interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR008280
8,280
Tubulin/FtsZ, C-terminal
Tub_FtsZ_C
Homologous_superfamily
101,891
false
false
This domain superfamily is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is pa...
[]
[]
[]
0
[ "SSF" ]
[ "SSF55307" ]
[ "" ]
[ 101891 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-114608", "R-BTA-190840", "R-BTA-2132295", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-2565942", "R-BTA-3371497", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-5610787", "R-BTA-5617833", "R-BTA-5620912", "R-BTA-5620924", "R-BTA-5626467", "R-BTA-5663220", ...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-190840", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371497", "REACTOME:R-BTA-380259", "REACTOME:R-BTA-380270", "REACTOME:R-BTA-380284", "REACTOME:R-BTA-380320", "REACTOME:R-BT...
233
[ "1ffx", "1fsz", "1ia0", "1jff", "1ofu", "1rlu", "1rq2", "1rq7", "1sa0", "1sa1", "1tub", "1tvk", "1w58", "1w59", "1w5a", "1w5b", "1w5e", "1w5f", "1z2b", "1z5v", "1z5w", "2bto", "2btq", "2hxf", "2hxh", "2p4n", "2q1x", "2q1y", "2r6r", "2r75", "2rhh", "2rhj"...
877
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 1501, 28555, 71153, 1, 681 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 60, 20, 36, 30, 1, 100, 43, 4, 44, 74, 4, 4, 185 ]
13
true
Homologous_superfamily
Tubulin/FtsZ, C-terminal
Tubulin/FtsZ, C-terminal
Tub_FtsZ_C
7
IPR008283
8,283
Peptidase M17, leucyl aminopeptidase, N-terminal
Peptidase_M17_N
Domain
23,314
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M17 (leucyl aminopeptidase family, clan MF), the type example being leucyl aminopeptidase from Bos taurus (Bovine). Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be c...
[ "GO:0070006", "GO:0006508" ]
[ "metalloaminopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02789" ]
[ "Peptidase_M17_N" ]
[ 23314 ]
1
[ "EC", "EC", "GP" ]
[ "3.4.11.1", "3.4.11.10", "GenProp1664" ]
[ "EC:3.4.11.1", "EC:3.4.11.10", "GP:GenProp1664" ]
3
[ "1bll", "1bpm", "1bpn", "1gyt", "1lam", "1lan", "1lap", "1lcp", "2ewb", "2j9a", "3h8e", "3h8f", "3h8g", "3jru", "3kzw", "3pei", "4ksi", "4zi6", "4zla", "5d8n", "5lhj", "5lhk", "6ome", "7y1s", "8d1x", "8pz0", "8pzm", "8pzy" ]
28
[ "PUB00001416", "PUB00003579", "PUB00004713" ]
[ "1555602", "7674922", "2395881" ]
[ "Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.", "Evolutionary families of metallopeptidases.", "Molecular structure of leucine aminopeptidase at 2.7-A resolution." ]
[ 1992, 1995, 1990 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 75, 18640, 4076, 523 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 14, 1, 9, 1, 2, 1, 3, 4, 1, 13 ]
10
true
Domain
Peptidase M17, leucyl aminopeptidase, N-terminal
Peptidase M17, leucyl aminopeptidase, N-terminal
Peptidase_M17_N
8
IPR008286
8,286
Orn/Lys/Arg decarboxylase, C-terminal
Prn/Lys/Arg_de-COase_C
Domain
19,996
false
false
Pyridoxal-dependent decarboxylases are bacterial proteins acting on ornithine, lysine, arginine and related substrates [ ]. One of the regions of sequence similarity contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group. Ornithine decarboxylase is a dodecamer composed of ...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03711" ]
[ "OKR_DC_1_C" ]
[ 19996 ]
1
[ "EC", "GP", "GP", "GP" ]
[ "4.1.1", "GenProp1279", "GenProp1433", "GenProp1596" ]
[ "EC:4.1.1", "GP:GenProp1279", "GP:GenProp1433", "GP:GenProp1596" ]
4
[ "1c4k", "1ord", "2vyc", "2x3l", "3n75", "3q16", "4upb", "4upf", "5fkx", "5fkz", "5fl2", "5xx1", "6q6i", "6q7l", "6q7m", "6y3x", "6yn5", "6yn6", "7p9b", "7pk6", "9e0m", "9e0o", "9e0q" ]
23
[ "PUB00001452", "PUB00006301", "PUB00006322", "PUB00006531", "PUB00014378", "PUB00014382", "PUB00014393", "PUB00016775", "PUB00016898", "PUB00035507", "PUB00070977", "PUB00079513", "PUB00079514", "PUB00079515" ]
[ "8181483", "8112347", "7748903", "10800595", "7663340", "9405048", "9063963", "10223296", "9914259", "17109392", "10673430", "10586514", "17504214", "11933250" ]
[ "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.", "Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.", "Pyridoxal phosphate-dependent enzymes.", "The molecular evolution of pyridoxal-5'-phospha...
[ 1994, 1994, 1995, 2000, 1995, 1997, 1996, 1999, 1998, 2006, 2000, 1999, 2007, 2001 ]
14
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 48, 18905, 848, 195 ]
4
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 5, 6 ]
3
true
Domain
Orn/Lys/Arg decarboxylase, C-terminal
Orn/Lys/Arg decarboxylase, C-terminal
Prn/Lys/Arg_de-COase_C
7
IPR008288
8,288
Poly [ADP-ribose] polymerase
PARP
Family
1,683
false
false
Poly(ADP-ribose) synthase and poly(ADP-ribose) polymerase (PARP, also known as ADPRT) catalyse the DNA-dependent covalent attachment of ADP-ribose to various nuclear proteins [ ]. They are used by the eukaryotic cell to cope with numerous environmental and endogenous genotoxic agents that cause DNA strand breaks. PARP ...
[ "GO:0003677", "GO:0003950", "GO:0008270", "GO:0051287", "GO:0005634" ]
[ "DNA binding", "NAD+ poly-ADP-ribosyltransferase activity", "zinc ion binding", "NAD binding", "nucleus" ]
[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "cellular_component" ]
5
[ "PIRSF" ]
[ "PIRSF000489" ]
[ "NAD_ADPRT" ]
[ 1683 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "2.4.2.-", "2.4.2.30", "PWY-5381", "PWY-5800", "PWY-6148", "PWY-6720", "PWY-7018", "PWY-7025", "PWY-7450", "PWY-7817", "PWY-7981", "R-CEL-5696394", "R-CEL-5696395", "R-CEL-5696400", "R-DME-110362", "R-DME-2173795", "R-DME-3108214", "R-DME-5685939", "R-DME-5696394", "R-DME-56963...
[ "EC:2.4.2.-", "EC:2.4.2.30", "METACYC:PWY-5381", "METACYC:PWY-5800", "METACYC:PWY-6148", "METACYC:PWY-6720", "METACYC:PWY-7018", "METACYC:PWY-7025", "METACYC:PWY-7450", "METACYC:PWY-7817", "METACYC:PWY-7981", "REACTOME:R-CEL-5696394", "REACTOME:R-CEL-5696395", "REACTOME:R-CEL-5696400", "...
48
[]
0
[ "PUB00001533", "PUB00003624", "PUB00011133", "PUB00011134" ]
[ "9034168", "3118181", "11781113", "6088227" ]
[ "A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.", "ADP-ribosylation of proteins. Enzymology and biological significance.", "Poly(ADP-ribose) polymerase: a guardian angel protecting the genome and suppressing tumorigenesis.", "Poly(ADP-ribose) polymerase is a zinc m...
[ 1997, 1987, 2001, 1984 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1683 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 5, 1, 2, 1, 4, 8, 1, 2, 2 ]
9
true
Family
Poly [ADP-ribose] polymerase
Poly [ADP-ribose] polymerase
PARP
7
IPR008289
8,289
Pentafunctional AroM protein
Pentafunct_AroM
Family
1,716
false
false
Each member of this group contains five functional domains catalysing five sequential steps of the shikimate pathway. Each domain corresponds to a monofunctional prokaryotic enzyme of the same pathway: 3-dehydroquinate synthase, 3-dehydroquinate dehydratase, shikimate 5-dehydrogenase, shikimate kinase, and 3-phosphoshi...
[ "GO:0003855", "GO:0003856", "GO:0003866", "GO:0004764", "GO:0004765", "GO:0009073" ]
[ "3-dehydroquinate dehydratase activity", "3-dehydroquinate synthase activity", "3-phosphoshikimate 1-carboxyvinyltransferase activity", "shikimate 3-dehydrogenase (NADP+) activity", "shikimate kinase activity", "aromatic amino acid family biosynthetic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
6
[ "HAMAP", "PIRSF" ]
[ "MF_03143", "PIRSF000514" ]
[ "Pentafunct_AroM", "Pentafunct_AroM" ]
[ 1651, 1634 ]
2
[ "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "1.1.1.25", "2.5.1.19", "2.7.1.71", "4.2.1.10", "4.2.3.4", "PWY-6163", "PWY-6164", "PWY-6416", "PWY-6707" ]
[ "EC:1.1.1.25", "EC:2.5.1.19", "EC:2.7.1.71", "EC:4.2.1.10", "EC:4.2.3.4", "METACYC:PWY-6163", "METACYC:PWY-6164", "METACYC:PWY-6416", "METACYC:PWY-6707" ]
9
[ "6hqv", "7u5s", "7u5t", "7u5u" ]
4
[ "PUB00011136" ]
[ "2848727" ]
[ "The Saccharomyces cerevisiae ARO1 gene. An example of the co-ordinate regulation of five enzymes on a single biosynthetic pathway." ]
[ 1988 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1716 ]
1
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1 ]
3
true
Family
Pentafunctional AroM protein
Pentafunctional AroM protein
Pentafunct_AroM
8
IPR008290
8,290
Phosphatidylinositol 3-kinase, Vps34 type
PI3K_Vps34
Family
4,699
false
false
Members of this family are Class III phosphatidylinositol 3-kinases (PI3Ks) (catalytic subunits). PI3K is a lipid kinase and a key signaling enzyme involved in cell survival and proliferation, cell motility and adhesion, cytoskeletal rearrangement and vesicle trafficking [ ]. The different PI3K isoforms have cell-speci...
[ "GO:0016303", "GO:0046854" ]
[ "1-phosphatidylinositol-3-kinase activity", "phosphatidylinositol phosphate biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF" ]
[ "PIRSF000587" ]
[ "PI3K_Vps34" ]
[ 4699 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "2.7.1.137", "PWY-6352", "R-CEL-1632852", "R-CEL-1660514", "R-CEL-1660516", "R-CEL-1660517", "R-CEL-5668599", "R-DDI-1632852", "R-DDI-1660514", "R-DDI-1660516", "R-DDI-1660517", "R-DDI-5668599", "R-HSA-109704", "R-HSA-1632852", "R-HSA-1660514", "R-HSA-1660516", "R-HSA-1660517", "R-...
[ "EC:2.7.1.137", "METACYC:PWY-6352", "REACTOME:R-CEL-1632852", "REACTOME:R-CEL-1660514", "REACTOME:R-CEL-1660516", "REACTOME:R-CEL-1660517", "REACTOME:R-CEL-5668599", "REACTOME:R-DDI-1632852", "REACTOME:R-DDI-1660514", "REACTOME:R-DDI-1660516", "REACTOME:R-DDI-1660517", "REACTOME:R-DDI-5668599"...
47
[ "2x6f", "2x6h", "2x6i", "2x6j", "2x6k", "3ls8", "4ph4", "5dfz", "5enn", "5kc2", "6i3u", "6ykg", "7bl1", "8sor", "9c82", "9mhf", "9mhg", "9mhh" ]
18
[ "PUB00001709", "PUB00005166", "PUB00007087", "PUB00011140", "PUB00011141", "PUB00011142" ]
[ "9247130", "8385367", "12151228", "10579926", "7628435", "8719881" ]
[ "Using structure to define the function of phosphoinositide 3-kinase family members.", "Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting.", "Structural insight into substrate specificity and regulatory mechanisms of phosphoinositide 3-kinases.", "Signaling by distinct cl...
[ 1997, 1993, 2002, 1999, 1995, 1995 ]
6
[ "IPR015433" ]
[]
1
0
1
[ "Eukaryota" ]
[ 4699 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 2, 2, 6, 3, 1, 5, 5, 1, 1, 7 ]
12
true
Family
Phosphatidylinositol 3-kinase, Vps34 type
Phosphatidylinositol 3-kinase, Vps34 type
PI3K_Vps34
2
IPR008291
8,291
Glucoamylase, starch-binding
Glucoamylase_SBD
Family
1,613
false
false
Glucoamylase (GA), also known as glucan 1,4-alpha-glucosidase, which belongs to family 15 ( ) in the classification of glycosyl hydrolases. GA catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or poly-saccharides. Studies of fungal GA have indicated 3 closely-clustered acidic resi...
[ "GO:0004339", "GO:2001070", "GO:0000272" ]
[ "glucan 1,4-alpha-glucosidase activity", "starch binding", "polysaccharide catabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PIRSF" ]
[ "PIRSF001031" ]
[ "Glu-a-glcsd_SBD" ]
[ 1613 ]
1
[ "EC", "METACYC" ]
[ "3.2.1.3", "PWY-5941" ]
[ "EC:3.2.1.3", "METACYC:PWY-5941" ]
2
[ "2vn4", "2vn7", "6fhv", "6fhw", "6frv" ]
5
[ "PUB00001422", "PUB00004952" ]
[ "1633799", "1970434" ]
[ "Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.", "Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori." ]
[ 1992, 1990 ]
2
[ "IPR000165" ]
[]
1
0
1
[ "Fungi" ]
[ 1613 ]
1
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Glucoamylase, starch-binding
Glucoamylase, starch-binding
Glucoamylase_SBD
8
IPR008292
8,292
Haptoglobin
Haptoglobin
Family
326
false
false
Haptoglobin is a plasma protein that binds haemoglobin. The resulting complex is too large to be excreted by the kidney, thereby preventing loss of iron and damage to the kidney. The haptoglobin-haemoglobin complex is degraded in the liver, which is also the site of haptoglobin synthesis. The mature haptoglobin molecul...
[ "GO:0030492", "GO:0005576" ]
[ "hemoglobin binding", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PIRSF" ]
[ "PIRSF001137" ]
[ "Haptoglobin" ]
[ 326 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2168880", "R-MMU-2168880", "R-MMU-6798695", "R-RNO-2168880", "R-RNO-6798695", "R-SSC-2168880", "R-SSC-6798695" ]
[ "REACTOME:R-HSA-2168880", "REACTOME:R-MMU-2168880", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-2168880", "REACTOME:R-RNO-6798695", "REACTOME:R-SSC-2168880", "REACTOME:R-SSC-6798695" ]
7
[ "4f4o", "4wjg", "8xmp", "8xmq", "8xmw", "9fmu", "9hej", "9hek", "9nb6" ]
9
[ "PUB00011145", "PUB00011146", "PUB00011147", "PUB00089999" ]
[ "3170608", "2987228", "8001969", "21248165" ]
[ "Complex events in the evolution of the haptoglobin gene cluster in primates.", "Nucleotide sequence of the haptoglobin and haptoglobin-related gene pair. The haptoglobin-related gene contains a retrovirus-like element.", "Parallel evolutionary events in the haptoglobin gene clusters of rhesus monkey and human....
[ 1988, 1985, 1994, 2011 ]
4
[ "IPR001314" ]
[]
1
0
1
[ "Bilateria" ]
[ 326 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 6 ]
3
true
Family
Haptoglobin
Haptoglobin
Haptoglobin
8
IPR008294
8,294
Meprin alpha/beta subunit
Meprin
Family
1,426
false
false
Meprins are metazoan zinc metallopeptidases belonging to MEROPS peptidase family M12 (clan MA(M)), subfamily M12A (astacin family). They are complex and structurally unique homo- or heterotetrameric glycoproteins composed of evolutionarily related alpha and/or beta subunits that contain disulphide-bridged dimers. The t...
[ "GO:0004222", "GO:0008270", "GO:0006508", "GO:0016020" ]
[ "metalloendopeptidase activity", "zinc ion binding", "proteolysis", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PIRSF" ]
[ "PIRSF001196" ]
[ "Meprin" ]
[ 1426 ]
1
[ "EC" ]
[ "3.4.24" ]
[ "EC:3.4.24" ]
1
[]
0
[ "PUB00005025", "PUB00005405", "PUB00006426", "PUB00071087", "PUB00071089" ]
[ "7670368", "8387703", "9857066", "23427141", "21693781" ]
[ "The astacin family of metalloendopeptidases.", "An adhesive domain detected in functionally diverse receptors.", "Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase.", "Meprin A metalloproteinase and its role in acute kidney injury.", "Proteomic an...
[ 1995, 1993, 1998, 2013, 2011 ]
5
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1426 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 4, 3, 6 ]
4
true
Family
Meprin alpha/beta subunit
Meprin alpha/beta subunit
Meprin
2
IPR008296
8,296
Tissue factor pathway inhibitor-like
TFPI-like
Family
1,581
false
false
Tissue factor pathway inhibitor (TFPI or TFPI1), also called lipoprotein-associated coagulation inhibitor (LACI) or extrinsic pathway inhibitor, is an anti-coagulation plasma protein that acts as a Kunitz-type serine protease inhibitor. Though TFPI lacks a membrane attachment signal, it remains associated with the endo...
[ "GO:0030414", "GO:0010466", "GO:0005576" ]
[ "peptidase inhibitor activity", "negative regulation of peptidase activity", "extracellular region" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PIRSF" ]
[ "PIRSF001620" ]
[ "TFPI" ]
[ 1581 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-140834", "R-HSA-9925563", "R-MMU-140834", "R-RNO-140834" ]
[ "REACTOME:R-HSA-140834", "REACTOME:R-HSA-9925563", "REACTOME:R-MMU-140834", "REACTOME:R-RNO-140834" ]
4
[ "4bd9", "7v1n" ]
2
[ "PUB00033197", "PUB00033202", "PUB00033203", "PUB00086369" ]
[ "16261634", "16689766", "16411383", "23746805" ]
[ "Tissue factor pathway inhibitor: structure, biology and involvement in disease.", "A GPI-anchored co-receptor for tissue factor pathway inhibitor controls its intracellular trafficking and cell surface expression.", "Structure, function and biology of tissue factor pathway inhibitor-2.", "A noncanonical mech...
[ 2006, 2006, 2005, 2013 ]
4
[]
[]
0
0
null
[ "Bilateria" ]
[ 1581 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 9, 8, 7 ]
4
true
Family
Tissue factor pathway inhibitor-like
Tissue factor pathway inhibitor-like
TFPI-like
6
IPR008297
8,297
Notch
Notch
Family
4,477
false
false
Notch cell surface receptors are large, single-pass type-1 transmembrane proteins found in a diverse range of metazoan species, from human to Caenorhabditis species. The fruit fly, Drosophila melanogaster, possesses only one Notch protein, whereas in C.elegans, two receptors have been found; by contrast, four Notch par...
