 | 19.1875 | [
{
"activation": 19.1875,
"uniref_id": "A0A7J3MMM9"
},
{
"activation": 19.0625,
"uniref_id": "D9Q197"
},
{
"activation": 18.8125,
"uniref_id": "UPI0035A59CF9"
},
{
"activation": 18.734375,
"uniref_id": "G5RXA6"
},
{
"activation": 18.703125,
"uniref_id": "A0A7W1... | [
{
"activation": 16.793657302856445,
"uniprot_id": "Q9UV63"
},
{
"activation": 16.700515747070312,
"uniprot_id": "A7TZT2"
},
{
"activation": 16.62702178955078,
"uniprot_id": "B5T072"
},
{
"activation": 16.575239181518555,
"uniprot_id": "Q8S4F6"
},
{
"activation": 1... | [
5435,
9107,
12382,
2502,
522,
5048,
11415,
9726,
7401,
7323
] | 0.240007 |
205 | Summary: A surface-exposed, glycine/aromatic–enriched loop/edge motif typical of exported proteins, most prominently the extracellular/periplasmic loops and strand–loop junctions of Gram-negative outer-membrane β-barrels (TonB-dependent receptors, porins, secretins, OM assembly factors). These segments are often flexib... | A surface-exposed, glycine/aromatic–enriched loop/edge motif typical of exported proteins, most prominently the extracellular/periplasmic loops and strand–loop junctions of Gram-negative outer-membrane β-barrels (TonB-dependent receptors, porins, secretins, OM assembly factors). These segments are often flexible, acidi... | Regional activation with multiple broad peaks along β-barrel domains, concentrated on coils/loops and adjacent strand–loop or helix–loop transitions (often low-pLDDT, glycine- and aromatic-rich); weaker spillover onto neighboring β-strands or short helices. In non-barrel secreted/extracellular proteins, the signal comp... | Membrane-associated | - TonB-dependent receptors (e.g., SusC-like carbohydrate and siderophore receptors): strong, multi-segment activation across extracellular loops and strand–loop transitions within the β-barrel.
- General porins (Omp family): a dominant peak on a flexible loop connecting β-strands that shapes the channel surface, with m... | 6,399,974 | 3.481271 | 20.828125 | [
{
"activation": 20.828125,
"uniref_id": "A0A7W1Z4H5"
},
{
"activation": 20.5,
"uniref_id": "A0AAW6FX90"
},
{
"activation": 20.484375,
"uniref_id": "A0A0S8ARG8"
},
{
"activation": 20.484375,
"uniref_id": "A0A1T5A276"
},
{
"activation": 20.46875,
"uniref_id": "A... | [
{
"activation": 19.329387664794922,
"uniprot_id": "Q8A1G1"
},
{
"activation": 14.323041915893555,
"uniprot_id": "P38370"
},
{
"activation": 9.96603775024414,
"uniprot_id": "G3XCY8"
},
{
"activation": 7.7329888343811035,
"uniprot_id": "P06971"
},
{
"activation": 7.... | [
12387,
3789,
4710,
4902,
5193,
3252,
5151,
6728,
7579,
11967
] | 0.182563 |
206 | Summary: Short amphipathic alpha‑helical interface segments—often parts of coiled‑coil/helix‑turn elements in non‑catalytic terminal or inter‑domain regions—that mediate assembly and docking within large macromolecular complexes (frequently in DNA/RNA replication, transcription, and ubiquitin/ESCRT pathways). These hel... | Short amphipathic alpha‑helical interface segments—often parts of coiled‑coil/helix‑turn elements in non‑catalytic terminal or inter‑domain regions—that mediate assembly and docking within large macromolecular complexes (frequently in DNA/RNA replication, transcription, and ubiquitin/ESCRT pathways). These helices show... | Regional activation on 10–35 aa windows with sharp residue‑level peaks inside alpha‑helices (sometimes spilling into adjacent turn/short beta). Multiple non‑contiguous activated segments per protein are common. In long eukaryotic proteins, activations are biased to mid‑to‑C‑terminal regions; in some proteins they occur... | Interaction site | - Replicative MCM helicase subunit (MCM4): C‑terminal amphipathic helix outside the AAA+ MCM domain, consistent with a regulatory/assembly interface.
- Atypical protein kinase RIO2: short N‑terminal pre‑kinase amphipathic helix used as an interface element rather than a catalytic motif.
- Phenylalanyl‑tRNA synthetase a... | 12,980,590 | 2.77411 | 21.5 | [
{
"activation": 21.5,
"uniref_id": "UPI00201B4384"
},
{
"activation": 20.40625,
"uniref_id": "A0A521EN84"
},
{
"activation": 19.546875,
"uniref_id": "A0A0F7LAI7"
},
{
"activation": 19.40625,
"uniref_id": "A0A317ZG09"
},
{
"activation": 19.375,
"uniref_id": "A0... | [
{
"activation": 16.208492279052734,
"uniprot_id": "A5K9S0"
},
{
"activation": 15.49179458618164,
"uniprot_id": "Q9UST7"
},
{
"activation": 15.335040092468262,
"uniprot_id": "Q8KA15"
},
{
"activation": 15.286652565002441,
"uniprot_id": "Q0P426"
},
{
"activation": 1... | [
3432,
7639,
6431,
10756,
12201,
13916,
6434,
3414,
9069,
2906
] | 0.434762 |
207 | Summary: Intrinsically disordered, Pro/Ser/Thr‑rich cytosolic linker and juxtamembrane tail regions that serve as multisite‑phosphorylated docking hubs in membrane‑proximal signaling scaffolds—typically flanking/bridging PH or FERM modules or lying immediately C‑terminal to a single‑pass transmembrane helix—integrating... | Intrinsically disordered, Pro/Ser/Thr‑rich cytosolic linker and juxtamembrane tail regions that serve as multisite‑phosphorylated docking hubs in membrane‑proximal signaling scaffolds—typically flanking/bridging PH or FERM modules or lying immediately C‑terminal to a single‑pass transmembrane helix—integrating phosphoi... | Extended regional activation across low‑complexity IDRs, especially (i) linkers between structured domains and PH/FERM units and (ii) cytosolic tails just after a transmembrane helix; minimal activation in folded catalytic cores; superimposed residue‑level peaks at known or putative Ser/Thr phosphosites and binding‑sen... | Disorder | - TORC2 component SIN1: strong activation in the disordered linker between the CRIM and SIN1‑type PH domains and at the CRIM C‑terminal surface that mediates substrate engagement; peaks align with phosphosites, while the structured core is inactive.
- Single‑pass guidance receptors (e.g., Plexin‑A): broad activation ac... | 5,979,070 | 3.5493 | 22.1875 | [
{
"activation": 22.1875,
"uniref_id": "A0A8T0HK09"
},
{
"activation": 22.109375,
"uniref_id": "UPI00115CD063"
},
{
"activation": 21.984375,
"uniref_id": "A0A182JHN4"
},
{
"activation": 21.953125,
"uniref_id": "A0A0D8Y4Y4"
},
{
"activation": 21.828125,
"uniref_... | [
{
"activation": 20.83467674255371,
"uniprot_id": "Q8VCE9"
},
{
"activation": 20.739744186401367,
"uniprot_id": "Q95YD4"
},
{
"activation": 20.651443481445312,
"uniprot_id": "Q9W5D0"
},
{
"activation": 20.59869384765625,
"uniprot_id": "Q8C115"
},
{
"activation": 20... | [
7286,
16187,
12415,
15385,
4812,
16004,
5045,
6608,
6565,
13270
] | 0.278581 |
208 | Summary: Generic structural signal for individual residues within well-ordered alpha-helical segments across diverse proteins; often highlights aromatic or charged side chains and is not tied to specific catalytic motifs.
Activation pattern: Residue-level peaks within alpha-helices (often a single residue or short dipe... | Generic structural signal for individual residues within well-ordered alpha-helical segments across diverse proteins; often highlights aromatic or charged side chains and is not tied to specific catalytic motifs. | Residue-level peaks within alpha-helices (often a single residue or short dipeptide), sparsely distributed across a protein; enrichment in high-confidence helical regions; typically not centered on annotated active sites. | Structural motif | - Cap-binding eIF4E family: a single tryptophan within a helix (part of the 4E-BP/cap-binding region).
- RNA dimethyladenosine methyltransferases: scattered residues (e.g., N/A/L/D/S/I) in helical segments, including a C‑terminal helix, away from SAM-binding sites.
- START-domain lipid-transfer proteins: a helical tyro... | 138,238,535 | 0.408585 | 11.046875 | [
{
"activation": 11.046875,
"uniref_id": "UPI0023EAB180"
},
{
"activation": 10.9921875,
"uniref_id": "A0A3D6DQF9"
},
{
"activation": 10.9296875,
"uniref_id": "A0A7W7N6J6"
},
{
"activation": 10.921875,
"uniref_id": "X1CY96"
},
{
"activation": 10.8203125,
"uniref... | [
{
"activation": 10.185346603393555,
"uniprot_id": "G7CFI3"
},
{
"activation": 10.100692749023438,
"uniprot_id": "Q7AJA5"
},
{
"activation": 10.043198585510254,
"uniprot_id": "Q8NBJ7"
},
{
"activation": 10.041419982910156,
"uniprot_id": "Q8NBK3"
},
{
"activation": ... | [
11770,
157,
3655,
4926,
178,
560,
11441,
5767,
1119,
3759
] | 0.120255 |
209 | Summary: PAS-associated C-terminal cap (PAC) motif and immediately adjacent PAS–linker segments of PAS/LOV sensory domains that couple stimulus sensing to downstream effector modules across two‑component sensors and other PAS-bearing signaling proteins
Activation pattern: Short regional activation with sharp residue-le... | PAS-associated C-terminal cap (PAC) motif and immediately adjacent PAS–linker segments of PAS/LOV sensory domains that couple stimulus sensing to downstream effector modules across two‑component sensors and other PAS-bearing signaling proteins | Short regional activation with sharp residue-level peaks at the C-terminal end of PAS domains (the PAC motif) and in the adjoining flexible loop/helix or linker to the effector; typically mid‑protein; catalytic cores and transmembranes largely inactive; enriched for acidic/polar residues | Structural motif | - Two-component histidine kinases/sensors (bacterial, archaeal, Dictyostelium, plant): activation on the PAC motif of N‑terminal PAS sensors and the PAS–histidine kinase linker (strongest; e.g., hybrid histidine kinases)
- Light/oxygen-sensing PAS/LOV receptors (e.g., FixL/LOV-HKs, phytochromes): activation on the LOV/... | 4,850,893 | 3.758402 | 29.984375 | [
{
"activation": 29.984375,
"uniref_id": "A0A661WEM2"
},
{
"activation": 29.953125,
"uniref_id": "UPI0024176A88"
},
{
"activation": 29.9375,
"uniref_id": "A0A524DGT1"
},
{
"activation": 29.921875,
"uniref_id": "A0A0Q1B3F6"
},
{
"activation": 29.890625,
"uniref_... | [
{
"activation": 28.30527114868164,
"uniprot_id": "P15939"
},
{
"activation": 28.21308708190918,
"uniprot_id": "Q8THF6"
},
{
"activation": 27.05776596069336,
"uniprot_id": "E5KK10"
},
{
"activation": 26.681655883789062,
"uniprot_id": "A5W4E3"
},
{
"activation": 26.... | [
8807,
15539,
1189,
3505,
2786,
14478,
2591,
6742,
12246,
14052
] | 0.151151 |
210 | Summary: Long, low-complexity, Ser/Pro/acidic-rich regulatory segments that adjoin or follow extended alpha‑helical scaffold domains (coiled‑coils/HEAT/ARM/FH2) in large eukaryotic scaffold proteins involved in cytoskeleton and membrane/trafficking systems; often C‑terminal, frequently containing proline‑rich tracts us... | Long, low-complexity, Ser/Pro/acidic-rich regulatory segments that adjoin or follow extended alpha‑helical scaffold domains (coiled‑coils/HEAT/ARM/FH2) in large eukaryotic scaffold proteins involved in cytoskeleton and membrane/trafficking systems; often C‑terminal, frequently containing proline‑rich tracts used for pa... | Predominantly regional/domain-level activation across long contiguous stretches (tens to >100 residues), often in the C‑terminal half; strong blocks within alpha‑helical scaffold domains (e.g., FH2) that extend into adjacent disordered/proline‑rich tails; frequent activation at helix-to-coil transitions; no single cons... | Compositional bias | Formins: high activation in the C‑terminal FH2 subregion and downstream DAD/IDR tail, with moderate signal in adjacent coiled‑coils; ESCRT Bro1/ALIX family: C‑terminal helical segment transitioning into a disordered tail; eIF4G translational scaffolds: HEAT-repeat alpha‑solenoids and flanking low‑complexity linkers; Nu... | 8,492,628 | 3.198367 | 19.5 | [
{
"activation": 19.5,
"uniref_id": "A0A4Y1RIV7"
},
{
"activation": 19.28125,
"uniref_id": "A0A392PS88"
},
{
"activation": 19.25,
"uniref_id": "A0A6B2KZT6"
},
{
"activation": 19.234375,
"uniref_id": "A0A392Q6V5"
},
{
"activation": 19.21875,
"uniref_id": "A0A9P6... | [
{
"activation": 19.12312889099121,
"uniprot_id": "P41832"
},
{
"activation": 18.903644561767578,
"uniprot_id": "O04532"
},
{
"activation": 18.901670455932617,
"uniprot_id": "O94532"
},
{
"activation": 18.900480270385742,
"uniprot_id": "Q5AAF4"
},
{
"activation": 1... | [
7499,
5676,
5944,
14342,
3071,
9673,
2233,
11657,
5508,
14677
] | 0.288146 |
211 | Summary: Coupling/switch segment of ABC-type P-loop NTPase heads—centered on the Q-loop and the adjacent alpha-helical subdomain that communicates ATP binding/hydrolysis to partner domains (e.g., transmembrane coupling helices, coiled coils, nuclease modules); the feature generalizes to analogous nucleotide-coupling el... | Coupling/switch segment of ABC-type P-loop NTPase heads—centered on the Q-loop and the adjacent alpha-helical subdomain that communicates ATP binding/hydrolysis to partner domains (e.g., transmembrane coupling helices, coiled coils, nuclease modules); the feature generalizes to analogous nucleotide-coupling elements in... | Regional activation (∼30–100 aa) immediately C‑terminal to the ATP-binding P‑loop, spanning the Q‑loop and following helix plus nearby flexible loops; often appears as two separated blocks in proteins with tandem or split NBDs; in membrane ABCs, confined to cytosolic NBDs; peaks on long helices and adjacent low‑pLDDT s... | Domain | - OLD/Gabija ATP-dependent nucleases: activation on the N‑terminal dimerization/helix segment of the ATPase head.
- ABCF/ABCE-type ARB1 (soluble ABC factors): strong peaks just C‑terminal to the Walker A site in each ABC domain (Q‑loop/adjacent helix).
- Membrane ABC exporters (e.g., Vi polysaccharide exporter) and pla... | 7,029,832 | 3.387403 | 25.671875 | [
{
"activation": 25.671875,
"uniref_id": "A0A176RWA0"
},
{
"activation": 25.640625,
"uniref_id": "UPI0021D10C16"
},
{
"activation": 25.640625,
"uniref_id": "UPI001F3C0D30"
},
{
"activation": 25.625,
"uniref_id": "UPI0019D1ED21"
},
{
"activation": 25.625,
"unire... | [
{
"activation": 19.451841354370117,
"uniprot_id": "P0DV58"
},
{
"activation": 17.46692657470703,
"uniprot_id": "P0DW47"
},
{
"activation": 16.738136291503906,
"uniprot_id": "P13520"
},
{
"activation": 16.249652862548828,
"uniprot_id": "J8H9C1"
},
{
"activation": 1... | [
4409,
668,
8630,
8778,
4800,
16165,
15049,
3273,
2331,
8033
] | 0.155988 |
212 | Summary: Structured ligand/cofactor/substrate-binding pocket environments in proteins, with strongest selectivity for aminoacyl‑tRNA synthetases (adenylate‑forming active site and adjacent signature loops), but generalizing to analogous cofactor/substrate‑binding regions (e.g., FAD, metal centers, molybdenum cofactor, ... | Structured ligand/cofactor/substrate-binding pocket environments in proteins, with strongest selectivity for aminoacyl‑tRNA synthetases (adenylate‑forming active site and adjacent signature loops), but generalizing to analogous cofactor/substrate‑binding regions (e.g., FAD, metal centers, molybdenum cofactor, nucleotid... | Ligand-binding site | Replace the tyrosinase bullet with: "Type‑3 copper proteins (tyrosinase, hemocyanin): activation on helices flanking the copper‑ligating histidines rather than on the histidines themselves." | 10,063,734 | 3.028627 | 22.078125 | [
{
"activation": 22.078125,
"uniref_id": "A0A944Q187"
},
{
"activation": 22,
"uniref_id": "UPI000FF8A412"
},
{
"activation": 21.9375,
"uniref_id": "UPI00380E1224"
},
{
"activation": 21.921875,
"uniref_id": "UPI00344D5B91"
},
{
"activation": 21.796875,
"uniref_i... | [
{
"activation": 20.13493537902832,
"uniprot_id": "P56456"
},
{
"activation": 19.896156311035156,
"uniprot_id": "P46207"
},
{
"activation": 19.36356544494629,
"uniprot_id": "P00958"
},
{
"activation": 19.23923683166504,
"uniprot_id": "P56192"
},
{
"activation": 19.... | [
14412,
8530,
11296,
3837,
15908,
3920,
6969,
2262,
2384,
875
] | 0.205362 | |
213 | Summary: An Arg/Gly/Pro-rich, mixed-charge low-complexity signature of eukaryotic nuclear and RNA granule–associated proteins—classically RGG/GAR- and related GP/PG-containing intrinsically disordered tracts used for RNA binding, RNP assembly, and granule scaffolding—with activation that can extend to nearby compact RN... | An Arg/Gly/Pro-rich, mixed-charge low-complexity signature of eukaryotic nuclear and RNA granule–associated proteins—classically RGG/GAR- and related GP/PG-containing intrinsically disordered tracts used for RNA binding, RNP assembly, and granule scaffolding—with activation that can extend to nearby compact RNA-binding... | - Predominantly long, continuous activation over intrinsically disordered, low-pLDDT regions (often terminal tails), enriched for glycine with interspersed Pro and variable charge (often Arg/Lys but not required; RGG/GAR common but not obligatory).
- Local maxima at RG/RGG and GP/PG patterns; basic clusters (e.g., NLS-... | Compositional bias | - Poly(A)-binding protein–interacting scaffold (PBP1): strong, sustained activation across a long, disordered low-complexity C-terminal region; structured N-terminus largely inactive.
- LSm complex subunit (Lsm4): highest activation at the Sm-domain C-terminus and into the short helix that transitions to the disordered... | 5,454,203 | 3.641179 | 20.109375 | [
{
"activation": 20.109375,
"uniref_id": "A0A8B7U0D1"
},
{
"activation": 20.03125,
"uniref_id": "A0A835ZMY6"
},
{
"activation": 20.015625,
"uniref_id": "UPI001879C010"
},
{
"activation": 20.015625,
"uniref_id": "A0A6P5QZF0"
},
{
"activation": 20,
"uniref_id": "... | [
{
"activation": 19.825164794921875,
"uniprot_id": "Q9CWT2"
},
{
"activation": 19.14789581298828,
"uniprot_id": "Q3MKQ2"
},
{
"activation": 18.923856735229492,
"uniprot_id": "Q9DD24"
},
{
"activation": 18.453548431396484,
"uniprot_id": "Q15170"
},
{
"activation": 1... | [
8900,
10267,
7510,
4986,
10543,
3187,
337,
1340,
16310,
15701
] | 0.250067 |
214 | Summary: Active-site β-strand termini and strand-to-loop segments that position acidic (Asp/Glu) and often histidine residues for divalent-metal coordination or general acid/base catalysis; a recurrent scaffold across phospho-/ester-bond enzymes (nucleases, phospholipases/lactonases, sphingomyelinases, MBL-like hydrola... | Active-site β-strand termini and strand-to-loop segments that position acidic (Asp/Glu) and often histidine residues for divalent-metal coordination or general acid/base catalysis; a recurrent scaffold across phospho-/ester-bond enzymes (nucleases, phospholipases/lactonases, sphingomyelinases, MBL-like hydrolases) and ... | Residue-level peaks on short contiguous segments (typically 5–7 residues) at β-strand termini or β-strand-to-loop boundaries within well-structured catalytic cores; multiple noncontiguous hotspots can occur within a domain; enriched for Asp/Glu and frequently His, often adjacent to metal-binding/catalytic residues or n... | Catalytic function | - DNA repair AP endonuclease 2: activation on β-strands near catalytic His/Asp within the metal-dependent active site.
- Holliday junction endonuclease (Hjc): strong peak on a strand-to-loop segment between Mg2+-binding acidic residues (D/E) that define the nuclease center.
- Bacterial serine/threonine protein kinase (... | 63,023,689 | 1.194055 | 14.039063 | [
{
"activation": 14.0390625,
"uniref_id": "UPI0025A3D009"
},
{
"activation": 14.0234375,
"uniref_id": "A0A946EEV1"
},
{
"activation": 14,
"uniref_id": "A0A6N8U327"
},
{
"activation": 13.96875,
"uniref_id": "A0A6N4TJT3"
},
{
"activation": 13.9453125,
"uniref_id"... | [
{
"activation": 11.705062866210938,
"uniprot_id": "Q6DDT4"
},
{
"activation": 11.667901039123535,
"uniprot_id": "Q8K370"
},
{
"activation": 11.632880210876465,
"uniprot_id": "P00557"
},
{
"activation": 11.583334922790527,
"uniprot_id": "O34769"
},
{
"activation": ... | [
5132,
13262,
14565,
6990,
14018,
3082,
3936,
9804,
1569,
5809
] | 0.437625 |
215 | Summary: Short β-strand–to–loop transition segments that serve as allosteric relay/switch motifs in sensory/regulatory domains (especially PAS/GAF-like), reused across diverse signaling proteins (two-component kinases, cyclic-nucleotide and c-di-GMP enzymes, photoreceptors, and transcription factors)
Activation pattern... | Short β-strand–to–loop transition segments that serve as allosteric relay/switch motifs in sensory/regulatory domains (especially PAS/GAF-like), reused across diverse signaling proteins (two-component kinases, cyclic-nucleotide and c-di-GMP enzymes, photoreceptors, and transcription factors) | Highly localized windows (≈8–20 aa) with residue-level peaks centered at the C-terminus of a β-strand and extending into the following coil; multiple such patches can occur per multidomain sensor. Enriched for polar/charged residues and glycine; histidines (including occasional di-His) may appear in some sensors. | Structural motif | - Diguanylate cyclases with regulatory GAF domains (e.g., DgcP): activation at the end of a GAF β-strand and the adjacent loop within the sensory module.
- NO-sensing enhancer-binding regulators (NorR): activation on a β-strand–coil junction inside the N-terminal GAF-like NO-sensor/transducer region.
- HTH-type transcr... | 13,166,138 | 2.759917 | 26.03125 | [
{
"activation": 26.03125,
"uniref_id": "A0A7C3NGP7"
},
{
"activation": 26,
"uniref_id": "A0A1F7FNK6"
},
{
"activation": 25.875,
"uniref_id": "A0A847HFC2"
},
{
"activation": 25.859375,
"uniref_id": "A0A955RKD4"
},
{
"activation": 25.8125,
"uniref_id": "A0A2N1UC... | [
{
"activation": 23.195430755615234,
"uniprot_id": "P49333"
},
{
"activation": 21.96615982055664,
"uniprot_id": "Q73RG3"
},
{
"activation": 21.785877227783203,
"uniprot_id": "P07168"
},
{
"activation": 21.75428009033203,
"uniprot_id": "Q9QYJ6"
},
{
"activation": 21... | [
222,
2598,
7600,
15353,
1440,
4146,
7086,
12962,
3313,
8587
] | 0.185724 |
216 | Summary: Terminal and domain-boundary regions: the feature targets N- and C‑terminal extensions and linkers (often low‑complexity, charged, and disordered, including signal/transit peptides and regulatory tails) and, within folded domains, conserved coil-to-secondary-structure junction residues (helix/strand capping si... | Terminal and domain-boundary regions: the feature targets N- and C‑terminal extensions and linkers (often low‑complexity, charged, and disordered, including signal/transit peptides and regulatory tails) and, within folded domains, conserved coil-to-secondary-structure junction residues (helix/strand capping sites; freq... | Mixed: extended regional activation along terminal tails and linkers (commonly enriched in E/D/K/R and S/T and often low pLDDT), together with sharp residue‑level peaks at conserved cap residues or short motifs at domain ends; can include structured terminal segments of catalytic domains. | Disorder | DNA primase small subunit (PriS): structured C‑terminal catalytic-lobe edge with peaks near active‑site–proximal positions; Ribonuclease A: N‑terminal signal peptide and propeptide; RNase H: short disordered linker immediately N‑terminal to the RNase H domain; tRNA methyltransferase TRM10: disordered, charged C‑termina... | 7,037,206 | 3.386354 | 19.578125 | [
{
"activation": 19.578125,
"uniref_id": "A0A6N7VKX7"
},
{
"activation": 19.234375,
"uniref_id": "UPI0004EF6066"
},
{
"activation": 19.125,
"uniref_id": "A0A6G5YH83"
},
{
"activation": 19.046875,
"uniref_id": "A0A444L4W2"
},
{
"activation": 19,
"uniref_id": "A0... | [
{
"activation": 15.00439167022705,
"uniprot_id": "P03709"
},
{
"activation": 11.67019271850586,
"uniprot_id": "Q12146"
},
{
"activation": 11.495302200317383,
"uniprot_id": "Q9Y248"
},
{
"activation": 11.236316680908203,
"uniprot_id": "Q9BRX5"
},
{
"activation": 9.... | [
15495,
12330,
14871,
4476,
15307,
8845,
14998,
15961,
1268,
7147
] | 0.054085 |
217 | Summary: Trp/Gly–enriched beta‑strand surface patches (often centered on a GGxW/GGW motif) that form CBM‑like carbohydrate‑interaction surfaces in glycan‑handling proteins; these occur predominantly in extracytoplasmic/lumenal enzymes but also in cytosolic glycan enzymes. The same sequence/structural signature is prese... | Trp/Gly–enriched beta‑strand surface patches (often centered on a GGxW/GGW motif) that form CBM‑like carbohydrate‑interaction surfaces in glycan‑handling proteins; these occur predominantly in extracytoplasmic/lumenal enzymes but also in cytosolic glycan enzymes. The same sequence/structural signature is present in the... | Regional activation across long, contiguous segments of beta‑strands with connecting coils; residue‑level peaks at exposed beta‑strands bearing Trp/Tyr and clustered glycines. Catalytic residues and signal peptides are typically not highlighted. In YidC, activation collapses to a short, strong patch overlapping the con... | Ligand-binding site | - Polysaccharide lyases (e.g., exo‑oligoalginate lyase): activation on a C‑terminal, beta‑sheet‑rich domain consistent with a CBM‑like carbohydrate‑binding surface rather than the catalytic site.
