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
IPR001874
1,874
Dehydroquinase, class II
DHquinase_II
Family
23,602
false
false
3-dehydroquinate dehydratase ( ), or dehydroquinase, catalyzes the conversion of 3-dehydroquinate into 3-dehydroshikimate. It is the third step in the shikimate pathway for the biosynthesis of aromatic amino acids from chorismate. Two classes of dehydroquinases exist, known as types I and II. Class-II enzymes are homod...
[ "GO:0003855" ]
[ "3-dehydroquinate dehydratase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00169", "PF01220", "PIRSF001399", "PTHR21272", "TIGR01088", "cd00466" ]
[ "AroQ", "DHquinase_II", "DHquinase_II", "", "aroQ", "DHQase_II" ]
[ 23187, 23555, 23042, 23428, 20156, 23082 ]
6
[ "EC", "GP", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME" ]
[ "4.2.1.10", "GenProp0001", "PWY-6163", "PWY-6416", "PWY-6707", "PDOC00789", "R-MTU-964903" ]
[ "EC:4.2.1.10", "GP:GenProp0001", "METACYC:PWY-6163", "METACYC:PWY-6416", "METACYC:PWY-6707", "PROSITEDOC:PDOC00789", "REACTOME:R-MTU-964903" ]
7
[ "1d0i", "1gqo", "1gtz", "1gu0", "1gu1", "1h05", "1h0r", "1h0s", "1j2y", "1uqr", "1v1j", "2bt4", "2c4v", "2c4w", "2c57", "2cjf", "2dhq", "2uyg", "2wks", "2xb8", "2xb9", "2xd9", "2xda", "2y71", "2y76", "2y77", "3kip", "3lwz", "3n59", "3n76", "3n7a", "3n86"...
79
[ "PUB00003743", "PUB00003855" ]
[ "1910148", "8170389" ]
[ "The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases.", "Characterization of a 3-dehydroquinase gene from Actinobacillus pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE." ]
[ 1991, 1994 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]
[ 21926, 1120, 2, 554 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Dehydroquinase, class II
Dehydroquinase, class II
DHquinase_II
7
IPR001875
1,875
Death effector domain
DED_dom
Domain
9,324
false
false
The death effector domain (DED) is a homotypic protein interaction module composed of a bundle of six α-helices. DED is related in sequence and structure to the death domain (DD, see ) and the caspase recruitment domain (CARD, see ), which work in similar pathways and show similar interaction properties [ ]. The dimeri...
[ "GO:0005515", "GO:0042981" ]
[ "protein binding", "regulation of apoptotic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01335", "PS50168", "SM00031" ]
[ "DED", "DED", "DED" ]
[ 7324, 9296, 6913 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50168", "R-BTA-140534", "R-BTA-2562578", "R-BTA-3371378", "R-BTA-5218900", "R-BTA-5357786", "R-BTA-5357905", "R-BTA-5675482", "R-BTA-69416", "R-BTA-75157", "R-HSA-111465", "R-HSA-112409", "R-HSA-140534", "R-HSA-168638", "R-HSA-2562578", "R-HSA-264870", "R-HSA-3371378", "R-HSA-...
[ "PROSITEDOC:PDOC50168", "REACTOME:R-BTA-140534", "REACTOME:R-BTA-2562578", "REACTOME:R-BTA-3371378", "REACTOME:R-BTA-5218900", "REACTOME:R-BTA-5357786", "REACTOME:R-BTA-5357905", "REACTOME:R-BTA-5675482", "REACTOME:R-BTA-69416", "REACTOME:R-BTA-75157", "REACTOME:R-HSA-111465", "REACTOME:R-HSA-...
72
[ "1a1w", "1a1z", "1n3k", "2bbr", "2bbz", "2f1s", "2gf5", "2ls7", "3cl3", "4iz5", "4iz7", "4iza", "4zbw", "5h31", "5h33", "5jqe", "5l08", "5lde", "6agw", "6m6o", "6p6b", "6p6c", "7dee", "7lvj", "7lvm", "7lxc", "7pdj", "8ybx", "8yd7", "8yd8", "8ym4", "8ym5"...
41
[ "PUB00015010", "PUB00015013", "PUB00015057" ]
[ "15173180", "11504623", "15226512" ]
[ "Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD.", "The death domain superfamily: a tale of two interfaces?", "The domains of apoptosis: a genomics perspective." ]
[ 2004, 2001, 2004 ]
3
[]
[ "IPR029546" ]
0
1
0
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "metagenomes" ]
[ 169, 9089, 2, 55, 9 ]
5
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 51, 20, 17 ]
4
true
Domain
Death effector domain
Death effector domain
DED_dom
8
IPR001879
1,879
GPCR, family 2, extracellular hormone receptor domain
GPCR_2_extracellular_dom
Domain
46,667
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:0004930", "GO:0016020" ]
[ "G protein-coupled receptor activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02793", "PS50227", "SM00008" ]
[ "HRM", "G_PROTEIN_RECEP_F2_3", "HormR" ]
[ 37549, 46443, 40788 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00559", "R-BTA-418555", "R-BTA-420092", "R-CEL-419812", "R-CFA-373080", "R-DME-350368", "R-DME-350376", "R-DME-350379", "R-DME-350411", "R-DME-350480", "R-DME-450728", "R-DRE-419812", "R-HSA-163359", "R-HSA-187024", "R-HSA-373080", "R-HSA-381676", "R-HSA-416476", "R-HSA-418555...
[ "PROSITEDOC:PDOC00559", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-CEL-419812", "REACTOME:R-CFA-373080", "REACTOME:R-DME-350368", "REACTOME:R-DME-350376", "REACTOME:R-DME-350379", "REACTOME:R-DME-350411", "REACTOME:R-DME-350480", "REACTOME:R-DME-450728", "REACTOME:R-DRE-4198...
43
[ "1u34", "2jnc", "2jnd", "2jod", "2l27", "2qkh", "2x57", "2xdg", "3aqf", "3c4m", "3c59", "3c5t", "3ehs", "3eht", "3ehu", "3h3g", "3iol", "3l2j", "3n7p", "3n7r", "3n7s", "3n93", "3n94", "3n95", "3n96", "4dlo", "4dlq", "4ers", "4hj0", "4lf3", "4rwf", "4rwg"...
227
[ "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1646711", "1314625", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", "Expression cloning of an adenylate cyclase-coupled calcitonin receptor.", ...
[ 1991, 1992, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]
11
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "freshwater metagenome" ]
[ 10, 46656, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 320, 21, 121, 106, 170 ]
6
true
Domain
GPCR, family 2, extracellular hormone receptor domain
GPCR, family 2, extracellular hormone receptor domain
GPCR_2_extracellular_dom
8
IPR001881
1,881
EGF-like calcium-binding domain
EGF-like_Ca-bd_dom
Domain
225,811
false
false
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown [ , , , , ] to be present in a large number of membrane-bound and extracellular, mostly animal, proteins. Many of these proteins require calcium for their biological function, and a calcium-binding site has been found at...