[ "GO:0007219", "GO:0030154", "GO:0050793", "GO:0016020" ]
[ "Notch signaling pathway", "cell differentiation", "regulation of developmental process", "membrane" ]
[ "biological_process", "biological_process", "biological_process", "cellular_component" ]
4
[ "PIRSF" ]
[ "PIRSF002279" ]
[ "Notch" ]
[ 4477 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-HSA-1912399", "R-HSA-1912408", "R-HSA-1912420", "R-HSA-210744", "R-HSA-2122947", "R-HSA-2122948", "R-HSA-2197563", "R-HSA-2644606", "R-HSA-2644607", "R-HSA-2660826", "R-HSA-2691232", "R-HSA-2894862", "R-HSA-2979096", "R-HSA-350054", "R-HSA-5083630", "R-HSA-8941856", "R-HSA-9013507...
[ "REACTOME:R-HSA-1912399", "REACTOME:R-HSA-1912408", "REACTOME:R-HSA-1912420", "REACTOME:R-HSA-210744", "REACTOME:R-HSA-2122947", "REACTOME:R-HSA-2122948", "REACTOME:R-HSA-2197563", "REACTOME:R-HSA-2644606", "REACTOME:R-HSA-2644607", "REACTOME:R-HSA-2660826", "REACTOME:R-HSA-2691232", "REACTOME...
45
[]
0
[ "PUB00013432", "PUB00053622", "PUB00053623", "PUB00053624", "PUB00053625", "PUB00053626", "PUB00053638" ]
[ "10221902", "19379690", "12354787", "11101851", "12668592", "16429119", "10206645" ]
[ "Notch signaling: cell fate control and signal integration in development.", "The canonical Notch signaling pathway: unfolding the activation mechanism.", "The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts.", "MAML1, a human homologue...
[ 1999, 2009, 2002, 2000, 2003, 2006, 1999 ]
7
[]
[ "IPR022331", "IPR022336", "IPR022355", "IPR022362" ]
0
4
0
[ "Eumetazoa" ]
[ 4477 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 2, 32, 5, 17 ]
5
true
Family
Notch
Notch
Notch
6
IPR008299
8,299
Prephenate dehydrogenase/arogenate dehydrogenase
Prep_DH/arog_DH
Family
160
false
false
Members of this group catalyse a step in tyrosine biosynthesis in the shikimate pathway, which is present only in bacteria, fungi, and plants. They contain both a prephenate dehydrogenase domain (PDH) and a regulatory domain.
[]
[]
[]
0
[ "NCBIFAM", "PIRSF" ]
[ "NF006408", "PIRSF006549" ]
[ "PRK08655.1-2", "PDH_arog_dh_reg" ]
[ 118, 132 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011045", "PUB00011066" ]
[ "9843375", "11450855" ]
[ "Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.", "A metabolic node in action: chorismate-utilizing enzymes in microorganisms." ]
[ 1998, 2001 ]
2
[]
[]
0
0
null
[ "Methanobacteriota", "bioreactor metagenome" ]
[ 159, 1 ]
2
[]
[]
0
true
Family
Prephenate dehydrogenase/arogenate dehydrogenase
Prephenate dehydrogenase/arogenate dehydrogenase
Prep_DH/arog_DH
3
IPR008300
8,300
Phosphate propanoyltransferase
PTAC
Family
4,152
false
false
This family includes phosphotransacylases (PTACs) required for the degradation of 1,2-propanediol (1,2-PD) [ ].
[ "GO:0016747" ]
[ "acyltransferase activity, transferring groups other than amino-acyl groups" ]
[ "molecular_function" ]
1
[ "NCBIFAM", "PFAM", "PIRSF", "PANTHER" ]
[ "NF011652", "PF06130", "PIRSF010130", "PTHR39453" ]
[ "PRK15070.1", "PTAC", "PduL", "" ]
[ 3998, 4152, 3556, 4024 ]
4
[ "EC", "GP", "GP", "METACYC", "METACYC" ]
[ "2.3.1.222", "GenProp0292", "GenProp1762", "PWY-5437", "PWY-7013" ]
[ "EC:2.3.1.222", "GP:GenProp0292", "GP:GenProp1762", "METACYC:PWY-5437", "METACYC:PWY-7013" ]
5
[ "5cuo", "5cup" ]
2
[ "PUB00075709", "PUB00104965" ]
[ "17158662", "25962918" ]
[ "PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2.", "The PduL Phosphotransacylase Is Used To Recycle Coenzyme A within the Pdu Microcompartment." ]
[ 2007, 2015 ]
2
[]
[]
0
0
null
[ "Bacteria", "Caudovirales sp. gcode 4", "Eukaryota", "metagenomes" ]
[ 4097, 1, 5, 49 ]
4
[]
[]
0
true
Family
Phosphate propanoyltransferase
Phosphate propanoyltransferase
PTAC
1
IPR008302
8,302
Peptidoglycan beta-N-acetylmuramidase NamZ
NamZ
Family
7,974
false
false
NamZ is an exo-beta-N-acetylmuramidase which catalyses an exo-lytic cleavage of beta-1,4-acetylmuramic acid from from the non-reducing ends of peptidoglycan chains [ ] and it is a founding member of a new family of glycosidases ( ). NamZ consists of a N-terminal catalytic domain with a Rossmann-like fold ( ) and a C-te...
[ "GO:0033922" ]
[ "peptidoglycan beta-N-acetylmuramidase activity" ]
[ "molecular_function" ]
1
[ "PIRSF", "PANTHER" ]
[ "PIRSF016719", "PTHR42915" ]
[ "UCP016719", "" ]
[ 7205, 7974 ]
2
[]
[]
[]
0
[ "4jja", "4k05" ]
2
[ "PUB00100156" ]
[ "33684445" ]
[ "The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases." ]
[ 2021 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 21, 7625, 137, 191 ]
4
[]
[]
0
true
Family
Peptidoglycan beta-N-acetylmuramidase NamZ
Peptidoglycan beta-N-acetylmuramidase NamZ
NamZ
1
IPR008303
8,303
Methanogenesis marker protein 14
Methan_mark_14
Family
252
false
false
Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [ ].
[]
[]
[]
0
[ "PFAM", "PIRSF", "NCBIFAM" ]
[ "PF09887", "PIRSF016937", "TIGR03285" ]
[ "DUF2114", "UCP016937", "methan_mark_14" ]
[ 252, 229, 243 ]
3
[ "GP" ]
[ "GenProp0722" ]
[ "GP:GenProp0722" ]
1
[]
0
[ "PUB00060475" ]
[ "22070167" ]
[ "ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process." ]
[ 2011 ]
1
[]
[]
0
0
null
[ "Archaea", "ecological metagenomes" ]
[ 246, 6 ]
2
[]
[]
0
true
Family
Methanogenesis marker protein 14
Methanogenesis marker protein 14
Methan_mark_14
3
IPR008304
8,304
Uncharacterised conserved protein UCP017998
UCP017998
Family
113
false
false
This family consists of several hypothetical archaeal and bacterial proteins of unknown function, including from Aquifex aeolicus. The structure of this protein has been solved [ ] but its function remains unknown. Members of this family seem to have an acyl-CoA N-acyltransferase topology.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF06557", "PIRSF017998" ]
[ "DUF1122", "UCP017998" ]
[ 113, 30 ]
2
[]
[]
[]
0
[ "2arh", "4zsv", "4zsx", "4zsz" ]
4
[ "PUB00100674" ]
[ "26243886" ]
[ "On the predictability of the orientation of protein domains joined by a spanning alpha-helical linker." ]
[ 2015 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "marine sediment metagenome" ]
[ 94, 18, 1 ]
3
[]
[]
0
true
Family
Uncharacterised conserved protein UCP017998
Uncharacterised conserved protein UCP017998
UCP017998
1
IPR008306
8,306
Uncharacterised conserved protein UCP018008
UCP018008
Family
699
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF018008" ]
[ "UCP018008" ]
[ 699 ]
1
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[ "IPR007362" ]
[]
1
0
1
[ "Archaea", "Bacteria", "freshwater metagenome" ]
[ 2, 696, 1 ]
3
[]
[]
0
true
Family
Uncharacterised conserved protein UCP018008
Uncharacterised conserved protein UCP018008
UCP018008
2
IPR008307
8,307
Uncharacterised conserved protein UCP018957
UCP018957
Family
845
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF018957" ]
[ "UCP018957" ]
[ 845 ]
1
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[ "IPR014923" ]
[]
1
0
1
[ "Bacteria", "Geodia barretti", "Nitrososphaeria", "ecological metagenomes" ]
[ 831, 2, 5, 7 ]
4
[]
[]
0
true
Family
Uncharacterised conserved protein UCP018957
Uncharacterised conserved protein UCP018957
UCP018957
4
IPR008308
8,308
YpbB protein
YpbB-like
Family
1,172
false
false
This entry represents the YpbB proteins from Bacillus subtilis and related proteins found mainly in Bacillales. YpbB assemble with RecS into a single complex able to interact with a protein of the replisome, the Single-Stranded DNA Binding protein (SSB), resulting in its targeting to active chromosome replication forks...
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF021350" ]
[ "UCP021350" ]
[ 1172 ]
1
[]
[]
[]
0
[]
0
[ "PUB00155446" ]
[ "21170359" ]
[ "The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Bacilli", "human gut metagenome" ]
[ 1171, 1 ]
2
[]
[]
0
true
Family
YpbB protein
YpbB protein
YpbB-like
3
IPR008309
8,309
Probable chaperone-like protein YdbL
YdbL
Family
3,402
false
false
This entry represents YdbL (previously uncharacterised) and related bacterial proteins. This protein contains a small β-sheet connected to small α-helices. YdbL probably acts as a chaperone-like protein that contributes to, but is not essential for, the formation of the YdbH-YnbE intermembrane bridge. It affects both t...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF07027", "PIRSF025560" ]
[ "DUF1318", "UCP025560" ]
[ 3402, 2163 ]
2
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "environmental samples", "unclassified sequences" ]
[ 3352, 5, 2, 43 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Probable chaperone-like protein YdbL
Probable chaperone-like protein YdbL
YdbL
4
IPR008310
8,310
UPF0735 ACT domain-containing protein
UPF0735_ACT_dom-cont
Family
2,610
false
false
Members of this family contain a regulatory ACT domain with an additional N-terminal extension of ~70 aa, and therefore may be a stand-alone regulatory protein.
[]
[]
[]
0
[ "HAMAP", "NCBIFAM", "PIRSF" ]
[ "MF_00707", "NF003361", "PIRSF025624" ]
[ "UPF0735", "PRK04435.1", "ACT_PheB" ]
[ 2329, 2609, 2537 ]
3
[]
[]
[]
0
[]
0
[ "PUB00002073" ]
[ "2537815" ]
[ "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein." ]
[ 1989 ]
1
[]
[]
0
0
null
[ "Bacteria", "metagenomes" ]
[ 2595, 15 ]
2
[]
[]
0
true
Family
UPF0735 ACT domain-containing protein
UPF0735 ACT domain-containing protein
UPF0735_ACT_dom-cont
3
IPR008311
8,311
Uncharacterised conserved protein UCP028101
UCP028101
Family
3,004
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF07433", "PIRSF028101" ]
[ "DUF1513", "UCP028101" ]
[ 3004, 2680 ]
2
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 2978, 4, 22 ]
3
[]
[]
0
true
Family
Uncharacterised conserved protein UCP028101
Uncharacterised conserved protein UCP028101
UCP028101
5
IPR008312
8,312
Type VI secretion system sheath protein TssB1
T6SS_TssB1
Family
7,756
false
false
This entry includes TssB1, which is a sheath protein of the bacterial type VI secretion system (T6SS) [ ]. The type VI secretion system (T6SS), also known as CIS contractile injection system [ ], is a supra-molecular bacterial complex that resembles phage tails. It is a toxin delivery systems which fires toxins into ta...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "PF05591", "PIRSF028301", "PTHR35850", "TIGR03358" ]
[ "T6SS_VipA", "UCP028301", "", "VI_chp_5" ]
[ 7755, 6899, 7286, 7262 ]
4
[ "GP" ]
[ "GenProp0735" ]
[ "GP:GenProp0735" ]
1
[ "3j9g", "3j9o", "4ps2", "4uqz", "5mxn", "5myu", "5n8n", "5ojq", "5urw", "5urx", "9n4v" ]
11
[ "PUB00093972", "PUB00093973", "PUB00093981", "PUB00160456" ]
[ "27288401", "31379775", "29307484", "39546591" ]
[ "TssA forms a gp6-like ring attached to the type VI secretion sheath.", "Baseplate Component TssK and Spatio-Temporal Assembly of T6SS in Pseudomonas aeruginosa.", "Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa.", "Archaeal type six secretion system mediates contact-dependent anta...
[ 2016, 2019, 2018, 2024 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 7688, 14, 54 ]
3
[]
[]
0
true
Family
Type VI secretion system sheath protein TssB1
Type VI secretion system sheath protein TssB1
T6SS_TssB1
3
IPR008313
8,313
Metal-independent alpha-mannosidase
GH125
Family
7,417
false
false
This family includes proteins from bacteria and fungi. It was originally identified as a protein of unknown function from Schizosaccharomyces pombe, which was isolated from a screen to identify novel genes required for meiosis [ ]. Members of this family have since been characterised from Streptococcus pneumoniae ( ) a...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER", "SMART" ]
[ "PF06824", "PIRSF028846", "PTHR31047", "SM01149" ]
[ "Glyco_hydro_125", "UCP028846", "", "DUF1237" ]
[ 7400, 6174, 7288, 7235 ]
4
[]
[]
[]
0
[ "2nvp", "2p0v", "3on6", "3p2c", "3qpf", "3qry", "3qsp", "3qt3", "3qt9", "5m7i", "5m7y", "6rqk" ]
12
[ "PUB00044889", "PUB00055745" ]
[ "16303567", "21388958" ]
[ "A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events.", "Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans." ]
[ 2005, 2011 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Methanophaga sp. ANME-1 ERB7", "Eukaryota", "metagenomes" ]
[ 4048, 1, 3313, 55 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 3, 1 ]
2
true
Family
Metal-independent alpha-mannosidase
Metal-independent alpha-mannosidase
GH125
9
IPR008314
8,314
N(4)-acetylcytidine amidohydrolase
AC4CH
Family
1,665
false
false
N(4)-acetylcytidine amidohydrolase catalyses the hydrolysis of N4-acetylcytidine (ac4C). It contains the human activating signal cointegrator homology (ASCH) domain with unknown function, although this domain has been suggested to be responsible for RNA binding during transcription activation, RNA processing and regula...
[]
[]
[]
0
[ "HAMAP", "NCBIFAM", "PIRSF", "PANTHER" ]
[ "MF_00684", "NF003443", "PIRSF029143", "PTHR38088" ]
[ "ac4C_amidohydr", "PRK04980.1", "UCP029143", "" ]
[ 1584, 1642, 1507, 1660 ]
4
[ "EC" ]
[ "3.5.1.135" ]
[ "EC:3.5.1.135" ]
1
[ "1te7", "9kyf", "9kyg", "9kyh" ]
4
[ "PUB00037702", "PUB00044668", "PUB00094246" ]
[ "15969587", "16322048", "31964920" ]
[ "G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination.", "The ASCH superfamily: novel domains with a fold related to the PUA domain and a potential role in RNA metabolism.", "YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N4-acylcytosine...
[ 2005, 2006, 2020 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 1659, 6 ]
2
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
N(4)-acetylcytidine amidohydrolase
N(4)-acetylcytidine amidohydrolase
AC4CH
3
IPR008316
8,316
Uncharacterised conserved protein UCP029876
UCP029876
Family
2,973
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF06304", "PIRSF029876" ]
[ "DUF1048", "UCP029876" ]
[ 2973, 728 ]
2
[]
[]
[]
0
[ "2hh6", "2o3l", "2o4t" ]
3
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[]
[]
0
0
null
[ "Bacteria", "bioreactor metagenome" ]
[ 2958, 15 ]
2
[]
[]
0
true
Family
Uncharacterised conserved protein UCP029876
Uncharacterised conserved protein UCP029876
UCP029876
3
IPR008317
8,317
Uncharacterised conserved protein UCP030561
UCP030561
Family
776
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Though the N-terminal half of these proteins is related to the N-terminal half of steroid delta-isomerase, the C-terminal half is predicted to be structurally unrelated. Both ...
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF030561" ]
[ "UCP030561" ]
[ 776 ]
1
[]
[]
[]
0
[ "2k54" ]
1
[ "PUB00011187" ]
[ "11751047" ]
[ "Structure and enzymology of Delta5-3-ketosteroid isomerase." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacterium", "bioreactor metagenome" ]
[ 763, 6, 6, 1 ]
4
[]
[]
0
true
Family
Uncharacterised conserved protein UCP030561
Uncharacterised conserved protein UCP030561
UCP030561
1
IPR008318
8,318
Uncharacterised conserved protein UCP030820
UCP030820
Family
5,968
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF06073", "PIRSF030820" ]
[ "DUF934", "UCP030820" ]
[ 5968, 4312 ]
2
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 5900, 6, 62 ]
3
[]
[]
0
true
Family
Uncharacterised conserved protein UCP030820
Uncharacterised conserved protein UCP030820
UCP030820
6
IPR008319
8,319
GyrI-like cyclopropanoid cyclopropyl hydrolase Lin2189-like
GyrI-like_CCH_Lin2189-like
Family
2,823
false
false
This family of prokaryotic GyrI-like proteins include Lin2189 protein from Listeria innocua ( ), a cyclopropanoid cyclopropyl hydrolase (CCHs) that can catalyse the hydrolysis of the potent DNA-alkylating agents yatakemycin (YTM) and CC-1065, protecting the cells. This protein shows three α-helices and six β-strands an...
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF031644" ]
[ "UCP031644" ]
[ 2823 ]
1
[]
[]
[]
0
[ "3b49", "5x5m", "5x5r" ]
3
[ "PUB00101004" ]
[ "29133784" ]
[ "GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection." ]
[ 2017 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Didymella rabiei", "Siphoviridae sp. ctP6p7", "ecological metagenomes" ]
[ 31, 2751, 1, 1, 39 ]
5
[]
[]
0
true
Family
GyrI-like cyclopropanoid cyclopropyl hydrolase Lin2189-like
GyrI-like cyclopropanoid cyclopropyl hydrolase Lin2189-like
GyrI-like_CCH_Lin2189-like
4
IPR008320
8,320
Uncharacterised conserved protein UCP032025
UCP032025
Family
2,731
false
false
This family consists of several hypothetical bacterial proteins of around 150 residues in length. Members of this family seem to be founds exclusively in the Class Alphaproteobacteria. The function of this family is unknown.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF07370", "PIRSF032025" ]
[ "DUF1489", "UCP032025" ]
[ 2731, 2685 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Pseudomonadati", "unclassified sequences" ]
[ 2711, 20 ]
2
[]
[]
0
true
Family
Uncharacterised conserved protein UCP032025
Uncharacterised conserved protein UCP032025
UCP032025
8
IPR008321
8,321
Uncharacterised conserved protein UCP032146
UCP032146
Family
2,636
false
false
This protein family is functionally uncharacterised.