- Glycoside hydrolases (e.g., alpha‑galactosidase): activation on an N‑terminal beta‑strand block that behaves as an accesso... | 7,687,372 | 3.297986 | 27.765625 | [
{
"activation": 27.765625,
"uniref_id": "A0A1M5UEH0"
},
{
"activation": 27.671875,
"uniref_id": "UPI002FCDFA4C"
},
{
"activation": 27.625,
"uniref_id": "UPI0024188DCE"
},
{
"activation": 27.609375,
"uniref_id": "A0A2M9Z6H7"
},
{
"activation": 27.59375,
"uniref... | [
{
"activation": 22.971946716308594,
"uniprot_id": "Q92AT0"
},
{
"activation": 22.646259307861328,
"uniprot_id": "Q8P3J4"
},
{
"activation": 21.928878784179688,
"uniprot_id": "Q76IQ9"
},
{
"activation": 21.215993881225586,
"uniprot_id": "P42592"
},
{
"activation": ... | [
15242,
5864,
13232,
8027,
10259,
8417,
11240,
7759,
10880,
13829
] | 0.217831 |
218 | Summary: Small-residue–rich segments within alpha-helical transmembrane domains of MFS-like 12‑TM solute carriers, especially the inner/gating helices (often TM4 and TM10) and their cytoplasmic-side termini/kinks, featuring glycine/alanine (GxxxG-like) motifs that enable tight helix packing and conformational switching... | Small-residue–rich segments within alpha-helical transmembrane domains of MFS-like 12‑TM solute carriers, especially the inner/gating helices (often TM4 and TM10) and their cytoplasmic-side termini/kinks, featuring glycine/alanine (GxxxG-like) motifs that enable tight helix packing and conformational switching in secon... | Multiple residue-level peaks distributed across several transmembrane helices; strongest on glycine/small residues within helices and at helix–loop boundaries or helical kinks; minimal activation in extramembrane loops; recurrent paired peaks in mid and late TMs consistent with the TM4/TM10 gating helices of the MFS fo... | Membrane-associated | - MFS myo-inositol porter (IolF): peaks in glycine-rich stretches of transmembrane helices, including the canonical inner helices.
- Aromatic acid MFS transporter (3‑(3‑hydroxy‑phenyl)propionate porter): strong activation in glycine-rich motifs in TM4 and TM10.
- Uncharacterized MFS permease (YhhS): activation at the C... | 16,997,327 | 2.504509 | 28.90625 | [
{
"activation": 28.90625,
"uniref_id": "UPI000AAB36AF"
},
{
"activation": 28.609375,
"uniref_id": "UPI0021AE8929"
},
{
"activation": 28.546875,
"uniref_id": "A0A524D648"
},
{
"activation": 28.546875,
"uniref_id": "A0A524G9M6"
},
{
"activation": 28.546875,
"uni... | [
{
"activation": 26.949275970458984,
"uniprot_id": "P39843"
},
{
"activation": 26.652484893798828,
"uniprot_id": "Q05940"
},
{
"activation": 26.47422218322754,
"uniprot_id": "P08194"
},
{
"activation": 26.277698516845703,
"uniprot_id": "P37621"
},
{
"activation": 2... | [
2896,
12632,
11505,
5710,
12445,
7349,
2285,
13808,
12668,
5233
] | 0.710257 |
219 | Summary: Short coil/turn connectors at secondary-structure junctions—especially the 4-6 residue loops that connect a helix to a beta-strand or immediately precede the start of a beta-strand; a generic structural motif enriched in glycine/proline and charged residues, common across enzyme folds (not cofactor-specific, t... | Short coil/turn connectors at secondary-structure junctions—especially the 4-6 residue loops that connect a helix to a beta-strand or immediately precede the start of a beta-strand; a generic structural motif enriched in glycine/proline and charged residues, common across enzyme folds (not cofactor-specific, though fre... | Residue-level peaks distributed across many noncontiguous short segments; each peak maps to a coil/turn between major secondary-structure elements (often helix-to-strand), with variable flexibility but often high-confidence, structured loops. | Structural motif | - ThDP-dependent benzaldehyde lyase: multiple short coil loops at helix–beta-strand transitions (e.g., GAKL, KQLPL) highlighted irrespective of local disorder.
- Acetolactate synthase large subunit (IlvB/ALS): activated coils within cofactor-binding regions (ThDP/FAD-annotated) and other helix–strand connectors (e.g., ... | 65,930,801 | 1.14896 | 14.898438 | [
{
"activation": 14.8984375,
"uniref_id": "A0A915ZED7"
},
{
"activation": 14.7734375,
"uniref_id": "A0A2P4PPS3"
},
{
"activation": 14.3515625,
"uniref_id": "A0A2Z6SBM4"
},
{
"activation": 14.1640625,
"uniref_id": "UPI0025474AC3"
},
{
"activation": 14.03125,
"un... | [
{
"activation": 13.03283977508545,
"uniprot_id": "Q9USY1"
},
{
"activation": 12.528860092163086,
"uniprot_id": "P33025"
},
{
"activation": 11.882006645202637,
"uniprot_id": "P0ADF6"
},
{
"activation": 11.374100685119629,
"uniprot_id": "P39358"
},
{
"activation": 1... | [
5477,
7884,
16233,
735,
12229,
16062,
14694,
5900,
14499,
4239
] | 0.307385 |
220 | Summary: Phenylalanine-focused residue identity feature: detects Phe (F) residues, with a preference for F-rich, hydrophobic stretches (e.g., signal peptides and transmembrane helices), but independent of secondary structure or specific function
Activation pattern: Residue-level peaks centered on F; short regional runs... | Phenylalanine-focused residue identity feature: detects Phe (F) residues, with a preference for F-rich, hydrophobic stretches (e.g., signal peptides and transmembrane helices), but independent of secondary structure or specific function | Residue-level peaks centered on F; short regional runs when multiple F residues cluster (often at N-termini, signal peptides, and transmembrane helices); low, uniform amplitudes across many proteins | Compositional bias | - Neuropeptide precursors: activates on every Phe across the signal peptide, propeptide, and mature peptide (e.g., F in “GFYGG-amide”), regardless of predicted secondary structure.
- Small single-pass membrane proteins: strong activation on clustered Phe within the transmembrane helix and adjacent hydrophobic regions i... | 204,792,981 | 0.015566 | 22.28125 | [
{
"activation": 22.28125,
"uniref_id": "A0A160TUZ9"
},
{
"activation": 21.796875,
"uniref_id": "UPI0031ECFF9C"
},
{
"activation": 21.6875,
"uniref_id": "A0A238VPB8"
},
{
"activation": 21.5,
"uniref_id": "A0A0E9VAW3"
},
{
"activation": 21.5,
"uniref_id": "A0A2J... | [
{
"activation": 17.99864387512207,
"uniprot_id": "H0YL14"
},
{
"activation": 17.76692771911621,
"uniprot_id": "Q9HBF5"
},
{
"activation": 17.701290130615234,
"uniprot_id": "P03086"
},
{
"activation": 17.585613250732422,
"uniprot_id": "O90299"
},
{
"activation": 17... | [
189,
2940,
6016,
7523,
15189,
12385,
12227,
6192,
16243,
6818
] | 0.001474 |
221 | Summary: Conserved small‑domain helix→loop→β segment predominantly found in fold‑type I (aspartate‑aminotransferase–like) PLP enzymes; in these it forms the PLP 5′‑phosphate–binding pocket and part of the intersubunit interface. In rare cases, a structurally analogous C‑terminal interface segment in non‑PLP sulfur‑tran... | Conserved small‑domain helix→loop→β segment predominantly found in fold‑type I (aspartate‑aminotransferase–like) PLP enzymes; in these it forms the PLP 5′‑phosphate–binding pocket and part of the intersubunit interface. In rare cases, a structurally analogous C‑terminal interface segment in non‑PLP sulfur‑transferases ... | Regional activation across mid‑to‑C‑terminal core segments (≈20–50 residues), with strongest signal at helix‑to‑loop transitions continuing into one or two β‑strands; frequently high‑confidence structured regions; minor adjacent peaks; generally not centered on the catalytic Schiff‑base Lys but on the nearby phosphate‑... | Ligand-binding site | - Aminotransferases (e.g., kynurenine/alpha‑aminoadipate aminotransferase/KAT): activation on a well‑structured helix→β transition in the small C‑terminal domain corresponding to the PLP 5′‑phosphate–binding loop.
- UDP‑sugar aminotransferases (e.g., UDP‑2‑acetamido‑2‑deoxy‑3‑oxo‑D‑glucuronate aminotransferase): activa... | 11,353,492 | 2.90804 | 25.296875 | [
{
"activation": 25.296875,
"uniref_id": "A0A920PM55"
},
{
"activation": 25.171875,
"uniref_id": "A0A941IBV6"
},
{
"activation": 25.046875,
"uniref_id": "A0A2W5S6K4"
},
{
"activation": 25.03125,
"uniref_id": "A0A3A0BFL0"
},
{
"activation": 25,
"uniref_id": "A0A... | [
{
"activation": 23.623126983642578,
"uniprot_id": "B8NM72"
},
{
"activation": 23.323579788208008,
"uniprot_id": "Q4WD47"
},
{
"activation": 22.932952880859375,
"uniprot_id": "P9WQ67"
},
{
"activation": 22.883569717407227,
"uniprot_id": "Q93WX6"
},
{
"activation": ... | [
14388,
10408,
594,
928,
3772,
11876,
11033,
3116,
4372,
3445
] | 0.186704 |
222 | Summary: Short flexible loop/turn segments that cap and initiate beta-strands (coil-to-beta transitions), especially in beta-rich, extracellular/lumenal repeat domains (e.g., Ig-like, cadherin, macroglobulin, filamin), but also present in lumenal/cytosolic beta-sandwich/alpha-beta folds.
Activation pattern: Residue-lev... | Short flexible loop/turn segments that cap and initiate beta-strands (coil-to-beta transitions), especially in beta-rich, extracellular/lumenal repeat domains (e.g., Ig-like, cadherin, macroglobulin, filamin), but also present in lumenal/cytosolic beta-sandwich/alpha-beta folds. | Residue-level peaks clustered into short contiguous segments that lie immediately N-terminal to, or span the first residues of, beta-strands; often occur at coil-to-strand boundaries with glycine/small/polar residues and recur many times across long extracellular regions of modular proteins. | Structural motif | Cadherins/protocadherins: loop within a cadherin repeat preceding a beta-strand; Ig-like adhesion molecules (ICAM): short loops just before beta-strands in Ig C2-type domains; Alpha-2-macroglobulin/complement/TEPs: multiple unstructured loops immediately preceding beta-strands across the macroglobulin architecture; TRI... | 17,754,605 | 2.46092 | 24.109375 | [
{
"activation": 24.109375,
"uniref_id": "UPI0025DBFECF"
},
{
"activation": 23.5625,
"uniref_id": "A0A967SV36"
},
{
"activation": 23.1875,
"uniref_id": "X1Q558"
},
{
"activation": 23.1875,
"uniref_id": "A0A9E7UNG4"
},
{
"activation": 23.125,
"uniref_id": "UPI00... | [
{
"activation": 19.191768646240234,
"uniprot_id": "A6NHR9"
},
{
"activation": 19.11136817932129,
"uniprot_id": "Q54F54"
},
{
"activation": 19.09998321533203,
"uniprot_id": "P43261"
},
{
"activation": 18.91299819946289,
"uniprot_id": "Q54K09"
},
{
"activation": 18.... | [
1440,
15353,
215,
3313,
9095,
4146,
7086,
7600,
2598,
6812
] | 0.347964 |
223 | Summary: Extracellular glycan-recognition surfaces and repeat-rich motifs—i.e., carbohydrate-binding modules (CBMs), lectin-like carbohydrate-recognition domains (ricin/L-type/PA14-like), beta-helix glycan-binding faces of depolymerases, and S/T-rich or GW/WT/GxT-containing adhesin repeats—used by secreted, cell-surfac... | Extracellular glycan-recognition surfaces and repeat-rich motifs—i.e., carbohydrate-binding modules (CBMs), lectin-like carbohydrate-recognition domains (ricin/L-type/PA14-like), beta-helix glycan-binding faces of depolymerases, and S/T-rich or GW/WT/GxT-containing adhesin repeats—used by secreted, cell-surface, or ER-... | Regional, multi-patch activation on short W/G/S/T/D/N-rich motifs and surface loops within carbohydrate-binding domains or low-complexity repeats; often immediately downstream of the signal peptide (not on the signal peptide itself), frequently in flexible/disordered N-terminal segments or linkers; multiple discontiguo... | Ligand-binding site | - Hyaluronate lyase (polysaccharide lyase): activation in a short, flexible N-terminal segment just after the signal peptide, consistent with an ancillary hyaluronan-binding patch rather than the catalytic core
- Polysaccharide lyases and glycoside hydrolases (including marine CAZymes): activation on CBMs and W/S/T-ric... | 5,683,863 | 3.599934 | 21.234375 | [
{
"activation": 21.234375,
"uniref_id": "X1VY43"
},
{
"activation": 20.828125,
"uniref_id": "UPI001669D80C"
},
{
"activation": 20.71875,
"uniref_id": "A0A955DUW1"
},
{
"activation": 20.609375,
"uniref_id": "A0A846HVQ0"
},
{
"activation": 20.59375,
"uniref_id":... | [
{
"activation": 19.06778335571289,
"uniprot_id": "P16397"
},
{
"activation": 17.68987274169922,
"uniprot_id": "Q8RQU9"
},
{
"activation": 16.84404754638672,
"uniprot_id": "P46071"
},
{
"activation": 16.706729888916016,
"uniprot_id": "Q51817"
},
{
"activation": 16.... | [
4888,
1324,
15441,
12824,
5077,
2541,
15589,
11877,
1585,
3685
] | 0.348629 |
224 | Summary: Helix–loop junctions and short alpha‑helical segments, with a strong bias toward the edges of transmembrane helices in multi‑pass membrane proteins and flexible capping loops within helical catalytic domains (e.g., the TRUD pseudouridine‑synthase domain)
Activation pattern: Mixed: (1) regional activation acros... | Helix–loop junctions and short alpha‑helical segments, with a strong bias toward the edges of transmembrane helices in multi‑pass membrane proteins and flexible capping loops within helical catalytic domains (e.g., the TRUD pseudouridine‑synthase domain) | Mixed: (1) regional activation across parts of a helical enzyme domain with peaks on flexible/low‑pLDDT loops; (2) sparse, residue‑level peaks within transmembrane helices or immediately adjacent cytosolic/periplasmic helices in large multi‑pass membrane proteins. Sequence tendency toward polar/charged helix‑cap residu... | Structural motif | - tRNA pseudouridine synthase (TruD/PUS7 family): activation spans the C‑terminal TRUD domain, peaking on a disordered loop within the domain.
- Copper‑exporting P‑type ATPase: two short patches in the cytoplasmic region (one within an α‑helix, one in an unstructured loop linking β‑strand to α‑helix).
- Cation diffusio... | 6,280,517 | 3.500113 | 16.890625 | [
{
"activation": 16.890625,
"uniref_id": "A0A2K8P6A5"
},
{
"activation": 16.875,
"uniref_id": "A0A1I7VNV9"
},
{
"activation": 16.734375,
"uniref_id": "UPI0033371DB4"
},
{
"activation": 16.6875,
"uniref_id": "A0A2K8NW63"
},
{
"activation": 16.671875,
"uniref_id"... | [
{
"activation": 10.693917274475098,
"uniprot_id": "P52129"
},
{
"activation": 7.992182731628418,
"uniprot_id": "Q3B8R1"
},
{
"activation": 6.776278972625732,
"uniprot_id": "P25280"
},
{
"activation": 6.483462333679199,
"uniprot_id": "A0A0H5SJ89"
},
{
"activation":... | [
15257,
11361,
15603,
4576,
15873,
15302,
2996,
12357,
5551,
963
] | 0.271732 |
225 | Summary: Hydrophobic repeat-domain scaffold segments—solenoids (LRR, ankyrin, TPR, WD and kelch beta-propellers) and Ig-like beta-sandwich repeats—and the short helix/coil linkers adjoining them, typically in the peripheral repeat arrays of large innate/adaptive-immunity and signaling scaffold proteins
Activation patte... | Hydrophobic repeat-domain scaffold segments—solenoids (LRR, ankyrin, TPR, WD and kelch beta-propellers) and Ig-like beta-sandwich repeats—and the short helix/coil linkers adjoining them, typically in the peripheral repeat arrays of large innate/adaptive-immunity and signaling scaffold proteins | Regional activation over long continuous tracts spanning successive repeats and adjacent linkers; broad plateaus with local peaks at repeat boundaries or just after a repeat; enriched for hydrophobic positions; often at domain-array peripheries (commonly C-terminal, sometimes N-terminal) of multidomain proteins; second... | Repeat | - Plant NLR (NB-ARC–LRR) disease-resistance proteins: within an LRR repeat and extending into the following linker
- Animal NLRs: LRR array repeats and neighboring linkers
- Apaf-1-like apoptosome adaptors: C-terminal WD-repeat/propeller blades and neighboring linkers
- Kelch/BTB substrate adaptors: kelch beta-propelle... | 4,707,283 | 3.788454 | 22.125 | [
{
"activation": 22.125,
"uniref_id": "A0CIR9"
},
{
"activation": 22,
"uniref_id": "UPI002191F979"
},
{
"activation": 21.96875,
"uniref_id": "A0A0C9XK71"
},
{
"activation": 21.921875,
"uniref_id": "A0AAD9S8T7"
},
{
"activation": 21.90625,
"uniref_id": "A0A9N9ZH... | [
{
"activation": 19.346912384033203,
"uniprot_id": "Q9ULJ7"
},
{
"activation": 19.027873992919922,
"uniprot_id": "Q3UP24"
},
{
"activation": 18.84731674194336,
"uniprot_id": "Q13075"
},
{
"activation": 18.344463348388672,
"uniprot_id": "Q7KLI1"
},
{
"activation": 1... | [
9697,
5798,
9935,
5079,
7108,
13908,
4947,
4794,
7393,
933
] | 0.210711 |
226 | Summary: A short glycine‑rich β–α junction/loop motif (β‑strand → coil → α‑helix or adjacent helix/coil → β) enriched in small/polar and basic residues (G/S/T/N, Lys/Arg) with frequent Pro and aromatics; in restriction–modification proteins these segments form target‑recognition elements within TRDs (strongest in Type ... | A short glycine‑rich β–α junction/loop motif (β‑strand → coil → α‑helix or adjacent helix/coil → β) enriched in small/polar and basic residues (G/S/T/N, Lys/Arg) with frequent Pro and aromatics; in restriction–modification proteins these segments form target‑recognition elements within TRDs (strongest in Type I specifi... | Regional activation as long blocks within TRDs of Type I specificity subunits and adenine DNA methyltransferases; otherwise one or a few narrow, residue‑level peaks at β–α junctions or short β‑strands, often centered on GG/GxG or Gly–Tyr/His–Gly motifs. | Structural motif | - Type I restriction–modification specificity subunits: activation in both target recognition domains at loop→helix→β segments; central helical linker remains inactive.
- N6‑adenine DNA methyltransferases (including BREX‑associated): activation concentrated in the C‑terminal target‑recognition domain (glycine/lysine‑ri... | 8,978,053 | 3.142782 | 20.828125 | [
{
"activation": 20.828125,
"uniref_id": "UPI003AA7CF7C"
},
{
"activation": 20.796875,
"uniref_id": "UPI001788575A"
},
{
"activation": 20.78125,
"uniref_id": "UPI00111F73B1"
},
{
"activation": 20.78125,
"uniref_id": "UPI0022B82E57"
},
{
"activation": 20.734375,
... | [
{
"activation": 19.088327407836914,
"uniprot_id": "Q49434"
},
{
"activation": 18.649934768676758,
"uniprot_id": "P19704"
},
{
"activation": 18.10209846496582,
"uniprot_id": "Q57594"
},
{
"activation": 17.751501083374023,
"uniprot_id": "P06990"
},
{
"activation": 1... | [
4589,
3306,
3513,
12097,
1226,
2212,
4585,
8257,
11942,
7471
] | 0.177903 |
227 | Summary: Boundary/junction segments of secreted and surface-exposed precursor proteins—most often the short, small/polar‑rich stretch immediately after signal peptide cleavage and the starts of luminal/extracellular domains (including catalytic and adhesion modules); in Gram‑negative autotransporters this extends to th... | Boundary/junction segments of secreted and surface-exposed precursor proteins—most often the short, small/polar‑rich stretch immediately after signal peptide cleavage and the starts of luminal/extracellular domains (including catalytic and adhesion modules); in Gram‑negative autotransporters this extends to the passeng... | Regional, contiguous blocks rather than single residues. Strong blocks at the N-terminus of the mature chain that decay over the first ~10–30 residues after signal peptide cleavage; additional blocks at the start of structured extracellular domains or at membrane-to-extracellular boundaries. In multi-domain secreted hy... | Post-translational modification | - Proprotein convertase (furin): minor activation at the luminal boundary of the transmembrane region and a stronger block at the N-terminus of the stabilizing P/Homo B (P) domain, matching a luminal domain start.