[ "GO:0005509" ]
[ "calcium ion binding" ]
[ "molecular_function" ]
1
[ "SMART" ]
[ "SM00179" ]
[ "EGF_CA" ]
[ 225811 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00913", "R-BTA-114608", "R-BTA-140834", "R-BTA-140837", "R-BTA-140875", "R-BTA-1474228", "R-BTA-1566948", "R-BTA-159740", "R-BTA-159763", "R-BTA-159782", "R-BTA-1971475", "R-BTA-2022870", "R-BTA-2022923", "R-BTA-2024101", "R-BTA-202733", "R-BTA-2129379", "R-BTA-216083", "R-BTA...
[ "PROSITEDOC:PDOC00913", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-140834", "REACTOME:R-BTA-140837", "REACTOME:R-BTA-140875", "REACTOME:R-BTA-1474228", "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-159740", "REACTOME:R-BTA-159763", "REACTOME:R-BTA-159782", "REACTOME:R-BTA-1971475", "REACTOME:R-BTA-2...
448
[ "1apo", "1apq", "1aut", "1bf9", "1c5m", "1ccf", "1dan", "1dva", "1dx5", "1edm", "1emn", "1emo", "1ezq", "1f0r", "1f0s", "1f7e", "1f7m", "1fak", "1fax", "1ff7", "1ffm", "1g2l", "1g2m", "1hj7", "1hz8", "1i0u", "1ioe", "1iqe", "1iqf", "1iqg", "1iqh", "1iqi"...
296
[ "PUB00000923", "PUB00001555", "PUB00002741", "PUB00003983", "PUB00004321", "PUB00004609", "PUB00004964" ]
[ "7606779", "3282918", "1527084", "6607417", "2288911", "6334307", "3534958" ]
[ "The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.", "Structure and function of epidermal growth factor-like regions in proteins.", "How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of...
[ 1995, 1988, 1992, 1984, 1990, 1984, 1986 ]
7
[ "IPR000742" ]
[ "IPR049883" ]
1
1
0
[ "Bacteria", "Eukaryota", "organismal metagenomes" ]
[ 175, 225631, 5 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 66, 101, 652, 115, 618, 405, 252, 598, 126 ]
9
true
Domain
EGF-like calcium-binding domain
EGF-like calcium-binding domain
EGF-like_Ca-bd_dom
2
IPR001882
1,882
Biotin-binding site
Biotin_BS
Binding_site
69,496
false
false
Biotin, which plays a catalytic role in some carboxyl transfer reactions, is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [ , , , ]. Sequence data reveal that the region around the biocytin (biotin-lysine) residue is well conserved and is evolutionary related to that ar...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00188" ]
[ "BIOTIN" ]
[ 69496 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00167", "R-BTA-196780", "R-BTA-70263", "R-BTA-70268", "R-CEL-196780", "R-CEL-71032", "R-DDI-196780", "R-DDI-200425", "R-DDI-70895", "R-DDI-75105", "R-HSA-163765", "R-HSA-196780", "R-HSA-200425", "R-HSA-2426168", "R-HSA-3371599", "R-HSA-70263", "R-HSA-70268", "R-HSA-70895", "...
[ "PROSITEDOC:PDOC00167", "REACTOME:R-BTA-196780", "REACTOME:R-BTA-70263", "REACTOME:R-BTA-70268", "REACTOME:R-CEL-196780", "REACTOME:R-CEL-71032", "REACTOME:R-DDI-196780", "REACTOME:R-DDI-200425", "REACTOME:R-DDI-70895", "REACTOME:R-DDI-75105", "REACTOME:R-HSA-163765", "REACTOME:R-HSA-196780", ...
47
[ "1a6x", "1bdo", "1dcz", "1dd2", "1o78", "2bdo", "2d5d", "2ejf", "2ejg", "2ejm", "2evb", "2jku", "2qf7", "3bdo", "3bg3", "3bg9", "3n6r", "3tw6", "3tw7", "3va7", "4hr7", "5csa", "5csk", "5csl", "5gu8", "5gu9", "5gua", "5i8i", "5ks8", "5mlk", "6g2d", "6g2h"...
96
[ "PUB00000064", "PUB00002482", "PUB00002740", "PUB00003560" ]
[ "2673009", "2896195", "1526981", "6438443" ]
[ "The mechanism of biotin-dependent enzymes.", "Evolutionary conservation among biotin enzymes.", "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.", "Formation of N epsilon-(biotinyl)lysine in biotin enzymes." ]
[ 1989, 1988, 1992, 1984 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 699, 51982, 16016, 799 ]
4
[ "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",...
[ 19, 2, 35, 9, 1, 13, 12, 2, 2, 28, 5, 2, 7 ]
13
true
Binding_site
Biotin-binding site
Biotin-binding site
Biotin_BS
8
IPR001883
1,883
GPCR, family 3, metabotropic glutamate receptor 7
GPCR_3_mGluR7
Family
1,296
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" ]
[ "PR01057" ]
[ "MTABOTROPC7R" ]
[ 1296 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "295", "R-HSA-418594", "R-HSA-420499", "R-MMU-418594", "R-MMU-420499", "R-RNO-418594", "R-RNO-420499" ]
[ "IUPHAR:295", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-420499", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-420499", "REACTOME:R-RNO-418594", "REACTOME:R-RNO-420499" ]
7
[ "2e4z", "3mq4", "5c5c", "9omo", "9omp" ]
5
[ "PUB00000774", "PUB00002720", "PUB00002840", "PUB00004090", "PUB00004161", "PUB00004309", "PUB00004961", "PUB00005138", "PUB00007343", "PUB00036049", "PUB00036050", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "8840028", "1320017", "8288585", "1847995", "8255296", "1309649", "8170923", "1656524", "9292726", "17266540", "10773016", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Human metabotropic glutamate receptor type 7: molecular cloning and mRNA distribution in the CNS.", "Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.", "Molecular characterization of a new metabotropic glutamate receptor mGluR7...
[ 1996, 1992, 1994, 1991, 1993, 1992, 1994, 1991, 1997, 2007, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]
17
[ "IPR000162" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 1296 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 8, 6, 8 ]
4
true
Family
GPCR, family 3, metabotropic glutamate receptor 7
GPCR, family 3, metabotropic glutamate receptor 7
GPCR_3_mGluR7
3
IPR001884
1,884
Translation elongation factor IF5A-like
IF5A-like
Family
10,347
false
false
Eukaryotic eIF-5A was initially thought to function as a translation initiation factor, based on its ability to stimulate methionyl-puromycin synthesis. However, subsequent work revealed a role for eIF5A in translation elongation [ , ]. Depletion or inactivation of eIF-5A in the yeast Saccharomyces cerevisiae (Baker's ...
[ "GO:0003723", "GO:0003746", "GO:0043022", "GO:0006414" ]
[ "RNA binding", "translation elongation factor activity", "ribosome binding", "translational elongation" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PIRSF", "PANTHER", "NCBIFAM" ]
[ "PIRSF003025", "PTHR11673", "TIGR00037" ]
[ "eIF5A", "", "eIF_5A" ]
[ 7213, 10241, 8006 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00274", "R-BTA-204626", "R-CEL-204626", "R-DDI-204626", "R-DME-204626", "R-DRE-204626", "R-GGA-204626", "R-HSA-204626", "R-MMU-204626", "R-RNO-204626", "R-SCE-204626", "R-SPO-204626" ]
[ "PROSITEDOC:PDOC00274", "REACTOME:R-BTA-204626", "REACTOME:R-CEL-204626", "REACTOME:R-DDI-204626", "REACTOME:R-DME-204626", "REACTOME:R-DRE-204626", "REACTOME:R-GGA-204626", "REACTOME:R-HSA-204626", "REACTOME:R-MMU-204626", "REACTOME:R-RNO-204626", "REACTOME:R-SCE-204626", "REACTOME:R-SPO-2046...