[]
[]
[]
0
[ "HAMAP", "NCBIFAM", "PFAM", "PIRSF" ]
[ "MF_00678", "NF002769", "PF06793", "PIRSF032146" ]
[ "UPF0262", "PRK02853.1", "UPF0262", "UCP032146" ]
[ 2282, 2584, 2636, 2228 ]
4
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati", "metagenomes" ]
[ 3, 2605, 28 ]
3
[]
[]
0
true
Family
Uncharacterised conserved protein UCP032146
Uncharacterised conserved protein UCP032146
UCP032146
3
IPR008322
8,322
Uncharacterised protein family UPF0261
UPF0261
Family
3,456
false
false
The proteins in this entry are functionally uncharacterised.
[]
[]
[]
0
[ "HAMAP", "PIRSF" ]
[ "MF_00677", "PIRSF033271" ]
[ "UPF0261", "UCP033271" ]
[ 676, 3348 ]
2
[]
[]
[]
0
[ "3wrw", "3wrx", "3wry", "9mpy" ]
4
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 89, 2635, 709, 23 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Zea mays" ]
[ 1, 1 ]
2
true
Family
Uncharacterised protein family UPF0261
Uncharacterised protein family UPF0261
UPF0261
8
IPR008323
8,323
Uncharacterised conserved protein UCP033563
UCP033563
Family
7,654
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function.
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF06245", "PIRSF033563", "PTHR36454" ]
[ "DUF1015", "UCP033563", "" ]
[ 7584, 5216, 7555 ]
3
[]
[]
[]
0
[]
0
[ "PUB00160784" ]
[ "38748582" ]
[ "YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of <i>Escherichia coli</i>." ]
[ 2024 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 122, 7041, 89, 402 ]
4
[]
[]
0
true
Family
Uncharacterised conserved protein UCP033563
Uncharacterised conserved protein UCP033563
UCP033563
1
IPR008325
8,325
EipA-like
EipA-like
Family
1,814
false
false
The member of this family for Brucella abortus, named EipA, has been characterised as a molecular determinant of virulence that functions to maintain cell envelope integrity [ ].
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF06577", "PIRSF033924" ]
[ "EipA", "UCP033924" ]
[ 1814, 1120 ]
2
[]
[]
[]
0
[ "5uc0" ]
1
[ "PUB00091721" ]
[ "30536925" ]
[ "Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus." ]
[ 2018 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 1797, 2, 15 ]
3
[]
[]
0
true
Family
EipA-like
EipA-like
EipA-like
8
IPR008326
8,326
Pyruvate dehydrogenase inhibitor-like
PdhI-like
Family
1,659
false
false
This entry represents Pyruvate dehydrogenase inhibitor from Bacillus subtilis (PdhI) and similar sequences from firmicutes. PdhI functions as an inhibitor of the pyruvate dehydrogenase [ ].
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF034852" ]
[ "UCP034852" ]
[ 1659 ]
1
[]
[]
[]
0
[]
0
[ "PUB00154956" ]
[ "36815589" ]
[ "Protein complexes in cells by AI-assisted structural proteomics." ]
[ 2023 ]
1
[]
[]
0
0
null
[ "Bacillota" ]
[ 1659 ]
1
[]
[]
0
true
Family
Pyruvate dehydrogenase inhibitor-like
Pyruvate dehydrogenase inhibitor-like
PdhI-like
7
IPR008327
8,327
Signal transduction response regulator, antiterminator
Sig_transdc_resp-reg_antiterm
Family
11,238
false
false
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt...
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF036382" ]
[ "RR_antiterm" ]
[ 11238 ]
1
[]
[]
[]
0
[ "1qo0", "1s8n", "1sd5", "6wsh", "6ww6" ]
5
[ "PUB00001238", "PUB00007866", "PUB00010651", "PUB00011096", "PUB00011157", "PUB00011190", "PUB00011191", "PUB00011192", "PUB00011193", "PUB00011194", "PUB00042804", "PUB00042805", "PUB00042806", "PUB00042807" ]
[ "8253087", "11406410", "12372152", "10966457", "10622255", "10500846", "10508151", "10893220", "11796212", "8918468", "16176121", "18076326", "11934609", "11489844" ]
[ "Antitermination of amidase expression in Pseudomonas aeruginosa is controlled by a novel cytoplasmic amide-binding protein.", "Histidine kinases and response regulator proteins in two-component signaling systems.", "Histidine protein kinases: key signal transducers outside the animal kingdom.", "Two-componen...
[ 1993, 2001, 2002, 2000, 1999, 1999, 1999, 2000, 2002, 1996, 2005, 2007, 2002, 2001 ]
14
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 10976, 5, 13, 244 ]
4
[]
[]
0
true
Family
Signal transduction response regulator, antiterminator
Signal transduction response regulator, antiterminator
Sig_transdc_resp-reg_antiterm
8
IPR008330
8,330
Peptidase M17, peptidase B
Pept_M17_PepB
Family
2,665
false
false
This family represents the peptidase B group of leucyl aminopeptidases, which are restricted to the gammaproteobacteria. They contain a C-terminal aminopeptidase catalytic domain and an N-terminal domain of unknown function. They are zinc-dependent exopeptidases ( ) and belong to MEROPS peptidase family M17 (leucyl ami...
[ "GO:0030145", "GO:0070006", "GO:0006508", "GO:0005737" ]
[ "manganese ion binding", "metalloaminopeptidase activity", "proteolysis", "cytoplasm" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "HAMAP", "NCBIFAM", "PIRSF" ]
[ "MF_00504", "NF003450", "PIRSF036388" ]
[ "Aminopeptidase_M17", "PRK05015.1", "Ctsl_amnpptdse_B" ]
[ 1269, 2663, 2550 ]
3
[ "EC" ]
[ "3.4.11.23" ]
[ "EC:3.4.11.23" ]
1
[ "6cxd", "6oad", "6ov8" ]
3
[ "PUB00000522", "PUB00001416", "PUB00003579", "PUB00004713", "PUB00011211", "PUB00011212", "PUB00011213", "PUB00011214", "PUB00011215" ]
[ "8439290", "1555602", "7674922", "2395881", "8703509", "10449417", "10970742", "10852868", "8506345" ]
[ "Evolutionary families of peptidases.", "Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.", "Evolutionary families of metallopeptidases.", "Molecular structure of leucine aminopeptidase at 2.7-A resolution.", "...
[ 1993, 1992, 1995, 1990, 1996, 1999, 2000, 2000, 1993 ]
9
[ "IPR011356" ]
[]
1
0
1
[ "Bacteria", "Opisthokonta", "unclassified sequences" ]
[ 2661, 2, 2 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Peptidase M17, peptidase B
Peptidase M17, peptidase B
Pept_M17_PepB
1
IPR008332
8,332
Methylguanine DNA methyltransferase, ribonuclease-like domain
MethylG_MeTrfase_N
Domain
26,694
false
false
The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase ( ) (also known as 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase). The major mutagenic and carcinogenic effect of methylating agents in DNA is the formation of O6-alkylguanine...
[ "GO:0003908", "GO:0006281" ]
[ "methylated-DNA-[protein]-cysteine S-methyltransferase activity", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02870" ]
[ "Methyltransf_1N" ]
[ 26694 ]
1
[ "EC", "REACTOME" ]
[ "2.1.1.63", "R-HSA-5657655" ]
[ "EC:2.1.1.63", "REACTOME:R-HSA-5657655" ]
2
[ "1eh6", "1eh7", "1eh8", "1qnt", "1sfe", "1t38", "1t39", "1wrj", "1yfh", "3kzy", "3kzz", "3l00", "4bhb", "4bhc", "4wx9", "4wxc", "4wxd", "4zyd", "4zye", "4zyg", "4zyh", "5llq", "6ga0", "6rla", "6rlb", "6sc2", "6y8p", "7csm", "7d4v", "7dkn", "7dqq", "7dqr"...
65
[ "PUB00000053", "PUB00004404" ]
[ "3052269", "1579490" ]
[ "Regulation and expression of the adaptive response to alkylating agents.", "Isolation and partial characterisation of a Chinese hamster O6-alkylguanine-DNA alkyltransferase cDNA." ]
[ 1988, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 132, 25525, 808, 229 ]
4
[ "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 2, 5, 2, 3 ]
5
true
Domain
Methylguanine DNA methyltransferase, ribonuclease-like domain
Methylguanine DNA methyltransferase, ribonuclease-like domain
MethylG_MeTrfase_N
2
IPR008333
8,333
Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
Cbr1-like_FAD-bd_dom
Domain
90,148
false
false
These sequences represent the FAD-binding domain found in NADH:cytochrome b5 reductases and nitrate reductases.
[]
[]
[]
0
[ "PFAM" ]
[ "PF00970" ]
[ "FAD_binding_6" ]
[ 90148 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp1554", "R-BTA-114608", "R-BTA-1237044", "R-BTA-196836", "R-BTA-211945", "R-BTA-6798695", "R-CFA-196836", "R-CFA-211945", "R-CFA-6798695", "R-DDI-114608", "R-DDI-196836", "R-DDI-211945", "R-DDI-6798695", "R-DRE-1237044", "R-HSA-114608", "R-HSA-1237044", "R-HSA-196836", "R-HS...
[ "GP:GenProp1554", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1237044", "REACTOME:R-BTA-196836", "REACTOME:R-BTA-211945", "REACTOME:R-BTA-6798695", "REACTOME:R-CFA-196836", "REACTOME:R-CFA-211945", "REACTOME:R-CFA-6798695", "REACTOME:R-DDI-114608", "REACTOME:R-DDI-196836", "REACTOME:R-DDI-211945"...
36
[ "1a8p", "1cne", "1cnf", "1fdr", "1gaq", "1gaw", "1gvh", "1i7p", "1ib0", "1krh", "1ndh", "1qfj", "1qx4", "1tvc", "1umk", "2bgi", "2bgj", "2cnd", "2eix", "2qdx", "2r6h", "2vnh", "2vni", "2vnj", "2vnk", "2xnc", "2xnj", "3crz", "3fpk", "3w2e", "3w2f", "3w2g"...
108
[ "PUB00000415", "PUB00002370", "PUB00005247" ]
[ "7893687", "8027025", "7812715" ]
[ "Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution.", "Structure-function relations for ferredoxin reductase.", "Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases." ]
[ 1995, 1994, 1994 ]
3
[ "IPR017927" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Vibrio phage VP-HS15", "plasmids", "unclassified sequences" ]
[ 738, 66718, 22118, 1, 2, 571 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 17, 5, 13, 11, 5, 28, 12, 8, 18, 32, 6, 3, 37 ]
13
true
Domain
Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
Cbr1-like_FAD-bd_dom
5
IPR008334
8,334
5'-Nucleotidase, C-terminal
5'-Nucleotdase_C
Domain
45,338
false
false
This entry is the C-terminal domain of 5'-nucleotidases. 5'-nucleotidases [ ] are enzymes that catalyse the hydrolysis of phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules. 5'-nucleotidase is a ubiquitous enzyme found in a wide variety of species and which occurs in differ...
[ "GO:0016787", "GO:0009166" ]
[ "hydrolase activity", "nucleotide catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02872" ]
[ "5_nucleotid_C" ]
[ 45338 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3", "R-HSA-196807", "R-HSA-73621", "R-HSA-74259", "R-HSA-9660826", "R-MMU-196807", "R-MMU-73621", "R-MMU-74259", "R-RNO-196807", "R-RNO-73621", "R-RNO-74259" ]
[ "EC:3.1.3", "REACTOME:R-HSA-196807", "REACTOME:R-HSA-73621", "REACTOME:R-HSA-74259", "REACTOME:R-HSA-9660826", "REACTOME:R-MMU-196807", "REACTOME:R-MMU-73621", "REACTOME:R-MMU-74259", "REACTOME:R-RNO-196807", "REACTOME:R-RNO-73621", "REACTOME:R-RNO-74259" ]
11
[ "1ho5", "1hp1", "1hpu", "1oi8", "1oid", "1oie", "1ush", "2ush", "2wdc", "2wdd", "2wde", "2wdf", "2z1a", "3ivd", "3ive", "3qfk", "3ztv", "3zu0", "4h1s", "4h1y", "4h2b", "4h2f", "4h2g", "4h2i", "4q7f", "4uwq", "4wwl", "5h7w", "6hxw", "6s7f", "6s7h", "6tve"...
71
[ "PUB00000512", "PUB00004869", "PUB00008988", "PUB00008989" ]
[ "1637327", "7846038", "9015312", "2550543" ]
[ "5'-Nucleotidase: molecular structure and functional aspects.", "The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family.", "Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endoth...
[ 1992, 1995, 1997, 1989 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 560, 36726, 7744, 24, 284 ]
5
[ "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]
[ 2, 20, 2, 7, 5, 2, 6 ]
7
true
Domain
5'-Nucleotidase, C-terminal
5'-Nucleotidase, C-terminal
5'-Nucleotdase_C
4
IPR008335
8,335
Eukaryotic molybdopterin oxidoreductase
Mopterin_OxRdtase_euk
Family
19,214
false
false
A number of different eukaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [ ] to share a few regions of sequence similarity. These enzymes include xanthine dehydrogenase ( ), aldehyde oxidase ( ), nitrate reductase ( ), and sulphite oxidase ( ). The multidomain redox enzyme NAD(P)H...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR00407" ]
[ "EUMOPTERIN" ]
[ 19214 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.7.1", "R-DME-1614517", "R-HSA-1614517", "R-MMU-1614517", "R-RNO-1614517" ]
[ "EC:1.7.1", "REACTOME:R-DME-1614517", "REACTOME:R-HSA-1614517", "REACTOME:R-MMU-1614517", "REACTOME:R-RNO-1614517" ]
5
[ "1ogp", "1sox", "2a99", "2a9a", "2a9b", "2a9c", "2a9d", "2bih", "2bii", "2blf", "2bpb", "2c9x", "2ca3", "2ca4", "2xts", "3hbg", "3hbp", "3hbq", "3hc2", "3r18", "3r19", "4pw3", "4pw9", "5k3x", "5wa0", "6y0k", "8s5s" ]
27
[ "PUB00000608", "PUB00002526", "PUB00002593", "PUB00002947", "PUB00005356" ]
[ "2015248", "2687265", "2249998", "7896804", "2204158" ]
[ "Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains.", "Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase.", "A conserved cysteine in molybdenum oxotransferase...
[ 1991, 1989, 1990, 1995, 1990 ]
5
[]
[ "IPR030835" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Harvfovirus sp.", "unclassified sequences" ]
[ 151, 8650, 10267, 1, 145 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 18, 2, 4, 1, 3, 1, 3, 15, 3, 39 ]
10
true
Family
Eukaryotic molybdopterin oxidoreductase
Eukaryotic molybdopterin oxidoreductase
Mopterin_OxRdtase_euk
6
IPR008336
8,336
DNA topoisomerase I, DNA binding, eukaryotic-type
TopoI_DNA-bd_euk
Domain
9,484
false
false
DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi...
[ "GO:0003677", "GO:0003917", "GO:0006265" ]
[ "DNA binding", "DNA topoisomerase type I (single strand cut, ATP-independent) activity", "DNA topological change" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF02919" ]
[ "Topoisom_I_N" ]
[ 9484 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.6.2.1", "R-CEL-4615885", "R-DDI-4615885", "R-HSA-4615885", "R-MMU-4615885", "R-RNO-4615885", "R-SCE-4615885", "R-SPO-4615885" ]
[ "EC:5.6.2.1", "REACTOME:R-CEL-4615885", "REACTOME:R-DDI-4615885", "REACTOME:R-HSA-4615885", "REACTOME:R-MMU-4615885", "REACTOME:R-RNO-4615885", "REACTOME:R-SCE-4615885", "REACTOME:R-SPO-4615885" ]
8
[ "1a31", "1a35", "1a36", "1ej9", "1k4s", "1k4t", "1lpq", "1nh3", "1ois", "1r49", "1rr8", "1rrj", "1sc7", "1seu", "1t8i", "1tl8", "2b9s", "6z01", "6z03" ]
19
[ "PUB00005230", "PUB00005437", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00020800", "PUB00081702", "PUB00081703", "PUB00081704", "PUB00081705" ]
[ "9488644", "7770916", "11395412", "12596227", "12042765", "14741206", "21087076", "20644584", "17722649", "17293019" ]
[ "Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.", "The mechanisms of DNA topoisomerases.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles of DNA topoisomerases: a molecular perspective.",...
[ 1998, 1995, 2001, 2003, 2002, 2004, 2010, 2010, 2007, 2007 ]
10
[]
[ "IPR048045" ]
0
1
0
[ "Archaea", "Eukaryota", "Megaviricetes", "metagenomes" ]
[ 99, 9324, 35, 26 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 12, 1, 7, 7, 19, 5, 2, 2, 10, 1, 1, 19 ]
12
true
Domain
DNA topoisomerase I, DNA binding, eukaryotic-type
DNA topoisomerase I, DNA binding, eukaryotic-type
TopoI_DNA-bd_euk
4
IPR008337
8,337
Capsule biosynthesis protein CapB
Capsule_biosynth_CapB
Family
1,315
false
false
Bacillus spp. are Gram-positive aerobic rods that are able to form endo- spores that allow them to survive in almost any environment. The many different species exhibit a wide variation of physiological abilities, their spores being resistant, for example, to heat, cold, disinfection and radiation. However, the spores ...
[ "GO:0045227", "GO:0016020" ]
[ "capsule polysaccharide biosynthetic process", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS", "NCBIFAM" ]
[ "PR01758", "TIGR04012" ]
[ "CAPSULEPROTB", "poly_gGlu_PgsB" ]
[ 1312, 1114 ]
2
[ "GP" ]
[ "GenProp0822" ]
[ "GP:GenProp0822" ]
1
[]
0
[ "PUB00011559", "PUB00011560" ]
[ "2536679", "8945528" ]
[ "Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis.", "Differential influence of the two Bacillus anthracis plasmids on regulation of virulence gene expression." ]
[ 1989, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "metagenomes" ]
[ 17, 1262, 36 ]
3
[]
[]
0
true
Family
Capsule biosynthesis protein CapB
Capsule biosynthesis protein CapB
Capsule_biosynth_CapB
6
IPR008338
8,338
Capsule biosynthesis protein CapC
Capsule_biosynth_CapC
Family
1,409
false
false
Bacillus spp. are Gram-positive aerobic rods that are able to form endo-spores that allow them to survive in almost any environment. The many different species exhibit a wide variation of physiological abilities, their spores being resistant, for example, to heat, cold, disinfection and radiation. However, the spores r...