- ECM modular glycoproteins with Sushi/EGF/nidogen repeats: sharp peak immediately after the signal peptid... | 12,090,215 | 2.845169 | 15.765625 | [
{
"activation": 15.765625,
"uniref_id": "A0A3B8ZDN8"
},
{
"activation": 15.625,
"uniref_id": "A0A3B8ZGG1"
},
{
"activation": 15.4296875,
"uniref_id": "A0A3B8ZHC1"
},
{
"activation": 15.359375,
"uniref_id": "A0A3B8ZHS9"
},
{
"activation": 15.34375,
"uniref_id":... | [
{
"activation": 12.754582405090332,
"uniprot_id": "P15636"
},
{
"activation": 10.521212577819824,
"uniprot_id": "P83543"
},
{
"activation": 9.72335433959961,
"uniprot_id": "P80561"
},
{
"activation": 8.502728462219238,
"uniprot_id": "P23916"
},
{
"activation": 7.4... | [
10085,
2461,
8470,
13331,
11464,
15549,
10402,
111,
11343,
12806
] | 0.352477 |
228 | Summary: Glycine-rich nucleotide cofactor–binding entry segment (loop + adjoining helix) at the start of enzyme domains—most often the SAM-binding motif I region of Class I methyltransferases; the feature also fires on structurally analogous pre-domain helix/loop segments at the starts of other domains
Activation patte... | Glycine-rich nucleotide cofactor–binding entry segment (loop + adjoining helix) at the start of enzyme domains—most often the SAM-binding motif I region of Class I methyltransferases; the feature also fires on structurally analogous pre-domain helix/loop segments at the starts of other domains | Regional activation in a single contiguous block (~30–60 aa) centered on a flexible loop that transitions into an alpha-helix; peaks often coincide with glycine-rich phosphate-binding motifs and annotated SAM-binding residues; typically occurs at domain starts or boundary regions with lower pLDDT that rise into ordered... | Ligand-binding site | - NSUN/C5-cytosine RNA methyltransferases (e.g., rRNA SSU methyltransferase B): activation on the core N-lobe adjacent to, but not necessarily including, catalytic Cys; captures the entry segment of the methyltransferase core
- Wybutosine-synthesizing enzyme TYW2: activation overlaps SAM-binding residues within the hel... | 6,994,603 | 3.392426 | 25.03125 | [
{
"activation": 25.03125,
"uniref_id": "UPI00265F7919"
},
{
"activation": 24.859375,
"uniref_id": "A0A970Y484"
},
{
"activation": 24.796875,
"uniref_id": "A0A7S4HSU2"
},
{
"activation": 24.78125,
"uniref_id": "A0A0D0QQU4"
},
{
"activation": 24.78125,
"uniref_i... | [
{
"activation": 23.15813446044922,
"uniprot_id": "Q5SK01"
},
{
"activation": 22.488054275512695,
"uniprot_id": "Q96P11"
},
{
"activation": 22.15087127685547,
"uniprot_id": "Q63ZY6"
},
{
"activation": 22.127519607543945,
"uniprot_id": "Q8GYE8"
},
{
"activation": 22... | [
14484,
15598,
7906,
535,
2121,
12599,
3832,
15368,
2472,
6905
] | 0.169707 |
229 | Summary: Mid-bilayer segments of alpha-helical transmembrane spans in multi-pass integral membrane proteins that mediate substrate/ion movement or energy-coupled ion translocation (antiporters, permeases, channels, and respiratory chain ion-pumping subunits), i.e., the hydrophobic core of selected TM helices enriched f... | Mid-bilayer segments of alpha-helical transmembrane spans in multi-pass integral membrane proteins that mediate substrate/ion movement or energy-coupled ion translocation (antiporters, permeases, channels, and respiratory chain ion-pumping subunits), i.e., the hydrophobic core of selected TM helices enriched for L/I/V/... | Long contiguous runs (≈10–40 aa) confined to transmembrane alpha-helices, often on multiple helices per protein but not all; strongest in the helix core and tapering at membrane boundaries; largely absent from cytosolic/periplasmic loops with only occasional weak spillover near helix–loop junctions; avoids catalytic/fu... | Membrane-associated | add “Respiratory chain complex I membrane subunits (e.g., NuoH/ND1): activation across core TM helices.” | 36,219,527 | 1.747967 | 10.914063 | [
{
"activation": 10.9140625,
"uniref_id": "UPI0012EE5776"
},
{
"activation": 10.859375,
"uniref_id": "A0A938W2D6"
},
{
"activation": 10.796875,
"uniref_id": "A0A7W0V4J9"
},
{
"activation": 10.734375,
"uniref_id": "UPI001F482675"
},
{
"activation": 10.71875,
"un... | [
{
"activation": 9.143138885498047,
"uniprot_id": "O34840"
},
{
"activation": 9.037500381469727,
"uniprot_id": "P16430"
},
{
"activation": 8.885462760925293,
"uniprot_id": "P31801"
},
{
"activation": 8.682798385620117,
"uniprot_id": "O34610"
},
{
"activation": 8.57... | [
3766,
2883,
424,
10999,
2497,
14149,
5547,
5502,
9272,
10804
] | 0.548642 |
230 | Summary: Cell wall/extracellular polymer interaction/catalysis modules: the feature targets mature catalytic or recognition regions of proteins that bind, remodel, or transfer groups within glycans (peptidoglycan, chitin, plant cell‑wall polysaccharides, glycoconjugates), ribose‑based polymers/metabolites (RNA, ADP‑rib... | Cell wall/extracellular polymer interaction/catalysis modules: the feature targets mature catalytic or recognition regions of proteins that bind, remodel, or transfer groups within glycans (peptidoglycan, chitin, plant cell‑wall polysaccharides, glycoconjugates), ribose‑based polymers/metabolites (RNA, ADP‑ribose), and... | Primarily long, contiguous, domain‑scale activation within catalytic/recognition cores. When present, signal peptides or transmembrane anchors are low with activation starting in the luminal/periplasmic mature domain; in soluble cytosolic/nuclear enzymes, activation concentrates in the catalytic subdomain and glycan/ri... | Catalytic function | - Peptidoglycan‑recognition proteins (amidase‑like PGRPs): activation on an N‑terminal disulfide‑bonded peptidoglycan‑binding loop.
- Endo‑chitosanases/glycoside hydrolases: activation across the catalytic core, including conserved aromatics lining the groove.
- Type II Golgi sialyltransferases: activation over the C‑t... | 5,507,586 | 3.631439 | 16.609375 | [
{
"activation": 16.609375,
"uniref_id": "A0A158KY41"
},
{
"activation": 16.203125,
"uniref_id": "A0A516LKR1"
},
{
"activation": 16.015625,
"uniref_id": "UPI003B51A3CD"
},
{
"activation": 16,
"uniref_id": "UPI00307DC3FC"
},
{
"activation": 16,
"uniref_id": "UPI... | [
{
"activation": 10.247147560119629,
"uniprot_id": "P0AA99"
},
{
"activation": 10.21037483215332,
"uniprot_id": "Q75R32"
},
{
"activation": 10.007862091064453,
"uniprot_id": "Q875I9"
},
{
"activation": 8.420145034790039,
"uniprot_id": "C0SP99"
},
{
"activation": 7.... | [
8689,
3479,
3779,
1158,
12598,
1578,
8087,
13037,
852,
13635
] | 0.365715 |
231 | Summary: Divalent metal–cofactor coordination and adjacent catalytic microenvironments: the feature highlights residues and short regions that chelate metals (Mg2+ in nucleases/NTPases; Zn2+/Cu+/Fe/heme via His/Cys/Met motifs) and the immediately neighboring loops/secondary-structure elements that shape nucleic-acid or... | Divalent metal–cofactor coordination and adjacent catalytic microenvironments: the feature highlights residues and short regions that chelate metals (Mg2+ in nucleases/NTPases; Zn2+/Cu+/Fe/heme via His/Cys/Met motifs) and the immediately neighboring loops/secondary-structure elements that shape nucleic-acid or cofactor... | Mixed: domain-level activation across the structured catalytic core of small enzymes (often strongest near acidic Mg2+-binding residues and DNA/RNA-contact loops); short, N‑terminal Cys/His/Met-rich stretches in metal-handling/membrane transporters; and residue-level peaks at single conserved hydrophobic positions that... | Ligand-binding site | - Holliday junction endonuclease (RusA): peaks on catalytic Asp residues that bind Mg2+ and on adjacent DNA-binding loops, with broad activation over the folded core.
- 6-pyruvoyl-tetrahydropterin synthase/QueD (6-PTPS family): activation around the Zn2+-coordinating His/Cys triad and catalytic loop of the small enzyme... | 3,336,780 | 4.132559 | 23.609375 | [
{
"activation": 23.609375,
"uniref_id": "A0A6V6ZHP7"
},
{
"activation": 23.546875,
"uniref_id": "UPI002636968D"
},
{
"activation": 23.234375,
"uniref_id": "UPI0027DE9E61"
},
{
"activation": 23.15625,
"uniref_id": "UPI002882EC38"
},
{
"activation": 23.140625,
"... | [
{
"activation": 7.562474250793457,
"uniprot_id": "P0AG74"
},
{
"activation": 7.449600696563721,
"uniprot_id": "O67766"
},
{
"activation": 7.404697418212891,
"uniprot_id": "Q38100"
},
{
"activation": 5.9775590896606445,
"uniprot_id": "D1L2Y9"
},
{
"activation": 5.9... | [
8279,
503,
3836,
6745,
7146,
5616,
2515,
9176,
2881,
366
] | 0.446383 |
232 | Summary: Surface-exposed loop/linker segments characteristic of extracytoplasmic (secreted/periplasmic) proteins—typically enriched in small/polar and acidic residues (Gly/Ser/Pro/Asp/Glu), often flexible or low-complexity—and spanning contiguous tracts within or adjacent to extracellular domains; in cytosolic proteins... | Surface-exposed loop/linker segments characteristic of extracytoplasmic (secreted/periplasmic) proteins—typically enriched in small/polar and acidic residues (Gly/Ser/Pro/Asp/Glu), often flexible or low-complexity—and spanning contiguous tracts within or adjacent to extracellular domains; in cytosolic proteins this red... | Primarily regional activation over long, contiguous coil/strand-rich stretches in extracellular domains; secondary pattern of isolated residue-level peaks at loop turns or helix caps, especially in non-secreted or membrane proteins. | Compositional bias | - Type IV pilin-like proteins: strong activation across the C-terminal polar/disordered region (coil/β) distinct from the N-terminal transmembrane helix.
- Papain-like cysteine proteases (e.g., Cathepsin B): activation across a β–loop–helix–β segment of the heavy chain with high structural confidence, not centered on c... | 3,918,178 | 3.971939 | 25.828125 | [
{
"activation": 25.828125,
"uniref_id": "A0A3D2TH57"
},
{
"activation": 25.546875,
"uniref_id": "A0A6M5YIR1"
},
{
"activation": 25.34375,
"uniref_id": "A0A5C5UYS5"
},
{
"activation": 25.234375,
"uniref_id": "A0A9E5TB61"
},
{
"activation": 25.234375,
"uniref_id... | [
{
"activation": 11.670327186584473,
"uniprot_id": "Q72JC2"
},
{
"activation": 8.002344131469727,
"uniprot_id": "Q00517"
},
{
"activation": 6.985475540161133,
"uniprot_id": "P45761"
},
{
"activation": 5.0614752769470215,
"uniprot_id": "Q8NK89"
},
{
"activation": 4.... | [
2656,
14903,
4827,
5723,
10951,
7252,
11844,
11788,
8242,
11805
] | 0.224907 |
233 | Summary: Ser/Thr/Gly-rich flexible loops in soluble cytosolic domains mediating phosphotransfer, phosphorylation, and protein–protein interactions—most prominently PTS phosphocarrier domains (EIIA/EIIB) and σ54-dependent regulatory C-termini—with generalization to ATPase/redox/chelation complexes, SEFIR adaptor domains... | Ser/Thr/Gly-rich flexible loops in soluble cytosolic domains mediating phosphotransfer, phosphorylation, and protein–protein interactions—most prominently PTS phosphocarrier domains (EIIA/EIIB) and σ54-dependent regulatory C-termini—with generalization to ATPase/redox/chelation complexes, SEFIR adaptor domains, and sel... | Regional activation: contiguous 20–200 aa stretches within soluble, non-membrane domains; in multi-domain PTS permeases, activation localizes to EIIB/EIIA rather than EIIC; in σ54-dependent regulators, long segments late in the sequence (C-terminal regions); segments are compositionally enriched in Ser/Thr and Gly and ... | Compositional bias | - PTS phosphotransfer components (EIIA/EIIB across mannitol/mannose/lactose/fructose/sorbitol/galactitol/chitobiose/ascorbate systems): activation on cytosolic phosphocarrier domains (around the phosphoacceptor His/Cys and adjacent S/T/G-rich loops), not on transmembrane EIIC.
- σ54-dependent enhancer-binding/regulator... | 23,665,704 | 2.173538 | 16.0625 | [
{
"activation": 16.0625,
"uniref_id": "UPI0019588935"
},
{
"activation": 15.9765625,
"uniref_id": "A0A0R2EYF1"
},
{
"activation": 15.796875,
"uniref_id": "R3TRZ1"
},
{
"activation": 15.734375,
"uniref_id": "A0A4P5QB77"
},
{
"activation": 15.6875,
"uniref_id": ... | [
{
"activation": 14.041474342346191,
"uniprot_id": "P23914"
},
{
"activation": 13.96640682220459,
"uniprot_id": "D0ZLR9"
},
{
"activation": 12.39552116394043,
"uniprot_id": "P46321"
},
{
"activation": 12.253423690795898,
"uniprot_id": "O31644"
},
{
"activation": 12... | [
14196,
2611,
6018,
835,
13675,
7912,
6897,
3782,
11219,
3843
] | 0.362587 |
234 | Summary: Rhodanese-like catalytic fold shared by cysteine-dependent sulfurtransferases and DSP/PTP-type phosphatases, with a consistent bias toward the C-terminal subdomain (helices/loops downstream of the catalytic Cys/P-loop) that scaffolds sulfur/phosphate transfer rather than the nucleophilic cysteine loop itself.
... | Rhodanese-like catalytic fold shared by cysteine-dependent sulfurtransferases and DSP/PTP-type phosphatases, with a consistent bias toward the C-terminal subdomain (helices/loops downstream of the catalytic Cys/P-loop) that scaffolds sulfur/phosphate transfer rather than the nucleophilic cysteine loop itself. | Regional, domain-internal activation as long contiguous stretches within the C-terminal half of Rhodanese/DSP/PTP catalytic domains; spans multiple helices and connecting loops; typically spares the catalytic Cys loop and immediate signature motif; occasionally extends into adjacent low-confidence C-terminal tails; min... | Domain | Rhodanese-domain fusions in MoeB/ThiF-like molybdopterin-synthesis systems: strong activation across the C-terminal rhodanese domain; Tyrosine-protein phosphatases (compact/viral-like and other small PTPs): broad activation over the C-terminal half of the PTP catalytic domain and into the C-terminus, not on the Cys loo... | 6,380,213 | 3.484364 | 26.59375 | [
{
"activation": 26.59375,
"uniref_id": "UPI002452DEEB"
},
{
"activation": 25.796875,
"uniref_id": "A0A2K2CV76"
},
{
"activation": 25.78125,
"uniref_id": "A0A525CRK1"
},
{
"activation": 25.75,
"uniref_id": "A0A5K1AXG3"
},
{
"activation": 25.703125,
"uniref_id":... | [
{
"activation": 23.00922393798828,
"uniprot_id": "Q8RUD6"
},
{
"activation": 22.621347427368164,
"uniprot_id": "O95396"
},
{
"activation": 22.20199203491211,
"uniprot_id": "Q38853"
},
{
"activation": 22.03966522216797,
"uniprot_id": "Q8TEA7"
},
{
"activation": 21.... | [
12790,
3046,
2866,
12964,
9137,
15472,
3057,
13411,
9894,
4402
] | 0.185873 |
235 | Summary: Well‑ordered alpha‑helical segments embedded in enzymatic catalytic cores, often flanking (but not sitting on) nucleotide- or metal‑cofactor binding sites across diverse enzyme families
Activation pattern: Sparse, residue‑level peaks concentrated on high‑confidence alpha helices within annotated catalytic doma... | Well‑ordered alpha‑helical segments embedded in enzymatic catalytic cores, often flanking (but not sitting on) nucleotide- or metal‑cofactor binding sites across diverse enzyme families | Sparse, residue‑level peaks concentrated on high‑confidence alpha helices within annotated catalytic domains; typically adjacent to active‑site or cofactor‑binding regions rather than on the canonical catalytic residues themselves; enriched at charged/polar and aliphatic positions; distributed throughout proteins witho... | Structural motif | - Processive glycosyltransferases (e.g., cellulose synthase, glucan biosynthesis GTs): peaks on helices in the catalytic subdomain/core helices of the GT domain
- Retroviral Pol polyproteins (reverse transcriptase, RNase H, integrase): peaks on helices within these catalytic domains, including near Mg2+-binding sites i... | 95,445,778 | 0.779007 | 13.929688 | [
{
"activation": 13.9296875,
"uniref_id": "UPI002E231615"
},
{
"activation": 13.921875,
"uniref_id": "A0A927X7Z8"
},
{
"activation": 13.90625,
"uniref_id": "A0A9D1KK95"
},
{
"activation": 13.8515625,
"uniref_id": "A0A938T1K2"
},
{
"activation": 13.796875,
"unir... | [
{
"activation": 12.155787467956543,
"uniprot_id": "F4J3R7"
},
{
"activation": 11.905960083007812,
"uniprot_id": "P46837"
},
{
"activation": 11.884845733642578,
"uniprot_id": "Q8N5C6"
},
{
"activation": 11.86119270324707,
"uniprot_id": "Q9U720"
},
{
"activation": 1... | [
8471,
7257,
11298,
1498,
697,
13618,
7857,
1704,
2436,
1150
] | 0.253212 |
236 | Summary: DNA-binding recognition helix and immediately preceding turn/loop of helix–turn–helix/winged-helix domains (the short Lys/Arg-rich coil-to-helix segment that contacts dsDNA), seen across bacterial transcription factors and related DNA-binding proteins, including the C-terminal domain IV of DnaA and the C-termi... | DNA-binding recognition helix and immediately preceding turn/loop of helix–turn–helix/winged-helix domains (the short Lys/Arg-rich coil-to-helix segment that contacts dsDNA), seen across bacterial transcription factors and related DNA-binding proteins, including the C-terminal domain IV of DnaA and the C-terminal DNA-b... | Residue-level peaks on short segments (typically 6–20 aa) at the loop/turn just before, and the N-terminus of, the recognition helix of HTH/wH domains; often one or two sharp peaks per domain, sometimes multiple short peaks spanning a DNA-binding domain (e.g., DnaA IV). Frequently occurs in mid-to-C-terminal regions fo... | Ligand-binding site | - AraC/XylS-type activators: strong activation within the C-terminal HTH DNA-binding region, especially the loop preceding and start of the recognition helix; secondary peak on the second HTH element.
- TetR-type repressors: a single short activation in the loop and first residues of the N-terminal HTH recognition heli... | 7,796,957 | 3.283832 | 29.390625 | [
{
"activation": 29.390625,
"uniref_id": "A0A2U1B461"
},
{
"activation": 29.09375,
"uniref_id": "A0A2S0KSV1"
},
{
"activation": 28.59375,
"uniref_id": "A0A3D1UYD4"
},
{
"activation": 28.4375,
"uniref_id": "UPI002E10DA9F"
},
{
"activation": 28.390625,
"uniref_id... | [
{
"activation": 26.30129623413086,
"uniprot_id": "P17410"
},
{
"activation": 25.445831298828125,
"uniprot_id": "P0A9E0"
},
{
"activation": 23.5181884765625,
"uniprot_id": "P77379"
},
{
"activation": 23.401763916015625,
"uniprot_id": "P09378"
},
{
"activation": 23.... | [
7353,
14878,
3557,
7797,
2923,
13251,
12191,
11123,
7923,
1992
] | 0.138149 |
237 | Summary: A short, flexible loop at the N-terminus of ABC-type nucleotide-binding domains that lies immediately upstream of the conserved Walker A/P-loop, typically forming a beta-hairpin/turn between two short beta-strands; i.e., a conserved pre-P-loop segment shared across ABC transporters and ABC-like ATPases.
Activa... | A short, flexible loop at the N-terminus of ABC-type nucleotide-binding domains that lies immediately upstream of the conserved Walker A/P-loop, typically forming a beta-hairpin/turn between two short beta-strands; i.e., a conserved pre-P-loop segment shared across ABC transporters and ABC-like ATPases. | Residue-level peaks confined to 5–15 aa segments within ABC NBDs; located ~15–30 residues N-terminal to, and not overlapping, the Walker A/P-loop; commonly a coil/loop connecting two beta-strands with lower confidence (flexible) structure; one peak per NBD (yielding two homologous peaks in two-NBD eukaryotic transporte... | Structural motif | - ECF transporter A components (EcfA/EcfA2): single strong peak in the N-terminal beta-hairpin immediately preceding the P-loop.
- Amino acid importer NBDs (e.g., tyrosine transporter): localized loop near residues 12–18 connecting beta-strands, upstream of the P-loop.
- Bacterial ABC transporter NBDs (generic): loop s... | 9,016,002 | 3.138564 | 24.203125 | [
{
"activation": 24.203125,
"uniref_id": "UPI0029A98C73"
},
{
"activation": 24.1875,
"uniref_id": "A0A841IUX2"
},
{
"activation": 24.140625,
"uniref_id": "A0A895XLC5"
},
{
"activation": 24.125,
"uniref_id": "UPI00366F847B"
},
{
"activation": 24.03125,
"uniref_i... | [
{
"activation": 22.91057014465332,
"uniprot_id": "Q8H1R4"
},
{
"activation": 22.52272605895996,
"uniprot_id": "Q9WY65"
},
{
"activation": 22.249267578125,
"uniprot_id": "P0DX43"
},
{
"activation": 22.2044620513916,
"uniprot_id": "Q2FRT7"
},
{
"activation": 22.1734... | [
1063,
15086,
4334,
9782,
7413,
13254,
4039,
15981,
4787,
8473
] | 0.213231 |
238 | Summary: Short glycine/proline- and acidic residue–enriched helix–loop micro-motifs that form flexible lids or anion-recognition loops at small-molecule/cofactor binding pockets across diverse enzymes, most often contacting phosphate/sulfate groups (including the phosphate of NAD/FMN) or porphyrins.
Activation pattern:... | Short glycine/proline- and acidic residue–enriched helix–loop micro-motifs that form flexible lids or anion-recognition loops at small-molecule/cofactor binding pockets across diverse enzymes, most often contacting phosphate/sulfate groups (including the phosphate of NAD/FMN) or porphyrins. | Regional activation in short (~15–30 aa) internal segments with sharp residue-level peaks at helix–coil junctions; multiple noncontiguous windows per protein are common; sequences frequently display GG/PP/TPP patterns and occasional aromatic (W/Y) residues. | Ligand-binding site | - Acid phosphatases: activation on a short helix-plus-loop within the catalytic domain, consistent with a phosphate-recognition loop near the active site.
- Sirtuins (NAD-dependent deacetylases): activation on a helix-to-coil segment in the catalytic core adjacent to the NAD pyrophosphate-binding region.
- P-type ATPas... | 48,234,960 | 1.461481 | 13.34375 | [
{
"activation": 13.34375,
"uniref_id": "A0A1E4ELL0"
},
{
"activation": 13.1484375,
"uniref_id": "A0A2E7CMG8"
},
{
"activation": 13.0703125,
"uniref_id": "A0A257VCE2"
},
{
"activation": 13,
"uniref_id": "A0A931EMQ3"
},
{
"activation": 12.9921875,
"uniref_id": "... | [
{
"activation": 11.429561614990234,
"uniprot_id": "Q9HIJ2"
},
{
"activation": 10.869362831115723,
"uniprot_id": "P36136"
},
{
"activation": 10.664434432983398,
"uniprot_id": "Q6MWZ7"
},
{
"activation": 10.462477684020996,
"uniprot_id": "Q9NQ88"
},
{
"activation": ... | [
1890,
11555,
14973,
11402,
10418,
5756,
13839,
14558,
914,
1517
] | 0.374322 |
239 | Summary: Accessory nucleic acid–recognition modules appended to NTPase machines: the feature tracks basic/glycine‑rich β–strand/helix patches in mid‑to‑C‑terminal domains (e.g., winged‑helix/HTH‑like, KH‑like, and related β‑rich surfaces) that contact DNA or RNA and couple to motor or catalytic cores, rather than the W... | Accessory nucleic acid–recognition modules appended to NTPase machines: the feature tracks basic/glycine‑rich β–strand/helix patches in mid‑to‑C‑terminal domains (e.g., winged‑helix/HTH‑like, KH‑like, and related β‑rich surfaces) that contact DNA or RNA and couple to motor or catalytic cores, rather than the Walker A/c... | Regional activation over contiguous mid/C‑terminal segments (often 50–150 aa) with multiple residue‑level peaks; typically outside the ATPase active site, sometimes spanning structured β/α elements and adjacent flexible/linker regions; enriched for Lys/Arg and Gly. | Ligand-binding site | - RecD/RecD2 helicases: activation on the C‑terminal accessory domain forming β/α surfaces that engage DNA/complex interfaces, not on the ATP‑binding P‑loop.
- PIF1 family helicases: activation across a mid‑to‑C‑terminal insert plus trailing flexible segment adjacent to the helicase core that mediates nucleic‑acid enga... | 3,539,702 | 4.073523 | 23.234375 | [
{
"activation": 23.234375,
"uniref_id": "UPI000A6A508D"
},
{
"activation": 23.125,
"uniref_id": "UPI002E791A20"
},
{
"activation": 22.703125,
"uniref_id": "A0A660SIW7"
},
{
"activation": 22.6875,
"uniref_id": "A0A832LEY0"
},
{
"activation": 22.640625,
"uniref_... | [
{
"activation": 8.605356216430664,
"uniprot_id": "Q8NG08"
},
{
"activation": 8.552336692810059,
"uniprot_id": "P57530"
},
{
"activation": 8.402889251708984,
"uniprot_id": "P04993"
},
{
"activation": 8.266046524047852,
"uniprot_id": "P32270"
},
{
"activation": 8.24... | [
11871,
11352,
12549,
6693,
2780,
3106,
1709,
12754,
6491,
4217
] | 0.449003 |
240 | Summary: Hydrophobic, glycine- and aromatic-enriched re-entrant/interface helices and adjoining loop segments at transmembrane-helix junctions in membrane proteins (primarily multi-pass), including C-terminal intramembrane tails; occasional low-scoring activations occur on long amphipathic/hydrophobic helices or tails ... | Hydrophobic, glycine- and aromatic-enriched re-entrant/interface helices and adjoining loop segments at transmembrane-helix junctions in membrane proteins (primarily multi-pass), including C-terminal intramembrane tails; occasional low-scoring activations occur on long amphipathic/hydrophobic helices or tails in otherw... | Regional activation over a single long, contiguous stretch that typically starts at the C-terminal end of one TM helix, peaks across a partially embedded re-entrant/amphipathic segment, and tapers into the next TM; in some proteins it instead covers a C-terminal cytosolic/intramembrane tail. Weak activations can also a... | Membrane-associated | - SEDS family peptidoglycan glycosyltransferases (FtsW/RodA): activation on glycine/Trp-rich periplasmic re-entrant/loop segments between core TMs that shape the transmembrane glycosyltransferase path.