12
[ "1bkb", "1eif", "1iz6", "1khi", "1x6o", "1xtd", "2eif", "3cpf", "3er0", "3hks", "5dat", "5dc3", "5dge", "5dgf", "5dlq", "5gak", "5hy6", "5mc6", "6q84", "6tnu", "7asi", "7asx", "7n4d", "7njh", "7nji", "7nrc", "7oya", "7oyc", "7oyd", "7rr5", "8a0e", "8aaf"...
58
[ "PUB00000742", "PUB00003672", "PUB00005808", "PUB00010716", "PUB00026734", "PUB00046010", "PUB00082267", "PUB00090482", "PUB00101067" ]
[ "8347280", "1903841", "9493264", "9753699", "12640443", "19424157", "23727016", "28392174", "23869404" ]
[ "Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation.", "Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.", "Crystal structure of the NAD complex of human...
[ 1993, 1991, 1998, 1998, 2003, 2009, 2013, 2017, 2013 ]
9
[]
[ "IPR022847" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "metagenomes" ]
[ 890, 8, 9391, 10, 48 ]
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", "Saccharomyces cerevisiae (strai...
[ 8, 3, 6, 1, 8, 6, 2, 16, 7, 2, 2, 19 ]
12
true
Family
Translation elongation factor IF5A-like
Translation elongation factor IF5A-like
IF5A-like
9
IPR001885
1,885
Lipoxygenase, mammalian
LipOase_mml
Family
5,012
false
false
Lipoxygenases ([ec:1.13.11.-]) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resist...
[ "GO:0005506", "GO:0016702" ]
[ "iron ion binding", "oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00467" ]
[ "MAMLPOXGNASE" ]
[ 5012 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...
[ "1.13.11", "1.13.11.-", "PWY-181", "PWY-5163", "PWY-5642", "PWY-6068", "PWY-6069", "PWY-6084", "PWY-6087", "PWY-6089", "PWY-6093", "PWY-6094", "PWY-6102", "PWY-6107", "PWY-6178", "PWY-6190", "PWY-6193", "PWY-6336", "PWY-6339", "PWY-6667", "PWY-7006", "PWY-7009", "PWY-7010...
[ "EC:1.13.11", "EC:1.13.11.-", "METACYC:PWY-181", "METACYC:PWY-5163", "METACYC:PWY-5642", "METACYC:PWY-6068", "METACYC:PWY-6069", "METACYC:PWY-6084", "METACYC:PWY-6087", "METACYC:PWY-6089", "METACYC:PWY-6093", "METACYC:PWY-6094", "METACYC:PWY-6102", "METACYC:PWY-6107", "METACYC:PWY-6178",...
116
[ "1lox", "2fnq", "2p0m", "3d3l", "3dy5", "3fg1", "3fg3", "3fg4", "3o8y", "3rde", "3v92", "3v98", "3v99", "3vf1", "4nre", "4qwt", "6n2w", "6ncf", "7laf", "7ttj", "7ttk", "7ttl", "8ghb", "8ghc", "8ghd", "8ghe", "8viy" ]
27
[ "PUB00000045", "PUB00000363", "PUB00002887", "PUB00005162" ]
[ "3017195", "1567851", "7508918", "8502991" ]
[ "Arachidonic acid metabolism.", "Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.", "A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus.", "The three-dimensional structure of an arachid...
[ 1986, 1992, 1994, 1993 ]
4
[ "IPR000907" ]
[]
1
0
1
[ "Eukaryota", "Thiohalocapsa halophila" ]
[ 5011, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 44, 20, 22, 27 ]
4
true
Family
Lipoxygenase, mammalian
Lipoxygenase, mammalian
LipOase_mml
7
IPR001887
1,887
Barnase
Barnase
Family
1,220
false
false
Barnase is the extracellular ribonuclease of Bacillus amyloliquefaciens, and barstar its specific intracellular inhibitor [ , ]. Expression of barstar is necessary to counter the lethal effect of expressed active barnase. Barnase hydrolyses phosphodiester bonds in RNA, poly- and oligo-ribonucleotides, resulting in 3'-n...
[ "GO:0003723", "GO:0004521" ]
[ "RNA binding", "RNA endonuclease activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PIRSF", "PRINTS", "CDD" ]
[ "PIRSF001013", "PR00117", "cd00933" ]
[ "Barnase", "BARNASE", "barnase" ]
[ 620, 1183, 189 ]
3
[ "EC" ]
[ "3.1.27.-" ]
[ "EC:3.1.27.-" ]
1
[ "1a2p", "1b20", "1b21", "1b27", "1b2s", "1b2u", "1b2x", "1b2z", "1b3s", "1ban", "1bao", "1bgs", "1bne", "1bnf", "1bng", "1bni", "1bnj", "1bnr", "1bns", "1brg", "1brh", "1bri", "1brj", "1brk", "1brn", "1brs", "1bsa", "1bsb", "1bsc", "1bsd", "1bse", "1buj"...
59
[ "PUB00000354", "PUB00003231", "PUB00005346" ]
[ "1888730", "3050134", "2696173" ]
[ "Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy.", "Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease.", "Barnase and barstar: two small proteins to fold and fit together." ]
[ 1991, 1988, 1989 ]
3
[ "IPR000026" ]
[]
1
0
1
[ "Bacteria", "Methanobacteriaceae", "Phytophthora kernoviae 00238/432", "bioreactor metagenome" ]
[ 1197, 15, 1, 7 ]
4
[]
[]
0
true
Family
Barnase
Barnase
Barnase
2
IPR001888
1,888
Transposase, type 1
Transposase_1
Family
9,861
false
false
Autonomous mobile genetic elements such as transposon or insertion sequences (IS) encode an enzyme, transposase, that is required for excising and inserting the mobile element. Transposases have been grouped into various families [ , , ]. This family includes the mariner transposase [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF01359" ]
[ "Transposase_1" ]
[ 9861 ]
1
[]
[]
[]
0
[ "2f7t", "3f2k", "3hos", "3hot", "3k9j", "3k9k", "4mda", "4mdb", "4r79", "4u7b", "5hoo" ]
11
[ "PUB00001294", "PUB00001812", "PUB00003820", "PUB00004452" ]
[ "8895590", "1718819", "1310791", "8041625" ]
[ "A purified mariner transposase is sufficient to mediate transposition in vitro.", "IS406 and IS407, two gene-activating insertion sequences for Pseudomonas cepacia.", "Isolation and analysis of IS6120, a new insertion sequence from Mycobacterium smegmatis.", "Sequence similarity of putative transposases link...