[ "GO:0045227", "GO:0016020" ]
[ "capsule polysaccharide biosynthetic process", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PRINTS", "NCBIFAM" ]
[ "PF14102", "PR01759", "TIGR04011" ]
[ "Caps_synth_CapC", "CAPSULEPROTC", "poly_gGlu_PgsC" ]
[ 1409, 893, 661 ]
3
[ "GP" ]
[ "GenProp0822" ]
[ "GP:GenProp0822" ]
1
[]
0
[ "PUB00011559", "PUB00011560" ]
[ "2536679", "8945528" ]
[ "Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis.", "Differential influence of the two Bacillus anthracis plasmids on regulation of virulence gene expression." ]
[ 1989, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Cladocopium goreaui", "metagenomes" ]
[ 97, 1273, 1, 38 ]
4
[]
[]
0
true
Family
Capsule biosynthesis protein CapC
Capsule biosynthesis protein CapC
Capsule_biosynth_CapC
5
IPR008339
8,339
Dishevelled family
Dishevelled_fam
Family
4,849
false
false
Wnt proteins constitute a large family of secreted signalling molecules that are involved in intercellular signalling during development. The name derives from the first 2 members of the family to be discovered: int-1 (mouse) and wingless (Wg) (Drosophila) [ ]. It is now recognised that Wnt signalling controls many cel...
[ "GO:0016055" ]
[ "Wnt signaling pathway" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01760" ]
[ "DISHEVELLED" ]
[ 4849 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-DME-201688", "R-DME-209440", "R-DME-350368", "R-DME-350369", "R-DME-350376", "R-DME-350411", "R-DME-350480", "R-DME-4086400", "R-DME-450728", "R-DME-4608870", "R-DME-4641258", "R-DME-4641262", "R-DME-5099900", "R-DME-5663220", "R-HSA-201681", "R-HSA-201688", "R-HSA-2028269", "R-...
[ "REACTOME:R-DME-201688", "REACTOME:R-DME-209440", "REACTOME:R-DME-350368", "REACTOME:R-DME-350369", "REACTOME:R-DME-350376", "REACTOME:R-DME-350411", "REACTOME:R-DME-350480", "REACTOME:R-DME-4086400", "REACTOME:R-DME-450728", "REACTOME:R-DME-4608870", "REACTOME:R-DME-4641258", "REACTOME:R-DME-...
49
[ "1fsh", "5lnp", "5suy", "5suz", "8wm9", "8wma" ]
6
[ "PUB00011232", "PUB00011233", "PUB00011234", "PUB00011235", "PUB00060615" ]
[ "9891778", "10967351", "10733430", "12072470", "9867820" ]
[ "Mechanisms of Wnt signaling in development.", "Wnt signaling function in Alzheimer's disease.", "Wnt signaling in oncogenesis and embryogenesis--a look outside the nucleus.", "A mutational analysis of dishevelled in Drosophila defines novel domains in the dishevelled protein as well as novel suppressing alle...
[ 1998, 2000, 2000, 2002, 1999 ]
5
[ "IPR015506" ]
[ "IPR008341", "IPR008342" ]
1
2
0
[ "Metazoa" ]
[ 4849 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 26, 1, 19, 8, 9 ]
6
true
Family
Dishevelled family
Dishevelled family
Dishevelled_fam
5
IPR008341
8,341
Dishevelled-2
DVL2
Family
342
false
false
Dishevelled (Dsh) proteins possess three conserved domains: an amino-terminal DIX domain, a central PDZ and a carboxyl-terminal DEP domain. They acts downstream of Fz receptors in the Wnt signalling pathway, which controls a variety of developmental and homeostatic events [ ]. Dishevelled-2 (DVL-2) participates in Wnt ...
[ "GO:0016055" ]
[ "Wnt signaling pathway" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01762" ]
[ "DISHEVELLED2" ]
[ 342 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-HSA-201681", "R-HSA-201688", "R-HSA-2028269", "R-HSA-4086400", "R-HSA-4608870", "R-HSA-4641258", "R-HSA-4641262", "R-HSA-5099900", "R-HSA-5368598", "R-HSA-5663220", "R-HSA-8856825", "R-HSA-8856828", "R-HSA-9673324", "R-MMU-201688", "R-MMU-2028269", "R-MMU-4086400", "R-MMU-4608870"...
[ "REACTOME:R-HSA-201681", "REACTOME:R-HSA-201688", "REACTOME:R-HSA-2028269", "REACTOME:R-HSA-4086400", "REACTOME:R-HSA-4608870", "REACTOME:R-HSA-4641258", "REACTOME:R-HSA-4641262", "REACTOME:R-HSA-5099900", "REACTOME:R-HSA-5368598", "REACTOME:R-HSA-5663220", "REACTOME:R-HSA-8856825", "REACTOME:...
30
[ "8wm9", "8wma" ]
2
[ "PUB00050960", "PUB00070944" ]
[ "19252499", "15353129" ]
[ "Inhibition of Wnt signaling by Dishevelled PDZ peptides.", "Characterization of function of three domains in dishevelled-1: DEP domain is responsible for membrane translocation of dishevelled-1." ]
[ 2009, 2004 ]
2
[ "IPR008339" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 342 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 2, 2 ]
3
true
Family
Dishevelled-2
Dishevelled-2
DVL2
1
IPR008342
8,342
Dishevelled-3
DVL3
Family
327
false
false
Dishevelled (Dsh) proteins possess three conserved domains: an amino-terminal DIX domain, a central PDZ and a carboxyl-terminal DEP domain. They acts downstream of Fz receptors in the Wnt signalling pathway, which controls a variety of developmental and homeostatic events [ ]. Dishevelled-3 (DVL-3) may play a role in t...
[ "GO:0016055" ]
[ "Wnt signaling pathway" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01763" ]
[ "DISHEVELLED3" ]
[ 327 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-201681", "R-HSA-201688", "R-HSA-4086400", "R-HSA-4641258", "R-HSA-4641262", "R-HSA-5368598", "R-HSA-5663220", "R-HSA-9673324", "R-MMU-201688", "R-MMU-4086400", "R-MMU-4641258", "R-MMU-4641262", "R-MMU-5663220" ]
[ "REACTOME:R-HSA-201681", "REACTOME:R-HSA-201688", "REACTOME:R-HSA-4086400", "REACTOME:R-HSA-4641258", "REACTOME:R-HSA-4641262", "REACTOME:R-HSA-5368598", "REACTOME:R-HSA-5663220", "REACTOME:R-HSA-9673324", "REACTOME:R-MMU-201688", "REACTOME:R-MMU-4086400", "REACTOME:R-MMU-4641258", "REACTOME:R...
13
[]
0
[ "PUB00070944" ]
[ "15353129" ]
[ "Characterization of function of three domains in dishevelled-1: DEP domain is responsible for membrane translocation of dishevelled-1." ]
[ 2004 ]
1
[ "IPR008339" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 327 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 4 ]
3
true
Family
Dishevelled-3
Dishevelled-3
DVL3
8
IPR008343
8,343
Mitogen-activated protein (MAP) kinase phosphatase
MKP
Family
9,044
false
false
MAP Kinase Phosphatases (MKPs) are members of the dual specificity phosphatase family [ , ]. MKPs constitute a class of phosphatases that reverse the activation of MAP (mitogen activated protein) kinases by dephosphorylating critical tyrosine and threonine residues [ ]. This regulation is mediated via interaction of a ...
[ "GO:0017017", "GO:0006470" ]
[ "MAP kinase tyrosine/serine/threonine phosphatase activity", "protein dephosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "PRINTS" ]
[ "PIRSF000939", "PR01764" ]
[ "MAPK_Ptase", "MAPKPHPHTASE" ]
[ 4133, 9032 ]
2
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "3.1.3.16", "3.1.3.48", "R-BTA-112409", "R-BTA-202670", "R-BTA-5675221", "R-CEL-112409", "R-CEL-202670", "R-CEL-5675221", "R-DME-112409", "R-DME-202670", "R-DME-5675221", "R-GGA-437980", "R-GGA-437986", "R-HSA-112409", "R-HSA-202670", "R-HSA-5675221", "R-HSA-9636569", "R-HSA-965281...
[ "EC:3.1.3.16", "EC:3.1.3.48", "REACTOME:R-BTA-112409", "REACTOME:R-BTA-202670", "REACTOME:R-BTA-5675221", "REACTOME:R-CEL-112409", "REACTOME:R-CEL-202670", "REACTOME:R-CEL-5675221", "REACTOME:R-DME-112409", "REACTOME:R-DME-202670", "REACTOME:R-DME-5675221", "REACTOME:R-GGA-437980", "REACTOME...
24
[ "1m3g", "1mkp", "1zzw", "2g6z", "2hxp", "2oud", "2vsw", "3ezz", "3lj8", "3tg3", "4jmk", "4y2e", "4yr8", "6mc1", "7u4o", "7u4r", "7umu", "7umv", "7un0", "7un4", "7y4c", "7y4d", "7y4e", "9bpn", "9bu4", "9nsb", "9nym", "9o8w", "9ok9", "9q7x", "9y55" ]
31
[ "PUB00011585", "PUB00011587", "PUB00056895", "PUB00056896" ]
[ "8221888", "8910287", "17057753", "15186772" ]
[ "MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.", "The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases.", "Protein tyrosine phosphatases: from genes, to ...
[ 1993, 1996, 2006, 2004 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Megaviridae environmental sample" ]
[ 9043, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 14, 3, 30, 33, 27 ]
6
true
Family
Mitogen-activated protein (MAP) kinase phosphatase
Mitogen-activated protein (MAP) kinase phosphatase
MKP
2
IPR008344
8,344
Transient receptor potential cation channel subfamily V member 5/6
TRPV5/TRPV6
Family
1,803
false
false
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six ...
[ "GO:0005262", "GO:0006816", "GO:0016020" ]
[ "calcium channel activity", "calcium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01765" ]
[ "ECACCHANNEL" ]
[ 1803 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-3295583", "R-MMU-3295583", "R-RNO-3295583" ]
[ "REACTOME:R-HSA-3295583", "REACTOME:R-MMU-3295583", "REACTOME:R-RNO-3295583" ]
3
[ "2rfa", "5iwk", "5iwp", "5iwr", "5iwt", "5wo6", "5wo7", "5wo8", "5wo9", "5woa", "6b5v", "6bo8", "6bo9", "6boa", "6bob", "6d7o", "6d7p", "6d7q", "6d7s", "6d7t", "6d7v", "6d7x", "6dmr", "6dmu", "6dmw", "6e2f", "6e2g", "6o1n", "6o1p", "6o1u", "6o20", "6pbe"...
68
[ "PUB00054048", "PUB00054049", "PUB00054050", "PUB00054054", "PUB00100009" ]
[ "18535090", "20025796", "20861159", "19297520", "29464560" ]
[ "TRP channels entering the structural era.", "Structure-functional intimacies of transient receptor potential channels.", "The role of transient receptor potential cation channels in Ca2+ signaling.", "Pharmacology of vanilloid transient receptor potential cation channels.", "Transient Receptor Potential (T...
[ 2008, 2009, 2010, 2009, 2018 ]
5
[ "IPR024862" ]
[ "IPR008345", "IPR008346" ]
1
2
0
[ "Bilateria" ]
[ 1803 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 10, 6, 6 ]
4
true
Family
Transient receptor potential cation channel subfamily V member 5/6
Transient receptor potential cation channel subfamily V member 5/6
TRPV5/TRPV6
7
IPR008345
8,345
Transient receptor potential cation channel subfamily V member 6
TrpV6
Family
276
false
false
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six ...
[ "GO:0005262", "GO:0006816", "GO:0016020" ]
[ "calcium channel activity", "calcium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01766" ]
[ "ECACCHANNEL1" ]
[ 276 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-3295583", "R-MMU-3295583", "R-RNO-3295583" ]
[ "REACTOME:R-HSA-3295583", "REACTOME:R-MMU-3295583", "REACTOME:R-RNO-3295583" ]
3
[ "5iwk", "5iwp", "5iwr", "5iwt", "5wo6", "5wo7", "5wo8", "5wo9", "5woa", "6bo8", "6bo9", "6boa", "6bob", "6d7o", "6d7p", "6d7q", "6d7s", "6d7t", "6d7v", "6d7x", "6e2f", "6e2g", "7d2k", "7k4a", "7k4b", "7k4c", "7k4d", "7k4e", "7k4f", "7s88", "7s89", "7s8b"...
40
[ "PUB00018944", "PUB00054048", "PUB00054049", "PUB00054050", "PUB00054054", "PUB00100009", "PUB00100010", "PUB00100011", "PUB00100012", "PUB00100013", "PUB00100014", "PUB00100015" ]
[ "11278579", "18535090", "20025796", "20861159", "19297520", "29464560", "11248124", "23612980", "11097838", "15184369", "29861107", "29258289" ]
[ "Expression of CaT-like, a novel calcium-selective channel, correlates with the malignancy of prostate cancer.", "TRP channels entering the structural era.", "Structure-functional intimacies of transient receptor potential channels.", "The role of transient receptor potential cation channels in Ca2+ signaling...
[ 2001, 2008, 2009, 2010, 2009, 2018, 2001, 2013, 2000, 2004, 2018, 2018 ]
12
[ "IPR008344" ]
[]
1
0
1
[ "Mammalia" ]
[ 276 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 4, 4 ]
3
true
Family
Transient receptor potential cation channel subfamily V member 6
Transient receptor potential cation channel subfamily V member 6
TrpV6
9
IPR008347
8,347
Transient receptor potential cation channel subfamily V member 1-4
TrpV1-4
Family
5,065
false
false
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six ...
[ "GO:0005216", "GO:0006811", "GO:0016020" ]
[ "monoatomic ion channel activity", "monoatomic ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01768" ]
[ "TRPVRECEPTOR" ]
[ 5065 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-3295583", "R-HSA-3295583", "R-HSA-9856530", "R-MMU-3295583", "R-MMU-9856530", "R-RNO-3295583", "R-RNO-9856530" ]
[ "REACTOME:R-CFA-3295583", "REACTOME:R-HSA-3295583", "REACTOME:R-HSA-9856530", "REACTOME:R-MMU-3295583", "REACTOME:R-MMU-9856530", "REACTOME:R-RNO-3295583", "REACTOME:R-RNO-9856530" ]
7
[ "2eta", "2etb", "2etc", "2f37", "2nyj", "2pnn", "3j5p", "3j5q", "3j5r", "3j9j", "3jxi", "3jxj", "3w9f", "3w9g", "4dx1", "4dx2", "4n5q", "5an8", "5hi9", "5irx", "5irz", "5is0", "6bbj", "6bo4", "6bo5", "6bwj", "6bwm", "6c8f", "6c8g", "6c8h", "6dvw", "6dvy"...
166
[ "PUB00054048", "PUB00054049", "PUB00054050", "PUB00054054", "PUB00100009" ]
[ "18535090", "20025796", "20861159", "19297520", "29464560" ]
[ "TRP channels entering the structural era.", "Structure-functional intimacies of transient receptor potential channels.", "The role of transient receptor potential cation channels in Ca2+ signaling.", "Pharmacology of vanilloid transient receptor potential cation channels.", "Transient Receptor Potential (T...
[ 2008, 2009, 2010, 2009, 2018 ]
5
[ "IPR024862" ]
[ "IPR008348" ]
1
1
0
[ "Opisthokonta" ]
[ 5065 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 25, 15, 18 ]
4
true
Family
Transient receptor potential cation channel subfamily V member 1-4
Transient receptor potential cation channel subfamily V member 1-4
TrpV1-4
8
IPR008348
8,348
Transient receptor potential cation channel subfamily V member 4
TrpV4
Family
1,890
false
false
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six ...
[ "GO:0005216", "GO:0006811", "GO:0016020" ]
[ "monoatomic ion channel activity", "monoatomic ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01769" ]
[ "VRL2RECEPTOR" ]
[ 1890 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-3295583", "R-HSA-9856530", "R-MMU-3295583", "R-MMU-9856530", "R-RNO-3295583", "R-RNO-9856530" ]
[ "REACTOME:R-HSA-3295583", "REACTOME:R-HSA-9856530", "REACTOME:R-MMU-3295583", "REACTOME:R-MMU-9856530", "REACTOME:R-RNO-3295583", "REACTOME:R-RNO-9856530" ]
6
[ "6bbj", "8fc7", "8fc8", "8fc9", "8fca", "8fcb", "8j1b", "8j1d", "8j1f", "8j1h", "8jkm", "9iqx", "9iqy" ]
13
[ "PUB00011598", "PUB00054048", "PUB00054049", "PUB00054050", "PUB00054054", "PUB00056698", "PUB00056699", "PUB00056700", "PUB00100009", "PUB00100016", "PUB00100017", "PUB00100018", "PUB00100019", "PUB00100020" ]
[ "11081638", "18535090", "20025796", "20861159", "19297520", "11827975", "12151520", "17233610", "29464560", "21336783", "29899501", "18695040", "18826956", "31493693" ]
[ "Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor.", "TRP channels entering the structural era.", "Structure-functional intimacies of transient receptor potential channels.", "The role of transient receptor potential cation channels in Ca2+ signaling.", ...
[ 2000, 2008, 2009, 2010, 2009, 2002, 2002, 2007, 2018, 2011, 2018, 2008, 2008, 2020 ]
14
[ "IPR008347" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1890 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 5, 5 ]
4
true
Family
Transient receptor potential cation channel subfamily V member 4
Transient receptor potential cation channel subfamily V member 4
TrpV4
4
IPR008349
8,349
Mitogen-activated protein (MAP) kinase, ERK1/2
MAPK_ERK1/2
Family
3,247
false
false
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra...
[ "GO:0004707", "GO:0005524", "GO:0006468" ]
[ "MAP kinase activity", "ATP binding", "protein phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR01770" ]
[ "ERK1ERK2MAPK" ]
[ 3247 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.24", "R-BTA-111995", "R-BTA-112409", "R-BTA-112411", "R-BTA-1181150", "R-BTA-1295596", "R-BTA-1502540", "R-BTA-162658", "R-BTA-170968", "R-BTA-198753", "R-BTA-202670", "R-BTA-2029482", "R-BTA-2173795", "R-BTA-2173796", "R-BTA-2559580", "R-BTA-2559582", "R-BTA-2559585", "R-B...
[ "EC:2.7.11.24", "REACTOME:R-BTA-111995", "REACTOME:R-BTA-112409", "REACTOME:R-BTA-112411", "REACTOME:R-BTA-1181150", "REACTOME:R-BTA-1295596", "REACTOME:R-BTA-1502540", "REACTOME:R-BTA-162658", "REACTOME:R-BTA-170968", "REACTOME:R-BTA-198753", "REACTOME:R-BTA-202670", "REACTOME:R-BTA-2029482",...