- Na+/H+ antiporters (NhaA family): activation across the connector between adjacent TMs (end-of-TM → mixed helix/coil... | 5,161,711 | 3.696297 | 23.78125 | [
{
"activation": 23.78125,
"uniref_id": "A0A969KJM4"
},
{
"activation": 23.78125,
"uniref_id": "A0A3D0VEX7"
},
{
"activation": 23.765625,
"uniref_id": "UPI002572D0B1"
},
{
"activation": 23.515625,
"uniref_id": "A0A349TK10"
},
{
"activation": 23.390625,
"uniref_... | [
{
"activation": 21.759939193725586,
"uniprot_id": "B8H092"
},
{
"activation": 21.164859771728516,
"uniprot_id": "P9WN97"
},
{
"activation": 20.977863311767578,
"uniprot_id": "P0ABG7"
},
{
"activation": 20.89983558654785,
"uniprot_id": "Q5GW40"
},
{
"activation": 2... | [
6691,
14925,
7736,
8812,
13681,
2493,
9200,
1222,
1046,
638
] | 0.186006 |
241 | Summary: Carbohydrate-interacting regions of secretory-pathway proteins (secreted or ER/Golgi luminal)—especially carbohydrate-active enzymes—covering glycan-binding/linker segments immediately after signal peptides (often glycine-rich with multiple tryptophans) and, when present inside catalytic domains, short substra... | Carbohydrate-interacting regions of secretory-pathway proteins (secreted or ER/Golgi luminal)—especially carbohydrate-active enzymes—covering glycan-binding/linker segments immediately after signal peptides (often glycine-rich with multiple tryptophans) and, when present inside catalytic domains, short substrate-contac... | Primarily long regional activation in extracellular or ER-luminal N-terminal stretches following signal peptides (low-confidence/disordered or accessory domains), with little/no signal in the signal peptide itself; occasional localized peaks within well-structured catalytic domains at loops/strands flanking the active ... | Ligand-binding site | Hyaluronate lyase (glycosaminoglycan lyase): activation across the N-terminal, mixed beta/coil region after the signal peptide; Beta-agarase (GH16): a focused patch around a loop/strand flanking the catalytic Glu nucleophile; Endo-1,4-beta-xylanase (GH10): an extended, disordered N-terminal segment between the signal p... | 3,393,544 | 4.11569 | 18.59375 | [
{
"activation": 18.59375,
"uniref_id": "UPI002A74EA6D"
},
{
"activation": 18.546875,
"uniref_id": "A0A517XSD3"
},
{
"activation": 18.5,
"uniref_id": "A0A2Z3HBB4"
},
{
"activation": 18.4375,
"uniref_id": "A0A934VSJ6"
},
{
"activation": 18.328125,
"uniref_id": "... | [
{
"activation": 15.393095970153809,
"uniprot_id": "Q8A5T1"
},
{
"activation": 6.406420707702637,
"uniprot_id": "P82593"
},
{
"activation": 6.077948093414307,
"uniprot_id": "O41043"
},
{
"activation": 5.771651268005371,
"uniprot_id": "P36581"
},
{
"activation": 5.7... | [
5250,
4442,
5321,
3090,
6686,
11628,
3131,
11446,
7300,
3195
] | 0.077676 |
242 | Summary: A short beta-strand–loop structural module common to alpha/beta enzyme folds (beta→loop, often continuing into an alpha-helix or a paired beta-strand), enriched in hydrophobic/aromatic residues with glycine/proline in the turn; typically an edge/core beta element that can border active sites but is not the cat... | A short beta-strand–loop structural module common to alpha/beta enzyme folds (beta→loop, often continuing into an alpha-helix or a paired beta-strand), enriched in hydrophobic/aromatic residues with glycine/proline in the turn; typically an edge/core beta element that can border active sites but is not the catalytic re... | Regional activation on short contiguous windows (~10–20 residues) centered on a beta-strand with an adjoining loop; clear residue-level peaks often at glycine in the loop; bias toward N-terminal regions but not restricted; compositionally enriched for aromatic and other hydrophobic residues with glycine/proline in the ... | Structural motif | - Peptidoglycan O-acetyltransferase (OatA): activation on a beta-strand–loop–alpha segment adjacent to catalytic residues in the C-terminal catalytic domain; includes a mutationally sensitive residue.
- GDSL/SGNH esterase/lipase: activation on the N-terminal beta-strand and adjacent coil of the hydrolase domain, distin... | 35,643,037 | 1.764011 | 14.585938 | [
{
"activation": 14.5859375,
"uniref_id": "A0A0G1VGG1"
},
{
"activation": 14.515625,
"uniref_id": "UPI000F6D2188"
},
{
"activation": 14.34375,
"uniref_id": "UPI0022E36950"
},
{
"activation": 14.3203125,
"uniref_id": "UPI000A9C29D3"
},
{
"activation": 14.296875,
... | [
{
"activation": 12.630366325378418,
"uniprot_id": "Q8BW56"
},
{
"activation": 11.982619285583496,
"uniprot_id": "P0A754"
},
{
"activation": 11.675260543823242,
"uniprot_id": "Q2FV54"
},
{
"activation": 11.635257720947266,
"uniprot_id": "Q7XXR3"
},
{
"activation": ... | [
1973,
9770,
1802,
5049,
7976,
15745,
16037,
9675,
7046,
3355
] | 0.481465 |
243 | Summary: Compact functional segments (~40–100 aa) enriched for acidic–aromatic signatures (e.g., EEL/I/T–x–Y–D–Y), cysteine clusters, glycine-rich or hydrophobic stretches—typified by the SET catalytic C-terminus/post-SET tail—but also occurring internally or near the N-terminus (e.g., transmembrane helices, low-comple... | Compact functional segments (~40–100 aa) enriched for acidic–aromatic signatures (e.g., EEL/I/T–x–Y–D–Y), cysteine clusters, glycine-rich or hydrophobic stretches—typified by the SET catalytic C-terminus/post-SET tail—but also occurring internally or near the N-terminus (e.g., transmembrane helices, low-complexity/basi... | Regional activation over contiguous windows (~40–100 aa), often at the C-terminus but not restricted to it; residue-level peaks on Y–D–Y, catalytic Cys/His, glycine clusters, or C-terminal targeting tripeptides; segments may be structured (catalytic/post-SET folds, TM helices) or flexible/disordered tails. | Compositional bias | • SET-domain histone lysine methyltransferases (post-SET/Cys-rich C-termini). • Organellar ribosomal proteins (uS9/uL2/uL3/eL6) with glycine clusters. • Membrane energy-transduction proteins (ATP synthase a; NQR-C; RnfG) with TM segments. • Bacterial motility/secretion outer-membrane components (secretins; flagellar L-... | 7,950,527 | 3.264327 | 21.453125 | [
{
"activation": 21.453125,
"uniref_id": "UPI001F2864BE"
},
{
"activation": 21.359375,
"uniref_id": "A0A956MNX8"
},
{
"activation": 21.28125,
"uniref_id": "A8ZQG1"
},
{
"activation": 21.171875,
"uniref_id": "UPI001BAE855A"
},
{
"activation": 20.9375,
"uniref_id... | [
{
"activation": 17.859189987182617,
"uniprot_id": "P17800"
},
{
"activation": 9.570049285888672,
"uniprot_id": "P26416"
},
{
"activation": 8.019671440124512,
"uniprot_id": "B6EJG2"
},
{
"activation": 7.815669059753418,
"uniprot_id": "Q52081"
},
{
"activation": 7.7... | [
10354,
15653,
2979,
9950,
5989,
8469,
1855,
1500,
5470,
5751
] | 0.246962 |
244 | Summary: Membrane-interfacial and juxtamembrane segments of integral membrane proteins—most often the cytosolic regions immediately following or connecting transmembrane helices (including C‑terminal cytosolic domains and linkers) in lipid‑modifying enzymes and transporters; the signal favors mixed α/β or coil-rich seg... | Membrane-interfacial and juxtamembrane segments of integral membrane proteins—most often the cytosolic regions immediately following or connecting transmembrane helices (including C‑terminal cytosolic domains and linkers) in lipid‑modifying enzymes and transporters; the signal favors mixed α/β or coil-rich segments wit... | - Long, contiguous activation across cytosolic domains that follow the last transmembrane helix
- Regional activation on juxtamembrane linkers and interfacial helix/coil/β junctions (often Pro/Gly- or aromatic-enriched)
- Occasional single‑residue peaks within helices or β‑strands in non‑membrane proteins (weak/off‑tar... | Membrane-associated | - Undecaprenyl‑phosphate glycosyl/phosphotransferases (e.g., WbaP/WecA‑like): strong, continuous activation across the C‑terminal cytosolic catalytic domain after the final transmembrane segment
- DHHC/palmitoyltransferases: broad activation on the proline‑rich C‑terminal cytosolic tail distal to the DHHC core and last... | 2,751,493 | 4.325421 | 23.296875 | [
{
"activation": 23.296875,
"uniref_id": "UPI0033C9C094"
},
{
"activation": 23.234375,
"uniref_id": "A0A7T0LKB7"
},
{
"activation": 23.203125,
"uniref_id": "UPI001A90C7A5"
},
{
"activation": 23.1875,
"uniref_id": "UPI00235430D8"
},
{
"activation": 23.046875,
"u... | [
{
"activation": 18.5845947265625,
"uniprot_id": "Q9UBU6"
},
{
"activation": 12.94796371459961,
"uniprot_id": "P26406"
},
{
"activation": 11.83786392211914,
"uniprot_id": "Q9ABR0"
},
{
"activation": 11.564373970031738,
"uniprot_id": "Q56770"
},
{
"activation": 11.4... | [
9600,
1134,
15427,
1686,
15890,
3012,
8200,
11431,
13734,
9689
] | 0.149321 |
245 | Summary: Short linear motifs embedded in intrinsically disordered, charge‑biased segments—often anchored by glycine and/or an aromatic residue—found in propeptides and terminal tails; in trafficking/adaptor proteins the feature can also weakly mark the structured binding surface that recognizes such motifs.
Activation ... | Short linear motifs embedded in intrinsically disordered, charge‑biased segments—often anchored by glycine and/or an aromatic residue—found in propeptides and terminal tails; in trafficking/adaptor proteins the feature can also weakly mark the structured binding surface that recognizes such motifs. | Primarily regional activation over 15–40 aa disordered stretches (typically N‑terminal in small secreted/adaptor proteins and internal/C‑terminal in large enzymatic/mobile‑element proteins), with occasional single‑residue peaks in structured loops or adaptor domains. | Sequence motif | - Non‑LTR retrotransposon reverse transcriptases (LINE/Jockey): activation on the basic, disordered C‑terminal tail beyond the RT domain.
- ESCRT‑0/clathrin adaptors (Vps27/Hrs): narrow peak within the VHS domain helix near the cargo‑sorting (D/ExxxLL) binding surface.
- Conotoxin precursors (Conus): regional activatio... | 4,267,942 | 3.886434 | 19.6875 | [
{
"activation": 19.6875,
"uniref_id": "A0A0N4YHR4"
},
{
"activation": 19.609375,
"uniref_id": "A0A4C1YHQ1"
},
{
"activation": 19.40625,
"uniref_id": "A0A3P7J5G1"
},
{
"activation": 19.40625,
"uniref_id": "A0A7I5EE51"
},
{
"activation": 19.1875,
"uniref_id": "A... | [
{
"activation": 12.249465942382812,
"uniprot_id": "Q8N2X6"
},
{
"activation": 12.135916709899902,
"uniprot_id": "P03239"
},
{
"activation": 11.650938034057617,
"uniprot_id": "Q0VG73"
},
{
"activation": 10.823450088500977,
"uniprot_id": "O00370"
},
{
"activation": ... | [
9657,
7641,
14365,
13945,
15108,
4415,
11462,
11893,
5092,
8824
] | 0.253181 |
246 | Summary: Intrinsically disordered, low-complexity regulatory segments enriched in acidic/serine/proline/glutamine/glycine residues in eukaryotic proteins—most prominently in transcription factors and in regulatory tails/linkers of signaling/scaffold proteins—corresponding to transactivation/repression or partner-intera... | Intrinsically disordered, low-complexity regulatory segments enriched in acidic/serine/proline/glutamine/glycine residues in eukaryotic proteins—most prominently in transcription factors and in regulatory tails/linkers of signaling/scaffold proteins—corresponding to transactivation/repression or partner-interaction reg... | Sparse, low-magnitude, residue-level peaks scattered across intrinsically disordered coil regions (low pLDDT), often at N- or C-terminal tails, linkers, and helix–coil boundaries; minimal signal within folded domains (homeobox, ETS, POU, kinase cores) with only occasional isolated residues activating. | Compositional bias | - Homeobox/HOX transcription factors: primary peaks in N-terminal disordered segments; occasional isolated residues at the start or within the homeobox helices.
- bHLH transcription factors: short, two-residue peaks in N-terminal disordered regions.
- BTB/POZ plus C2H2 zinc-finger transcription factors: peaks in disord... | 197,146,769 | 0.053617 | 22.4375 | [
{
"activation": 22.4375,
"uniref_id": "A0A822CRK9"
},
{
"activation": 22.375,
"uniref_id": "A0A5B7GKA0"
},
{
"activation": 22.28125,
"uniref_id": "A0A6V7J8E6"
},
{
"activation": 21.78125,
"uniref_id": "A0AAV2ZLB5"
},
{
"activation": 21.75,
"uniref_id": "K0QZJ2... | [
{
"activation": 12.459465980529785,
"uniprot_id": "A6NHT5"
},
{
"activation": 12.392393112182617,
"uniprot_id": "Q8NA77"
},
{
"activation": 12.031893730163574,
"uniprot_id": "Q96EL1"
},
{
"activation": 11.968871116638184,
"uniprot_id": "Q2NL68"
},
{
"activation": ... | [
13385,
5459,
13094,
9146,
12501,
16265,
5437,
9044,
8944,
15106
] | 0.066037 |
247 | Summary: Intrinsically disordered, low‑complexity acidic/Ser/Pro‑rich regulatory regions in eukaryotic proteins—phosphorylation‑dense linkers and tails that flank or connect structured domains (coiled‑coils, DNA‑binding, or catalytic modules) in transcription/chromatin regulators, chromosome cohesion/mitotic factors, a... | Intrinsically disordered, low‑complexity acidic/Ser/Pro‑rich regulatory regions in eukaryotic proteins—phosphorylation‑dense linkers and tails that flank or connect structured domains (coiled‑coils, DNA‑binding, or catalytic modules) in transcription/chromatin regulators, chromosome cohesion/mitotic factors, and cytosk... | Regional, long‑stretch activation concentrated in IDRs (low pLDDT, coil) with compositional bias for acidic/polar and Ser/Pro residues; minimal to absent on folded helices/coiled‑coils and DNA‑binding cores; activation often starts at structured–disordered boundaries and peaks in SP/TP‑rich, phosphosite‑dense segments;... | Disorder | - INO80 chromatin‑remodeling subunit: disordered C‑terminal tail with polar/charged bias activated; structured N‑terminal helix not.
- Shugoshin (chromosome cohesion/segregation): long disordered, acidic/basic‑rich C‑terminal half activated; N‑terminal coiled‑coil off.
- Heat shock factor (HSF2): C‑terminal disordered ... | 5,309,698 | 3.66803 | 19.078125 | [
{
"activation": 19.078125,
"uniref_id": "UPI002093067D"
},
{
"activation": 19.078125,
"uniref_id": "UPI000FCD2AB8"
},
{
"activation": 19.03125,
"uniref_id": "A0A7J7V3T1"
},
{
"activation": 19.015625,
"uniref_id": "A0A643C050"
},
{
"activation": 19.015625,
"uni... | [
{
"activation": 18.09166717529297,
"uniprot_id": "Q8NBZ0"
},
{
"activation": 18.031831741333008,
"uniprot_id": "P0C1Z6"
},
{
"activation": 14.855363845825195,
"uniprot_id": "Q9BWC9"
},
{
"activation": 14.83574390411377,
"uniprot_id": "Q9NTI7"
},
{
"activation": 14... | [
6412,
11697,
3937,
6289,
1128,
3627,
13148,
11931,
6093,
9458
] | 0.365111 |
248 | Summary: SAM-dependent nucleic‑acid methyltransferase catalytic core (class I MTase fold): the cofactor-binding Rossmann-like module and adjacent substrate-recognition/base‑flipping loops used by DNA and RNA methyltransferases; frequently overlaps the glycine‑rich SAM-binding loop and Lys/Arg‑rich nucleic‑acid–contacti... | SAM-dependent nucleic‑acid methyltransferase catalytic core (class I MTase fold): the cofactor-binding Rossmann-like module and adjacent substrate-recognition/base‑flipping loops used by DNA and RNA methyltransferases; frequently overlaps the glycine‑rich SAM-binding loop and Lys/Arg‑rich nucleic‑acid–contacting surfac... | Regional activation across a single, long contiguous segment of the catalytic domain with residue-level peaks in flexible loops and helix–turn elements bordering the SAM-binding pocket; often emphasizes N‑terminal/central portions in classical Type II enzymes or the C‑terminal MTase domain in multi-domain proteins; com... | Domain | - Type II DNA methyltransferases (e.g., M.HphI, M.SfiI): activation over the N‑terminal/central catalytic core, including the N‑terminal glycine‑rich SAM-loop and adjacent helices/strands
- DNA adenine methylase (Dam): sharp peak on a catalytic/substrate‑recognition loop essential for methylation but not on SAM‑binding... | 6,481,700 | 3.468582 | 23.84375 | [
{
"activation": 23.84375,
"uniref_id": "A0A947GJT8"
},
{
"activation": 23.578125,
"uniref_id": "UPI00156165AB"
},
{
"activation": 23.46875,
"uniref_id": "UPI003568C884"
},
{
"activation": 23.46875,
"uniref_id": "A0A0F9JDN7"
},
{
"activation": 23.453125,
"unire... | [
{
"activation": 22.061866760253906,
"uniprot_id": "P50193"
},
{
"activation": 20.83429718017578,
"uniprot_id": "P24582"
},
{
"activation": 20.81012725830078,
"uniprot_id": "P14871"
},
{
"activation": 20.58753776550293,
"uniprot_id": "Q71TL0"
},
{
"activation": 20.... | [
5259,
4073,
1040,
6900,
13742,
13840,
13095,
7984,
681,
2311
] | 0.164676 |
249 | Summary: P-loop NTPase motor core (emphasis on ASCE/RecA-like motors), most strongly in nucleic-acid–associated ATPases (replicative helicases, RecA/Rad51 recombinases, DNA packaging/translocation motors) and more weakly in P-loop NMP kinases; occasionally shows low-level activation in other P-loop classes (e.g., TRAFA... | P-loop NTPase motor core (emphasis on ASCE/RecA-like motors), most strongly in nucleic-acid–associated ATPases (replicative helicases, RecA/Rad51 recombinases, DNA packaging/translocation motors) and more weakly in P-loop NMP kinases; occasionally shows low-level activation in other P-loop classes (e.g., TRAFAC signal/... | Long, contiguous regional activation spanning much of the NTPase core; residue-level peaks frequently at the glycine-rich Walker A P-loop (GxxxxGKT/S) and the acidic Walker B motif (hhhhDE), with additional hotspots in sensor/“finger” elements and DNA-binding loops (e.g., L1/L2) or subunit-interface helices. In helicas... | Domain | - Replicative DNA helicases (DnaB/SF4): activation across the C-terminal RecA-like ATPase domain, covering the P-loop ATP-binding site and the catalytic acidic region (Walker B/sensor motifs), with strong peaks near essential acidic residues.
- RecA/Rad51/RadA recombinases: activation over the central helical/DNA-bindi... | 5,778,244 | 3.583465 | 25.28125 | [
{
"activation": 25.28125,
"uniref_id": "UPI0018EA2C44"
},
{
"activation": 25.046875,
"uniref_id": "A0A0T6B1N0"
},
{
"activation": 24.90625,
"uniref_id": "A0AAW8XH69"
},
{
"activation": 24.859375,
"uniref_id": "UPI0020235ECB"
},
{
"activation": 24.75,
"uniref_i... | [
{
"activation": 22.9301815032959,
"uniprot_id": "Q5ZIW1"
},
{
"activation": 22.748199462890625,
"uniprot_id": "B5X582"
},
{
"activation": 22.73612403869629,
"uniprot_id": "P04530"
},
{
"activation": 22.513141632080078,
"uniprot_id": "P03006"
},
{
"activation": 22.... | [
16175,
11518,
4087,
7183,
13541,
15120,
1719,
11517,
13129,
487
] | 0.191427 |
250 | Summary: Beta-strand–rich ligand-recognition modules, most commonly carbohydrate-binding modules (CBMs/lectin-like beta-sandwich or beta-solenoid domains) in secreted/extracellular or luminal proteins, and structurally analogous loop/strand interaction surfaces in non-CAZyme proteins (e.g., the PINIT interaction domain... | Beta-strand–rich ligand-recognition modules, most commonly carbohydrate-binding modules (CBMs/lectin-like beta-sandwich or beta-solenoid domains) in secreted/extracellular or luminal proteins, and structurally analogous loop/strand interaction surfaces in non-CAZyme proteins (e.g., the PINIT interaction domain of SUMO ... | Regional activation over long contiguous stretches, typically in the C-terminal portions of multidomain proteins; strongest over loops connecting beta-strands within beta-sandwich/solenoid folds; moderate pLDDT (≈60–85) indicative of flexible, surface-exposed segments; enriched in small/polar residues (G, S, T, N, D); ... | Ligand-binding site | - GH2 beta-galactosidase/glucuronidase: activation across the C-terminal half in flexible beta/coil segments near N‑glycosylation sequons, outside catalytic residues.
- Xylanase/deacetylase with CBM6: activation confined to the C-terminal portion of the CBM6 domain, especially loops linking beta-strands that form the c... | 8,588,884 | 3.187096 | 22.625 | [
{
"activation": 22.625,
"uniref_id": "A0A090WYR5"
},
{
"activation": 22.328125,
"uniref_id": "A0A836XJP2"
},
{
"activation": 21.765625,
"uniref_id": "V4UNY6"
},
{
"activation": 21.734375,
"uniref_id": "V4SVJ2"
},
{
"activation": 21.59375,
"uniref_id": "UPI0029... | [
{
"activation": 19.275129318237305,
"uniprot_id": "Q5AZ85"
},
{
"activation": 19.177082061767578,
"uniprot_id": "Q5B5P1"
},
{
"activation": 19.169818878173828,
"uniprot_id": "Q8RJP2"
},
{
"activation": 18.47469711303711,
"uniprot_id": "Q9SCU8"
},
{
"activation": 1... | [
3963,
12378,
6488,
15715,
5106,
11044,
2574,
11575,
2437,
7098
] | 0.302388 |
251 | Summary: C-terminal transmembrane module of eukaryotic multi-pass membrane proteins—specifically the last 1–3 α-helices and their short connecting loops—encompassing the second repeat/bundle in duplicated transporter architectures or the terminal membrane anchor, often forming the permeation/gating segment in channels/... | C-terminal transmembrane module of eukaryotic multi-pass membrane proteins—specifically the last 1–3 α-helices and their short connecting loops—encompassing the second repeat/bundle in duplicated transporter architectures or the terminal membrane anchor, often forming the permeation/gating segment in channels/transport... | Membrane-associated | 14,435,522 | 2.667873 | 13.828125 | [
{
"activation": 13.828125,
"uniref_id": "A0A183TPH6"
},
{
"activation": 13.7109375,
"uniref_id": "A0A2G9TQ24"
},
{
"activation": 13.65625,
"uniref_id": "A0A8X7XKM4"
},
{
"activation": 13.53125,
"uniref_id": "UPI00398E6DFA"
},
{
"activation": 13.515625,
"uniref... | [
{
"activation": 11.69742202758789,
"uniprot_id": "Q9SYY4"
},
{
"activation": 11.50705337524414,
"uniprot_id": "P27544"
},
{
"activation": 11.394344329833984,
"uniprot_id": "Q15629"
},
{
"activation": 11.259286880493164,
"uniprot_id": "Q4Q5G6"
},
{
"activation": 11... | [
2486,
5923,
2735,
8885,
2316,
4932,
14564,
6683,
12975,
12290
] | 0.45978 | ||
252 | Summary: Detector of long, hydrophilic “mature protein body” segments: the feature activates on contiguous stretches that constitute the principal functional module(s) of a protein—often the first major domain immediately following any short N‑terminal leader/signal peptide—and extends across both structured cores and ... | Detector of long, hydrophilic “mature protein body” segments: the feature activates on contiguous stretches that constitute the principal functional module(s) of a protein—often the first major domain immediately following any short N‑terminal leader/signal peptide—and extends across both structured cores and intrinsic... | Domain-level/regional activation on one or more long continuous segments; frequently turns on just after a signal peptide or short low-confidence N-terminus and can concentrate in the first 40–60 residues of the first domain. In multi-domain proteins it may select specific domains (including small accessory modules) an... | Domain | - Insect Yellow/MRJP secreted proteins: off on the N‑terminal signal peptide, uniformly on across the mature secreted domain.
- MEP-pathway HMBPP reductase (IspH/LytB): on a contiguous N‑terminal subdomain (including ligand/cofactor-associated positions), off across the remainder of the enzyme.