[ 1996, 1991, 1992, 1994 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Nocardioides" ]
[ 9859, 2 ]
2
[ "Homo sapiens" ]
[ 4 ]
1
true
Family
Transposase, type 1
Transposase, type 1
Transposase_1
1
IPR001889
1,889
Herpesvirus thymidine kinase
Herpes_TK
Family
1,237
false
false
The thymidine kinase from Herpesviridae catalyses the reaction: ATP + THYMIDINE = ADP + THYMIDINE 5'-PHOSPHATE. The enzyme is not subject to feedback inhibition by its product and the crystal structure of the enzyme from Human herpesvirus 1 (HHV-1) has been reported [ ].
[ "GO:0004797", "GO:0005524", "GO:0006230" ]
[ "thymidine kinase activity", "ATP binding", "TMP biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM" ]
[ "MF_04029", "PF00693" ]
[ "HSV_KITH", "Herpes_TK" ]
[ 858, 1236 ]
2
[ "EC", "METACYC" ]
[ "2.7.1.21", "PWY-7199" ]
[ "EC:2.7.1.21", "METACYC:PWY-7199" ]
2
[ "1e2h", "1e2i", "1e2j", "1e2k", "1e2l", "1e2m", "1e2n", "1e2p", "1ki2", "1ki3", "1ki4", "1ki6", "1ki7", "1ki8", "1kim", "1of1", "1osn", "1p6x", "1p72", "1p73", "1p75", "1p7c", "1qhi", "1vtk", "2ki5", "2vtk", "3f0t", "3rdp", "3vtk", "4ivp", "4ivq", "4ivr"...
38
[ "PUB00003924" ]
[ "7552712" ]
[ "Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Herpesvirales", "Pseudomonadati" ]
[ 1234, 3 ]
2
[]
[]
0
true
Family
Herpesvirus thymidine kinase
Herpesvirus thymidine kinase
Herpes_TK
2
IPR001890
1,890
RNA-binding, CRM domain
RNA-binding_CRM
Domain
19,987
false
false
The CRM domain is an ~100-amino acid RNA-binding domain. The name chloroplast RNA splicing and ribosome maturation (CRM) has been suggested to reflect the functions established for the four characterised members of the family: Zea mays (Maize) CRS1 ( ), CAF1 ( ) and CAF2 ( ) proteins and the Escherichia coli protein Yh...
[ "GO:0003723" ]
[ "RNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01985", "PS51295", "SM01103" ]
[ "CRS1_YhbY", "CRM", "CRS1_YhbY" ]
[ 19867, 19931, 19643 ]
3
[]
[]
[]
0
[ "1jo0", "1ln4", "1rq8", "8a22", "8apn", "8apo" ]
6
[ "PUB00019352", "PUB00019354", "PUB00043746", "PUB00043747", "PUB00044700" ]
[ "12429100", "11565746", "12881426", "17105995", "18065687" ]
[ "Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins.", "CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin.", "Group II intron splicing factors derived by diversification of an ancient RNA-binding domain.", "The CRM domain...
[ 2002, 2001, 2003, 2007, 2007 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 707, 10452, 8677, 151 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 74, 1, 42, 97 ]
4
true
Domain
RNA-binding, CRM domain
RNA-binding, CRM domain
RNA-binding_CRM
7
IPR001891
1,891
Malic oxidoreductase
Malic_OxRdtase
Family
38,323
false
false
Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during the Calvin cycle of photosynthesis [ ]. There are 3 forms of the enzyme...
[ "GO:0004470", "GO:0016616" ]
[ "malic enzyme activity", "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor" ]
[ "molecular_function", "molecular_function" ]
2
[ "PIRSF", "PRINTS" ]
[ "PIRSF000106", "PR00072" ]
[ "ME", "MALOXRDTASE" ]
[ 35272, 28793 ]
2
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.1.1", "1.1.1.38", "PWY-3641", "PWY-7115", "PWY-7118", "PWY-7384", "PWY-7686", "R-HSA-1989781", "R-HSA-70268", "R-HSA-9818025", "R-HSA-9837999", "R-HSA-9861718", "R-MMU-70268", "R-MMU-9837999", "R-MMU-9861718", "R-RNO-70268", "R-RNO-9861718" ]
[ "EC:1.1.1", "EC:1.1.1.38", "METACYC:PWY-3641", "METACYC:PWY-7115", "METACYC:PWY-7118", "METACYC:PWY-7384", "METACYC:PWY-7686", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-70268", "REACTOME:R-HSA-9818025", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9861718", "REACTOME:R-MMU-70268", "REACTOME:R...
17
[ "1do8", "1efk", "1efl", "1gq2", "1gz3", "1gz4", "1llq", "1o0s", "1pj2", "1pj3", "1pj4", "1pjl", "1qr6", "1vl6", "1ww8", "2a9f", "2aw5", "2dvm", "2hae", "3nv9", "3wja", "5cee", "5ou5", "6ags", "6c7n", "6urf", "6w29", "6w2n", "6w49", "6w53", "6w56", "6w57"...
52
[ "PUB00000616", "PUB00002681", "PUB00002876", "PUB00004541", "PUB00057828" ]
[ "1911848", "1993674", "8300616", "2103472", "2644282" ]
[ "Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate.", "Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.", "Cloning and analysis of the C4 photosynthetic NAD-d...
[ 1991, 1991, 1994, 1990, 1989 ]
5
[]
[ "IPR023667", "IPR048182" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 299, 22025, 15688, 311 ]
4
[ "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",...
[ 25, 1, 6, 25, 1, 16, 10, 2, 31, 15, 1, 2, 87 ]
13
true
Family
Malic oxidoreductase
Malic oxidoreductase
Malic_OxRdtase
7
IPR001892
1,892
Small ribosomal subunit protein uS13
Ribosomal_uS13
Family
34,983
false
false
Small ribosomal subunit protein uS13, previously known as Ribosomal protein S13, is one of the proteins from the small ribosomal subunit. In Escherichia coli, it is known to be involved in binding fMet-tRNA and, hence, in the initiation of translation. It is a basic protein of 115 to 177 amino-acid residues that contai...
[ "GO:0003723", "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "RNA binding", "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "HAMAP", "PFAM", "PIRSF" ]
[ "MF_01315", "PF00416", "PIRSF002134" ]
[ "Ribosomal_uS13", "Ribosomal_S13", "Ribosomal_S13" ]
[ 30930, 34944, 31846 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00556", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CFA-156827", "R-CFA-1799339", "R-CFA-72649", "R-CFA-72689", "R-CFA-72695", "R-CFA-72702", "R-CFA-72706", "R...
[ "PROSITEDOC:PDOC00556", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CFA-156827"...
109
[ "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1mj1", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l"...
1,801
[ "PUB00000201", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00059102" ]
[ "1872840", "11297922", "11290319", "11114498", "22096102" ]
[ "The primary structure of rat ribosomal protein S18.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "The structure of the eukaryotic ribosome at 3.0 A resolution." ]
[ 1991, 2001, 2001, 2000, 2011 ]
5
[]
[ "IPR019977", "IPR019980" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 912, 23339, 10241, 491 ]
4
[ "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",...