281
[ "1gol", "1pme", "1tvo", "1wzy", "2erk", "2fys", "2gph", "2ojg", "2oji", "2ojj", "2y9q", "2z7l", "2zoq", "3c9w", "3erk", "3i5z", "3i60", "3o71", "3qyw", "3qyz", "3r63", "3sa0", "3tei", "3w55", "3zu7", "3zuv", "4erk", "4fmq", "4fux", "4fuy", "4fv0", "4fv1"...
235
[ "PUB00005115", "PUB00007546", "PUB00011603", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]
[ "3291115", "8607979", "10487205", "12368087", "12471243", "15078142", "15320712" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Dynamics and organization of MAP kinase signal pathways.", "The stress-activated protein kinase pathways.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the huma...
[ 1988, 1995, 1999, 2002, 2002, 2004, 2004 ]
7
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3247 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 3, 16, 10, 6 ]
6
true
Family
Mitogen-activated protein (MAP) kinase, ERK1/2
Mitogen-activated protein (MAP) kinase, ERK1/2
MAPK_ERK1/2
6
IPR008350
8,350
Mitogen-activated protein (MAP) kinase, ERK3/4
MAPK_ERK3/4
Family
2,222
false
false
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra...
[ "GO:0004707", "GO:0005524", "GO:0006468" ]
[ "MAP kinase activity", "ATP binding", "protein phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR01771" ]
[ "ERK3ERK4MAPK" ]
[ 2222 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.11.24", "R-GGA-5687128", "R-HSA-5687128", "R-MMU-5687128", "R-RNO-5687128" ]
[ "EC:2.7.11.24", "REACTOME:R-GGA-5687128", "REACTOME:R-HSA-5687128", "REACTOME:R-MMU-5687128", "REACTOME:R-RNO-5687128" ]
5
[ "6yky", "6ylc", "6yll", "7aqb" ]
4
[ "PUB00005115", "PUB00011603", "PUB00011604", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]
[ "3291115", "10487205", "10657254", "12368087", "12471243", "15078142", "15320712" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "The stress-activated protein kinase pathways.", "Cloning and characterization of mouse extracellular-signal-regulated protein kinase 3 as a unique gene product of 100 kDa.", "Evolution of protein kinase signaling...
[ 1988, 1999, 2000, 2002, 2002, 2004, 2004 ]
7
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2222 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 6, 7, 6 ]
4
true
Family
Mitogen-activated protein (MAP) kinase, ERK3/4
Mitogen-activated protein (MAP) kinase, ERK3/4
MAPK_ERK3/4
3
IPR008351
8,351
Mitogen-activated protein (MAP) kinase, JNK
MAPK_JNK
Family
8,083
false
false
MAP (Mitogen Activated Protein) kinases participate in kinase cascades, whereby at least 3 protein kinases act in series, culminating in activation of MAP kinase [ ]. MAP kinases are activated by dual phosphorylation on both tyrosine and threonine residues of a conserved TXY motif. JNK (Jun N-terminal Kinase), also kno...
[ "GO:0004707", "GO:0005524", "GO:0006468" ]
[ "MAP kinase activity", "ATP binding", "protein phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR01772" ]
[ "JNKMAPKINASE" ]
[ 8083 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.24", "R-CEL-193648", "R-CEL-2559580", "R-CEL-2871796", "R-CEL-450321", "R-CEL-450341", "R-CEL-9007892", "R-DME-193648", "R-DME-209397", "R-DME-209409", "R-DME-209425", "R-DME-209459", "R-DME-2559580", "R-DME-2871796", "R-DME-450321", "R-DME-450341", "R-DME-9007892", "R-DRE-...
[ "EC:2.7.11.24", "REACTOME:R-CEL-193648", "REACTOME:R-CEL-2559580", "REACTOME:R-CEL-2871796", "REACTOME:R-CEL-450321", "REACTOME:R-CEL-450341", "REACTOME:R-CEL-9007892", "REACTOME:R-DME-193648", "REACTOME:R-DME-209397", "REACTOME:R-DME-209409", "REACTOME:R-DME-209425", "REACTOME:R-DME-209459", ...
58
[ "1jnk", "1pmn", "1pmu", "1pmv", "1ukh", "1uki", "2b1p", "2exc", "2g01", "2gmx", "2h96", "2no3", "2o0u", "2o2u", "2ok1", "2p33", "2r9s", "2waj", "2xrw", "2xs0", "2zdt", "2zdu", "3cgf", "3cgo", "3da6", "3e7o", "3elj", "3fi2", "3fi3", "3fv8", "3g90", "3g9l"...
108
[ "PUB00008480", "PUB00011603", "PUB00060226", "PUB00075320" ]
[ "11790549", "10487205", "12074577", "25500773" ]
[ "The JNK signal transduction pathway.", "The stress-activated protein kinase pathways.", "Isolation of novel rice (Oryza sativa L.) multiple stress responsive MAP kinase gene, OsMSRMK2, whose mRNA accumulates rapidly in response to environmental cues.", "The JNK-like MAPK KGB-1 of Caenorhabditis elegans promo...
[ 2002, 1999, 2002, 2014 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 8083 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 3, 67, 3, 49, 22, 1, 26, 5 ]
8
true
Family
Mitogen-activated protein (MAP) kinase, JNK
Mitogen-activated protein (MAP) kinase, JNK
MAPK_JNK
1
IPR008352
8,352
Mitogen-activated protein (MAP) kinase HOG-like
MAPK_HOG-like
Family
9,400
false
false
This entry represents MAP kinases including HOG1, MAP 14/13/12 and similar MAP kinases. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription [ ]. The HOG pathway is mediated b...
[ "GO:0004707", "GO:0005524", "GO:0006468" ]
[ "MAP kinase activity", "ATP binding", "protein phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR01773" ]
[ "P38MAPKINASE" ]
[ 9400 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.24", "R-CEL-168638", "R-CEL-171007", "R-CEL-198753", "R-CEL-2559580", "R-CEL-418592", "R-CEL-432142", "R-CEL-4420097", "R-CEL-450302", "R-CEL-450341", "R-CEL-525793", "R-CEL-5675221", "R-CEL-6798695", "R-CFA-168638", "R-CFA-198753", "R-CFA-418592", "R-CFA-432142", "R-CFA-44...
[ "EC:2.7.11.24", "REACTOME:R-CEL-168638", "REACTOME:R-CEL-171007", "REACTOME:R-CEL-198753", "REACTOME:R-CEL-2559580", "REACTOME:R-CEL-418592", "REACTOME:R-CEL-432142", "REACTOME:R-CEL-4420097", "REACTOME:R-CEL-450302", "REACTOME:R-CEL-450341", "REACTOME:R-CEL-525793", "REACTOME:R-CEL-5675221", ...
163
[ "1a9u", "1bl6", "1bl7", "1bmk", "1cm8", "1di9", "1ian", "1kv1", "1kv2", "1lew", "1lez", "1m7q", "1ouk", "1ouy", "1ove", "1oz1", "1r39", "1r3c", "1w7h", "1w82", "1w83", "1w84", "1wbn", "1wbo", "1wbs", "1wbt", "1wbv", "1wbw", "1wfc", "1yqj", "1yw2", "1ywr"...
403
[ "PUB00005115", "PUB00011603", "PUB00011605", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00085486", "PUB00088415" ]
[ "3291115", "10487205", "12452429", "12368087", "12471243", "15078142", "15320712", "16778768", "29085028" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "The stress-activated protein kinase pathways.", "In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance.", "Evolution of protein kinase signaling from yeast to man.", "The prote...
[ 1988, 1999, 2002, 2002, 2002, 2004, 2004, 2006, 2017 ]
9
[ "IPR050117" ]
[ "IPR038783", "IPR038784", "IPR038785", "IPR038786" ]
1
4
0
[ "Eukaryota" ]
[ 9400 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 4, 15, 3, 17, 12, 2, 22, 1, 2 ]
9
true
Family
Mitogen-activated protein (MAP) kinase HOG-like
Mitogen-activated protein (MAP) kinase HOG-like
MAPK_HOG-like
5
IPR008353
8,353
Peptidase S1B, exfoliative toxin
Peptidase_S1B_tx
Family
745
false
false
This group of serine peptidases belong to MEROPS peptidase family S1, subfamily S1B (clan PA(S)). The type example is glutamyl endopeptidase I of Staphylococcus aureus, a well-characterised and specialised human pathogen expressing a variety of virulence factors to enable successful infection of the host. Symptoms usua...
[ "GO:0004252", "GO:0006508" ]
[ "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR01774" ]
[ "EXFOLTOXIN" ]
[ 745 ]
1
[ "EC", "METACYC" ]
[ "3.4.21.-", "PWY-7884" ]
[ "EC:3.4.21.-", "METACYC:PWY-7884" ]
2
[ "1agj", "1dt2", "1dua", "1due", "1exf", "1qtf", "1qy6", "1wcz", "2as9", "2o8l", "2vid", "2w7s", "2w7u", "3ufa", "4jcn", "4k1s", "4k1t", "4mvn", "5c2z", "5mm8", "6e0u", "6pym", "6q12", "6q24", "6tya", "6u1b", "6yv5", "6yv6", "8dax", "8t3i", "8t3j", "9bsh"...
35
[ "PUB00011606", "PUB00011608", "PUB00011609" ]
[ "10627489", "11544350", "10194458" ]
[ "Exotoxins of Staphylococcus aureus.", "Toxic shock syndrome and bacterial superantigens: an update.", "Clinical, microbial, and biochemical aspects of the exfoliative toxins causing staphylococcal scalded-skin syndrome." ]
[ 2000, 2001, 1999 ]
3
[ "IPR008256" ]
[]
1
0
1
[ "Bacteria", "Bilateria", "Caudoviricetes", "Methanosarcina", "human gut metagenome" ]
[ 729, 2, 7, 6, 1 ]
5
[]
[]
0
true
Family
Peptidase S1B, exfoliative toxin
Peptidase S1B, exfoliative toxin
Peptidase_S1B_tx
4
IPR008356
8,356
Protein-tyrosine phosphatase, KIM-containing
Tyr_Pase_KIM-con
Family
4,386
false
false
Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is ...
[ "GO:0004725", "GO:0006470" ]
[ "protein tyrosine phosphatase activity", "protein dephosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR01778", "PTHR46198" ]
[ "KIMPTPASE", "" ]
[ 3801, 4379 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3.48", "R-HSA-5675221", "R-HSA-9008059", "R-MMU-5675221", "R-RNO-5675221" ]
[ "EC:3.1.3.48", "REACTOME:R-HSA-5675221", "REACTOME:R-HSA-9008059", "REACTOME:R-MMU-5675221", "REACTOME:R-RNO-5675221" ]
5
[ "1jln", "1zc0", "2a3k", "2a8b", "2bij", "2bv5", "2cjz", "2gp0", "2hvl", "2qdc", "2qdm", "2qdp", "3d42", "3d44", "3o4s", "3o4t", "3o4u", "5ovr", "5ovx", "5ow1", "6h8r", "6h8s", "8sls", "8slt", "8slu", "9eex", "9eey", "9eez" ]
28
[ "PUB00011676", "PUB00035793", "PUB00035794", "PUB00035795", "PUB00035796", "PUB00035797", "PUB00035798" ]
[ "9857190", "9818190", "14625689", "12678841", "16672235", "8948575", "9646865" ]
[ "PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.", "Protein tyrosine phosphatases: mechanisms of catalysis and regulation.", "Receptor and nonreceptor protein tyrosine phosphatase...
[ 1998, 1998, 2003, 2003, 2006, 1996, 1998 ]
7
[]
[ "IPR016334" ]
0
1
0
[ "Opisthokonta" ]
[ 4386 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 2, 33, 13, 23 ]
5
true
Family
Protein-tyrosine phosphatase, KIM-containing
Protein-tyrosine phosphatase, KIM-containing
Tyr_Pase_KIM-con
1
IPR008357
8,357
Lantibiotic leader peptide-processing serine protease
Lanit_process
Family
309
false
false
Lantibiotic genes reside on the bacterial chromosome, where they cluster with genes that adapt and secrete them to the extracellular space. Many of these so-called 'pathogenicity islands' have been characterised, including the epidermin (epi) cluster in Staphylococcus epidermis, and the nisin (nis) cluster in Lactococc...
[ "GO:0004252", "GO:0006508" ]
[ "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "PRINTS", "CDD" ]
[ "PIRSF037875", "PR01779", "cd07482" ]
[ "Peptidase_S8_lp", "LANTIPROCESS", "Peptidases_S8_Lantibiotic_specific_protease" ]
[ 137, 242, 236 ]
3
[]
[]
[]
0
[ "3qfh", "3t41", "4mzd" ]
3
[ "PUB00011677", "PUB00011678", "PUB00011679", "PUB00081192", "PUB00081193" ]
[ "11133423", "12066186", "8478324", "8550430", "10473390" ]
[ "The group I strain of Streptococcus mutans, UA140, produces both the lantibiotic mutacin I and a nonlantibiotic bacteriocin, mutacin IV.", "Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis.", "Characterization of the Lactococcus lactis nisin A operon genes nis...
[ 2001, 2002, 1993, 1996, 1999 ]
5
[ "IPR015500" ]
[]
1
0
1
[ "Bacteria" ]
[ 309 ]
1
[]
[]
0
true
Family
Lantibiotic leader peptide-processing serine protease
Lantibiotic leader peptide-processing serine protease
Lanit_process
6
IPR008358
8,358
Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB
Sig_transdc_His_kin/Pase_MprB
Family
2,031
false
false
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt...
[ "GO:0000155", "GO:0004673", "GO:0000160", "GO:0016020" ]
[ "phosphorelay sensor kinase activity", "protein histidine kinase activity", "phosphorelay signal transduction system", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01780" ]
[ "LANTIREGPROT" ]
[ 2031 ]
1
[]
[]
[]
0
[]
0
[ "PUB00000966", "PUB00007866", "PUB00010651", "PUB00011096", "PUB00011679", "PUB00011680", "PUB00013246", "PUB00013247", "PUB00013562", "PUB00013563", "PUB00020801", "PUB00042804", "PUB00042805", "PUB00042806", "PUB00042807" ]
[ "9989504", "11406410", "12372152", "10966457", "8478324", "8161176", "8868347", "10426948", "8029829", "1482126", "11145881", "16176121", "18076326", "11934609", "11489844" ]
[ "Structure of CheA, a signal-transducing histidine kinase.", "Histidine kinases and response regulator proteins in two-component signaling systems.", "Histidine protein kinases: key signal transducers outside the animal kingdom.", "Two-component signal transduction.", "Characterization of the Lactococcus la...
[ 1999, 2001, 2002, 2000, 1993, 1994, 1996, 1999, 1994, 1992, 2000, 2005, 2007, 2002, 2001 ]
15
[]
[]
0
0
null
[ "Bacteria", "Ichthyophthirius multifiliis", "Siphoviridae sp. cto3L1", "metagenomes" ]
[ 2016, 1, 1, 13 ]
4
[]
[]
0
true
Family
Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB
Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB
Sig_transdc_His_kin/Pase_MprB
9
IPR008359
8,359
Linker-for-activation of T cells (LAT) protein
Linker_for_activat_Tcells_prot
Family
370
false
false
A key event in the regulation of the adaptive immune response is the binding of major histocompatibility complex (MHC)-peptide complexes to T cell antigen receptors (TCRs). The formation of such ternary complexes induces significant biochemical changes within T cells of the host animal. The first detectable response of...
[ "GO:0007165", "GO:0016020" ]
[ "signal transduction", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF15234", "PR01781", "PTHR15586" ]
[ "LAT", "LATPROTEIN", "" ]
[ 370, 313, 350 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-114604", "R-HSA-202433", "R-HSA-2424491", "R-HSA-2454202", "R-HSA-2871796", "R-HSA-2871809", "R-HSA-5673001", "R-MMU-114604", "R-MMU-202433", "R-MMU-2424491", "R-MMU-2454202", "R-MMU-2871796", "R-MMU-2871809", "R-MMU-5673001", "R-RNO-114604", "R-RNO-202433", "R-RNO-2424491", ...
[ "REACTOME:R-HSA-114604", "REACTOME:R-HSA-202433", "REACTOME:R-HSA-2424491", "REACTOME:R-HSA-2454202", "REACTOME:R-HSA-2871796", "REACTOME:R-HSA-2871809", "REACTOME:R-HSA-5673001", "REACTOME:R-MMU-114604", "REACTOME:R-MMU-202433", "REACTOME:R-MMU-2424491", "REACTOME:R-MMU-2454202", "REACTOME:R-...
21
[]
0
[ "PUB00011681" ]
[ "11756537" ]
[ "Effect of redox balance alterations on cellular localization of LAT and downstream T-cell receptor signaling pathways." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Euteleostomi" ]
[ 370 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 6, 6 ]
3
true
Family
Linker-for-activation of T cells (LAT) protein
Linker-for-activation of T cells (LAT) protein
Linker_for_activat_Tcells_prot
7
IPR008361
8,361
Melanin-concentrating hormone receptor
MCH_rcpt
Family
1,340
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01783" ]
[ "MCHRECEPTOR" ]
[ 1340 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-375276", "R-HSA-416476", "R-HSA-418594", "R-HSA-5620922", "R-MMU-375276", "R-MMU-416476", "R-MMU-418594", "R-MMU-5620922", "R-RNO-375276", "R-RNO-416476", "R-RNO-418594", "R-RNO-5620922", "R-SSC-375276", "R-SSC-416476", "R-SSC-418594", "R-SSC-5620922" ]
[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-5620922", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-5620922", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418594", "REACTOME:R-RNO-5...
16
[ "8wss", "8wst", "8wwh", "8wwi", "8wwj", "8wwk", "8wwl", "8wwm", "8wwn", "8yns", "8ynt" ]
11
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00007849", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "2111655", "2830256", "8386361", "8170923", "10421368", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "Molecular characterization of the melanin-concentrating-hormone receptor.", "The G protei...
[ 1990, 1988, 1993, 1994, 1999, 2003, 1994, 2005, 2009, 2006, 2013 ]
11
[ "IPR000276" ]
[ "IPR004047", "IPR008362" ]
1
2
0
[ "Deuterostomia" ]
[ 1340 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 5, 1, 1 ]
4
true
Family
Melanin-concentrating hormone receptor
Melanin-concentrating hormone receptor
MCH_rcpt
1
IPR008362
8,362
Melanin-concentrating hormone receptor 2
MCHR2
Family
313
false
false
This entry represents a group of proteins from vertebrates, including human Melanin-concentrating hormone receptor 2 (MCHR2 or MCH2). Melanin-concentrating hormone (MCH) is a cyclic peptide originally identified in teleost fish [ ]. In fish, MCH is released from the pituitary and causes lightening of skin pigment cells...