- Protein-only RNase P (... | 58,799,999 | 1.263423 | 13.070313 | [
{
"activation": 13.0703125,
"uniref_id": "A0A1F5NQV8"
},
{
"activation": 13.0546875,
"uniref_id": "A0A352D3A1"
},
{
"activation": 13,
"uniref_id": "A0A1F7JIH5"
},
{
"activation": 12.9921875,
"uniref_id": "A0A1F6IUX6"
},
{
"activation": 12.9453125,
"uniref_id":... | [
{
"activation": 9.588882446289062,
"uniprot_id": "J7I4B7"
},
{
"activation": 8.813721656799316,
"uniprot_id": "P76291"
},
{
"activation": 8.763687133789062,
"uniprot_id": "Q5WPU9"
},
{
"activation": 8.652180671691895,
"uniprot_id": "P62407"
},
{
"activation": 8.57... | [
1079,
7106,
14696,
4336,
5209,
802,
10276,
3537,
4340,
12203
] | 0.433962 |
253 | Summary: Extracellular glycan‑targeting catalytic surfaces: the feature marks the substrate‑binding grooves and adjacent catalytic regions of secreted carbohydrate‑active enzymes—especially polysaccharide lyases and glycosidases that act on glycosaminoglycans, uronate‑rich and sialylated polysaccharides—with enrichment... | Extracellular glycan‑targeting catalytic surfaces: the feature marks the substrate‑binding grooves and adjacent catalytic regions of secreted carbohydrate‑active enzymes—especially polysaccharide lyases and glycosidases that act on glycosaminoglycans, uronate‑rich and sialylated polysaccharides—with enrichment for arom... | Long, contiguous domain‑level activation across the main catalytic domain (often the N‑terminal half after the signal peptide), with residue‑level peaks on beta‑strands and flanking loops that shape the glycan‑binding cleft and harbor/abut catalytic acids/bases; signal peptides are not activated, and activation can inc... | Ligand-binding site | - Heparan/heparin lyases (GAG lyases): strong activation beginning at the start of the mature enzyme and spanning the N‑terminal catalytic core, peaking on central loops/strands that form the binding groove.
- Hyaluronate lyases (multiple Gram‑positive lineages): extended activation over the catalytic domain that binds... | 6,451,702 | 3.473221 | 30.96875 | [
{
"activation": 30.96875,
"uniref_id": "A0A511QN75"
},
{
"activation": 30.96875,
"uniref_id": "UPI0031E1E508"
},
{
"activation": 30.9375,
"uniref_id": "UPI000D7D02D2"
},
{
"activation": 30.9375,
"uniref_id": "A0A182S6G5"
},
{
"activation": 30.90625,
"uniref_id... | [
{
"activation": 27.67464828491211,
"uniprot_id": "T2KNA3"
},
{
"activation": 27.12897300720215,
"uniprot_id": "Q59289"
},
{
"activation": 26.331090927124023,
"uniprot_id": "Q21FJ0"
},
{
"activation": 26.049758911132812,
"uniprot_id": "C6XZB6"
},
{
"activation": 25... | [
8705,
5533,
10821,
7166,
4317,
14521,
909,
6471,
9573,
9626
] | 0.166025 |
254 | Summary: Short gly/ser/thr-rich secondary-structure transition/capping motifs (β–α linkers and helix N-caps) that act as flexible hinge/linker segments, often bordering ligand- or nucleotide-binding pockets across many enzyme folds, rather than marking specific catalytic residues.
Activation pattern: Residue-level peak... | Short gly/ser/thr-rich secondary-structure transition/capping motifs (β–α linkers and helix N-caps) that act as flexible hinge/linker segments, often bordering ligand- or nucleotide-binding pockets across many enzyme folds, rather than marking specific catalytic residues. | Residue-level peaks on short segments (~8–15 aa), typically at boundaries between elements (coil→helix N-caps, β-strand→loop, or helix→β transitions). Often multiple discontiguous peaks within one domain. Compositionally biased toward small/polar residues (G, S, T) with frequent D/E/H; commonly proximal to—but not nece... | Structural motif | - Isochorismatase family (enterobactin synthase component B): short N-terminal helix capped by coil within the isochorismatase domain.
- Dienelactone hydrolase/carboxymethylenebutenolidase (α/β-hydrolase fold): well-structured β→α connecting loop linking a strand to the following helix.
- ADP-dependent ribose-1-phospha... | 75,857,615 | 1.008707 | 10.09375 | [
{
"activation": 10.09375,
"uniref_id": "A0A9D9D5L7"
},
{
"activation": 10.0078125,
"uniref_id": "A0A9D6CTH9"
},
{
"activation": 10.0078125,
"uniref_id": "A0A1S4DIT3"
},
{
"activation": 9.9921875,
"uniref_id": "A0A835RI16"
},
{
"activation": 9.9453125,
"uniref_... | [
{
"activation": 9.071608543395996,
"uniprot_id": "P0A006"
},
{
"activation": 8.8763427734375,
"uniprot_id": "Q9FMX7"
},
{
"activation": 8.618935585021973,
"uniprot_id": "P39155"
},
{
"activation": 8.55487060546875,
"uniprot_id": "P0ADI4"
},
{
"activation": 8.50801... | [
4266,
7078,
76,
13935,
15337,
13292,
6361,
7291,
8103,
16018
] | 0.298064 |
255 | Summary: Signal-peptide–cleaved, periplasmic/extracellular N‑terminal interaction regions immediately downstream of the signal peptide—most prominently the N‑terminal domains of Gram‑negative outer‑membrane systems (e.g., POTRA1 of Omp85/TamA and early N‑segments of TonB‑dependent receptors)—characterized by low hydrop... | Signal-peptide–cleaved, periplasmic/extracellular N‑terminal interaction regions immediately downstream of the signal peptide—most prominently the N‑terminal domains of Gram‑negative outer‑membrane systems (e.g., POTRA1 of Omp85/TamA and early N‑segments of TonB‑dependent receptors)—characterized by low hydrophobicity ... | - Primary: long, contiguous regional activation across residues ~20–150 immediately C‑terminal to a signal peptide, spanning mixed helix/strand/loop elements within periplasmic N‑terminal domains (no transmembrane segments).
- Secondary: isolated, low‑amplitude residue‑level peaks in unrelated proteins (often within he... | Membrane-associated | - Omp85/TamA outer‑membrane assembly proteins: strong regional activation confined to the periplasmic POTRA1 domain (not POTRA2/3 or the β‑barrel), especially an internal α‑helix used for partner binding.
- TonB‑dependent receptors (hemophore/hemophilin receptors): activation on early N‑terminal segments preceding the ... | 3,758,092 | 4.013654 | 23.859375 | [
{
"activation": 23.859375,
"uniref_id": "UPI0039E26CE7"
},
{
"activation": 23.71875,
"uniref_id": "UPI0013D84568"
},
{
"activation": 23.640625,
"uniref_id": "A0A1F9AJV6"
},
{
"activation": 23.59375,
"uniref_id": "A0A9D5VP03"
},
{
"activation": 23.5625,
"uniref... | [
{
"activation": 21.230913162231445,
"uniprot_id": "P26366"
},
{
"activation": 20.855440139770508,
"uniprot_id": "P63883"
},
{
"activation": 20.313705444335938,
"uniprot_id": "Q70M91"
},
{
"activation": 19.890384674072266,
"uniprot_id": "Q8YQ14"
},
{
"activation": ... | [
2626,
6909,
9999,
9816,
11538,
15109,
2299,
10712,
5554,
3469
] | 0.135091 |
256 | Summary: Conserved loop→α-helix (β–α connector) segment within well‑structured domain cores that scaffolds catalytic, gate, or pore/interaction surfaces across macromolecular processing proteins. The feature most often maps to N‑proximal propeptide/gate segments of proteasome α/β core subunits and to inner‑face/interdo... | Conserved loop→α-helix (β–α connector) segment within well‑structured domain cores that scaffolds catalytic, gate, or pore/interaction surfaces across macromolecular processing proteins. The feature most often maps to N‑proximal propeptide/gate segments of proteasome α/β core subunits and to inner‑face/interdomain conn... | Regional activation on contiguous 15–60 residue blocks within folded domain cores (or N‑terminal propeptides). Typical topology is a short loop followed by a long α‑helix (often just C‑terminal to a catalytic/functional β‑strand), with family‑specific hotspots: N‑terminal Gly/Thr‑rich patches in proteasome β precursors... | Structural motif | - Proteasome core α/β subunits (including immunoproteasome; archaeal/bacterial): N‑terminal segments that gate/configure the proteolytic chamber—β propeptides preceding catalytic Thr1 and α N‑terminal gating tails.
- Sliding clamps/processivity factors (bacterial β clamp, archaeal/eukaryotic PCNA, viral clamp proteins,... | 4,285,193 | 3.8824 | 14.804688 | [
{
"activation": 14.8046875,
"uniref_id": "A0A3N5N490"
},
{
"activation": 14.2578125,
"uniref_id": "A0A2E8YNH3"
},
{
"activation": 14.1484375,
"uniref_id": "A0AAD4NAQ6"
},
{
"activation": 14.0859375,
"uniref_id": "A0A3D6DB47"
},
{
"activation": 14.078125,
"unir... | [
{
"activation": 12.534268379211426,
"uniprot_id": "P21578"
},
{
"activation": 11.641602516174316,
"uniprot_id": "Q9Y7P0"
},
{
"activation": 9.015978813171387,
"uniprot_id": "P99026"
},
{
"activation": 9.012948989868164,
"uniprot_id": "Q29384"
},
{
"activation": 8.... | [
12560,
15542,
6223,
12357,
5072,
15873,
1955,
4423,
2996,
7084
] | 0.322501 |
257 | Summary: Compositionally biased intrinsically disordered regions enriched in Thr/Gly (often TG/GT repeats) and other small polar residues (S/N/D/Q), typically occurring in propeptides and signal-peptide–adjacent segments of secreted/lumenal proteins, in extracellular passenger/linker repeats, and in flexible acidic/bas... | Compositionally biased intrinsically disordered regions enriched in Thr/Gly (often TG/GT repeats) and other small polar residues (S/N/D/Q), typically occurring in propeptides and signal-peptide–adjacent segments of secreted/lumenal proteins, in extracellular passenger/linker repeats, and in flexible acidic/basic tails ... | Predominantly regional/domain-level activation across long, contiguous low-pLDDT segments; strong signal in C-terminal portions of signal peptides and propeptides, continuous disordered tails, and repetitive low-complexity passenger/linker regions; intermittent residue-level peaks within repeat-rich beta-solenoid passe... | Compositional bias | - Gram-negative autotransporter adhesins/invasins: activation across the S/G-rich, repetitive beta-helical passenger domains; no signal on the N-terminal signal peptide core or C-terminal beta-barrel translocator.
- Plant EPIDERMAL PATTERNING FACTOR family precursors: activation on the C-terminal half of the signal pep... | 4,954,309 | 3.737308 | 20.828125 | [
{
"activation": 20.828125,
"uniref_id": "A0A944C0G0"
},
{
"activation": 20.46875,
"uniref_id": "K1MHC6"
},
{
"activation": 20.4375,
"uniref_id": "A0A255XQ68"
},
{
"activation": 20.28125,
"uniref_id": "UPI0007074F97"
},
{
"activation": 20.28125,
"uniref_id": "U... | [
{
"activation": 19.451732635498047,
"uniprot_id": "P9WIN9"
},
{
"activation": 17.68681526184082,
"uniprot_id": "Q8DP63"
},
{
"activation": 16.08958625793457,
"uniprot_id": "O05403"
},
{
"activation": 5.747707366943359,
"uniprot_id": "P9WIC5"
},
{
"activation": 5.7... | [
13765,
9493,
4208,
1078,
16367,
7200,
4315,
8047,
13546,
1248
] | 0.164636 |
258 | Summary: N-terminal small-domain helix–loop–helix segment of the aminotransferase-like (fold type I) PLP enzyme superfamily that shapes the PLP/substrate entrance and gating surface, often including residues that contact polar or phosphorylated groups on substrates (the phosphate/sugar-phosphate recognition and active-... | N-terminal small-domain helix–loop–helix segment of the aminotransferase-like (fold type I) PLP enzyme superfamily that shapes the PLP/substrate entrance and gating surface, often including residues that contact polar or phosphorylated groups on substrates (the phosphate/sugar-phosphate recognition and active-site gati... | Predominantly regional activation: a single contiguous block (~30–100 aa) most often in the N-terminal third of the protein spanning one or two helices with an intervening loop; peaks typically occur in the loop or adjacent helix. Minimal activation elsewhere in the protein. Rarely, isolated residue-level peaks appear ... | Ligand-binding site | - Threonine O-3-phosphate decarboxylase domain (CobD in AdoCbl biosynthesis): strong activation on the N-terminal 25–70 segment containing a substrate phosphate-binding residue and flanking helices that form the entrance to the PLP site.
- Alpha-oxoamine synthases (e.g., 8-amino-7-oxononanoate synthase/BioF): activatio... | 5,448,670 | 3.642194 | 28.703125 | [
{
"activation": 28.703125,
"uniref_id": "A0A2G2ZIC0"
},
{
"activation": 28.578125,
"uniref_id": "A0A699IAC3"
},
{
"activation": 28.53125,
"uniref_id": "A0AAD3RJJ2"
},
{
"activation": 28.4375,
"uniref_id": "A0A978UGE4"
},
{
"activation": 28.375,
"uniref_id": "U... | [
{
"activation": 25.586519241333008,
"uniprot_id": "Q9STR4"
},
{
"activation": 25.550939559936523,
"uniprot_id": "P37821"
},
{
"activation": 25.439189910888672,
"uniprot_id": "Q01912"
},
{
"activation": 25.404163360595703,
"uniprot_id": "Q93ZN9"
},
{
"activation": ... | [
13319,
13863,
11509,
8037,
14055,
383,
414,
2003,
8721,
6287
] | 0.137037 |
259 | Summary: Glycine-rich flavin (FAD/FMN) cofactor-binding loop and adjacent aromatic (often Trp) stacking region within the Rossmann-like flavin-binding subdomain of flavoprotein oxidoreductases—most prominently ETF-dependent acyl‑CoA dehydrogenases and two‑component/FADH2‑dependent monooxygenases involved in β‑oxidation... | Glycine-rich flavin (FAD/FMN) cofactor-binding loop and adjacent aromatic (often Trp) stacking region within the Rossmann-like flavin-binding subdomain of flavoprotein oxidoreductases—most prominently ETF-dependent acyl‑CoA dehydrogenases and two‑component/FADH2‑dependent monooxygenases involved in β‑oxidation, sterol ... | Regional activation spanning the flavin-binding subdomain, with strongest peaks on poly‑glycine/GxGxxG motifs that cradle the dinucleotide pyrophosphate and on nearby Trp/Tyr that pack against the isoalloxazine; typically a long, contiguous stretch rather than isolated residues | Ligand-binding site | - Acyl‑CoA dehydrogenases (ETF‑dependent; medium/long/branched‑chain, isovaleryl‑, glutaryl‑): activation on the N‑terminal FAD‑binding glycine‑rich loop and neighboring aromatic residue in the FAD pocket
- Peroxisomal acyl‑CoA oxidases and mitochondrial β‑oxidation flavoproteins: activation on the same FAD‑binding gly... | 6,295,124 | 3.49779 | 29.375 | [
{
"activation": 29.375,
"uniref_id": "UPI001AE6E32B"
},
{
"activation": 29.25,
"uniref_id": "A0A5B8NC74"
},
{
"activation": 29.21875,
"uniref_id": "UPI0021F2D9D8"
},
{
"activation": 29.1875,
"uniref_id": "UPI001661D4AC"
},
{
"activation": 29.078125,
"uniref_id... | [
{
"activation": 25.585723876953125,
"uniprot_id": "I6Y3Q0"
},
{
"activation": 25.43045997619629,
"uniprot_id": "Q8X1D8"
},
{
"activation": 25.194272994995117,
"uniprot_id": "P96855"
},
{
"activation": 25.103073120117188,
"uniprot_id": "A0R502"
},
{
"activation": 2... | [
7522,
6118,
7061,
9754,
2410,
14037,
10169,
10262,
15719,
12922
] | 0.138182 |
260 | Summary: Metal-dependent nuclease catalytic regions and adjoining charged, substrate-binding loops involved in nucleic-acid end processing, with strongest representation in RecB-like/Exonuclease V nuclease folds (including DNA2 and Cas4) but extending to viral DNA nucleases and RNA 5′-end nucleases (DXO/RAI1)
Activatio... | Metal-dependent nuclease catalytic regions and adjoining charged, substrate-binding loops involved in nucleic-acid end processing, with strongest representation in RecB-like/Exonuclease V nuclease folds (including DNA2 and Cas4) but extending to viral DNA nucleases and RNA 5′-end nucleases (DXO/RAI1) | Predominantly domain-level/regional activation across the nuclease lobe as long, dense stretches; peaks around H/D/E/K-rich, metal-coordinating neighborhoods (and Fe–S–binding cysteines in Cas4); minimal signal in non-nuclease modules (e.g., helicase domains); can extend into adjacent flexible inter-domain linkers abut... | Catalytic function | - RecB/Exonuclease V-like nucleases (e.g., bacterial RecBCD/AddAB): activation blankets the nuclease domain, not the helicase lobe.
- DNA2 helicase/nuclease: strong activation confined to the N-terminal nuclease domain (β–α–loop segment), tapering near the [4Fe–4S] Cys sites; no signal in the C-terminal helicase.
- CRI... | 6,543,885 | 3.459034 | 26.34375 | [
{
"activation": 26.34375,
"uniref_id": "A0A091QIX2"
},
{
"activation": 26.328125,
"uniref_id": "UPI0011C10636"
},
{
"activation": 26.28125,
"uniref_id": "A0A842QYV0"
},
{
"activation": 26.15625,
"uniref_id": "A0A7Y2GGQ9"
},
{
"activation": 26.109375,
"uniref_i... | [
{
"activation": 21.58362579345703,
"uniprot_id": "C4R7Q5"
},
{
"activation": 21.378496170043945,
"uniprot_id": "Q9FKK6"
},
{
"activation": 21.271387100219727,
"uniprot_id": "G4RJY8"
},
{
"activation": 21.06207275390625,
"uniprot_id": "Q9Y7L4"
},
{
"activation": 21... | [
4544,
4928,
9398,
4116,
6930,
13868,
9473,
2495,
3758,
11207
] | 0.168224 |
261 | Summary: Intrinsically disordered, low‑complexity linker/stalk segments enriched in A/P/T/S (with frequent Gly and Pro; A‑P and P‑T‑P patterns) that serve as flexible tethers between domains or subunits—prototypically the long mid‑protein linkers around the PSBD that connect lipoyl “swinging‑arm” domains to the catalyt... | Intrinsically disordered, low‑complexity linker/stalk segments enriched in A/P/T/S (with frequent Gly and Pro; A‑P and P‑T‑P patterns) that serve as flexible tethers between domains or subunits—prototypically the long mid‑protein linkers around the PSBD that connect lipoyl “swinging‑arm” domains to the catalytic core i... | Regional activation on long, continuous low‑complexity IDRs (often hundreds of residues; typically mid‑protein in E2/E3BP); secondary occurrences are short N‑ or internal low‑complexity patches in otherwise structured proteins | Disorder | - 2‑oxoacid dehydrogenase E2 acyltransferases (E2p/E2o/E2b): activation on the long A/P/T/S‑rich linkers connecting N‑terminal lipoyl domains, the PSBD, and the C‑terminal catalytic acyltransferase core (flexible tethers for “swinging arms” and subunit binding).
- E3‑binding proteins (PDH E3BP): activation across exten... | 6,004,542 | 3.545049 | 22.515625 | [
{
"activation": 22.515625,
"uniref_id": "UPI001CBD05A8"
},
{
"activation": 22.515625,
"uniref_id": "A0A926GGP6"
},
{
"activation": 22.5,
"uniref_id": "A0A8K0Y1Z3"
},
{
"activation": 22.5,
"uniref_id": "A0A956GMY1"
},
{
"activation": 22.484375,
"uniref_id": "A0... | [
{
"activation": 21.338342666625977,
"uniprot_id": "P20285"
},
{
"activation": 20.96337890625,
"uniprot_id": "P10515"
},
{
"activation": 20.757909774780273,
"uniprot_id": "P11181"
},
{
"activation": 20.744516372680664,
"uniprot_id": "P11961"
},
{
"activation": 20.6... | [
8194,
167,
14734,
3245,
12865,
16296,
15242,
8027,
15028,
10731
] | 0.15957 |
262 | Summary: Post-transit mature-domain signature of plant chloroplast proteins, especially small thylakoid membrane and lumen components: the feature activates on the folded regions of chloroplast proteins once the N‑terminal transit peptide ends (when present), covering PSI/PSII, chloroplast NDH, and cytochrome b6f small... | Post-transit mature-domain signature of plant chloroplast proteins, especially small thylakoid membrane and lumen components: the feature activates on the folded regions of chloroplast proteins once the N‑terminal transit peptide ends (when present), covering PSI/PSII, chloroplast NDH, and cytochrome b6f small subunits... | Domain-level activation in long continuous tracts that begin sharply at (or just after) the organellar transit-peptide cleavage site (chloroplast or mitochondrial) and span the mature chain; for small membrane proteins this coincides with one or more hydrophobic TM helices (frequent short glycine spacings), while for s... | Taxonomic bias | - Photosystem core small subunits (PSI/PSII): activation across single-pass TM helices and adjacent short loops (e.g., PsaI/PsaJ/PsaK/PsaG; PsbH/PsbI/PsbK/PsbL/M/N/T/X).
- Cytochrome b6f small subunits (PetG/PetL/PetM/PetN): activation on their hydrophobic helices, often with GxxxG-like spacings.
- Chloroplast NDH smal... | 19,526,831 | 2.365776 | 20.109375 | [
{
"activation": 20.109375,
"uniref_id": "A0A2P5EA92"
},
{
"activation": 19.90625,
"uniref_id": "A0A8T2Z7H8"
},
{
"activation": 19.875,
"uniref_id": "A0A445DU87"
},
{
"activation": 19.734375,
"uniref_id": "UPI0005ECA66B"
},
{
"activation": 19.703125,
"uniref_id... | [
{
"activation": 17.716064453125,
"uniprot_id": "A0A2K3DMP5"
},
{
"activation": 17.503206253051758,
"uniprot_id": "Q41387"
},
{
"activation": 16.92387580871582,
"uniprot_id": "Q9FL44"
},
{
"activation": 16.720260620117188,
"uniprot_id": "Q9FG89"
},
{
"activation": ... | [
10974,
13769,
14784,
2468,
13855,
7360,
1941,
10997,
579,
5206
] | 0.488364 |
263 | Summary: FAD-dependent oxidoreductase catalytic-site/capping-region signature: glycine-rich, aromatic-lined loops that cradle the FAD isoalloxazine ring and gate the substrate channel, shared across GMC sugar/alcohol oxidases, MAO/LSD1-like amine oxidases, and BBE-like secondary-metabolism flavoenzymes (including stero... | FAD-dependent oxidoreductase catalytic-site/capping-region signature: glycine-rich, aromatic-lined loops that cradle the FAD isoalloxazine ring and gate the substrate channel, shared across GMC sugar/alcohol oxidases, MAO/LSD1-like amine oxidases, and BBE-like secondary-metabolism flavoenzymes (including sterol/cholest... | Regional activation focused on mid-to-C-terminal segments of the FAD catalytic domain, with residue-level peaks on glycine clusters and nearby aromatic residues; distinct from the N-terminal Rossmann/ADP-binding motif and from signal peptides | Ligand-binding site | - GMC-type sugar/alcohol oxidases (e.g., glucose oxidase, aryl-alcohol oxidase, choline/cholesterol oxidase): activation on the C-terminal capping and re-face loops that shape the substrate channel over FAD, enriched for Gly-Gly motifs and aromatic residues.
- FAD-dependent amine oxidases (monoamine/polyamine oxidases;... | 7,694,985 | 3.296996 | 27.734375 | [
{
"activation": 27.734375,
"uniref_id": "A0A6A0H014"
},
{
"activation": 27.609375,
"uniref_id": "UPI001FE7488E"
},
{
"activation": 27.5625,
"uniref_id": "UPI00325E6461"
},
{
"activation": 27.515625,
"uniref_id": "A0A2P5HYA4"
},
{
"activation": 27.40625,
"unire... | [
{
"activation": 24.836101531982422,
"uniprot_id": "Q945K2"
},
{
"activation": 24.668153762817383,
"uniprot_id": "H6AGY0"
},
{
"activation": 24.4848690032959,
"uniprot_id": "Q7X2H8"
},
{
"activation": 24.29315757751465,
"uniprot_id": "Q5UPL2"
},
{
"activation": 24.... | [
6988,
3984,
14611,
11764,
1908,
11153,
5413,
7442,
5440,
2407
] | 0.178366 |
264 | Summary: Small-residue–enriched transmembrane α-helices (including signal peptides), especially those carrying GxxxG/small-xxx-small “glycine-zipper” motifs that form helix–helix packing interfaces in multi-pass or oligomeric membrane proteins across diverse taxa
Activation pattern: Regional activation on contiguous, h... | Small-residue–enriched transmembrane α-helices (including signal peptides), especially those carrying GxxxG/small-xxx-small “glycine-zipper” motifs that form helix–helix packing interfaces in multi-pass or oligomeric membrane proteins across diverse taxa | Regional activation on contiguous, hydrophobic segments of transmembrane length; strong residue-level peaks at small residues (G, A, V, L, I), often at GxxxG/glycine-zipper positions; frequent aromatic capping (W/Y) near helix boundaries; multiple activated helices per protein are common; negligible activation in solub... | Membrane-associated | - Two-component histidine kinases (e.g., UhpB): activation confined to the N-terminal multi-pass sensor TM helices; no activation on the cytosolic kinase domain.
- Mitochondrial respiratory chain small membrane subunits and assembly factors: activation on short, glycine-rich TM helices mediating subunit packing.