[ 12, 1, 2, 3, 1, 2, 5, 2, 14, 7, 3, 3, 27 ]
13
true
Family
Small ribosomal subunit protein uS13
Small ribosomal subunit protein uS13
Ribosomal_uS13
9
IPR001894
1,894
Cathelicidin-like
Cathelicidin-like
Family
1,469
false
false
Cathelicidins-related peptides from reptiles are also included in this family. They are potent antimicrobial peptides with low cytotoxicity, being interesting candidates as antimicrobial agents [ ]. Cathelicidins are antimicrobial peptides and, together with defensins, form a large group of cationic peptides with amphi...
[ "GO:0006952", "GO:0005576" ]
[ "defense response", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PANTHER" ]
[ "PTHR10206" ]
[ "" ]
[ 1469 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00729", "R-BTA-6798695", "R-BTA-6803157", "R-GGA-6798695", "R-GGA-6803157", "R-HSA-6798695", "R-HSA-6803157", "R-MMU-6798695", "R-MMU-6803157" ]
[ "PROSITEDOC:PDOC00729", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6803157", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-6803157", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6803157", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-6803157" ]
9
[ "1kwi", "1lxe", "1n5h", "1n5p", "1pfp", "4eyc" ]
6
[ "PUB00001695", "PUB00048248", "PUB00095113", "PUB00095114" ]
[ "7589491", "18818205", "23065264", "25100358" ]
[ "Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain.", "Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles.", "Cathelicidins: family of antimicrobial peptides. A review.", "Vipericidins: a...
[ 1995, 2008, 2012, 2014 ]
4
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1469 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 5, 5 ]
3
true
Family
Cathelicidin-like
Cathelicidin-like
Cathelicidin-like
9
IPR001895
1,895
Ras guanine-nucleotide exchange factors catalytic domain
RASGEF_cat_dom
Domain
64,128
false
false
This entry represents the catalytic domain of the Ras guanine-nucleotide exchange factors. Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP [ ] in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. The balance...
[ "GO:0005085", "GO:0007264" ]
[ "guanyl-nucleotide exchange factor activity", "small GTPase-mediated signal transduction" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00617", "PS50009", "SM00147", "cd00155" ]
[ "RasGEF", "RASGEF_CAT", "RasGEF", "RasGEF" ]
[ 63783, 62801, 61494, 44617 ]
4
[ "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "GenProp1511", "GenProp1548", "PDOC00594", "R-BTA-354192", "R-BTA-392517", "R-BTA-5673001", "R-CEL-1433557", "R-CEL-1433559", "R-CEL-179812", "R-CEL-180336", "R-CEL-1855204", "R-CEL-186763", "R-CEL-193648", "R-CEL-1963640", "R-CEL-2179392", "R-CEL-354192", "R-CEL-354194", "R-CEL-37...
[ "GP:GenProp1511", "GP:GenProp1548", "PROSITEDOC:PDOC00594", "REACTOME:R-BTA-354192", "REACTOME:R-BTA-392517", "REACTOME:R-BTA-5673001", "REACTOME:R-CEL-1433557", "REACTOME:R-CEL-1433559", "REACTOME:R-CEL-179812", "REACTOME:R-CEL-180336", "REACTOME:R-CEL-1855204", "REACTOME:R-CEL-186763", "RE...
234
[ "1bkd", "1nvu", "1nvv", "1nvw", "1nvx", "1xd2", "1xd4", "1xdv", "2byv", "2ii0", "2ije", "3cf6", "3ksy", "3qxl", "3t6a", "3t6g", "4f7z", "4jgw", "4l9m", "4mgi", "4mgk", "4mgy", "4mgz", "4mh0", "4nyi", "4nyj", "4nym", "4uru", "4urv", "4urw", "4urx", "4ury"...
116
[ "PUB00000728", "PUB00001017", "PUB00001237", "PUB00004087", "PUB00004162", "PUB00081668" ]
[ "7786285", "15335949", "8094051", "1898771", "8259209", "9438849" ]
[ "Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins.", "Ras regulation: putting back the GTP.", "Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase.", "The GTPase superfamily: conserved structure and molecular mechanism.", "Proteins regu...
[ 1995, 1992, 1993, 1991, 1993, 1998 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "organismal metagenomes" ]
[ 154, 63948, 24, 2 ]
4
[ "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...
[ 26, 325, 37, 176, 103, 4, 148, 5, 2 ]
9
true
Domain
Ras guanine-nucleotide exchange factors catalytic domain
Ras guanine-nucleotide exchange factors catalytic domain
RASGEF_cat_dom
1
IPR001896
1,896
Plant virus coat protein
Plant_vir_prot
Family
1,484
false
false
This family of membrane/coat proteins are found in a number of different ssRNA plant virus families that include Potexvirus, Hordeivirus and Carlavirus.
[]
[]
[]
0
[ "PFAM" ]
[ "PF01307" ]
[ "Plant_vir_prot" ]
[ 1484 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses" ]
[ 2, 4, 1478 ]
3
[]
[]
0
true
Family
Plant virus coat protein
Plant virus coat protein
Plant_vir_prot
9
IPR001897
1,897
Porin, gammaproteobacterial
Porin_gammaproteobac
Family
10,045
false
false
Porins are found in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts, where they form ion-selective channels for small hydrophilic molecules (up to ~600 D) [ , ]. X-ray structure analyses of several bacterial porins [ , , ] have revealed a 16-stranded anti-parallel β-barrel structure enclosi...
[ "GO:0015288", "GO:0034220", "GO:0009279", "GO:0016020" ]
[ "porin activity", "monoatomic ion transmembrane transport", "cell outer membrane", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR00183" ]
[ "ECOLIPORIN" ]
[ 10045 ]
1
[]
[]
[]
0
[ "1bt9", "1gfm", "1gfn", "1gfo", "1gfp", "1gfq", "1hxt", "1hxu", "1hxx", "1mpf", "1opf", "1osm", "1pho", "2j1n", "2j4u", "2omf", "2xe1", "2xe2", "2xe3", "2xe5", "2xg6", "2zfg", "2zld", "2zle", "3fyx", "3hw9", "3hwb", "3k19", "3k1b", "3nb3", "3nsg", "3o0e"...
93
[ "PUB00001604", "PUB00003334", "PUB00003475", "PUB00003829", "PUB00005073" ]
[ "1707373", "7525973", "1725488", "1373213", "2178269" ]
[ "The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.", "Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.", "A common channel-forming motif in evolutionarily distant porins.", "Porins and specific channels of bacterial out...
[ 1991, 1994, 1991, 1992, 1990 ]
5
[ "IPR001702" ]
[]
1
0
1
[ "Bacteria", "Caudoviricetes", "Eukaryota", "metagenomes" ]
[ 10016, 9, 12, 8 ]
4
[ "Escherichia coli (strain K12)" ]
[ 8 ]
1
true
Family
Porin, gammaproteobacterial
Porin, gammaproteobacterial
Porin_gammaproteobac
9
IPR001900
1,900
Ribonuclease II/R
RNase_II/R
Domain
46,563
false
false
This entry represents the catalytic domain of ribonuclease II [ ]. It includes characterised and related sequences to exoribonuclease II (RNase II) and ribonuclease R, a bacterial 3' --> 5' exoribonuclease homologous to RNase II [ , , ].