[ "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS", "CDD" ]
[ "PR01784", "cd15339" ]
[ "MCH2RECEPTOR", "7tmA_MCHR2" ]
[ 311, 229 ]
2
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME" ]
[ "281", "R-HSA-375276", "R-HSA-416476", "R-HSA-418594" ]
[ "IUPHAR:281", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594" ]
4
[ "8wst" ]
1
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00007849", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00087043", "PUB00087044", "PUB00092609", "PUB00092610", "PUB00092615", "PUB00092616", "PUB00092621", "PUB000926...
[ "2111655", "2830256", "8386361", "8170923", "10421368", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293", "23237917", "18957321", "20940434", "22503476", "24386514", "23140243", "19458711", "23251911", "22032986", "23407534", "22975406", "23445222", ...
[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "Molecular characterization of the melanin-concentrating-hormone receptor.", "The G protei...
[ 1990, 1988, 1993, 1994, 1999, 2003, 1994, 2005, 2009, 2006, 2013, 2013, 2008, 2010, 2012, 2013, 2013, 2009, 2012, 2012, 2013, 2013, 2013, 2005 ]
24
[ "IPR008361" ]
[]
1
0
1
[ "Chordata" ]
[ 313 ]
1
[ "Danio rerio", "Homo sapiens" ]
[ 4, 1 ]
2
true
Family
Melanin-concentrating hormone receptor 2
Melanin-concentrating hormone receptor 2
MCHR2
3
IPR008363
8,363
Paraoxonase1
Paraoxonase1
Family
220
false
false
The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysis of the toxic metabolites of a variety of organophosphorus insecticides. The enzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenyl acetate), and hence...
[ "GO:0004064", "GO:0005576" ]
[ "arylesterase activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01786" ]
[ "PARAOXONASE1" ]
[ 220 ]
1
[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.1.2", "3.1.1.81", "3.1.8.1", "PWY-5489", "PWY-5490", "PWY-8065", "R-HSA-2142688", "R-HSA-9754706", "R-MMU-2142688", "R-MMU-9754706", "R-RNO-2142688", "R-RNO-9754706" ]
[ "EC:3.1.1.2", "EC:3.1.1.81", "EC:3.1.8.1", "METACYC:PWY-5489", "METACYC:PWY-5490", "METACYC:PWY-8065", "REACTOME:R-HSA-2142688", "REACTOME:R-HSA-9754706", "REACTOME:R-MMU-2142688", "REACTOME:R-MMU-9754706", "REACTOME:R-RNO-2142688", "REACTOME:R-RNO-9754706" ]
12
[ "1v04", "3sre", "3srg", "4hho", "4hhq", "4q1u", "6g82", "6gmu", "6h0a", "9r0q" ]
10
[ "PUB00001973", "PUB00007849", "PUB00011231", "PUB00011685" ]
[ "8661009", "10421368", "11038162", "7749820" ]
[ "The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family.", "Molecular characterization of the melanin-concentrating-hormone receptor.", "Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters.", "A polymorphism of the paraoxonase gene a...
[ 1996, 1999, 2000, 1995 ]
4
[ "IPR002640" ]
[]
1
0
1
[ "Eutheria" ]
[ 220 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 6 ]
3
true
Family
Paraoxonase1
Paraoxonase1
Paraoxonase1
3
IPR008364
8,364
Paraoxonase2
Paraoxonase2
Family
508
false
false
The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysis of the toxic metabolites of a variety of organophosphorus insecticides. The enzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenyl acetate), and hence...
[ "GO:0004064", "GO:0005576" ]
[ "arylesterase activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01787" ]
[ "PARAOXONASE2" ]
[ 508 ]
1
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.1.2", "3.1.1.81", "R-BTA-2142688", "R-HSA-2142688", "R-HSA-9754706", "R-MMU-2142688", "R-MMU-9754706", "R-RNO-2142688", "R-RNO-9754706" ]
[ "EC:3.1.1.2", "EC:3.1.1.81", "REACTOME:R-BTA-2142688", "REACTOME:R-HSA-2142688", "REACTOME:R-HSA-9754706", "REACTOME:R-MMU-2142688", "REACTOME:R-MMU-9754706", "REACTOME:R-RNO-2142688", "REACTOME:R-RNO-9754706" ]
9
[]
0
[ "PUB00001973", "PUB00011231" ]
[ "8661009", "11038162" ]
[ "The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family.", "Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters." ]
[ 1996, 2000 ]
2
[ "IPR002640" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 508 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 2, 6 ]
3
true
Family
Paraoxonase2
Paraoxonase2
Paraoxonase2
2
IPR008365
8,365
Prostanoid receptor
Prostanoid_rcpt
Family
9,000
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR01788", "PTHR11866" ]
[ "PROSTANOIDR", "" ]
[ 8010, 8681 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-391908", "R-BTA-416476", "R-BTA-416482", "R-BTA-418594", "R-BTA-428930", "R-CFA-391908", "R-CFA-416476", "R-HSA-391908", "R-HSA-392851", "R-HSA-416476", "R-HSA-416482", "R-HSA-418555", "R-HSA-418594", "R-HSA-428930", "R-MMU-391908", "R-MMU-392851", "R-MMU-416476", "R-MMU-416...
[ "REACTOME:R-BTA-391908", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-416482", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-428930", "REACTOME:R-CFA-391908", "REACTOME:R-CFA-416476", "REACTOME:R-HSA-391908", "REACTOME:R-HSA-392851", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-416482", "REACTOME:R-HSA-418...
29
[ "5yhl", "5ywy", "6ak3", "6iiu", "6iiv", "6m9t", "7cx2", "7cx3", "7cx4", "7d7m", "7wu9", "8gcm", "8gcp", "8gd9", "8gda", "8gdb", "8gdc", "8iq4", "8iq6", "8iuk", "8iul", "8ium", "8x79", "8x7a", "8xjk", "8xjl", "8xjm", "8xjn", "8xjo", "8zvz", "8zw0", "9au0"...
44
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "2111655", "2830256", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "The G protein-coupled receptor repertoires of human and mouse.", "GCRDb: a G-protein-coup...
[ 1990, 1988, 1993, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
10
[ "IPR000276" ]
[ "IPR000141", "IPR000370", "IPR000376", "IPR001105", "IPR001244", "IPR001923" ]
1
6
0
[ "Eukaryota" ]
[ 9000 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 26, 2, 31, 27, 37 ]
5
true
Family
Prostanoid receptor
Prostanoid receptor
Prostanoid_rcpt
2
IPR008366
8,366
Nuclear factor of activated T cells (NFAT)
NFAT
Family
8,806
false
false
Antigenic stimulation of T lymphocytes initiates a complex series of intracellular signal transduction pathways that leads to the expression of a panel of immunoregulatory genes, whose function is critical to the initiation and coordination of the immune response. The multi-subunit nuclear factor of activated T cells (...
[ "GO:0003700", "GO:0006355" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR01789", "PTHR12533" ]
[ "NUCFACTORATC", "" ]
[ 7316, 8798 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2025928", "R-HSA-2871809", "R-HSA-4086398", "R-HSA-5607763", "R-HSA-8877330", "R-MMU-2025928", "R-MMU-2871809", "R-MMU-4086398", "R-MMU-5607763", "R-RNO-2025928", "R-RNO-2871809", "R-RNO-5607763" ]
[ "REACTOME:R-HSA-2025928", "REACTOME:R-HSA-2871809", "REACTOME:R-HSA-4086398", "REACTOME:R-HSA-5607763", "REACTOME:R-HSA-8877330", "REACTOME:R-MMU-2025928", "REACTOME:R-MMU-2871809", "REACTOME:R-MMU-4086398", "REACTOME:R-MMU-5607763", "REACTOME:R-RNO-2025928", "REACTOME:R-RNO-2871809", "REACTOM...
12
[ "1a02", "1a66", "1imh", "1nfa", "1owr", "1p7h", "1pzu", "1s9k", "2as5", "2o93", "2yrp", "3qrf", "8ow4", "8r07", "8r3f" ]
15
[ "PUB00011687" ]
[ "10652349" ]
[ "Identification of amino acid residues and protein kinases involved in the regulation of NFATc subcellular localization." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Metazoa" ]
[ 8806 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 37, 8, 34, 48, 29 ]
5
true
Family
Nuclear factor of activated T cells (NFAT)
Nuclear factor of activated T cells (NFAT)
NFAT
9
IPR008367
8,367
Regucalcin
Regucalcin
Family
2,543
false
false
Regucalcin, also known as senesence marker protein-30 (SMP30), was discovered in 1978 as a Ca 2+ binding protein that does not contain EF-hand motifs, suggesting a novel class of Ca 2+ binding protein. It is primarily localised to the liver and kidney cortex of animals. Expression of its mRNA in the liver and renal cor...
[ "GO:0005509", "GO:0030234" ]
[ "calcium ion binding", "enzyme regulator activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR01791" ]
[ "REGUCALCIN" ]
[ 2543 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "3.1.1.17", "PWY-2221", "PWY-5530", "PWY-7165", "PWY-8142" ]
[ "EC:3.1.1.17", "METACYC:PWY-2221", "METACYC:PWY-5530", "METACYC:PWY-7165", "METACYC:PWY-8142" ]
5
[ "3g4e", "3g4h", "4gn7", "4gn8", "4gn9", "4gna", "4gnb", "4gnc" ]
8
[ "PUB00011463", "PUB00011526", "PUB00011527", "PUB00018983", "PUB00018984", "PUB00018985", "PUB00018986" ]
[ "1315924", "8232287", "9278268", "8348951", "1618342", "2177680", "9586564" ]
[ "Reversible effect of calcium-binding protein regucalcin on the Ca(2+)-induced inhibition of deoxyuridine 5'-triphosphatase activity in rat liver cytosol.", "Regulatory effect of regucalcin on (Ca(2+)-Mg2+)-ATPase in rat liver plasma membranes: comparison with the activation by Mn2+ and Co2+.", "Inhibitory effe...
[ 1992, 1993, 1997, 1993, 1992, 1990, 1998 ]
7
[ "IPR005511" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Halobacteriales", "ecological metagenomes" ]
[ 359, 2163, 7, 14 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 1, 3 ]
4
true
Family
Regucalcin
Regucalcin
Regucalcin
9
IPR008368
8,368
Voltage-dependent calcium channel, gamma subunit
VDCC_gsu
Family
6,391
false
false
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d...
[ "GO:0006816", "GO:0016020" ]
[ "calcium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01792" ]
[ "VDCCGAMMA" ]
[ 6391 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-399719", "R-BTA-5682910", "R-HSA-112308", "R-HSA-399719", "R-HSA-5576892", "R-HSA-5576893", "R-HSA-5682910", "R-HSA-9856532", "R-MMU-112308", "R-MMU-399719", "R-MMU-5576892", "R-MMU-5576893", "R-MMU-5682910", "R-RNO-112308", "R-RNO-399719", "R-RNO-5576892", "R-RNO-5576893", ...
[ "REACTOME:R-BTA-399719", "REACTOME:R-BTA-5682910", "REACTOME:R-HSA-112308", "REACTOME:R-HSA-399719", "REACTOME:R-HSA-5576892", "REACTOME:R-HSA-5576893", "REACTOME:R-HSA-5682910", "REACTOME:R-HSA-9856532", "REACTOME:R-MMU-112308", "REACTOME:R-MMU-399719", "REACTOME:R-MMU-5576892", "REACTOME:R-M...
18
[ "3jbr", "5gjv", "5gjw", "5kbs", "5kbt", "5kbu", "5kk2", "5vot", "5vou", "5vov", "5weo", "6dlz", "6dm0", "6dm1", "6jp5", "6jp8", "6jpa", "6jpb", "6njl", "6njm", "6njn", "6o9g", "6qkc", "6qkz", "7jpk", "7jpl", "7jpv", "7jpw", "7jpx", "7ldd", "7lde", "7lep"...
127
[ "PUB00007806", "PUB00036034" ]
[ "11170751", "14657414" ]
[ "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family.", "International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels." ]
[ 2001, 2003 ]
2
[ "IPR004031" ]
[ "IPR005421", "IPR005422", "IPR005423", "IPR008369", "IPR008370", "IPR008371", "IPR008372" ]
1
7
0
[ "Bilateria" ]
[ 6391 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 23, 14, 23, 20 ]
4
true
Family
Voltage-dependent calcium channel, gamma subunit
Voltage-dependent calcium channel, gamma subunit
VDCC_gsu
1
IPR008369
8,369
Voltage-dependent calcium channel, gamma-5 subunit
VDCC_g5su
Family
959
false
false
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d...
[ "GO:0006816", "GO:0016020" ]
[ "calcium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01793" ]
[ "VDCCGAMMA5" ]
[ 959 ]
1
[]
[]
[]
0
[ "7ryy", "7rz4", "7rz5", "7rz6", "7rz7", "7rz8", "8ss2", "8ss3", "8ss4", "8ss5", "8ss6", "8ss7", "8ss8", "8ss9", "8ssa", "8ssb" ]
16
[ "PUB00007806", "PUB00036034" ]
[ "11170751", "14657414" ]
[ "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family.", "International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels." ]
[ 2001, 2003 ]
2
[ "IPR008368" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 959 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 3, 2 ]
4
true
Family
Voltage-dependent calcium channel, gamma-5 subunit
Voltage-dependent calcium channel, gamma-5 subunit
VDCC_g5su
7
IPR008370
8,370
Voltage-dependent calcium channel, gamma-6 subunit
VDCC_g6su
Family
398
false
false
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d...
[ "GO:0006816", "GO:0016020" ]
[ "calcium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01794" ]
[ "VDCCGAMMA6" ]
[ 398 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5576892", "R-HSA-5576893", "R-MMU-5576892", "R-MMU-5576893", "R-RNO-5576892", "R-RNO-5576893" ]
[ "REACTOME:R-HSA-5576892", "REACTOME:R-HSA-5576893", "REACTOME:R-MMU-5576892", "REACTOME:R-MMU-5576893", "REACTOME:R-RNO-5576892", "REACTOME:R-RNO-5576893" ]
6
[]
0
[ "PUB00007806", "PUB00036034" ]
[ "11170751", "14657414" ]
[ "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family.", "International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels." ]
[ 2001, 2003 ]
2
[ "IPR008368" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 398 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 4, 3 ]
3
true
Family
Voltage-dependent calcium channel, gamma-6 subunit
Voltage-dependent calcium channel, gamma-6 subunit
VDCC_g6su
2
IPR008371
8,371
Voltage-dependent calcium channel, gamma-7 subunit
VDCC_g7su
Family
654
false
false
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d...
[ "GO:0006816", "GO:0016020" ]
[ "calcium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01795" ]
[ "VDCCGAMMA7" ]
[ 654 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5576892", "R-HSA-5576893", "R-HSA-9856532", "R-MMU-5576892", "R-MMU-5576893", "R-RNO-5576892", "R-RNO-5576893" ]
[ "REACTOME:R-HSA-5576892", "REACTOME:R-HSA-5576893", "REACTOME:R-HSA-9856532", "REACTOME:R-MMU-5576892", "REACTOME:R-MMU-5576893", "REACTOME:R-RNO-5576892", "REACTOME:R-RNO-5576893" ]
7
[]
0
[ "PUB00007806", "PUB00036034" ]
[ "11170751", "14657414" ]
[ "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family.", "International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels." ]
[ 2001, 2003 ]
2
[ "IPR008368" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 654 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 2, 3, 2 ]
4
true
Family
Voltage-dependent calcium channel, gamma-7 subunit
Voltage-dependent calcium channel, gamma-7 subunit
VDCC_g7su
2
IPR008372
8,372
Voltage-dependent calcium channel, gamma-8 subunit
VDCC_g8su
Family
201
false
false
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d...
[ "GO:0006816", "GO:0016020" ]
[ "calcium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01796" ]
[ "VDCCGAMMA8" ]
[ 201 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-399719", "R-HSA-5576892", "R-HSA-5576893", "R-HSA-5682910", "R-MMU-399719", "R-MMU-5576892", "R-MMU-5576893", "R-MMU-5682910", "R-RNO-399719", "R-RNO-5576892", "R-RNO-5576893", "R-RNO-5682910" ]
[ "REACTOME:R-HSA-399719", "REACTOME:R-HSA-5576892", "REACTOME:R-HSA-5576893", "REACTOME:R-HSA-5682910", "REACTOME:R-MMU-399719", "REACTOME:R-MMU-5576892", "REACTOME:R-MMU-5576893", "REACTOME:R-MMU-5682910", "REACTOME:R-RNO-399719", "REACTOME:R-RNO-5576892", "REACTOME:R-RNO-5576893", "REACTOME:R...
12
[ "6qkc", "6qkz", "7ldd", "7lde", "7lep", "7oca", "7ocd", "7oce", "7ocf", "7qhb", "7qhh", "8ayl", "8aym", "8ayn", "8ayo" ]
15
[ "PUB00007806", "PUB00036034" ]
[ "11170751", "14657414" ]
[ "A cluster of three novel Ca2+ channel gamma subunit genes on chromosome 19q13.4: evolution and expression profile of the gamma subunit gene family.", "International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels." ]
[ 2001, 2003 ]
2
[ "IPR008368" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 201 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2 ]
3
true
Family
Voltage-dependent calcium channel, gamma-8 subunit
Voltage-dependent calcium channel, gamma-8 subunit
VDCC_g8su
4
IPR008373
8,373
Saposin
Saposin
Family
4,319
false
false
Sphingolipids are bioactive compounds found in lower and higher eukaryotes. They are involved in the regulation of various cellular functions, such as growth, differentiation and apoptosis, and are believed to be essential in a healthy diet. Sphigolipids are degraded in the lysosome, and the products from their hydroly...
[ "GO:0006665", "GO:0005764" ]
[ "sphingolipid metabolic process", "lysosome" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01797" ]
[ "SAPOSIN" ]
[ 4319 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5683826", "R-HSA-114608", "R-HSA-375276", "R-HSA-418594", "R-HSA-5683826", "R-HSA-5688031", "R-HSA-5688849", "R-HSA-5688890", "R-HSA-6798695", "R-HSA-9840310", "R-MMU-114608", "R-MMU-375276", "R-MMU-418594", "R-MMU-5683826", "R-MMU-6798695", "R-MMU-9840310", "R-RNO-114608", ...
[ "REACTOME:R-BTA-5683826", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-5683826", "REACTOME:R-HSA-5688031", "REACTOME:R-HSA-5688849", "REACTOME:R-HSA-5688890", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9840310", "REACTOME:R-MMU-114608", "REACTOME:R-...