- Orga... | 22,058,957 | 2.243846 | 22.96875 | [
{
"activation": 22.96875,
"uniref_id": "A0A2E4HZ59"
},
{
"activation": 22.84375,
"uniref_id": "UPI001CD98481"
},
{
"activation": 22.59375,
"uniref_id": "UPI001AE7134F"
},
{
"activation": 22.578125,
"uniref_id": "A0A1G8U8Z7"
},
{
"activation": 22.484375,
"unire... | [
{
"activation": 15.402898788452148,
"uniprot_id": "P24022"
},
{
"activation": 15.298337936401367,
"uniprot_id": "Q9Z4N4"
},
{
"activation": 15.112924575805664,
"uniprot_id": "P80696"
},
{
"activation": 14.605398178100586,
"uniprot_id": "Q01074"
},
{
"activation": ... | [
4575,
7006,
77,
1925,
2390,
4662,
2647,
3343,
1322,
10025
] | 0.371651 |
265 | Summary: Crotonase-fold acyl-CoA enzyme core: an internal β/α segment enriched in small hydrophobics and glycine that lines the hydrophobic acyl‑CoA binding tunnel adjacent to the catalytic glutamate in enoyl‑CoA hydratase/isomerase–type enzymes; the feature weakly cross-activates on other hydrophobic helical/β element... | Crotonase-fold acyl-CoA enzyme core: an internal β/α segment enriched in small hydrophobics and glycine that lines the hydrophobic acyl‑CoA binding tunnel adjacent to the catalytic glutamate in enoyl‑CoA hydratase/isomerase–type enzymes; the feature weakly cross-activates on other hydrophobic helical/β elements and som... | Regional activation: long, contiguous internal segments (~100–200 aa) within the catalytic core, typically starting around residue 90–150 and extending to ~220–260; strongest just downstream of the catalytic Glu across adjacent helices and short β-strands. Outside this family, only weak, isolated residue-level peaks ap... | Ligand-binding site | - 3,2-trans-enoyl-CoA isomerase (crotonase superfamily): activation rises near the catalytic glutamate and peaks in the following helix/short β region that helps form the acyl‑CoA channel.
- 1,2-epoxyphenylacetyl-CoA isomerase (enoyl‑CoA hydratase-like): strong activation across an internal helix–β segment with high st... | 7,861,501 | 3.275588 | 23.375 | [
{
"activation": 23.375,
"uniref_id": "UPI000CB973EA"
},
{
"activation": 23.34375,
"uniref_id": "A0A947NRU4"
},
{
"activation": 23.3125,
"uniref_id": "A0A7S1ESY4"
},
{
"activation": 23.1875,
"uniref_id": "A0A229YC26"
},
{
"activation": 23.1875,
"uniref_id": "UP... | [
{
"activation": 20.545818328857422,
"uniprot_id": "Q13011"
},
{
"activation": 20.491209030151367,
"uniprot_id": "P77467"
},
{
"activation": 20.34308624267578,
"uniprot_id": "Q96DC8"
},
{
"activation": 20.33230209350586,
"uniprot_id": "Q589W8"
},
{
"activation": 20... | [
543,
13017,
3772,
6786,
5847,
1963,
4372,
11033,
857,
691
] | 0.145737 |
266 | Summary: Extended, hydrophobic alpha-helical membrane-active domains that insert into or remodel lipid bilayers—helical bundles/heptad-repeat blocks used for pore formation, protein translocation, or membrane fusion across diverse systems (toxins, secretion translocons, viral fusion proteins, bacteriocins, organellar t... | Extended, hydrophobic alpha-helical membrane-active domains that insert into or remodel lipid bilayers—helical bundles/heptad-repeat blocks used for pore formation, protein translocation, or membrane fusion across diverse systems (toxins, secretion translocons, viral fusion proteins, bacteriocins, organellar translocas... | Domain-level regional activation over long, contiguous blocks of hydrophobic/amphipathic helices (often coiled-coil/heptad-repeat rich); typically spans tens to a few hundred residues, frequently toward the C-terminus; not driven by a short consensus motif and shows minimal residue-level spiking. Occasionally, activati... | Membrane-associated | - Type III secretion system translocon pore proteins (e.g., YopB/YopD, PopB/PopD, SipB/SipC): activation on their long hydrophobic helical segments that insert into host membranes to form the translocation pore.
- Viral fusion/entry glycoproteins (class I/II/III; e.g., HA2, paramyxovirus F, coronavirus S2; rotavirus VP... | 6,096,346 | 3.529876 | 24.890625 | [
{
"activation": 24.890625,
"uniref_id": "A0A953BYV7"
},
{
"activation": 24.078125,
"uniref_id": "UPI00061AF30A"
},
{
"activation": 24.078125,
"uniref_id": "UPI00054CDB2E"
},
{
"activation": 24,
"uniref_id": "UPI001E4AF736"
},
{
"activation": 23.984375,
"uniref... | [
{
"activation": 21.413223266601562,
"uniprot_id": "Q2G179"
},
{
"activation": 19.85671615600586,
"uniprot_id": "P17452"
},
{
"activation": 19.681488037109375,
"uniprot_id": "Q06114"
},
{
"activation": 18.69828987121582,
"uniprot_id": "Q9I739"
},
{
"activation": 18... | [
1534,
10349,
12361,
11273,
9218,
3175,
14401,
14633,
15803,
6051
] | 0.231148 |
267 | Summary: Enzymes that bind and transform nitrogen‑containing heteroaromatic metabolites, with strongest preference for NADPH‑dependent DHFR‑like pterin reductases (DHFR, FolM and the reductase domain of RibD) and broader activation across soluble enzymes acting on nucleobases and ring intermediates in riboflavin, histi... | Enzymes that bind and transform nitrogen‑containing heteroaromatic metabolites, with strongest preference for NADPH‑dependent DHFR‑like pterin reductases (DHFR, FolM and the reductase domain of RibD) and broader activation across soluble enzymes acting on nucleobases and ring intermediates in riboflavin, histidine, tet... | Predominantly domain‑level activation spanning long, contiguous regions of the soluble catalytic core, often beginning at/near the N‑terminus; in bifunctional proteins, strongest over the DHFR‑like reductase domain with variable secondary signal on companion deaminase domains; in kinases/deaminases/hydrolases of nucleo... | Domain | - Dihydrofolate reductase (DHFR): strong, continuous activation across the DHFR core, including the NADPH- and pterin‑binding pocket
- RibD/RibG (bifunctional DAROPP deaminase/reductase): dominant activation on the C‑terminal DHFR‑like reductase domain; secondary signal on the N‑terminal cytidine‑deaminase‑like domain
... | 4,474,142 | 3.839251 | 22.546875 | [
{
"activation": 22.546875,
"uniref_id": "A0A356TLR4"
},
{
"activation": 22.375,
"uniref_id": "UPI0030D26F7E"
},
{
"activation": 22.3125,
"uniref_id": "UPI003627A2C1"
},
{
"activation": 22.28125,
"uniref_id": "A0A7C6KM90"
},
{
"activation": 22.25,
"uniref_id": ... | [
{
"activation": 20.061115264892578,
"uniprot_id": "P33312"
},
{
"activation": 19.678333282470703,
"uniprot_id": "Q9STY4"
},
{
"activation": 19.127418518066406,
"uniprot_id": "Q9P7L3"
},
{
"activation": 18.854433059692383,
"uniprot_id": "O26337"
},
{
"activation": ... | [
7142,
13317,
15718,
1315,
789,
15561,
5951,
3314,
13980,
13653
] | 0.182678 |
268 | Summary: Interfacial alpha‑helical end/capping and short helix‑turn segments at domain and membrane boundaries (including hydrophobic TM helices and their caps), often featuring aromatic anchors (F/Y/W) and small turn‑formers (G/S) with nearby acidic/histidine residues; in soluble enzymes this extends over long helical... | Interfacial alpha‑helical end/capping and short helix‑turn segments at domain and membrane boundaries (including hydrophobic TM helices and their caps), often featuring aromatic anchors (F/Y/W) and small turn‑formers (G/S) with nearby acidic/histidine residues; in soluble enzymes this extends over long helical runs and... | Mixed: regional activation across one or more helices (including entire TM segments) and adjacent turns; pronounced residue‑level peaks at helix caps/turns (often aromatics or small residues); frequently situated in low‑to‑moderate confidence, flexible linker zones between structured elements | Structural motif | - Viral holins: activation over a C‑terminal periplasmic segment spanning a short helix→turn→coil, with peaks on interfacial residues (e.g., H/E/F/D) that cap/anchor the helix at the membrane boundary.
- Diguanylate cyclases (GGDEF): a helix‑turn segment immediately N‑terminal to the catalytic domain, peaking on a Y–S/... | 6,034,939 | 3.539999 | 19.75 | [
{
"activation": 19.75,
"uniref_id": "UPI0006681836"
},
{
"activation": 19.671875,
"uniref_id": "UPI001B802BCF"
},
{
"activation": 19.59375,
"uniref_id": "A0A2M9YI18"
},
{
"activation": 19.5,
"uniref_id": "A0A7M2V535"
},
{
"activation": 19.328125,
"uniref_id": ... | [
{
"activation": 10.693586349487305,
"uniprot_id": "P0DUD7"
},
{
"activation": 8.519912719726562,
"uniprot_id": "Q9NZD4"
},
{
"activation": 5.31169319152832,
"uniprot_id": "G3JF10"
},
{
"activation": 5.098668575286865,
"uniprot_id": "P22234"
},
{
"activation": 4.94... | [
14639,
11118,
12486,
9438,
8,
362,
3223,
16307,
8520,
4135
] | 0.265723 |
269 | Summary: Secretory-pathway glycoprotein ectodomains that are cysteine- and/or Ser/Thr/Pro-rich—disulfide‑bonded and glycosylated—most prominently the C‑terminal portion of the zona pellucida (ZP) domain and its adjacent low‑complexity linker/stalk in secreted/type I membrane precursors; the same signal extends to disul... | Secretory-pathway glycoprotein ectodomains that are cysteine- and/or Ser/Thr/Pro-rich—disulfide‑bonded and glycosylated—most prominently the C‑terminal portion of the zona pellucida (ZP) domain and its adjacent low‑complexity linker/stalk in secreted/type I membrane precursors; the same signal extends to disulfide‑rich... | Regional/domain-level activation over long contiguous stretches of extracellular/luminal sequence; strongest at the C‑terminal half of ZP domains and the immediately downstream disordered linker; little to no activation on signal peptides, transmembrane helices, or cytosolic tails; captures both structured disulfide-bo... | Compositional bias | - Zona pellucida family glycoproteins (uromodulin/tectorins/ZP1–4/cuticlins): activation across the C‑terminal ZP module and the downstream linker before the transmembrane anchor
- Secreted proteases and protease inhibitors (serine proteases, metalloproteases; serpins, Kunitz/Kazal domains): activation on disulfide‑sta... | 5,685,828 | 3.599588 | 23.0625 | [
{
"activation": 23.0625,
"uniref_id": "UPI000423F62F"
},
{
"activation": 23.03125,
"uniref_id": "A0A517ZGT2"
},
{
"activation": 23,
"uniref_id": "UPI0027BA7813"
},
{
"activation": 22.984375,
"uniref_id": "UPI001EF280AA"
},
{
"activation": 22.84375,
"uniref_id"... | [
{
"activation": 6.413620471954346,
"uniprot_id": "P31196"
},
{
"activation": 4.926114559173584,
"uniprot_id": "P16397"
},
{
"activation": 4.884152412414551,
"uniprot_id": "P73515"
},
{
"activation": 4.83622932434082,
"uniprot_id": "P76002"
},
{
"activation": 4.825... | [
1005,
4276,
5328,
5341,
1943,
605,
13162,
1773,
151,
5545
] | 0.519073 |
270 | Summary: Hydrophobic transmembrane α-helices of multi-pass small‑molecule transporters (permeases), with strong enrichment for cation‑coupled exchangers/symporters and Na+-coupled metabolite carriers; the feature preferentially marks the first N‑terminal signal/anchor helix and one or two conserved core (pore/gating) h... | Hydrophobic transmembrane α-helices of multi-pass small‑molecule transporters (permeases), with strong enrichment for cation‑coupled exchangers/symporters and Na+-coupled metabolite carriers; the feature preferentially marks the first N‑terminal signal/anchor helix and one or two conserved core (pore/gating) helices ra... | Regional activation on long contiguous hydrophobic stretches (~15–25 aa) corresponding to individual TM helices; often initiates at the extreme N‑terminus and can extend across adjacent TM segments. Residue‑level peaks fall on aliphatic residues. Within a transporter, only a subset of TMs (e.g., TM1 and a mid‑core heli... | Membrane-associated | - Na+/H+ antiporters (CPA/CPA2; SLC9; bacterial NhaA/NhaB; plant NHX): strong signal on the N‑terminal signal/anchor helix and a central transport helix.
- Na+/dicarboxylate and sulfate symporters (DASS/SLC13): selected core TMs forming the ion/substrate pathway.
- Neurotransmitter sodium symporters (SLC6) and amino‑ac... | 8,155,540 | 3.238868 | 24.265625 | [
{
"activation": 24.265625,
"uniref_id": "UPI001E62E264"
},
{
"activation": 24.078125,
"uniref_id": "UPI0028FCEFA6"
},
{
"activation": 24.03125,
"uniref_id": "A0A090QW11"
},
{
"activation": 23.90625,
"uniref_id": "A0A2X3CQZ3"
},
{
"activation": 23.90625,
"unire... | [
{
"activation": 23.098583221435547,
"uniprot_id": "P0ABN9"
},
{
"activation": 22.80397605895996,
"uniprot_id": "Q9I2S5"
},
{
"activation": 21.621042251586914,
"uniprot_id": "Q04671"
},
{
"activation": 21.1239013671875,
"uniprot_id": "Q9AV23"
},
{
"activation": 20.... | [
6138,
1562,
4095,
5497,
8231,
14907,
6339,
2912,
3308,
5162
] | 0.202117 |
271 | Summary: Structural signal for hydrophobic/aromatic residues that build the beta-strand cores of folded beta-sheet domains—most prominently C2 beta-sandwich and WW modules, but also other beta-rich interaction domains (SH2/SH3/PH/PTB/PDZ/GRAM) and, in some cases, alpha/beta enzyme folds with central beta-sheets (e.g., ... | Structural signal for hydrophobic/aromatic residues that build the beta-strand cores of folded beta-sheet domains—most prominently C2 beta-sandwich and WW modules, but also other beta-rich interaction domains (SH2/SH3/PH/PTB/PDZ/GRAM) and, in some cases, alpha/beta enzyme folds with central beta-sheets (e.g., GNAT N-te... | Residue-level sparse peaks confined to folded beta-sheet domains, concentrated on hydrophobic/aromatic positions within DSSP E strands (often showing an alternating pattern on one face of a sheet). Domain-level restriction to these beta-sheet regions; minimal or absent in Ca2+-binding loops, disordered linkers, transme... | Structural motif | - Synaptotagmins (tandem C2 Ca2+-lipid sensors): peaks on hydrophobic beta-strands of both C2 domains, not on Ca2+-binding loops.
- DOC2 family (double C2-like proteins): alternating hydrophobic residues in beta-strands across both C2 domains.
- Plant and animal C2-domain proteins: localized peaks on beta-strands withi... | 70,904,038 | 1.076238 | 9.460938 | [
{
"activation": 9.4609375,
"uniref_id": "A0A852KLD0"
},
{
"activation": 9.4296875,
"uniref_id": "A0A6F9BZ51"
},
{
"activation": 9.40625,
"uniref_id": "A0A0D2TU09"
},
{
"activation": 9.3828125,
"uniref_id": "A0A8D2N9A6"
},
{
"activation": 9.3515625,
"uniref_id"... | [
{
"activation": 9.026074409484863,
"uniprot_id": "P47709"
},
{
"activation": 9.003668785095215,
"uniprot_id": "P70610"
},
{
"activation": 8.86963939666748,
"uniprot_id": "Q9JIR3"
},
{
"activation": 8.803121566772461,
"uniprot_id": "P40748"
},
{
"activation": 8.786... | [
4656,
629,
4021,
8913,
6079,
15709,
12803,
7932,
3788,
11976
] | 0.125572 |
272 | Summary: Proline- and acidic/polar–enriched loop/turn elements at helix boundaries (helix caps, kinks, and hinge loops) and short linear interaction/catalytic loops; a generic structural motif recurring across many folds and functions
Activation pattern: Predominantly residue-level peaks clustered at helix–loop junctio... | Proline- and acidic/polar–enriched loop/turn elements at helix boundaries (helix caps, kinks, and hinge loops) and short linear interaction/catalytic loops; a generic structural motif recurring across many folds and functions | Predominantly residue-level peaks clustered at helix–loop junctions and sharp turns (often involving Pro and Asp/Glu/Ser/Thr), occasionally extending over longer low‑complexity acidic/proline-rich segments; number and spacing of peaks vary with the density of helices and flexible loops in each protein | Structural motif | - Retroviral Pol/Gag-Pol: proline-rich late-domain–like motifs (e.g., PxxP/PPxY/P(T/S)AP) and acidic active-site/linker loops in integrase/RNase H–like regions.
- Plant R2R3-MYB transcription factors: conserved helix-turn-helix caps/hinges in the R2/R3 repeats (e.g., Cys around the R2 helix cap and Pro near the R3 cap ... | 143,226,835 | 0.373136 | 17.96875 | [
{
"activation": 17.96875,
"uniref_id": "UPI002241045A"
},
{
"activation": 17.859375,
"uniref_id": "UPI001A9AB11D"
},
{
"activation": 17.671875,
"uniref_id": "A0A937ZWH6"
},
{
"activation": 17.546875,
"uniref_id": "A0A3E0KRE6"
},
{
"activation": 17.515625,
"uni... | [
{
"activation": 15.248934745788574,
"uniprot_id": "F4J3R7"
},
{
"activation": 14.926526069641113,
"uniprot_id": "Q7CRQ0"
},
{
"activation": 14.89022159576416,
"uniprot_id": "Q8BRJ3"
},
{
"activation": 14.841861724853516,
"uniprot_id": "Q8IUW5"
},
{
"activation": 1... | [
2884,
12904,
10632,
2803,
3111,
10825,
4059,
9497,
4066,
6074
] | 0.104351 |
273 | Summary: Iron–sulfur (Fe–S) cluster–binding segments and ferredoxin-like electron-carrier domains, especially [2Fe–2S] ferredoxin folds and Cys-based Fe–S ligation motifs (e.g., CX3CX2C of radical‑SAM enzymes and IscA/SufA cluster-handling loops) that mediate electron transfer or radical chemistry across diverse redox ... | Iron–sulfur (Fe–S) cluster–binding segments and ferredoxin-like electron-carrier domains, especially [2Fe–2S] ferredoxin folds and Cys-based Fe–S ligation motifs (e.g., CX3CX2C of radical‑SAM enzymes and IscA/SufA cluster-handling loops) that mediate electron transfer or radical chemistry across diverse redox systems; ... | Primarily regional/domain-level activation over metallocofactor-binding modules (Fe–S foremost), with pronounced residue-level peaks around ligand-bearing loops (Cys/His/Asp/Glu) and adjacent β-strands/loops; long contiguous stretches are highlighted in ferredoxin domains, while generic FAD/NAD-binding cores show littl... | Ligand-binding site | - Adrenodoxin-type [2Fe–2S] ferredoxins and the N-terminal ferredoxin domains of aromatic/alkane dioxygenase reductases: activation spans the ferredoxin fold and peaks at the Cys ligation loops adjacent to the [2Fe–2S] cluster.
- Organellar ferredoxins (chloroplast/mitochondrial Fdx): activation across the core [2Fe–2S... | 20,070,346 | 2.338322 | 16.71875 | [
{
"activation": 16.71875,
"uniref_id": "A0A158K202"
},
{
"activation": 16.515625,
"uniref_id": "A0A8J3FAW1"
},
{
"activation": 16.375,
"uniref_id": "A0A2V6QNG9"
},
{
"activation": 16.203125,
"uniref_id": "A0A0B8QJD3"
},
{
"activation": 15.9609375,
"uniref_id":... | [
{
"activation": 15.150434494018555,
"uniprot_id": "O23344"
},
{
"activation": 14.54281997680664,
"uniprot_id": "Q8IED5"
},
{
"activation": 14.392463684082031,
"uniprot_id": "Q3C1E0"
},
{
"activation": 14.370468139648438,
"uniprot_id": "Q9C7Y4"
},
{
"activation": 1... | [
14462,
5733,
5722,
14867,
1927,
9975,
15640,
10791,
9086,
5201
] | 0.448001 |
274 | Summary: Conserved PLP-anchoring active‑site segment centered on the Schiff‑base–forming lysine and the adjacent glycine/acidic‑residue–rich phosphate‑binding loop (“PLP anchor”) shared across diverse PLP‑dependent enzymes—most prominently fold‑type I families (aminotransferases, alpha‑oxoamine synthases, C–S lyases, S... | Conserved PLP-anchoring active‑site segment centered on the Schiff‑base–forming lysine and the adjacent glycine/acidic‑residue–rich phosphate‑binding loop (“PLP anchor”) shared across diverse PLP‑dependent enzymes—most prominently fold‑type I families (aminotransferases, alpha‑oxoamine synthases, C–S lyases, SHMT, cyst... | Regional activation on short internal segments (~15–40 aa) with residue‑level peaks at the catalytic Lys and neighboring Gly‑rich and Asp/Glu residues that bind the PLP phosphate; recurring in orthologs across taxa; independent of subcellular localization | Ligand-binding site | - Aminotransferases (class I/II; broad substrate range, including dTDP/UDP‑sugar aminotransferases for cell‑surface glycan modification): activation on the catalytic Lys + glycine‑rich phosphate‑binding loop of the PLP site
- Alpha‑oxoamine synthases (ALAS/HemA, serine palmitoyltransferase/SPT, BioF/AONS/KBL): activati... | 10,022,203 | 3.032762 | 20.640625 | [
{
"activation": 20.640625,
"uniref_id": "UPI002AD2C19D"
},
{
"activation": 20.046875,
"uniref_id": "A0A3L7U7V7"
},
{
"activation": 19.859375,
"uniref_id": "X1D9G8"
},
{
"activation": 19.703125,
"uniref_id": "A0A1B8YLL3"
},
{
"activation": 19.703125,
"uniref_id... | [
{
"activation": 18.031051635742188,
"uniprot_id": "O25130"
},
{
"activation": 17.798187255859375,
"uniprot_id": "D3QY10"
},
{
"activation": 17.71963882446289,
"uniprot_id": "A0R5M7"
},
{
"activation": 17.644269943237305,
"uniprot_id": "Q03046"
},
{
"activation": 1... | [
16356,
11718,
12278,
11817,
5954,
15720,
5833,
938,
14766,
1618
] | 0.251466 |
275 | Summary: Intrinsically disordered, poly‑proline–rich low‑complexity regions with EVH1/SH3/profilin‑recognition motifs (FP4/FPPPP, PxxP) that act as multivalent docking modules; strongly enriched in actin‑assembly contexts (FH1 tracts, Ena/VASP ligands) but also occurring in other proteins with long PRRs (e.g., receptor... | Intrinsically disordered, poly‑proline–rich low‑complexity regions with EVH1/SH3/profilin‑recognition motifs (FP4/FPPPP, PxxP) that act as multivalent docking modules; strongly enriched in actin‑assembly contexts (FH1 tracts, Ena/VASP ligands) but also occurring in other proteins with long PRRs (e.g., receptor/ion‑chan... | Extended regional activation over long Pro/Gly/Ser‑rich stretches with repeated PP/FP motifs; multiple adjacent segments light up; typically outside folded domains (e.g., FH1 before FH2, interdomain linkers, or cytosolic tails). | Interaction site | - Formins/formin-like proteins: FH1 polyproline regions binding profilin–actin.
- Ena/VASP-binding ligands (zyxin/lamellipodin): EVH1-binding FP4 motifs in PRRs.
- WASP/WAVE NPFs: central PRRs with SH3/profilin-binding segments.
- Membrane proteins with cytosolic tails (receptors and ion channels, e.g., TRP family): ta... | 5,734,624 | 3.591043 | 19.046875 | [
{
"activation": 19.046875,
"uniref_id": "A0A8B9SK56"
},
{
"activation": 19.015625,
"uniref_id": "A0A8B9SK84"
},
{
"activation": 18.84375,
"uniref_id": "UPI00383113E7"
},
{
"activation": 18.828125,
"uniref_id": "A0AAD9Q0M4"
},
{
"activation": 18.8125,
"uniref_i... | [
{
"activation": 18.302824020385742,
"uniprot_id": "Q27J81"
},
{
"activation": 18.15524673461914,
"uniprot_id": "Q9C0D6"
},
{
"activation": 18.083166122436523,
"uniprot_id": "Q9Y613"
},
{
"activation": 17.285890579223633,
"uniprot_id": "Q9NZ56"
},
{
"activation": 1... | [
1086,
6185,
7466,
7032,
7436,
13364,
14981,
4673,
11986,
2554
] | 0.261638 |
276 | Summary: Short, acidic (Asp/Glu–rich) active‑site segment that either coordinates a divalent metal cofactor (Mg2+/Mn2+) when present or stabilizes/positions anionic cofactors or substrates (e.g., ATP/PPi, phosphate, flavin/NADP phosphates), recurring across M24 metallopeptidases, ATP‑dependent ligases/kinases, cofactor... | Short, acidic (Asp/Glu–rich) active‑site segment that either coordinates a divalent metal cofactor (Mg2+/Mn2+) when present or stabilizes/positions anionic cofactors or substrates (e.g., ATP/PPi, phosphate, flavin/NADP phosphates), recurring across M24 metallopeptidases, ATP‑dependent ligases/kinases, cofactor‑attachme... | Compact mid‑chain windows (~10–30 aa), typically beta–loop–alpha; residue‑level peaks on Asp/Glu (often near His/Gly; Pro frequent in X‑Pro peptidases). Peaks often coincide with metal‑binding or other catalytic carboxylates; segments may be well‑structured or flexible catalytic loops. | Ligand-binding site | - Xaa‑Pro aminopeptidases/prolidases (M24): activation on catalytic carboxylates that chelate Mn2+ and contact substrate.