[ "GO:0003723", "GO:0004540" ]
[ "RNA binding", "RNA nuclease activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "SMART" ]
[ "PF00773", "SM00955" ]
[ "RNB", "RNB" ]
[ 46552, 45360 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.1.13.1", "PDOC00904", "R-CEL-429958", "R-CEL-450385", "R-CEL-450513", "R-CEL-9930044", "R-HSA-1368108", "R-HSA-1989781", "R-HSA-2151201", "R-HSA-2426168", "R-HSA-380994", "R-HSA-381340", "R-HSA-400206", "R-HSA-429958", "R-HSA-450385", "R-HSA-450513", "R-HSA-450604", "R-HSA-67912...
[ "EC:3.1.13.1", "PROSITEDOC:PDOC00904", "REACTOME:R-CEL-429958", "REACTOME:R-CEL-450385", "REACTOME:R-CEL-450513", "REACTOME:R-CEL-9930044", "REACTOME:R-HSA-1368108", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-2426168", "REACTOME:R-HSA-380994", "REACTOME:R-HSA-381340", ...
36
[ "2id0", "2ix0", "2ix1", "2r7d", "2r7f", "2vnu", "2wp8", "4ifd", "4pmw", "4ro1", "5c0w", "5c0x", "5g06", "5jea", "5k36", "5vzj", "5xgu", "6d6q", "6d6r", "6f3h", "6f4a", "6fsz", "6h25", "6lqs", "7ajt", "7aju", "7am1", "7d4i", "7dcy", "7dic", "7did", "7dol"...
48
[ "PUB00015537", "PUB00017190", "PUB00017191", "PUB00045119" ]
[ "11948193", "15604703", "9829834", "16806266" ]
[ "Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II.", "Ribosomal RNA processing and an RNase R family member in chloroplasts of Arabidopsis.", "The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitocho...
[ 2002, 2004, 1998, 2006 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 400, 28860, 16738, 16, 549 ]
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",...
[ 14, 2, 11, 7, 2, 12, 11, 3, 11, 21, 3, 5, 36 ]
13
true
Domain
Ribonuclease II/R
Ribonuclease II/R
RNase_II/R
2
IPR001901
1,901
Protein translocase complex, SecE/Sec61-gamma subunit
Translocase_SecE/Sec61-g
Family
29,265
false
false
Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component [ ]. From there, the mature proteins are either targeted to the outer membra...
[ "GO:0006605", "GO:0006886", "GO:0016020" ]
[ "protein targeting", "intracellular protein transport", "membrane" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PROSITE" ]
[ "MF_00422", "PF00584", "PS01067" ]
[ "SecE", "SecE", "SECE_SEC61G" ]
[ 26720, 28862, 14195 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00818", "R-BTA-9609523", "R-CEL-9609523", "R-CFA-9609523", "R-DDI-9609523", "R-DME-9609523", "R-HSA-1222387", "R-HSA-1236974", "R-HSA-1799339", "R-HSA-9609523", "R-HSA-9760173", "R-MMU-9609523", "R-SCE-9609523", "R-SPO-9609523" ]
[ "PROSITEDOC:PDOC00818", "REACTOME:R-BTA-9609523", "REACTOME:R-CEL-9609523", "REACTOME:R-CFA-9609523", "REACTOME:R-DDI-9609523", "REACTOME:R-DME-9609523", "REACTOME:R-HSA-1222387", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-9609523", "REACTOME:R-HSA-9760173", "REACTOME:...
14
[ "1rh5", "1rhz", "2akh", "2aki", "2ww9", "2wwa", "2wwb", "2yxq", "2yxr", "2zjs", "2zqp", "3bo0", "3bo1", "3din", "3dkn", "3dl8", "3j45", "3j46", "3j7q", "3j7r", "3jc2", "3mp7", "4cg5", "4cg6", "4cg7", "4v4n", "4v6m", "4v7i", "5a6u", "5abb", "5aww", "5ch4"...
95
[ "PUB00000955", "PUB00004170", "PUB00007064", "PUB00007065", "PUB00007066" ]
[ "9393849", "8107851", "2202721", "11336818", "10418149" ]
[ "Protein translocation in the three domains of life: variations on a theme.", "Evolutionary conservation of components of the protein translocation complex.", "The sec and prl genes of Escherichia coli.", "SecB, a molecular chaperone with two faces.", "Effects of pre-protein overexpression on SecB synthesis...
[ 1997, 1994, 1990, 2001, 1999 ]
5
[]
[ "IPR005807", "IPR008158" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 753, 23162, 4905, 445 ]
4
[ "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",...
[ 15, 1, 1, 6, 1, 1, 3, 1, 5, 10, 1, 1, 7 ]
13
true
Family
Protein translocase complex, SecE/Sec61-gamma subunit
Protein translocase complex, SecE/Sec61-gamma subunit
Translocase_SecE/Sec61-g
8
IPR001902
1,902
SLC26A/SulP transporter
SLC26A/SulP_fam
Family
66,639
false
false
The SLC26A/SulP family is a large and ubiquitous family with members derived from archaea, bacteria, fungi, plants and animals. Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues. Many of these p...
[ "GO:0055085", "GO:0016020" ]
[ "transmembrane transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PANTHER", "NCBIFAM" ]
[ "PTHR11814", "TIGR00815" ]
[ "", "sulP" ]
[ 66565, 28426 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00870", "R-BTA-174362", "R-BTA-427601", "R-CEL-174362", "R-CEL-427601", "R-HSA-174362", "R-HSA-3560792", "R-HSA-427601", "R-HSA-5619046", "R-HSA-5619085", "R-HSA-9662361", "R-MMU-174362", "R-MMU-427601", "R-RNO-174362", "R-RNO-427601", "R-SCE-174362", "R-SCE-427601", "R-SPO-17...
[ "PROSITEDOC:PDOC00870", "REACTOME:R-BTA-174362", "REACTOME:R-BTA-427601", "REACTOME:R-CEL-174362", "REACTOME:R-CEL-427601", "REACTOME:R-HSA-174362", "REACTOME:R-HSA-3560792", "REACTOME:R-HSA-427601", "REACTOME:R-HSA-5619046", "REACTOME:R-HSA-5619085", "REACTOME:R-HSA-9662361", "REACTOME:R-MMU-...
20
[ "2kln", "3llo", "3mgl", "3oir", "4dgf", "4dgh", "5eus", "5euu", "5euw", "5eux", "5euz", "5ezb", "6ki1", "6rtc", "6rtf", "7ch1", "7lgu", "7lgw", "7lh2", "7lh3", "7lhv", "7s8x", "7s9a", "7s9b", "7s9c", "7s9d", "7s9e", "7sun", "7v73", "7v74", "7v75", "7wk1"...
69
[ "PUB00018267", "PUB00072168", "PUB00072277", "PUB00075356" ]
[ "10662676", "24710176", "23506885", "21070944" ]
[ "The STAS domain - a link between anion transporters and antisigma-factor antagonists.", "Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters.", "The SLC26 gene family of anion transporters and channels.", "Structure of a SLC26 anion transporter STAS domain ...
[ 2000, 2014, 2013, 2010 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 127, 30068, 36050, 394 ]
4
[ "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",...