22
[ "1m12", "1n69", "1sn6", "2dob", "2gtg", "2qyp", "2r0r", "2r1q", "2rb3", "2z9a", "3bqp", "3bqq", "3rfi", "4ddj", "4uex", "4v2o", "5nxb", "5u85", "6slr", "7p4t", "8equ", "9avs", "9axg", "9i63" ]
24
[ "PUB00011688", "PUB00011689" ]
[ "2515150", "2019586" ]
[ "Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats.", "Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease." ]
[ 1989, 1991 ]
2
[]
[ "IPR021165" ]
0
1
0
[ "Eukaryota", "Kangiella spongicola" ]
[ 4318, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 1, 1, 5, 4, 12, 28, 4, 18, 2 ]
9
true
Family
Saposin
Saposin
Saposin
9
IPR008374
8,374
SF-assemblin/beta-giardin
SF_assemblin/giardin_b
Family
2,145
false
false
Striated fibre assemblin (SFA), an acidic 33kDa protein, is the major component of striated microtubule-associated fibres (SMAFs) in the flagellar basal apparatus of green flagellates. In Chlamydomonas, and other green flagellates, the SMAFs form a cross-like pattern and run alongside the proximal parts of four bundles...
[ "GO:0005200" ]
[ "structural constituent of cytoskeleton" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF06705", "PR01799", "PTHR40412" ]
[ "SF-assemblin", "SFASSEMBLIN", "" ]
[ 2048, 467, 603 ]
3
[]
[]
[]
0
[]
0
[ "PUB00011691", "PUB00088847" ]
[ "8491776", "19214572" ]
[ "SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil.", "Changes in beta-giardin sequence of Giardia intestinalis sensitive and resistant to albendazole strains." ]
[ 1993, 2009 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 3, 2142 ]
2
[]
[]
0
true
Family
SF-assemblin/beta-giardin
SF-assemblin/beta-giardin
SF_assemblin/giardin_b
9
IPR008375
8,375
Staphylococcus aureus exotoxin
Staph_exotoxin
Family
447
false
false
Staphylococcus aureus is a well-characterised and specialised prokaryotic human pathogen, expressing a variety of virulence factors to enable successful infection of the host. Symptoms usually manifest in cases of food poisoning, pyrogenic fever and toxic shock syndrome, and can prove lethal in immunocompromised patien...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01800" ]
[ "STAPHEXOTOXN" ]
[ 447 ]
1
[]
[]
[]
0
[ "1m4v", "1ts2", "1ts4", "1ts5", "1v1o", "1v1p", "2ij0", "2qej", "2qil", "2r61", "2rdg", "2rdh", "2tss", "2z8l", "3kls", "3km9", "3mfg", "3o13", "3prx", "3r2i", "3r2t", "3tss", "3ury", "3v05", "4dxf", "4dxg", "4o1n", "4rco", "4rfb", "4rgt", "4rh6", "4tss"...
42
[ "PUB00011690" ]
[ "10899837" ]
[ "Identification of a novel gene cluster encoding staphylococcal exotoxin-like proteins: characterization of the prototypic gene and its protein product, SET1." ]
[ 2000 ]
1
[ "IPR013307" ]
[]
1
0
1
[ "Bacteria" ]
[ 447 ]
1
[]
[]
0
true
Family
Staphylococcus aureus exotoxin
Staphylococcus aureus exotoxin
Staph_exotoxin
7
IPR008376
8,376
Chaperone Ric-8 A/B
Chaperone_Ric-8_A/B
Domain
3,345
false
false
The chaperones Ric-8, also known as Synembryns, specifically bind and fold nascent G alpha proteins prior to G protein heterotrimer formation, promoting their stability and activity. Mammalian Chaperone Ric-8A assists the folding of GNAI1, GNAO1, GNA13 and GNAQ but doesn't fold Gα proteins GNAS nor GNAL [ ]. It also ac...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01802" ]
[ "SYNEMBRYN" ]
[ 3345 ]
1
[]
[]
[]
0
[ "6n85", "6n86", "6nmg", "6nmj", "6tyl", "6ukt", "6vu5", "6vu8", "8el7", "8el8" ]
10
[ "PUB00011692", "PUB00011693", "PUB00018998", "PUB00155427", "PUB00155473", "PUB00155474", "PUB00155475", "PUB00155476", "PUB00155477" ]
[ "10985349", "11102364", "12509430", "22114146", "16275912", "29844055", "31155309", "32103024", "36931277" ]
[ "RIC-8 (Synembryn): a novel conserved protein that is required for G(q)alpha signaling in the C. elegans nervous system.", "A role for RIC-8 (Synembryn) and GOA-1 (G(o)alpha) in regulating a subset of centrosome movements during early embryogenesis in Caenorhabditis elegans.", "Mammalian Ric-8A (synembryn) is a...
[ 2000, 2000, 2003, 2011, 2005, 2018, 2019, 2020, 2023 ]
9
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3345 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 19, 2, 7, 4, 11 ]
6
true
Domain
Chaperone Ric-8 A/B
Chaperone Ric-8 A/B
Chaperone_Ric-8_A/B
5
IPR008377
8,377
Trypanosome sialidase
Sialidase_trypan
Family
4,564
false
false
Trypanosoma cruzi is a kinetoplastid protozoan parasite of humans and other animals, the causative agent of Chagas disease. It is transmitted via an insect vector, and exists as an intracellular form, the amastigote, or as a trypomastigote form in the blood after infection. In the human host, chronic infection by T. cr...
[ "GO:0004308" ]
[ "exo-alpha-sialidase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01803" ]
[ "TCSIALIDASE" ]
[ 4564 ]
1
[ "EC" ]
[ "3.2.1.18" ]
[ "EC:3.2.1.18" ]
1
[ "1dil", "1dim", "1mr5", "1ms0", "1ms1", "1ms3", "1ms4", "1ms5", "1ms8", "1ms9", "1mz5", "1mz6", "1n1s", "1n1t", "1n1v", "1n1y", "1s0i", "1s0j", "1wcs", "2a75", "2ags", "2ah2", "2fhr", "2sil", "2sim", "3b69", "3opz", "3pjq", "3sil", "4bbw", "4fj6", "4q6k"...
42
[ "PUB00011694", "PUB00011695" ]
[ "2034687", "1695668" ]
[ "The major 85-kDa surface antigen of the mammalian-stage forms of Trypanosoma cruzi is a family of sialidases.", "The major 85-kD surface antigen of the mammalian form of Trypanosoma cruzi is encoded by a large heterogeneous family of simultaneously expressed genes." ]
[ 1991, 1990 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Iainarchaeum sp.", "Trypanosoma", "unclassified sequences" ]
[ 428, 1, 4129, 6 ]
4
[]
[]
0
true
Family
Trypanosome sialidase
Trypanosome sialidase
Sialidase_trypan
1
IPR008379
8,379
Band 4.1, C-terminal
Band_4.1_C
Domain
13,576
false
false
There is a unique sequence domain at the C terminus of all known 4.1 proteins, known as the C-terminal domain (CTD). Mammalian CTDs are associated with a growing number of protein-protein interactions, although such activities have yet to be associated with invertebrate CTDs. Mammalian CTDs are generally defined by seq...
[ "GO:0003779", "GO:0005198", "GO:0005856" ]
[ "actin binding", "structural molecule activity", "cytoskeleton" ]
[ "molecular_function", "molecular_function", "cellular_component" ]
3
[ "PFAM" ]
[ "PF05902" ]
[ "4_1_CTD" ]
[ 13576 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6794361", "R-DME-6794361", "R-HSA-399719", "R-HSA-6794361", "R-HSA-9662360", "R-HSA-9662361", "R-MMU-399719", "R-MMU-6794361", "R-RNO-399719", "R-RNO-6794361" ]
[ "REACTOME:R-BTA-6794361", "REACTOME:R-DME-6794361", "REACTOME:R-HSA-399719", "REACTOME:R-HSA-6794361", "REACTOME:R-HSA-9662360", "REACTOME:R-HSA-9662361", "REACTOME:R-MMU-399719", "REACTOME:R-MMU-6794361", "REACTOME:R-RNO-399719", "REACTOME:R-RNO-6794361" ]
10
[ "8i8y" ]
1
[ "PUB00011236" ]
[ "11432737" ]
[ "Properties of the C-terminal domain of 4.1 proteins." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 13576 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 182, 4, 44, 51, 44 ]
6
true
Domain
Band 4.1, C-terminal
Band 4.1, C-terminal
Band_4.1_C
5
IPR008380
8,380
HAD-superfamily hydrolase, subfamily IG, 5'-nucleotidase
HAD-SF_hydro_IG_5-nucl
Family
13,995
false
false
This family includes a 5'-nucleotidase, , specific for purines (IMP and GMP) [ ]. These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognised by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stan...
[]
[]
[]
0
[ "PFAM", "PANTHER", "NCBIFAM" ]
[ "PF05761", "PTHR12103", "TIGR02244" ]
[ "5_nucleotid", "", "HAD-IG-Ncltidse" ]
[ 13988, 13733, 10559 ]
3
[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3", "GenProp1469", "GenProp1753", "R-BTA-2161541", "R-BTA-74259", "R-BTA-9755088", "R-DDI-2161541", "R-DDI-74259", "R-DDI-9755088", "R-GGA-421178", "R-HSA-2161541", "R-HSA-74259", "R-HSA-9755088", "R-MMU-2161541", "R-MMU-74259", "R-MMU-9755088", "R-RNO-2161541", "R-RNO-74259",...
[ "EC:3.1.3", "GP:GenProp1469", "GP:GenProp1753", "REACTOME:R-BTA-2161541", "REACTOME:R-BTA-74259", "REACTOME:R-BTA-9755088", "REACTOME:R-DDI-2161541", "REACTOME:R-DDI-74259", "REACTOME:R-DDI-9755088", "REACTOME:R-GGA-421178", "REACTOME:R-HSA-2161541", "REACTOME:R-HSA-74259", "REACTOME:R-HSA-9...
22
[ "2bde", "2j2c", "2jc9", "2jcm", "2xcv", "2xcw", "2xcx", "2xjb", "2xjc", "2xjd", "2xje", "2xjf", "4g63", "4h4b", "4ohf", "5cqz", "5cr7", "5k7y", "5l4z", "5l50", "5opk", "5opl", "5opm", "5opn", "5opo", "5opp", "6dd3", "6ddb", "6ddc", "6ddh", "6ddk", "6ddl"...
46
[ "PUB00015569" ]
[ "9371705" ]
[ "Bovine cytosolic IMP/GMP-specific 5'-nucleotidase: cloning and expression of active enzyme in Escherichia coli." ]
[ 1997 ]
1
[]
[ "IPR016695" ]
0
1
0
[ "Bacteria", "Eukaryota", "hydrothermal vent metagenome" ]
[ 322, 13671, 2 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 21, 3, 18, 13, 26, 22, 17, 21, 54 ]
9
true
Family
HAD-superfamily hydrolase, subfamily IG, 5'-nucleotidase
HAD-superfamily hydrolase, subfamily IG, 5'-nucleotidase
HAD-SF_hydro_IG_5-nucl
9
IPR008381
8,381
Succinate dehydrogenase assembly factor 3, mitochondrial
SDHAF3/Sdh7
Family
2,988
false
false
Succinate dehydrogenase assembly factor 3 (SDHAF3, also known as Sdh7 in budding yeasts) is a mitochondrial protein involved in assembly of succinate dehydrogenase. It is a member of the LYR protein family [ ].
[ "GO:0034553", "GO:0005739" ]
[ "mitochondrial respiratory chain complex II assembly", "mitochondrion" ]
[ "biological_process", "cellular_component" ]
2
[ "PANTHER" ]
[ "PTHR13137" ]
[ "" ]
[ 2988 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9854311", "R-HSA-9854311", "R-MMU-9854311" ]
[ "REACTOME:R-BTA-9854311", "REACTOME:R-HSA-9854311", "REACTOME:R-MMU-9854311" ]
3
[]
0
[ "PUB00089688" ]
[ "24954417" ]
[ "The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase." ]
[ 2014 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2988 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 2, 2, 2, 2, 3, 1, 4, 1, 1 ]
9
true
Family
Succinate dehydrogenase assembly factor 3, mitochondrial
Succinate dehydrogenase assembly factor 3, mitochondrial
SDHAF3/Sdh7
9
IPR008382
8,382
SPHK1-interactor/A-kinase anchor 110kDa
SPHK1-interactor_AKAP_110
Family
3,517
false
false
This family consists of several mammalian protein kinase A anchoring protein 3 (PRKA3) or A-kinase anchor protein 110kDa (AKAP 110) sequences. Agents that increase intracellular cAMP are potent stimulators of sperm motility. Anchoring inhibitor peptides, designed to disrupt the interaction of the cAMP-dependent protein...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10226" ]
[ "" ]
[ 3517 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011239", "PUB00052585" ]
[ "10319321", "12080051" ]
[ "Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein.", "Cloning and characterization of a protein kinase A anchoring protein (AKAP)-related protein that interacts with and regulates sphingosine kinase 1 activity." ]
[ 1999, 2002 ]
2
[]
[ "IPR020799" ]
0
1
0
[ "Vertebrata" ]
[ 3517 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 13, 12, 25 ]
4
true
Family
SPHK1-interactor/A-kinase anchor 110kDa
SPHK1-interactor/A-kinase anchor 110kDa
SPHK1-interactor_AKAP_110
2
IPR008383
8,383
Apoptosis inhibitory 5
API5
Family
3,503
false
false
This family consists of apoptosis inhibitory protein 5 (API5) sequences from several organisms. Apoptosis or programmed cell death is a physiological form of cell death that occurs in embryonic development and organ formation. It is characterised by biochemical and morphological changes such as DNA fragmentation and ce...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05918", "PTHR12758" ]
[ "API5", "" ]
[ 3499, 3374 ]
2
[]
[]
[]
0
[ "3u0r", "3v6a", "6l4o" ]
3
[ "PUB00011538", "PUB00011539", "PUB00098158" ]
[ "10393420", "9307294", "22334682" ]
[ "Molecular cloning and fine mapping of API5L1, a novel human gene strongly related to an antiapoptotic gene.", "AAC-11, a novel cDNA that inhibits apoptosis after growth factor withdrawal.", "Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules." ]
[ 1999, 1997, 2012 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Halocatena marina" ]
[ 3502, 1 ]
2
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 31, 2, 1, 4, 2, 1, 4, 18 ]
8
true
Family
Apoptosis inhibitory 5
Apoptosis inhibitory 5
API5
4
IPR008384
8,384
Actin-related protein 2/3 complex subunit 4
ARPC4
Family
5,542
false
false
Arp2/3 binds to pre-existing actin filaments and nucleates new daughter filaments, and thus becomes incorporated into the dynamic actin network at the leading edge of motile cells and other actin-based protrusive structures [ ]. In order to nucleate filaments, Arp2/3 must bind to a member of the N-WASp/SCAR family prot...
[ "GO:0030041", "GO:0034314", "GO:0005885", "GO:0015629" ]
[ "actin filament polymerization", "Arp2/3 complex-mediated actin nucleation", "Arp2/3 protein complex", "actin cytoskeleton" ]
[ "biological_process", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF05856", "PIRSF039100", "PTHR22629" ]
[ "ARPC4", "ARPC4", "" ]
[ 5542, 4292, 5415 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-2029482", "R-BTA-3928662", "R-BTA-5663213", "R-BTA-8856828", "R-CEL-2029482", "R-CEL-3928662", "R-CEL-5663213", "R-CEL-8856828", "R-DDI-2029482", "R-DDI-5663213", "R-HSA-2029482", "R-HSA-3928662", "R-HSA-5663213", "R-HSA-8856828", "R-HSA-9664422", "R-MMU-2029482", "R-MMU-39286...
[ "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-3928662", "REACTOME:R-BTA-5663213", "REACTOME:R-BTA-8856828", "REACTOME:R-CEL-2029482", "REACTOME:R-CEL-3928662", "REACTOME:R-CEL-5663213", "REACTOME:R-CEL-8856828", "REACTOME:R-DDI-2029482", "REACTOME:R-DDI-5663213", "REACTOME:R-HSA-2029482", "REACTOM...
24
[ "1k8k", "1tyq", "1u2v", "2p9i", "2p9k", "2p9l", "2p9n", "2p9p", "2p9s", "2p9u", "3dwl", "3dxk", "3dxm", "3rse", "3ukr", "3uku", "3ule", "4jd2", "4xei", "4xf2", "6dec", "6uhc", "6w17", "6w18", "6yw6", "6yw7", "7aqk", "7jpn", "7t5q", "7tpt", "8e9b", "8p94"...
40
[ "PUB00020552", "PUB00022758", "PUB00035127", "PUB00035128" ]
[ "9889097", "15505213", "9600938", "11752435" ]
[ "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex.", "Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.", "The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formati...
[ 1998, 2004, 1998, 2001 ]
4
[]
[]
0
0
null
[ "Candidatus Heimdallarchaeum", "Eukaryota" ]
[ 2, 5540 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 1, 1, 9, 6, 1, 5, 6, 1, 1, 8 ]
12
true
Family
Actin-related protein 2/3 complex subunit 4
Actin-related protein 2/3 complex subunit 4
ARPC4
9
IPR008385
8,385
African swine fever virus, Inner membrane protein p54
ASFV_p54
Family
196
false
false
This entry represents Inner membrane protein p54 from African swine fever virus (ASFV). This inner envelope protein is involved in the intracellular microtubule-dependent transport of viral capsid toward viral factories through its interaction with host dynein [ ]. It sems to induce caspase-3 activation and apoptosis [...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05568" ]
[ "ASFV_J13L" ]
[ 196 ]
1
[]
[]
[]
0
[]
0
[ "PUB00100307", "PUB00100308" ]
[ "15225638", "11559815" ]
[ "The African swine fever virus dynein-binding protein p54 induces infected cell apoptosis.", "African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein." ]
[ 2004, 2001 ]
2
[]
[]
0
0
null
[ "African swine fever virus", "Bacteria", "Eukaryota" ]
[ 176, 7, 13 ]
3
[]
[]
0
true
Family
African swine fever virus, Inner membrane protein p54
African swine fever virus, Inner membrane protein p54
ASFV_p54
3
IPR008386
8,386
ATP synthase, F0 complex, subunit E, mitochondrial
ATP_synth_F0_esu_mt
Family
3,141
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0015078", "GO:0015986" ]
[ "proton transmembrane transporter activity", "proton motive force-driven ATP synthesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER" ]
[ "PF05680", "PTHR12427" ]
[ "ATP-synt_E", "" ]
[ 3139, 1628 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-163210", "R-BTA-8949613", "R-HSA-163210", "R-HSA-8949613", "R-MMU-163210", "R-MMU-8949613", "R-RNO-163210", "R-RNO-8949613", "R-SSC-163210", "R-SSC-8949613" ]
[ "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-RNO-163210", "REACTOME:R-RNO-8949613", "REACTOME:R-SSC-163210", "REACTOME:R-SSC-8949613" ]
10
[ "6tt7", "6za9", "6zbb", "6ziq", "6zit", "6ziu", "6zmr", "6zna", "6zpo", "6zqm", "6zqn", "7ajb", "7ajc", "7ajd", "7aje", "7ajf", "7ajg", "7ajh", "7aji", "7ajj", "8h9f", "8h9j", "8h9m", "8h9q", "8h9s", "8h9t", "8h9u", "8h9v", "8khf", "8ki3", "9b0x", "9b3j"...