- Phosphopantetheinyl transferases (e.g., PptT): activation on acidic Mg2+‑binding loop for PPAT chemistry.
- Biotin/lipoate protein ligases (BirA/LplA): activation on flexible acidic loop coordinat... | 15,798,401 | 2.577657 | 19.75 | [
{
"activation": 19.75,
"uniref_id": "A0A2E5P1T0"
},
{
"activation": 19.609375,
"uniref_id": "A0A382BHP3"
},
{
"activation": 19.609375,
"uniref_id": "A0A351XCZ3"
},
{
"activation": 19.5625,
"uniref_id": "UPI0031E5683B"
},
{
"activation": 19.5625,
"uniref_id": "... | [
{
"activation": 18.206613540649414,
"uniprot_id": "Q166H0"
},
{
"activation": 17.026559829711914,
"uniprot_id": "Q9Y5B9"
},
{
"activation": 16.772384643554688,
"uniprot_id": "Q9NQH7"
},
{
"activation": 16.64657974243164,
"uniprot_id": "Q0V147"
},
{
"activation": 1... | [
4282,
786,
14295,
15278,
5174,
6277,
11041,
15484,
6636,
9471
] | 0.233748 |
277 | Summary: PAPS-dependent sulfotransferase catalytic core (Sulfotransferase family 1), capturing the PAPS-binding (2′-phosphosulfate/3′-phosphate) loops and the adjacent acceptor-substrate binding cleft used to transfer sulfate to tyrosine, glycans, lipids, or small molecules across TPST/CHST/SULT enzymes in diverse taxa... | PAPS-dependent sulfotransferase catalytic core (Sulfotransferase family 1), capturing the PAPS-binding (2′-phosphosulfate/3′-phosphate) loops and the adjacent acceptor-substrate binding cleft used to transfer sulfate to tyrosine, glycans, lipids, or small molecules across TPST/CHST/SULT enzymes in diverse taxa | Broad, contiguous activation across the catalytic domain, often beginning near the N-terminus of the mature lumenal/cytosolic domain; superimposed residue-level peaks at PAPS-binding sites and catalytic residues and at peptide/sugar acceptor-contacting positions; minimal activation in signal peptides/transmembranes and... | Domain | - Tyrosylprotein sulfotransferases (TPST1/TPST2): strong peaks over the peptide-substrate binding segment and the catalytic acidic residue, with partial overlap of the PAPS-binding site; disulfide-forming Cys in the lumenal core often highlighted.
- Glycosaminoglycan/carbohydrate sulfotransferases (CHST family; e.g., H... | 5,613,301 | 3.612426 | 23.890625 | [
{
"activation": 23.890625,
"uniref_id": "UPI0027368680"
},
{
"activation": 23.875,
"uniref_id": "A0A3D8LF89"
},
{
"activation": 23.84375,
"uniref_id": "UPI001CD3B1B1"
},
{
"activation": 23.8125,
"uniref_id": "UPI0005A282D7"
},
{
"activation": 23.703125,
"unire... | [
{
"activation": 20.596412658691406,
"uniprot_id": "Q91XQ5"
},
{
"activation": 19.800535202026367,
"uniprot_id": "A8XLL3"
},
{
"activation": 19.77566909790039,
"uniprot_id": "O53699"
},
{
"activation": 19.680397033691406,
"uniprot_id": "O60704"
},
{
"activation": 1... | [
15633,
2367,
14970,
6981,
3061,
14449,
3680,
14955,
1963,
14166
] | 0.16643 |
278 | Summary: P-loop (Walker A) phosphate-binding loop of NTP-binding proteins—most prominently the ABC transporter nucleotide-binding domains—and equivalent ATP-binding loops in P-loop kinases; the feature centers on residues that coordinate the β/γ phosphates (Lys of GxxxxGKT/S and nearby Gly/Ser/Thr) and can also pick up... | P-loop (Walker A) phosphate-binding loop of NTP-binding proteins—most prominently the ABC transporter nucleotide-binding domains—and equivalent ATP-binding loops in P-loop kinases; the feature centers on residues that coordinate the β/γ phosphates (Lys of GxxxxGKT/S and nearby Gly/Ser/Thr) and can also pick up adjacent... | Residue-level peaks confined to 1–3 positions within the ATP-binding loop, typically the Walker A lysine and immediately neighboring small residues; occasionally a peak on the H-loop histidine. Signals occur as two separate peaks in proteins with two NBDs. In many bacterial ABC ATP-binding proteins the peak lies early ... | Ligand-binding site | - ABC transporter nucleotide-binding domains (importers/exporters, including bacteriocin/microcin processing/export): strong peak on the Walker A lysine within the ATP-binding site.
- Energy-coupling factor (ECF) transporter A subunits: sharp peak within the ATP-binding site, including the H-loop histidine adjacent to ... | 27,637,249 | 2.018401 | 30.59375 | [
{
"activation": 30.59375,
"uniref_id": "A0A0H2ZFE5"
},
{
"activation": 30.203125,
"uniref_id": "A0A3M1UNK7"
},
{
"activation": 30.140625,
"uniref_id": "UPI0022256DBF"
},
{
"activation": 29.984375,
"uniref_id": "UPI001EDA5A05"
},
{
"activation": 29.96875,
"unir... | [
{
"activation": 26.001293182373047,
"uniprot_id": "Q9AT00"
},
{
"activation": 25.97861671447754,
"uniprot_id": "Q8LEF6"
},
{
"activation": 25.49846839904785,
"uniprot_id": "Q8PHQ3"
},
{
"activation": 25.46359634399414,
"uniprot_id": "P9WQK5"
},
{
"activation": 25.... | [
4352,
6965,
11403,
15587,
3249,
2683,
9041,
2623,
15259,
12336
] | 0.725541 |
279 | Summary: Short, functionally important secondary-structure microenvironments: strongest on acidic/histidine-rich flexible loops adjacent to metal-binding sites in HD-family nucleases and other metal-dependent hydrolases, but also firing as single-site peaks on core residues within alpha-helical scaffolds (coiled-coils ... | Short, functionally important secondary-structure microenvironments: strongest on acidic/histidine-rich flexible loops adjacent to metal-binding sites in HD-family nucleases and other metal-dependent hydrolases, but also firing as single-site peaks on core residues within alpha-helical scaffolds (coiled-coils and nucle... | Bimodal: (1) regional activation over low-pLDDT coil/helix stretches in catalytic domains enriched for H/E/D/G, often encompassing HE/HD diads and a metal-binding His; (2) sharp single-residue peaks within well-ordered helices (coiled-coils, LBD helices, short cytosolic helices) or at a conserved beta-strand position i... | Ligand-binding site | - Cas3 HD nuclease: broad activation across the N-terminal HD nuclease domain, including the Mg2+-binding His and adjacent flexible loop.
- Metalloproteases/peptidases (zincins): activation on the HExxH motif loop and surrounding acidic residues.
- Deubiquitinases (e.g., MINDY/USP-like): extended activation on N-termin... | 5,761,959 | 3.586288 | 24.828125 | [
{
"activation": 24.828125,
"uniref_id": "A0A2N5UTQ1"
},
{
"activation": 24.5,
"uniref_id": "UPI0038CD3E37"
},
{
"activation": 24.453125,
"uniref_id": "A0A651FI08"
},
{
"activation": 24.296875,
"uniref_id": "A0A7C5HVT5"
},
{
"activation": 24.234375,
"uniref_id"... | [
{
"activation": 19.34659194946289,
"uniprot_id": "P29934"
},
{
"activation": 8.735766410827637,
"uniprot_id": "P0ADN0"
},
{
"activation": 7.619899272918701,
"uniprot_id": "Q02ML8"
},
{
"activation": 7.368430137634277,
"uniprot_id": "P38036"
},
{
"activation": 7.21... | [
13629,
13848,
6238,
8437,
6022,
15339,
7082,
6865,
2838,
3243
] | 0.167282 |
280 | Summary: A well‑ordered secondary‑structure block (helix/strand neighborhood) in the core of soluble domains—most prominently the CAP/SCP (PR‑1/PRY/CRISP/antigen 5) domain of secreted proteins—and, more generally, analogous structured patches that flank rather than coincide with catalytic residues in diverse enzymes.
A... | A well‑ordered secondary‑structure block (helix/strand neighborhood) in the core of soluble domains—most prominently the CAP/SCP (PR‑1/PRY/CRISP/antigen 5) domain of secreted proteins—and, more generally, analogous structured patches that flank rather than coincide with catalytic residues in diverse enzymes. | Regional activation over long, contiguous stretches (often 50–100 aa) within the mature domain; peaks on alpha helices and adjacent beta strands/coils in well‑structured regions; typically post‑signal peptide in secreted proteins; tends to sit near (but not on) annotated catalytic/metal‑binding residues; rare weak sing... | Domain | - CAP/SCP/TAPS superfamily (PR‑1/PRY/CRISP/venom antigen 5): activation spans the central/C‑terminal half of the CAP domain, covering β‑strand–helix elements in the structured core of the secreted mature protein.
- Neutral sphingomyelinases: activation on a β/α‑rich subdomain distant from the Mg2+‑binding/catalytic res... | 4,882,607 | 3.751886 | 22.78125 | [
{
"activation": 22.78125,
"uniref_id": "A0A522PN89"
},
{
"activation": 22.640625,
"uniref_id": "D4JXN1"
},
{
"activation": 22.59375,
"uniref_id": "UPI001AAEBAA5"
},
{
"activation": 22.546875,
"uniref_id": "A0A173SPE2"
},
{
"activation": 22.546875,
"uniref_id":... | [
{
"activation": 19.121639251708984,
"uniprot_id": "I7M6D6"
},
{
"activation": 16.41411590576172,
"uniprot_id": "Q06469"
},
{
"activation": 16.193878173828125,
"uniprot_id": "Q59PV6"
},
{
"activation": 16.167865753173828,
"uniprot_id": "Q41495"
},
{
"activation": 1... | [
12851,
9873,
5285,
6264,
3246,
6167,
3606,
4497,
6734,
4449
] | 0.205501 |
281 | Summary: Active-site-adjacent beta-strand/loop module that shapes the phosphate/pyrophosphate-binding cleft in nucleotide/phosphate-processing enzymes—most prominently in the Nudix fold—typically positioned immediately C-terminal to the family’s signature catalytic motif (e.g., Nudix box, HIT triad, HhH-GPD) and often ... | Active-site-adjacent beta-strand/loop module that shapes the phosphate/pyrophosphate-binding cleft in nucleotide/phosphate-processing enzymes—most prominently in the Nudix fold—typically positioned immediately C-terminal to the family’s signature catalytic motif (e.g., Nudix box, HIT triad, HhH-GPD) and often enriched ... | Regional, contiguous 10–20 aa blocks centered on a beta-strand and extending into a flanking loop/short helix; highest signal on residues within the strand and neighboring coil. Usually within the catalytic domain but outside the signature motif itself (often just C-terminal to it); sometimes overlaps substrate/metal-b... | Ligand-binding site | - MutT-like 8-oxo-(d)GTP diphosphatases (Nudix): activation on a beta-strand/short-helix segment C-terminal to the Nudix box within the Nudix domain.
- snoRNA/mRNA decapping enzymes (NUDT16/DCP2-like): activation on a beta-strand transitioning into helix inside the Nudix domain, away from the Nudix box and annotated me... | 10,181,981 | 3.016946 | 20.75 | [
{
"activation": 20.75,
"uniref_id": "A0A7W9HA08"
},
{
"activation": 20.609375,
"uniref_id": "UPI003B20EA1C"
},
{
"activation": 20.609375,
"uniref_id": "UPI001420DC92"
},
{
"activation": 20.453125,
"uniref_id": "A0A0Q7JWZ6"
},
{
"activation": 20.4375,
"uniref_i... | [
{
"activation": 18.642608642578125,
"uniprot_id": "Q6ZVK8"
},
{
"activation": 18.229421615600586,
"uniprot_id": "Q9NV35"
},
{
"activation": 18.02935791015625,
"uniprot_id": "P96590"
},
{
"activation": 17.95071029663086,
"uniprot_id": "O95989"
},
{
"activation": 17... | [
7940,
3119,
9627,
484,
9971,
16279,
15868,
5667,
6524,
7770
] | 0.201893 |
282 | Summary: Conserved non-cysteine loop/helix-boundary elements of the Radical SAM core domain that shape the AdoMet-binding/active-site pocket across diverse Radical SAM enzymes (recognizing the core fold and glycine-rich GGxTP/GGxEP-type loops adjacent to, but not including, the CxxxCxxC [4Fe-4S] ligands)
Activation pat... | Conserved non-cysteine loop/helix-boundary elements of the Radical SAM core domain that shape the AdoMet-binding/active-site pocket across diverse Radical SAM enzymes (recognizing the core fold and glycine-rich GGxTP/GGxEP-type loops adjacent to, but not including, the CxxxCxxC [4Fe-4S] ligands) | Domain-restricted activation confined to the Radical SAM core with multiple sharp peaks on short loops and secondary-structure boundaries; frequent hits on glycine-rich segments (e.g., GGxTP/GGxEP) near the SAM pocket; consistently avoids the Fe–S ligating cysteines and shows little/no signal in accessory domains (e.g.... | Ligand-binding site | - Oxygen-independent coproporphyrinogen III oxidase (HemN/HemN-like): loop at the start of an alpha-helix in the Radical SAM core, including a SAM-binding Arg; no activation in non-core regions
- Ribosomal protein uS12 methylthiotransferase (RimO): multiple peaks within the Radical SAM core; no activation in the N-term... | 6,288,778 | 3.498798 | 22.984375 | [
{
"activation": 22.984375,
"uniref_id": "A0A7W4HJA9"
},
{
"activation": 22.890625,
"uniref_id": "UPI0030B83D1E"
},
{
"activation": 22.890625,
"uniref_id": "A0A328EEY6"
},
{
"activation": 22.859375,
"uniref_id": "A0A117LTD6"
},
{
"activation": 22.796875,
"unire... | [
{
"activation": 20.757423400878906,
"uniprot_id": "O31067"
},
{
"activation": 20.6874942779541,
"uniprot_id": "A0A384LP51"
},
{
"activation": 20.681535720825195,
"uniprot_id": "A5D7B1"
},
{
"activation": 20.606945037841797,
"uniprot_id": "P32131"
},
{
"activation"... | [
12345,
3425,
8727,
16330,
6726,
13929,
1262,
6179,
15787,
14717
] | 0.181676 |
283 | Summary: Non-cytosolic juxtamembrane linkers/loops that tether extracellular or periplasmic domains to nearby transmembrane helices—most often the lumenal/periplasmic “stem” immediately preceding a TM (sometimes spilling into the TM N-terminus), with occasional activation on other membrane-facing loops within the same ... | Non-cytosolic juxtamembrane linkers/loops that tether extracellular or periplasmic domains to nearby transmembrane helices—most often the lumenal/periplasmic “stem” immediately preceding a TM (sometimes spilling into the TM N-terminus), with occasional activation on other membrane-facing loops within the same extracyto... | Regional activation over contiguous 20–100+ residue stretches in extracytoplasmic loops/linkers adjacent to TMs; peaks often in coil/short helix/β segments and may include the first residues of the following TM; activation frequently drops sharply within the TM core; secondary weaker peaks can occur on other periplasmi... | Membrane-associated | - Apolipoprotein N-acyltransferase (Lnt): activation across a TM-to-domain junction and on periplasmic CN-hydrolase loops away from the catalytic triad
- SecD (protein translocase): strong activation on the C‑terminal periplasmic segment required for export, terminating at the start of the following TM
- Class C GPCR (... | 5,775,239 | 3.583986 | 17.234375 | [
{
"activation": 17.234375,
"uniref_id": "UPI003BAF2678"
},
{
"activation": 17.21875,
"uniref_id": "A0A2M9G1X5"
},
{
"activation": 17.203125,
"uniref_id": "UPI003B50F413"
},
{
"activation": 17.203125,
"uniref_id": "UPI001CD1CC39"
},
{
"activation": 17.203125,
"... | [
{
"activation": 11.531561851501465,
"uniprot_id": "O59179"
},
{
"activation": 8.624343872070312,
"uniprot_id": "P39012"
},
{
"activation": 8.351970672607422,
"uniprot_id": "O94702"
},
{
"activation": 8.275179862976074,
"uniprot_id": "C5M545"
},
{
"activation": 8.2... | [
16020,
7456,
10508,
16083,
7914,
7756,
120,
3097,
3871,
12161
] | 0.358082 |
284 | Summary: Short alpha-helical Gxxx[C/S/T] motif in the catalytic ATP-binding (HATPase_c; Bergerat fold) domain of histidine kinases, positioned adjacent to the glycine-rich/ATP‑lid region that engages ADP/ATP; the feature highlights the small/polar residue (often Cys/Ser/Thr) and its upstream Gly, a hallmark shared acro... | Short alpha-helical Gxxx[C/S/T] motif in the catalytic ATP-binding (HATPase_c; Bergerat fold) domain of histidine kinases, positioned adjacent to the glycine-rich/ATP‑lid region that engages ADP/ATP; the feature highlights the small/polar residue (often Cys/Ser/Thr) and its upstream Gly, a hallmark shared across divers... | Residue-level peaks. Typically 1–2 strong peaks with 2–5 total residues per protein, localized to a mid-to-C-terminal helix of the HK CA (HATPase_c) domain next to the glycine-rich loop/ATP lid; adjacent small peaks on nearby Gly or within the same helix are common. Charged residues are rarely included. Occasional very... | Ligand-binding site | - Quorum-sensing sensor kinase CqsS: sharp peak at a cysteine within the CA-domain helix with a supporting upstream glycine (GxxxC).
- Plant ethylene receptor (hybrid sensor histidine kinase, ETR1/ERS family): strong serine peak in the CA-domain helix adjacent to annotated ADP-binding residues, with minor nearby peaks;... | 9,742,926 | 3.061024 | 35.0625 | [
{
"activation": 35.0625,
"uniref_id": "A0A838W6I7"
},
{
"activation": 35.0625,
"uniref_id": "A0A2V2UEB2"
},
{
"activation": 35.03125,
"uniref_id": "UPI0026ED3954"
},
{
"activation": 35,
"uniref_id": "A0A923R5G5"
},
{
"activation": 35,
"uniref_id": "UPI00281615... | [
{
"activation": 33.512237548828125,
"uniprot_id": "O34206"
},
{
"activation": 33.41213607788086,
"uniprot_id": "Q9RQQ9"
},
{
"activation": 33.066261291503906,
"uniprot_id": "Q8THF6"
},
{
"activation": 32.838531494140625,
"uniprot_id": "P21865"
},
{
"activation": 3... | [
586,
7418,
14936,
2984,
169,
31,
5799,
2016,
4385,
1736
] | 0.191407 |
285 | Summary: Seven‑transmembrane–like multi-pass membrane architecture, highlighting hydrophobic TM helices and the outer-facing loop framework—most pronounced in chemosensory/GPCR-like families (often around the TM4–second loop–TM5 region)—but also seen in other multi-pass membrane proteins (enzymes/transporters). Topolog... | Seven‑transmembrane–like multi-pass membrane architecture, highlighting hydrophobic TM helices and the outer-facing loop framework—most pronounced in chemosensory/GPCR-like families (often around the TM4–second loop–TM5 region)—but also seen in other multi-pass membrane proteins (enzymes/transporters). Topology is agno... | Regional activation over long hydrophobic stretches across multiple TM helices (often TM2–TM7) with spillover into adjacent external loops; highest peaks at helix–loop boundaries (frequently TM4–loop–TM5); low in disordered termini but may extend into structured cytosolic/luminal helices near the membrane; occasional f... | Membrane-associated | - Nematode serpentine receptor (class beta): broad activation across the seven-helix bundle, maximal across TM4–second loop–TM5; weak in termini.
- Insect gustatory receptor: strong on TM4 and the large TM4–TM5 loop, with residue‑level peaks.
- Drosophila odorant receptor: continuous activation in TM3–TM6 and connectin... | 4,950,309 | 3.738115 | 19.578125 | [
{
"activation": 19.578125,
"uniref_id": "A0A1I7WQ82"
},
{
"activation": 19.5625,
"uniref_id": "A0ABD2IYX2"
},
{
"activation": 18.96875,
"uniref_id": "A0ABD2JBV9"
},
{
"activation": 18.9375,
"uniref_id": "A0A8R1E7Q9"
},
{
"activation": 18.921875,
"uniref_id": "... | [
{
"activation": 16.85735511779785,
"uniprot_id": "A0A3B1DZW5"
},
{
"activation": 16.33957290649414,
"uniprot_id": "Q20961"
},
{
"activation": 16.27328872680664,
"uniprot_id": "Q20411"
},
{
"activation": 15.070655822753906,
"uniprot_id": "O45767"
},
{
"activation":... | [
10274,
13582,
13413,
7718,
6124,
1056,
10539,
1031,
5784,
2529
] | 0.2768 |
286 | Summary: N-terminal regulatory/sensing modules of transcriptional regulators—most strongly the CheY-like receiver (REC) domains of two-component response regulators and analogous N-terminal ligand/signal-binding or dimerization regions that precede a C-terminal HTH (LuxR-type/NarL-FixJ) DNA-binding domain; the feature ... | N-terminal regulatory/sensing modules of transcriptional regulators—most strongly the CheY-like receiver (REC) domains of two-component response regulators and analogous N-terminal ligand/signal-binding or dimerization regions that precede a C-terminal HTH (LuxR-type/NarL-FixJ) DNA-binding domain; the feature favors th... | Primarily domain-level, long contiguous activation across the N-terminus (≈80–150 aa), often starting at the initiator Met and dropping sharply at the boundary with the C-terminal HTH/DNA-binding region; sequence signal often includes early acidic dipeptides (DD) and basic residue enrichment. Secondary, weaker behavior... | Domain | - Two-component response regulators (NarL/FixJ family): activation spans the N-terminal REC receiver domain; the C-terminal HTH_luxR DNA-binding domain is not activated (e.g., biofilm/curli regulator-type proteins like CsgD).
- LuxR-family quorum-sensing regulators: activation on the N-terminal autoinducer (AHL)-bindin... | 6,147,388 | 3.521538 | 14.742188 | [
{
"activation": 14.7421875,
"uniref_id": "A0A510UPW4"
},
{
"activation": 14.6015625,
"uniref_id": "UPI0027DDE07A"
},
{
"activation": 14.453125,
"uniref_id": "UPI0024B63F84"
},
{
"activation": 14.4140625,
"uniref_id": "A0A0A0BZZ0"
},
{
"activation": 14.3125,
"u... | [
{
"activation": 12.295353889465332,
"uniprot_id": "Q7AKE4"
},
{
"activation": 11.527090072631836,
"uniprot_id": "P52106"
},
{
"activation": 11.440817832946777,
"uniprot_id": "P14204"
},
{
"activation": 11.286986351013184,
"uniprot_id": "P39404"
},
{
"activation": ... | [
1733,
2704,
12576,
7376,
13201,
3677,
3271,
202,
5288,
3044
] | 0.265561 |
287 | Summary: Extracytoplasmic ligand/sensor domains, especially the bilobed periplasmic-binding protein (PBP)/“venus flytrap” (VFT) fold, with preference for receptor-associated VFT/PBP modules and selected periplasmic interaction domains. The feature highlights the binding-pocket/hinge and adjacent structural elements use... | Extracytoplasmic ligand/sensor domains, especially the bilobed periplasmic-binding protein (PBP)/“venus flytrap” (VFT) fold, with preference for receptor-associated VFT/PBP modules and selected periplasmic interaction domains. The feature highlights the binding-pocket/hinge and adjacent structural elements used for sma... | Domain-level activation across a long, contiguous stretch of the N-terminal extracellular/periplasmic domain (typically ~80–300 aa), with residue-level peaks on flexible coil/loop and hinge regions (often GP/GG-rich) and neighboring helix/strand that frame the binding site; minimal activation in signal peptides, transm... | Ligand-binding site | - Receptor-type nucleotide cyclases (adenylate/guanylate cyclases): activation on the extracellular ligand-binding/sensor domain (PBP/VFT-like), including sites near glycosylation and mutationally validated activity determinants.