[ 74, 15, 27, 16, 1, 53, 37, 3, 54, 41, 3, 3, 66 ]
13
true
Family
SLC26A/SulP transporter
SLC26A/SulP transporter
SLC26A/SulP_fam
9
IPR001903
1,903
Spike glycoprotein fusion domain, Rhabdovirus
Rhabdo_glycop_FD
Domain
6,142
false
false
This entry represents the elongated fusion domain FD (also known as domain IV). The glycoprotein G from rhabdoviruses, such as rabies virus (RABV), Mokola virus (MOKV) and European bat lyssavirus 1 (EBLV) [ , , , , , ] attaches the virus to host cellular receptor, and induces endocytosis of the virion. It forms the gly...
[ "GO:0019031" ]
[ "viral envelope" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF00974" ]
[ "Rhabdo_glycop_FD" ]
[ 6142 ]
1
[]
[]
[]
0
[ "4d6w", "5i2m", "5i2s", "5mdm", "5oy9", "5oyl", "6lgw", "6lgx", "6tit", "6tmr", "7u9g", "8a1e", "8zhw", "8zhz", "9hgn", "9hh9", "9hhr", "9i8q", "9kef", "9kep", "9kfb" ]
21
[ "PUB00003167", "PUB00005582", "PUB00155794", "PUB00155795", "PUB00155796", "PUB00155797" ]
[ "9000093", "1660200", "35714192", "32150590", "35985336", "28188244" ]
[ "Low pH-induced pore formation by spike proteins of enveloped viruses.", "Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein.", "Structure of the rabies virus glycoprotein trimer bound to a prefusion-specific neutralizing antibody.", "Crystal structure of Mokola virus gly...
[ 1996, 1991, 2022, 2020, 2022, 2017 ]
6
[]
[]
0
0
null
[ "Protostomia", "Riboviria", "Shewanella intestini" ]
[ 29, 6112, 1 ]
3
[]
[]
0
true
Domain
Spike glycoprotein fusion domain, Rhabdovirus
Spike glycoprotein fusion domain, Rhabdovirus
Rhabdo_glycop_FD
6
IPR001905
1,905
Ammonium transporter
Ammonium_transpt
Family
40,771
false
false
All functionally characterised members of the ammonium transporter family are ammonia or ammonium uptake transporters. Some, but not others, also transport methylammonium. Uptake of ammonium/ammonia by AtmB protein from E. coli is electrogenic. Following sequestration of NH4+ at the periplasmic face, NH4+ is deprotonat...
[ "GO:0008519", "GO:0072488", "GO:0016020" ]
[ "ammonium channel activity", "ammonium transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PANTHER", "NCBIFAM" ]
[ "PTHR43029", "TIGR00836" ]
[ "", "amt" ]
[ 30501, 37137 ]
2
[ "PROSITEDOC" ]
[ "PDOC00937" ]
[ "PROSITEDOC:PDOC00937" ]
1
[ "1u77", "1u7c", "1u7g", "1xqe", "1xqf", "2b2f", "2b2h", "2b2i", "2b2j", "2nmr", "2nop", "2now", "2npc", "2npd", "2npe", "2npg", "2npj", "2npk", "2ns1", "2nuu", "3c1g", "3c1h", "3c1i", "3c1j", "4nh2", "5aex", "5aez", "5af1", "5ah3", "5aid", "5fuf", "6b21"...
39
[ "PUB00097855", "PUB00097856" ]
[ "32662768", "30211659" ]
[ "A two-lane mechanism for selective biological ammonium transport.", "The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB." ]
[ 2020, 2019 ]
2
[]
[ "IPR019879" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 615, 26233, 13333, 590 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosacchar...
[ 22, 4, 1, 1, 4, 23, 3, 3, 22 ]
9
true
Family
Ammonium transporter
Ammonium transporter
Ammonium_transpt
1
IPR001906
1,906
Terpene synthase, N-terminal domain
Terpene_synth_N
Domain
22,613
false
false
Sequences containing this domain belong to the terpene synthase family [ ]. It has been suggested that this gene family be designated tps (for terpene synthase). Sequence comparisons reveal similarities between the monoterpene (C 10 ) synthases, sesquiterpene (C 15 ) synthases and the diterpene (C 20 ) synthases. It ha...
[ "GO:0010333", "GO:0016829" ]
[ "terpene synthase activity", "lyase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF01397" ]
[ "Terpene_synth" ]
[ 22613 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP" ]
[ "4.2.3", "GenProp1471", "GenProp1638", "GenProp1709", "GenProp1739", "GenProp1760" ]
[ "EC:4.2.3", "GP:GenProp1471", "GP:GenProp1638", "GP:GenProp1709", "GP:GenProp1739", "GP:GenProp1760" ]
6
[ "1hx9", "1hxa", "1hxc", "1hxg", "1n1b", "1n1z", "1n20", "1n21", "1n22", "1n23", "1n24", "2j5c", "2ong", "2onh", "3g4d", "3g4f", "3lz9", "3m00", "3m01", "3m02", "3n0f", "3n0g", "3p5p", "3p5r", "3pya", "3pyb", "3s9v", "3sae", "3sdq", "3sdr", "3sdt", "3sdu"...
94
[ "PUB00002995", "PUB00011119", "PUB00097281" ]
[ "9268308", "9268298", "28841019" ]
[ "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase.", "Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expre...
[ 1997, 1997, 2017 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 22610, 3 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 151, 132, 183 ]
3
true
Domain
Terpene synthase, N-terminal domain
Terpene synthase, N-terminal domain
Terpene_synth_N
8
IPR001907
1,907
ATP-dependent Clp protease proteolytic subunit
ClpP
Family
72,797
false
false
Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin [ ] and is a member of peptidase family S14. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP [ , ], ...
[ "GO:0004176", "GO:0004252", "GO:0006508" ]
[ "ATP-dependent peptidase activity", "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PRINTS", "NCBIFAM", "CDD" ]
[ "MF_00444", "PR00127", "TIGR00493", "cd07017" ]
[ "ClpP", "CLPPROTEASEP", "clpP", "S14_ClpP_2" ]
[ 56921, 72330, 15058, 64039 ]
4
[ "EC", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21.92", "GenProp0251", "GenProp1108", "GenProp1137", "PDOC00358", "R-BTA-9837999", "R-CEL-9837999", "R-HSA-9837999", "R-MMU-9837999" ]
[ "EC:3.4.21.92", "GP:GenProp0251", "GP:GenProp1108", "GP:GenProp1137", "PROSITEDOC:PDOC00358", "REACTOME:R-BTA-9837999", "REACTOME:R-CEL-9837999", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-9837999" ]
9
[ "1tg6", "1tyf", "1y7o", "1yg6", "1yg8", "2c8t", "2cby", "2ce3", "2f6i", "2fzs", "2zl0", "2zl2", "2zl3", "2zl4", "3hln", "3ktg", "3kth", "3kti", "3ktj", "3ktk", "3mt6", "3p2l", "3q7h", "3qwd", "3st9", "3sta", "3tt6", "3tt7", "3v5e", "3v5i", "4emm", "4emp"...
190
[ "PUB00000953", "PUB00002564", "PUB00081432", "PUB00081434", "PUB00081435", "PUB00081437", "PUB00085963", "PUB00085964" ]
[ "9390554", "2197275", "17499722", "10320569", "2103893", "18824507", "19038348", "17302811" ]
[ "The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.", "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.", "ClpP: a distinctive family of cylindrical energy-dependent serine proteases.", "New insights into t...