35
[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020649", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "11309608", "15473999", "15078220", "15701797", "20450191", "18937357", "1385979", "9741106" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Functional analysis of subu...
[ 2001, 2004, 2004, 2005, 2010, 2008, 1992, 1998 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 9, 3132 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", ...
[ 1, 2, 1, 1, 3, 1, 2, 5, 1, 1, 3 ]
11
true
Family
ATP synthase, F0 complex, subunit E, mitochondrial
ATP synthase, F0 complex, subunit E, mitochondrial
ATP_synth_F0_esu_mt
6
IPR008387
8,387
ATP synthase-coupling factor 6, mitochondrial
ATP_synth_f6_mt
Family
2,159
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0015078", "GO:0015986" ]
[ "proton transmembrane transporter activity", "proton motive force-driven ATP synthesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF05511", "PIRSF002455", "PTHR12441" ]
[ "ATP-synt_F6", "ATP_synthase_coupling_factor_6", "" ]
[ 2157, 1141, 2036 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-163210", "R-BTA-8949613", "R-BTA-9837999", "R-DME-163210", "R-DME-8949613", "R-DME-9837999", "R-HSA-163210", "R-HSA-8949613", "R-HSA-9837999", "R-MMU-163210", "R-MMU-8949613", "R-MMU-9837999", "R-RNO-163210", "R-RNO-8949613", "R-RNO-9837999" ]
[ "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-BTA-9837999", "REACTOME:R-DME-163210", "REACTOME:R-DME-8949613", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-...
15
[ "1vzs", "2cly", "2wss", "4b2q", "5ara", "5are", "5arh", "5ari", "5fij", "5fik", "5fil", "6j5i", "6j5j", "6j5k", "6tt7", "6yy0", "6z1r", "6z1u", "6ziq", "6zit", "6ziu", "6zpo", "6zqm", "6zqn", "7ajb", "7ajc", "7ajd", "7aje", "7ajf", "7ajg", "7ajh", "7aji"...
46
[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020607", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "11309608", "15473999", "15078220", "16045926", "20450191", "18937357", "1385979", "9741106" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Structure of the F1-binding...
[ 2001, 2004, 2004, 2005, 2010, 2008, 1992, 1998 ]
8
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2159 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 9, 4, 4, 3, 4 ]
6
true
Family
ATP synthase-coupling factor 6, mitochondrial
ATP synthase-coupling factor 6, mitochondrial
ATP_synth_f6_mt
3
IPR008389
8,389
ATPase, V0 complex, subunit e1/e2
ATPase_V0-cplx_e1/e2_su
Family
4,338
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0046961", "GO:1902600", "GO:0033179" ]
[ "proton-transporting ATPase activity, rotational mechanism", "proton transmembrane transport", "proton-transporting V-type ATPase, V0 domain" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF05493", "PTHR12263" ]
[ "ATP_synt_H", "" ]
[ 4299, 3899 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1222556", "R-BTA-77387", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-77387", "R-CEL-917977", "R-CEL-9639288", "R-CEL-983712", "R-HSA-1222556", "R-HSA-77387", "R-HSA-917977", "R-HSA-9639288", "R-HSA-983712", "R-HSA-9857377", "R-MMU-1222556", "R-MM...
[ "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-77387", "REACTOME:R-CEL-917977", "REACTOME:R-CEL-9639288", "REACTOME:R-CEL-983712", "REACTOME:R-HSA-1222556", "REACTOME:R-HSA-...
34
[ "5tj5", "5vox", "5voy", "5voz", "6c6l", "6m0r", "6m0s", "6o7t", "6o7u", "6o7v", "6o7w", "6o7x", "6pe4", "6pe5", "6vq6", "6vq7", "6vq8", "6vqc", "6vqg", "6vqh", "6wlw", "6wm2", "6wm3", "6wm4", "6xbw", "7fda", "7fdb", "7fdc", "7khr", "7tao", "7tap", "7tmr"...
70
[ "PUB00011242", "PUB00020603", "PUB00020604", "PUB00020608", "PUB00020609", "PUB00020638", "PUB00042803", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "9556572", "15473999", "15078220", "15907459", "15629643", "12544825", "12163484", "20450191", "18937357", "1385979", "9741106" ]
[ "Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disci...
[ 1998, 2004, 2004, 2005, 2005, 2003, 2002, 2010, 2008, 1992, 1998 ]
11
[]
[ "IPR017385" ]
0
1
0
[ "Eukaryota" ]
[ 4338 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 4, 8, 7, 6, 1, 2, 7, 1, 1, 6 ]
12
true
Family
ATPase, V0 complex, subunit e1/e2
ATPase, V0 complex, subunit e1/e2
ATPase_V0-cplx_e1/e2_su
8
IPR008390
8,390
AWPM-19-like
AWPM-19
Family
2,578
false
false
Members of this family are 19kDa membrane proteins. The levels of the plant protein AWPM-19 increase dramatically when there is an increase level of abscisic acid. The increase presence of this protein leads to greater tolerance of freezing [ ]. The rice homologue, OsPM19L1, is induced by osmotic stress and may be asso...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05512", "PTHR33294" ]
[ "AWPM-19", "" ]
[ 2576, 2485 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011243", "PUB00088044" ]
[ "9249988", "26505346" ]
[ "Accumulation of 19-kDa plasma membrane polypeptide during induction of freezing tolerance in wheat suspension-cultured cells by abscisic acid.", "Characterization of OsPM19L1 encoding an AWPM-19-like family protein that is dramatically induced by osmotic stress in rice." ]
[ 1997, 2015 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2578 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 11, 19, 14 ]
3
true
Family
AWPM-19-like
AWPM-19-like
AWPM-19
8
IPR008391
8,391
Acetyl xylan esterase domain
AXE1_dom
Domain
7,825
false
false
This domain can be found in several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part o...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05448" ]
[ "AXE1" ]
[ 7825 ]
1
[]
[]
[]
0
[ "1l7a", "1ods", "1odt", "1vlq", "2xlb", "2xlc", "3fcy", "3fvr", "3fvt", "3fyt", "3fyu", "3m81", "3m82", "3m83", "5fdf", "5gma", "5hfn", "5jib", "6agq", "6fkx", "7xmj" ]
21
[ "PUB00011244" ]
[ "10878123" ]
[ "The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 68, 7562, 80, 115 ]
4
[ "Arabidopsis thaliana" ]
[ 7 ]
1
true
Domain
Acetyl xylan esterase domain
Acetyl xylan esterase domain
AXE1_dom
8
IPR008392
8,392
Drosophila accessory gland-specific peptide 26Ab
Acp26Ab
Family
23
false
false
This family consists of accessory gland-specific 26Ab peptides or male accessory gland secretory protein 355B from different Drosophila species. Drosophila males, like males of most other insects, transfer a group of specific proteins (Acp26Ab and Acp26Aa in Drosophila) to the females during mating. These proteins are ...
[ "GO:0007617", "GO:0005576" ]
[ "mating behavior", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05777" ]
[ "Acp26Ab" ]
[ 23 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011245" ]
[ "1361475" ]
[ "Polymorphism and divergence in the Mst26A male accessory gland gene region in Drosophila." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Sophophora" ]
[ 23 ]
1
[ "Drosophila melanogaster" ]
[ 2 ]
1
true
Family
Drosophila accessory gland-specific peptide 26Ab
Drosophila accessory gland-specific peptide 26Ab
Acp26Ab
7
IPR008393
8,393
Adenovirus late L2 mu core
Adenovirus_late_L2_mu_core
Family
311
false
false
The late transcription region 2 (L2) of Adenovirus type 2 has an ORF of 80 residues positioned between nucleotides 17,676 and 17,915. It encodes an 11K polypeptide, which has the initiating methionine residue removed, leaving a 79-residue product. The L2 region that encoded 11K polypeptide is arginine rich (21%) and ha...
[ "GO:0003677", "GO:0019013" ]
[ "DNA binding", "viral nucleocapsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05829" ]
[ "Adeno_PX" ]
[ 311 ]
1
[]
[]
[]
0
[ "9lr9" ]
1
[ "PUB00011541" ]
[ "3357209" ]
[ "Identification of the gene coding for the precursor of adenovirus core protein X." ]
[ 1988 ]
1
[]
[]
0
0
null
[ "Mycobacterium simiae", "Nesidiocoris tenuis", "Viruses" ]
[ 1, 1, 309 ]
3
[]
[]
0
true
Family
Adenovirus late L2 mu core
Adenovirus late L2 mu core
Adenovirus_late_L2_mu_core
9
IPR008394
8,394
Enterobacteria AfaD invasin
AfaD
Family
665
false
false
This family consists of several AfaD and related proteins from Escherichia coli and Salmonella bacteria. The afa gene clusters encode an afimbrial adhesive sheath produced by E. coli. The adhesive sheath is composed of two proteins, AfaD and AfaE, which are independently exposed at the bacterial cell surface. AfaE is r...
[]
[]
[]
0
[ "PFAM", "CDD" ]
[ "PF05775", "cd18776" ]
[ "AfaD", "AfaD-like" ]
[ 664, 629 ]
2
[]
[]
[]
0
[ "2axw", "2fvn", "2ixq", "3uiy", "3uiz", "4or1", "4phx", "5d55", "5y9g", "5y9h" ]
10
[ "PUB00011246", "PUB00039446", "PUB00040832", "PUB00097369", "PUB00139344", "PUB00139345", "PUB00139346", "PUB00139347" ]
[ "10981717", "16421447", "16965519", "25232738", "27400770", "29125121", "22497887", "10074069" ]
[ "Characterization of the AfaD-like family of invasins encoded by pathogenic Escherichia coli associated with intestinal and extra-intestinal infections.", "Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.", "The solution structure of the invasive tip complex from A...
[ 2000, 2006, 2006, 2014, 2016, 2017, 2012, 1999 ]
8
[]
[]
0
0
null
[ "Gammaproteobacteria" ]
[ 665 ]
1
[]
[]
0
true
Family
Enterobacteria AfaD invasin
Enterobacteria AfaD invasin
AfaD
5
IPR008395
8,395
Agenet-like domain
Agenet-like_dom
Domain
16,763
false
false
Fragile X messenger ribonucleoprotein 1 (FMR1/FMRP), and its autosomal paralogues, RNA-binding proteins FXR1/2 (Fragile X-related protein 1/2), comprise a family of RNA-binding proteins that are involved the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05641" ]
[ "Agenet" ]
[ 16763 ]
1
[ "REACTOME" ]
[ "R-HSA-6802952" ]
[ "REACTOME:R-HSA-6802952" ]
1
[ "2bkd", "3h8z", "3kuf", "3o8v", "4ova", "4qvz", "4qw2", "5zwx", "5zwz", "6ie4", "6ie5", "6ie6", "6ie7", "7yt9", "7yta" ]
15
[ "PUB00011247", "PUB00039656", "PUB00054919", "PUB00060514", "PUB00060515", "PUB00086467", "PUB00090595", "PUB00090596", "PUB00091115", "PUB00091337", "PUB00103107", "PUB00103108" ]
[ "12575993", "16407062", "16000371", "12950170", "21072162", "19795213", "28960184", "29713264", "25416280", "25464849", "30382101", "30425322" ]
[ "The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains.", "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.", "The RNA-binding protein fragile X-related 1 regulates somite formation in Xenopus laevis.", ...
[ 2003, 2006, 2005, 2003, 2010, 2010, 2017, 2018, 2015, 2014, 2018, 2019 ]
12
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 122, 16641 ]
2
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 111, 5, 32, 16, 44, 20, 116 ]
7
true
Domain
Agenet-like domain
Agenet-like domain
Agenet-like_dom
6
IPR008397
8,397
Alginate lyase domain
Alginate_lyase_dom
Domain
10,726
false
false
Alginate is a family of 1-4-linked copolymers of beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyse the depolymerisation of alginates by beta -elimination, generating a molecule conta...
[ "GO:0016829", "GO:0042597" ]
[ "lyase activity", "periplasmic space" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05426" ]
[ "Alginate_lyase" ]
[ 10726 ]
1
[ "EC", "METACYC" ]
[ "4.2.2.3", "PWY-6986" ]
[ "EC:4.2.2.3", "METACYC:PWY-6986" ]
2
[ "1hv6", "1qaz", "3nfv", "3nnb", "4e1y", "4f10", "4f13", "4nei", "4ojz", "4ok2", "4ok4", "4ozv", "4ozw", "7bjt", "7bm6", "7fhu", "7fhv", "7fhw", "7fhx", "7fhy", "7fhz", "7fi0", "7fi1", "7fi2", "7sa8", "7wxj", "7wxk", "7wxl", "7wxm", "7wxn", "7wxo", "7wxp"...
53
[ "PUB00011248" ]
[ "9683471" ]
[ "Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "metagenomes" ]
[ 8433, 2225, 36, 32 ]
4
[]
[]
0
true
Domain
Alginate lyase domain
Alginate lyase domain
Alginate_lyase_dom
1
IPR008398
8,398
Allexivirus 40kDa
Allexi_40kDa
Family
184
false
false
This family of sequences contains the 40kDa polypeptides from garlic viruses (Allexiviruses), which do not resemble any other plant virus gene products reported so far [ ]. Rod-shaped flexuous viruses have been isolated from garlic plants, Allium sativum. Infection by this virus creates typical mosaic symptoms. The cor...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF05549", "PIRSF005512" ]
[ "Allexi_40kDa", "Allexi_40kDa" ]
[ 184, 157 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011537", "PUB00043798" ]
[ "8376963", "18092468" ]
[ "Novel rod-shaped viruses isolated from garlic, Allium sativum, possessing a unique genome organization.", "Allexivirus transmitted by eriophyid mites in garlic plants." ]
[ 1993, 2007 ]
2
[]
[]
0
0
null
[ "Tymovirales" ]
[ 184 ]
1
[]
[]
0
true
Family
Allexivirus 40kDa
Allexivirus 40kDa
Allexi_40kDa
7
IPR008399
8,399
Anthrax toxin receptor, C-terminal
Anthrax_toxin_rcpt_C
Domain
4,096
false
false
Anthrax is an acute disease in humans and animals, which is caused by the bacterium Bacillus anthracis. While the disease can be lethal, there are effective vaccines against anthrax, and some forms of the disease respond well to antibiotic treatment. The anthrax toxin consists of the proteins protective antigen (PA), l...
[ "GO:0038023", "GO:0016020" ]
[ "signaling receptor activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05586" ]
[ "Ant_C" ]
[ 4096 ]
1
[ "REACTOME" ]
[ "R-HSA-5210891" ]
[ "REACTOME:R-HSA-5210891" ]
1
[]
0
[ "PUB00022677", "PUB00031351" ]
[ "15079089", "15243628" ]
[ "Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor.", "Crystal structure of a complex between anthrax toxin and its host cell receptor." ]
[ 2004, 2004 ]
2
[]
[]
0
0
null
[ "Metazoa" ]
[ 4096 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 7, 6, 10 ]
4
true
Domain
Anthrax toxin receptor, C-terminal
Anthrax toxin receptor, C-terminal
Anthrax_toxin_rcpt_C
5
IPR008400
8,400
Anthrax toxin receptor, extracellular domain
Anthrax_toxin_rcpt_extracel
Domain
4,271
false
false
Anthrax is an acute disease in humans and animals, which is caused by the bacterium Bacillus anthracis. While the disease can be lethal, there are effective vaccines against anthrax, and some forms of the disease respond well to antibiotic treatment. The anthrax toxin consists of the proteins protective antigen (PA), l...
[ "GO:0038023", "GO:0016020" ]
[ "signaling receptor activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05587" ]
[ "Anth_Ig" ]
[ 4271 ]
1
[ "REACTOME" ]
[ "R-HSA-5210891" ]
[ "REACTOME:R-HSA-5210891" ]
1
[]
0
[ "PUB00022677", "PUB00031351" ]
[ "15079089", "15243628" ]
[ "Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor.", "Crystal structure of a complex between anthrax toxin and its host cell receptor." ]
[ 2004, 2004 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4271 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 21, 10, 15 ]
4
true
Domain
Anthrax toxin receptor, extracellular domain
Anthrax toxin receptor, extracellular domain
Anthrax_toxin_rcpt_extracel
6
IPR008401
8,401
Apc13
Apc13
Family
2,698
false
false
The anaphase-promoting complex (APC) is a conserved multi-subunit ubiquitin ligase required for the degradation of key cell cycle regulators. Members of this family are components of the anaphase-promoting complex homologous to Apc13 [ ].
[ "GO:0005680" ]
[ "anaphase-promoting complex" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF05839", "PTHR28672" ]
[ "Apc13p", "" ]
[ 2381, 1490 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-983168", "R-HSA-983168", "R-MMU-983168", "R-XTR-983168" ]
[ "REACTOME:R-BTA-983168", "REACTOME:R-HSA-983168", "REACTOME:R-MMU-983168", "REACTOME:R-XTR-983168" ]
4
[ "4ui9", "5a31", "5g04", "5g05", "5khr", "5khu", "5l9t", "5l9u", "5lcw", "6q6g", "6q6h", "6tlj", "6tm5", "6tnt", "8a3t", "8a5y", "8a61", "8pkp", "8tar", "8tau", "9gaw", "9n9r", "9n9s" ]
23
[ "PUB00011249" ]
[ "12477395" ]
[ "Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2698 ]
1
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "...
[ 3, 1, 2, 2, 1, 1, 3, 2, 1, 1, 3 ]
11
true
Family
Apc13
Apc13
Apc13
1
IPR008402
8,402
Anaphase-promoting complex subunit 15/mnd2, N-terminal
APC_su15/mnd2_N
Domain
1,149
false
false
This entry represents a conserved region found at the N-terminal of budding yeast Mnd2 and its homologue, anaphase-promoting complex subunit 15 (Apc15), from fission yeasts [ ]. They are part of the anaphase promoting complex/cyclosome (APC/C) [ , ]. The anaphase-promoting complex (APC) or cyclosome is a multi-subunit ...
[ "GO:0031145", "GO:0005680" ]
[ "anaphase-promoting complex-dependent catabolic process", "anaphase-promoting complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05841" ]
[ "Apc15p" ]
[ 1149 ]
1
[]
[]
[]
0
[ "8a3t", "8a5y", "8a61" ]
3
[ "PUB00011249", "PUB00055007", "PUB00059221" ]
[ "12477395", "12609981", "18485873" ]
[ "Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes.", "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-promoting complex.", "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex." ]
[ 2002, 2003, 2008 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1149 ]
1
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1 ]
3
true
Domain
Anaphase-promoting complex subunit 15/mnd2, N-terminal
Anaphase-promoting complex subunit 15/mnd2, N-terminal
APC_su15/mnd2_N
3