- Class C GPCRs (metabotropic/taste receptors): activation on the N-terminal VFT ligand-bi... | 5,283,125 | 3.673048 | 27.265625 | [
{
"activation": 27.265625,
"uniref_id": "A0A955Y5G1"
},
{
"activation": 27.140625,
"uniref_id": "A0A6J6PUC7"
},
{
"activation": 26.984375,
"uniref_id": "A0A1Q9AN26"
},
{
"activation": 26.875,
"uniref_id": "A0A935FL74"
},
{
"activation": 26.765625,
"uniref_id":... | [
{
"activation": 24.537704467773438,
"uniprot_id": "Q99280"
},
{
"activation": 24.413251876831055,
"uniprot_id": "Q27675"
},
{
"activation": 24.201196670532227,
"uniprot_id": "Q26896"
},
{
"activation": 22.75293731689453,
"uniprot_id": "Q54ET0"
},
{
"activation": 2... | [
15366,
9042,
14587,
11316,
5844,
1642,
8984,
11307,
10947,
1279
] | 0.174392 |
288 | Summary: Feature for extracytoplasmic/surface-facing segments of secreted or surface-associated proteins, emphasizing low-complexity, S/T‑rich, glycosylation-prone loops and short host-targeting/adhesion motifs (e.g., RxLR‑dEER); in non-secretory contexts it preferentially marks analogous flexible linkers or occasional... | Feature for extracytoplasmic/surface-facing segments of secreted or surface-associated proteins, emphasizing low-complexity, S/T‑rich, glycosylation-prone loops and short host-targeting/adhesion motifs (e.g., RxLR‑dEER); in non-secretory contexts it preferentially marks analogous flexible linkers or occasional solvent-... | Primarily regional activation: long, contiguous stretches in ectodomains immediately after signal peptides or within surface/adhesin regions; superimposed residue-level peaks on short targeting/recognition motifs (RxLR‑dEER) and N‑linked glycosylation sequons (N‑X‑S/T). For intracellular or strongly structured proteins... | Post-translational modification | RxLR effectors: activation overlaps the N‑terminal RxLR‑dEER host-targeting region in a low-confidence/disordered segment. Fimbrial tip pilins (Porphyromonas): a continuous band across the mature adhesive domain, with peaks in β‑strands and adjacent coils. Secreted fungal class II heme peroxidases: broad activation acr... | 4,711,615 | 3.787534 | 27.40625 | [
{
"activation": 27.40625,
"uniref_id": "C7R9B1"
},
{
"activation": 27.1875,
"uniref_id": "A0A2K9B193"
},
{
"activation": 26.875,
"uniref_id": "A0A948JIQ2"
},
{
"activation": 26.765625,
"uniref_id": "UPI001C65CEC7"
},
{
"activation": 26.765625,
"uniref_id": "UP... | [
{
"activation": 14.84835433959961,
"uniprot_id": "Q6UDL0"
},
{
"activation": 14.19074535369873,
"uniprot_id": "P0CK95"
},
{
"activation": 5.502745628356934,
"uniprot_id": "P35828"
},
{
"activation": 5.297048568725586,
"uniprot_id": "Q22HI5"
},
{
"activation": 5.08... | [
2589,
6683,
7541,
14564,
12290,
5615,
4197,
4490,
2756,
10160
] | 0.112886 |
289 | Summary: Short membrane-interfacial helix/loop motifs at transmembrane-helix boundaries (helix caps or re-entrant segments) in inner-membrane transporters and related complexes, characterized by hydrophobic, glycine-rich sequences with prominent aromatic anchors (especially tryptophan); commonly at N-terminal TM starts... | Short membrane-interfacial helix/loop motifs at transmembrane-helix boundaries (helix caps or re-entrant segments) in inner-membrane transporters and related complexes, characterized by hydrophobic, glycine-rich sequences with prominent aromatic anchors (especially tryptophan); commonly at N-terminal TM starts or TM–TM... | Regional activation on short (∼8–15 aa) hydrophobic windows immediately adjacent to or within a TM segment, with residue-level peaks on aromatics (W/F/Y) and glycine doublets/triplets; often a coil–helix–coil or short helix flanked by loops; frequently near the N-terminus but also in internal TM domains; minimal activa... | Membrane-associated | - Multidrug ABC transporter permeases (e.g., DrrC): activation on a short coil–helix–coil segment linking two TM helices within the ABC transmembrane type-2 domain.
- ABCG family transporters: activation on an aromatic-rich short helix (WW/WF clusters) within the C-terminal transmembrane domain.
- ATP synthase F0 subun... | 6,485,204 | 3.468042 | 23.59375 | [
{
"activation": 23.59375,
"uniref_id": "UPI00378C5D22"
},
{
"activation": 23.265625,
"uniref_id": "A0A373NEZ8"
},
{
"activation": 23.09375,
"uniref_id": "A0A9E5KMG8"
},
{
"activation": 23.078125,
"uniref_id": "A0A4Q9DND2"
},
{
"activation": 23.015625,
"uniref_... | [
{
"activation": 21.440961837768555,
"uniprot_id": "P68183"
},
{
"activation": 20.913976669311523,
"uniprot_id": "P29824"
},
{
"activation": 20.755048751831055,
"uniprot_id": "D4GP37"
},
{
"activation": 20.5111083984375,
"uniprot_id": "Q55472"
},
{
"activation": 20... | [
1644,
9858,
9693,
2062,
13647,
1628,
15635,
3630,
3986,
871
] | 0.180517 |
290 | Summary: Short basic–hydrophobic amphipathic α-helical segments used for membrane targeting/insertion and secretion signals (e.g., N‑terminal signal peptides, transmembrane helices with flanking Lys‑rich “positive‑inside” motifs, and transit‑peptide‑like stretches), plus transient or surface-exposed amphipathic helices... | Short basic–hydrophobic amphipathic α-helical segments used for membrane targeting/insertion and secretion signals (e.g., N‑terminal signal peptides, transmembrane helices with flanking Lys‑rich “positive‑inside” motifs, and transit‑peptide‑like stretches), plus transient or surface-exposed amphipathic helices embedded... | Regional activation in short (≈10–30 aa) segments, most often at N-termini or within single helices or disordered termini; strong preference for hydrophobic/aromatic residues (F, L, I, V, W) interleaved with Lys and neutral polar residues (N, S, T, Q); acidic residues and His are disfavored. Peaks frequently occur at L... | Membrane-associated | - Signal peptides of secreted protein precursors — activation over the hydrophobic h‑region and adjoining Lys‑rich n‑region.
- Viral single‑pass membrane proteins — activation on the TM helix and immediately cytosolic Lys clusters (positive‑inside motif).
- Mitochondrial/chloroplast targeting peptides — activation on b... | 26,946,909 | 2.043697 | 27.265625 | [
{
"activation": 27.265625,
"uniref_id": "A5KQQ9"
},
{
"activation": 27.203125,
"uniref_id": "UPI00257C0875"
},
{
"activation": 26.875,
"uniref_id": "A0A2P1UCN0"
},
{
"activation": 26.859375,
"uniref_id": "UPI00232DE949"
},
{
"activation": 26.859375,
"uniref_id... | [
{
"activation": 13.674667358398438,
"uniprot_id": "Q96253"
},
{
"activation": 10.009393692016602,
"uniprot_id": "Q9XTR1"
},
{
"activation": 9.981302261352539,
"uniprot_id": "Q2LKX9"
},
{
"activation": 9.728744506835938,
"uniprot_id": "P27265"
},
{
"activation": 9.... | [
3755,
8924,
8570,
1135,
14105,
1083,
14280,
13704,
5323,
5716
] | 0.150205 |
291 | Summary: Hydrophobic, secondary-structure “cap” segments at the distal end of domains—most prominently the C‑terminal portion of PCI helical‑solenoid/winged‑helix scaffolds in large eukaryotic complexes—and analogous short α/β elements near the C‑termini or edges of diverse enzyme folds that form non‑catalytic interact... | Hydrophobic, secondary-structure “cap” segments at the distal end of domains—most prominently the C‑terminal portion of PCI helical‑solenoid/winged‑helix scaffolds in large eukaryotic complexes—and analogous short α/β elements near the C‑termini or edges of diverse enzyme folds that form non‑catalytic interaction/packi... | Regional activation. In PCI-domain subunits, long contiguous stretches (often 80–150 aa) within the mid-to-C‑terminal portion of the PCI solenoid/WH subdomain show strong signal (often lower pLDDT due to flexibility). In enzymes, activation appears as short, localized patches (∼8–30 aa) on single helices, β‑strands, or... | Interaction site | - PCI-domain scaffolds in megadalton assemblies (proteasome lid RPNs, COP9 signalosome, eIF3, TREX‑2/SAC3): activation on the C‑terminal portion of the PCI helical solenoid and its winged‑helix subdomain, consistent with interaction/assembly surfaces.
- Crotonase/enoyl‑CoA hydratase–isomerase family (peroxisomal/mitoch... | 6,079,098 | 3.532709 | 16.3125 | [
{
"activation": 16.3125,
"uniref_id": "A0A379X575"
},
{
"activation": 16.171875,
"uniref_id": "M6GMA9"
},
{
"activation": 15.9921875,
"uniref_id": "A0A8S9NH07"
},
{
"activation": 15.984375,
"uniref_id": "A0AAD4TSI2"
},
{
"activation": 15.84375,
"uniref_id": "A... | [
{
"activation": 14.432299613952637,
"uniprot_id": "A0A384LP51"
},
{
"activation": 14.072768211364746,
"uniprot_id": "A5D7B1"
},
{
"activation": 13.702864646911621,
"uniprot_id": "P32131"
},
{
"activation": 13.567609786987305,
"uniprot_id": "O31067"
},
{
"activatio... | [
14259,
3531,
562,
1634,
5472,
170,
11813,
4205,
13064,
13060
] | 0.279502 |
292 | Summary: An amphipathic, hydrophobic–aromatic interaction surface with interspersed Lys/Arg that forms lipid/phosphate-bearing ligand interfaces or pocket “lids,” and, by extension, analogous hydrophobic/basic patches used for membrane contact or protein assembly across diverse folds (e.g., CRAL‑TRIO, FERM/PH-like, Ros... | An amphipathic, hydrophobic–aromatic interaction surface with interspersed Lys/Arg that forms lipid/phosphate-bearing ligand interfaces or pocket “lids,” and, by extension, analogous hydrophobic/basic patches used for membrane contact or protein assembly across diverse folds (e.g., CRAL‑TRIO, FERM/PH-like, Rossmann-lik... | Regional, domain-internal activation over long contiguous stretches (typically 20–100 residues) spanning mixed secondary structure (α-helices, β-strands, connecting loops). Activation is strongest on well-structured faces that line hydrophobic cavities or assembly interfaces, with occasional sharper peaks on flexible g... | Ligand-binding site | - SEC14/CRAL-TRIO lipid transfer proteins: activation across the CRAL‑TRIO pocket/portal including the flexible “lid” that gates lipid exchange, highlighting the hydrophobic cavity-lining face.
- FERM/4.1 membrane–cytoskeleton linkers: activation on the C‑terminal FERM lobe (PH‑like) corresponding to the lipid (e.g., P... | 4,915,111 | 3.745251 | 16.375 | [
{
"activation": 16.375,
"uniref_id": "UPI0011B217B7"
},
{
"activation": 16.28125,
"uniref_id": "A0A8S5UTP2"
},
{
"activation": 16.21875,
"uniref_id": "A0A950SNM5"
},
{
"activation": 16.1875,
"uniref_id": "A0A7S5YBX0"
},
{
"activation": 16.078125,
"uniref_id": ... | [
{
"activation": 13.49096965789795,
"uniprot_id": "P03735"
},
{
"activation": 9.632661819458008,
"uniprot_id": "P68716"
},
{
"activation": 8.585267066955566,
"uniprot_id": "P24280"
},
{
"activation": 8.401148796081543,
"uniprot_id": "A6ZQI5"
},
{
"activation": 8.39... | [
4048,
9104,
4959,
16068,
8907,
8242,
11766,
299,
558,
13475
] | 0.268104 |
293 | Summary: Intrinsically disordered, low‑complexity segments used for protein–protein interactions, with a strong compositional bias (polar/charged, Pro/Gly) and particular sensitivity to phenylalanine‑containing short repeats (e.g., FG/FSFG) in large eukaryotic regulatory/scaffold proteins; avoids structured catalytic o... | Intrinsically disordered, low‑complexity segments used for protein–protein interactions, with a strong compositional bias (polar/charged, Pro/Gly) and particular sensitivity to phenylalanine‑containing short repeats (e.g., FG/FSFG) in large eukaryotic regulatory/scaffold proteins; avoids structured catalytic or coiled‑... | Residue-level peaks clustered within long IDRs: multiple short peaks across the sequence, often within regions annotated as Disordered/Low complexity and with low pLDDT; highest responses on FG/FSFG/FxFG motifs and on polar/Pro/Gly‑rich tracts (occasionally hydrophobic residues when embedded in low‑confidence helices);... | Disorder | - Nucleoporins (FG-repeat channel proteins): activates on disordered FG/FSFG/FxFG repeat regions that form the permeability barrier.
- SET-domain histone methyltransferases: activates on long disordered linkers outside the folded RRM/SET/Post‑SET domains.
- Spindle assembly regulators: activates on low‑confidence helic... | 140,571,580 | 0.391848 | 23.359375 | [
{
"activation": 23.359375,
"uniref_id": "A0A1Y2CWE1"
},
{
"activation": 22.59375,
"uniref_id": "A0A2T9Z490"
},
{
"activation": 22.5,
"uniref_id": "A0A139HNR9"
},
{
"activation": 22.40625,
"uniref_id": "A0A0V0Y2V1"
},
{
"activation": 22.390625,
"uniref_id": "A0... | [
{
"activation": 18.15363121032715,
"uniprot_id": "Q9VIF5"
},
{
"activation": 17.738309860229492,
"uniprot_id": "P40457"
},
{
"activation": 17.426156997680664,
"uniprot_id": "P40021"
},
{
"activation": 17.35735511779785,
"uniprot_id": "Q8NEV8"
},
{
"activation": 17... | [
15240,
8291,
3418,
5905,
3519,
1072,
5315,
11450,
2081,
12463
] | 0.060256 |
294 | Summary: Conserved hydrophobic residue (Leu/Val/Ile/Phe/Met/Ala) at the start of a short beta-strand or immediately preceding loop in small, soluble beta-containing domains—a beta-strand initiation/edge anchor recurring at orthologous positions. Not expected in predominantly helical/coiled-coil proteins, membrane trans... | Conserved hydrophobic residue (Leu/Val/Ile/Phe/Met/Ala) at the start of a short beta-strand or immediately preceding loop in small, soluble beta-containing domains—a beta-strand initiation/edge anchor recurring at orthologous positions. Not expected in predominantly helical/coiled-coil proteins, membrane transporters, ... | Predominantly residue-level peaks (1–3 per protein) on a single hydrophobe at the first position of a short beta-strand or just N-terminal to it. Activation requires a predicted beta-strand with reasonable confidence (e.g., pLDDT ≥70); it is absent when the local region is disordered or helical. The motif is sparse and... | Structural motif | - Histone H1 (globular H15 domain): many somatic H1 isoforms show a single Leu within a short beta-strand around positions ~90–110; oocyte-specific variants (e.g., H1B4/H1M) may lack this site.
- Gas vesicle transcriptional activator GvpE: hydrophobe marking the start of a beta-strand adjacent to the DNA-binding region... | 74,696,050 | 1.024138 | 18.8125 | [
{
"activation": 18.8125,
"uniref_id": "UPI00352042B5"
},
{
"activation": 18.75,
"uniref_id": "X6KGL9"
},
{
"activation": 18.6875,
"uniref_id": "UPI00333AD5D8"
},
{
"activation": 18.65625,
"uniref_id": "UPI00399C0228"
},
{
"activation": 18.59375,
"uniref_id": "... | [
{
"activation": 17.39885711669922,
"uniprot_id": "P74103"
},
{
"activation": 15.408947944641113,
"uniprot_id": "P33754"
},
{
"activation": 15.378223419189453,
"uniprot_id": "Q99816"
},
{
"activation": 15.349770545959473,
"uniprot_id": "P40193"
},
{
"activation": 1... | [
7777,
3750,
2586,
15312,
14111,
10981,
2377,
12763,
2214,
11850
] | 0.349181 |
295 | Summary: Alpha-helical transmembrane segments of polytopic integral membrane proteins, especially the permease/helical cores of transporters and channels
Activation pattern: Residue-level peaks concentrated within UniProt/predicted transmembrane alpha-helices, often with multiple peaks across several helices; minimal t... | Alpha-helical transmembrane segments of polytopic integral membrane proteins, especially the permease/helical cores of transporters and channels | Residue-level peaks concentrated within UniProt/predicted transmembrane alpha-helices, often with multiple peaks across several helices; minimal to no activation in soluble/cytosolic domains or disordered tails; occasional peaks at helix termini or immediately adjacent helical segments; consistently in high-confidence ... | Membrane-associated | - Na+/H+ exchanger (SLC9/NHE): peaks on multiple transmembrane helices; no activation on disordered N- or C-terminal cytosolic regions.
- K+/H+ antiporter (CemA/CPA-family): discrete residues within or at the ends of annotated transmembrane helices, including the C‑terminal TM.
- P-type heavy-metal ATPase (Cd/Zn-transp... | 59,376,953 | 1.253659 | 13.132813 | [
{
"activation": 13.1328125,
"uniref_id": "UPI00307EAF8A"
},
{
"activation": 13.1171875,
"uniref_id": "A0A3P3QQ80"
},
{
"activation": 13.0703125,
"uniref_id": "UPI0003F9AD61"
},
{
"activation": 13.0625,
"uniref_id": "A0A8J7FMJ0"
},
{
"activation": 13.03125,
"un... | [
{
"activation": 11.257569313049316,
"uniprot_id": "Q8Y5E4"
},
{
"activation": 10.89908218383789,
"uniprot_id": "Q59998"
},
{
"activation": 10.83758544921875,
"uniprot_id": "P56783"
},
{
"activation": 10.836812019348145,
"uniprot_id": "Q1KVU2"
},
{
"activation": 10... | [
14918,
16154,
13307,
16192,
10348,
9830,
14706,
1533,
12611,
11737
] | 0.387985 |
296 | Summary: Surface-exposed patches in mature extracellular/periplasmic domains of secreted proteins—typically loops and helix/strand edges that form or flank ligand/substrate-binding surfaces or extracellular interaction sites, rather than cytosolic segments or transmembrane helices. This captures a broad secretome signa... | Surface-exposed patches in mature extracellular/periplasmic domains of secreted proteins—typically loops and helix/strand edges that form or flank ligand/substrate-binding surfaces or extracellular interaction sites, rather than cytosolic segments or transmembrane helices. This captures a broad secretome signal across ... | Regional activation: contiguous clusters within extracytoplasmic domains, enriched in loop and secondary-structure transition regions and in polar/charged/small residues; minimal to none in cytosolic tails and transmembrane helices; often adjacent to or partially overlapping annotated binding or catalytic sites but not... | Interaction site | - Penicillin-binding proteins (periplasmic transglycosylase/transpeptidase domains): activation exclusively in the extracytoplasmic domains, highlighting multiple loop patches near but not at catalytic residues; no activation in the cytosolic N-terminus or the transmembrane helix.
- Intrinsic factor (cobalamin-binding ... | 36,471,273 | 1.74104 | 12.867188 | [
{
"activation": 12.8671875,
"uniref_id": "UPI00077321E5"
},
{
"activation": 12.84375,
"uniref_id": "A0A9E4J8G8"
},
{
"activation": 12.7734375,
"uniref_id": "UPI0036BFF721"
},
{
"activation": 12.7109375,
"uniref_id": "A0A935N3W5"
},
{
"activation": 12.6640625,
... | [
{
"activation": 10.113901138305664,
"uniprot_id": "I7M6D6"
},
{
"activation": 9.913625717163086,
"uniprot_id": "P47032"
},
{
"activation": 9.731535911560059,
"uniprot_id": "P47033"
},
{
"activation": 9.64976978302002,
"uniprot_id": "F7C0L1"
},
{
"activation": 9.64... | [
5128,
2678,
5763,
2798,
2232,
9733,
14898,
134,
14946,
10717
] | 0.421378 |
297 | Summary: C-terminal segment of classical bacterial N-terminal signal peptides—the h-region terminus and adjacent small-residue–rich c-region just upstream of the signal peptidase cleavage site—characteristic of secreted/periplasmic proteins across diverse taxa.
Activation pattern: Regional activation: a single short wi... | C-terminal segment of classical bacterial N-terminal signal peptides—the h-region terminus and adjacent small-residue–rich c-region just upstream of the signal peptidase cleavage site—characteristic of secreted/periplasmic proteins across diverse taxa. | Regional activation: a single short window (~8–15 residues) near positions ~15–30 from the start methionine, usually at the helix-to-coil transition at the end of the signal peptide and extending into the flexible c-region; enriched for hydrophobic (A/L/V/I/F/M) and small polar (S/T/G) residues with few charges; prolin... | Post-translational modification | - Secreted alpha-amylases (GH13): activation on the C-terminal half of the N-terminal signal peptide.
- Endo-β-N-acetylglucosaminidases (glycosidases): activation within the signal peptide segment preceding the mature domain.
- Pectate lyases (polysaccharide lyases): activation confined to the signal peptide region.
- ... | 29,528,451 | 1.952211 | 21.859375 | [
{
"activation": 21.859375,
"uniref_id": "A0AAU3KT91"
},
{
"activation": 21.640625,
"uniref_id": "UPI0014883A9E"
},
{
"activation": 21.453125,
"uniref_id": "UPI003264158B"
},
{
"activation": 21.4375,
"uniref_id": "X5MC72"
},
{
"activation": 21.4375,
"uniref_id"... | [
{
"activation": 17.843402862548828,
"uniprot_id": "P01077"
},
{
"activation": 17.677265167236328,
"uniprot_id": "Q9X6Z2"
},
{
"activation": 17.5003604888916,
"uniprot_id": "P71014"
},
{
"activation": 17.244800567626953,
"uniprot_id": "Q0Z8B6"
},
{
"activation": 16... | [
4232,
7067,
5035,
15681,
15282,
14034,
3566,
15208,
11957,
12236
] | 0.556304 |
298 | Summary: Phosphate-rich cofactor/ligand–interacting catalytic cores and adjacent structured α/β frameworks: the feature highlights proteins that bind or process ATP/ADP/AMP/ADP‑ribose and related phosphate-bearing moieties (pyrophosphate; CoA adenylate), including adenylate‑forming ligases, cyclase/polymerase‑like enzy... | Phosphate-rich cofactor/ligand–interacting catalytic cores and adjacent structured α/β frameworks: the feature highlights proteins that bind or process ATP/ADP/AMP/ADP‑ribose and related phosphate-bearing moieties (pyrophosphate; CoA adenylate), including adenylate‑forming ligases, cyclase/polymerase‑like enzymes, ADP‑... | Predominantly domain-/regional-level activation spanning long, well-structured segments (helices and β-strands) with local peaks at phosphate/adenylate-contact residues (glycine-rich loops; Asp/Lys/His/Ser/Thr). Occasional sharp, residue-level spikes occur on key ATP-/phosphate-binding/catalytic residues. Activation of... | Ligand-binding site | - ADP-ribosylhydrolase (DRAG): strong activation across the ADP-ribose–binding core.
- RNA 3′-phosphate cyclase-like protein (RCL1): broad activation over the catalytic C-terminal core with peaks in β-loop regions.
- Urease accessory protein F (UreF): activation over the helical interface that couples to the phosphate-... | 8,334,339 | 3.217181 | 18.046875 | [
{
"activation": 18.046875,
"uniref_id": "UPI00258938A7"
},
{
"activation": 17.921875,
"uniref_id": "A0A256XX24"
},
{
"activation": 17.734375,
"uniref_id": "A0A8T5MIJ9"
},
{
"activation": 17.71875,
"uniref_id": "A0A256YVZ9"
},
{
"activation": 17.71875,
"uniref_... | [
{
"activation": 15.139704704284668,
"uniprot_id": "P77231"
},
{
"activation": 14.981828689575195,
"uniprot_id": "O53080"
},
{
"activation": 13.088692665100098,
"uniprot_id": "P54922"
},
{
"activation": 12.998207092285156,
"uniprot_id": "Q9NX46"
},
{
"activation": ... | [
11748,
4736,
7275,
6923,
8836,
12053,
1772,
4004,
13136,
13678
] | 0.24912 |
299 | Summary: Surface-exposed helix–loop “recognition/capping” segments that flank conserved functional motifs and form interaction surfaces (DNA-recognition helices in HTH regulators, and substrate/metal/cofactor-proximal lids or adjacent helices in enzymes), typically enriched in Gly/GxG, Pro turns, and aromatic residues.... | Surface-exposed helix–loop “recognition/capping” segments that flank conserved functional motifs and form interaction surfaces (DNA-recognition helices in HTH regulators, and substrate/metal/cofactor-proximal lids or adjacent helices in enzymes), typically enriched in Gly/GxG, Pro turns, and aromatic residues. | Regional activation on contiguous segments (often 40–120 aa, sometimes a single short helix) that span a loop-to-helix transition and adjacent helix; peaks frequently lie just before or after canonical motif residues (e.g., HTH consensus, DDxxD/E, histidine boxes, catalytic Asp, nucleotide-binding sites). Occasional di... | Interaction site | - WYL-domain transcriptional regulators (e.g., PafB/PafBC): strong activation on the flexible interdomain region linking the N-terminal HTH to the C-terminal WYL domain, a putative regulatory/interaction segment.
- TrmB-family HTH regulators (sugar-sensing): activation over the N‑terminal HTH DNA-binding region, includ... | 9,717,694 | 3.063617 | 21.59375 | [
{
"activation": 21.59375,
"uniref_id": "UPI00249C594B"
},
{
"activation": 21.484375,
"uniref_id": "UPI00156E5B7F"
},
{
"activation": 21.15625,
"uniref_id": "A0A2N3YFT9"
},
{
"activation": 21,
"uniref_id": "A0A970CTC3"
},
{
"activation": 20.984375,
"uniref_id":... | [
{
"activation": 17.309423446655273,
"uniprot_id": "P9WIL9"
},
{
"activation": 17.096874237060547,
"uniprot_id": "P9WIM1"
},
{
"activation": 16.275766372680664,
"uniprot_id": "A0QS56"
},
{
"activation": 14.861090660095215,
"uniprot_id": "P0DX74"
},
{
"activation": ... | [
558,
13475,
16068,
8242,
7461,
9104,
8907,
4048,
292,
12875
] | 0.205227 |
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