[ 1997, 1990, 2007, 1999, 1990, 2008, 2009, 2007 ]
8
[ "IPR023562" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 34, 46552, 24496, 665, 1050 ]
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",...
[ 35, 1, 1, 3, 1, 3, 3, 1, 36, 2, 68 ]
11
true
Family
ATP-dependent Clp protease proteolytic subunit
ATP-dependent Clp protease proteolytic subunit
ClpP
6
IPR001908
1,908
Melanocortin receptor 3-5
MC3-5R
Family
4,410
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:0004977", "GO:0007186", "GO:0016020" ]
[ "melanocortin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00535" ]
[ "MELNOCORTINR" ]
[ 4410 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-375276", "R-BTA-418555", "R-DRE-375276", "R-HSA-375276", "R-HSA-418555", "R-HSA-9856649", "R-MMU-375276", "R-MMU-418555", "R-RNO-375276", "R-SSC-375276", "R-SSC-418555" ]
[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418555", "REACTOME:R-DRE-375276", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-375276", "REACTOME:R-SSC-375276", "REACTOME:R-SSC-418555" ]
11
[ "6w25", "7aue", "7f53", "7f54", "7f55", "7f58", "7piu", "7piv", "8inr", "8ioc", "8iod", "8kig", "8qj2", "8w8w", "8w8x", "8w8y", "8wky", "8wkz", "9k3f", "9k3h", "9k3k" ]
21
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00099937", "PUB00099938", "PUB00099939", "PUB00099940", "PUB00099941" ]
[ "2111655", "2830256", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293", "25163632", "32248247", "19036988", "12646665", "23869017" ]
[ "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, 2014, 2020, 2008, 2003, 2013 ]
15
[ "IPR001671" ]
[ "IPR000155", "IPR000621", "IPR002122" ]
1
3
0
[ "Vertebrata" ]
[ 4410 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 11, 17, 5 ]
4
true
Family
Melanocortin receptor 3-5
Melanocortin receptor 3-5
MC3-5R
1
IPR001910
1,910
Inosine/uridine-preferring nucleoside hydrolase domain
Inosine/uridine_hydrolase_dom
Domain
37,646
false
false
Inosine-uridine preferring nucleoside hydrolase ( ) (IU-nucleoside hydrolase or IUNH) is an enzyme first identified in protozoan [ ] that catalyses the hydrolysis of all of the commonly occuring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substr...
[ "GO:0016799" ]
[ "hydrolase activity, hydrolyzing N-glycosyl compounds" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF01156" ]
[ "IU_nuc_hydro" ]
[ 37646 ]
1
[ "GP", "GP", "GP", "GP" ]
[ "GenProp1369", "GenProp1430", "GenProp1465", "GenProp1540" ]
[ "GP:GenProp1369", "GP:GenProp1430", "GP:GenProp1465", "GP:GenProp1540" ]
4
[ "1ezr", "1hoz", "1hp0", "1kic", "1kie", "1mas", "1q8f", "1r4f", "1yoe", "2c40", "2ff1", "2ff2", "2mas", "3b9g", "3b9x", "3epw", "3epx", "3fz0", "3g5i", "3mkm", "3mkn", "3t8i", "3t8j", "4i70", "4i71", "4i72", "4i73", "4i74", "4i75", "4kl0", "4kpn", "4kpo"...
56
[ "PUB00000434", "PUB00000435" ]
[ "8634237", "8634238" ]
[ "Inosine-uridine nucleoside hydrolase from Crithidia fasciculata. Genetic characterization, crystallization, and identification of histidine 241 as a catalytic site residue.", "Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata." ]
[ 1996, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 318, 25929, 11084, 7, 308 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",...
[ 18, 2, 6, 4, 3, 3, 18, 1, 3, 63 ]
10
true
Domain
Inosine/uridine-preferring nucleoside hydrolase domain
Inosine/uridine-preferring nucleoside hydrolase domain
Inosine/uridine_hydrolase_dom
5
IPR001912
1,912
Small ribosomal subunit protein uS4, N-terminal
Ribosomal_uS4_N
Domain
61,517
false
false
This entry represents the domain found at the N terminus of the small ribosomal subunit uS4. Small ribosomal subunit protein uS4 was previously known as Ribosomal protein S4 in bacteria and plants and S9 in fungi and animals. S4 is known to bind directly to 16S ribosomal RNA. The crystal structure of a bacterial S4 pro...
[ "GO:0019843" ]
[ "rRNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "SMART" ]
[ "PF00163", "SM01390" ]
[ "Ribosomal_S4", "Ribosomal_S4" ]
[ 60740, 60099 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00549", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-6791226", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", ...
[ "PROSITEDOC:PDOC00549", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827"...
99
[ "1c05", "1c06", "1eg0", "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qd7", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo"...
1,812
[ "PUB00001317", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "9707415", "11297922", "11290319", "11114498" ]
[ "The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies o...
[ 1998, 2001, 2001, 2000 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctNZc11", "unclassified sequences" ]
[ 882, 24964, 35168, 1, 502 ]
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",...
[ 16, 2, 2, 4, 1, 7, 7, 2, 14, 7, 3, 3, 26 ]
13
true
Domain
Small ribosomal subunit protein uS4, N-terminal
Small ribosomal subunit protein uS4, N-terminal
Ribosomal_uS4_N
9
IPR001913
1,913
Equine arteritis virus GP2b envelope glycoprotein
Equi_arteri_GP2b
Family
142
false
false
Equine arteritis virus (EAV) is an enveloped, positive-strand RNA virus belonging to the family Arteriviridae. EAV virions contain six different envelope proteins. GP5 (previously named GL) and the unglycosylated membrane protein M are the major envelope proteins, while the glycoproteins GP2b (previously named Gs), GP3...
[ "GO:0019031" ]
[ "viral envelope" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF01309" ]
[ "EAV_GS" ]
[ 142 ]
1
[]
[]
[]
0
[]
0
[ "PUB00003515", "PUB00005632", "PUB00076655" ]
[ "7745690", "8938984", "14645556" ]
[ "The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer.", "Comparison of nucleic and amino acid sequences and phylogenetic analysis of the Gs protein of various equine arteritis virus isolates.", "Intra- and intermolecular disulfide bonds ...
[ 1995, 1996, 2003 ]
3
[]
[]
0
0
null
[ "Equine arteritis virus" ]
[ 142 ]
1
[]
[]
0
true
Family
Equine arteritis virus GP2b envelope glycoprotein
Equine arteritis virus GP2b envelope glycoprotein
Equi_arteri_GP2b
8
IPR001915
1,915
Peptidase M48
Peptidase_M48
Domain
88,033
false
false
This entry represents the largely extracellular catalytic region of CAAX prenyl protease homologues such as Human FACE-1 protease. These are metallopeptidases, with the characteristic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds ...
[ "GO:0004222", "GO:0006508" ]
[ "metalloendopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01435" ]
[ "Peptidase_M48" ]
[ 88033 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24.-", "PWY-8119", "R-BTA-169911", "R-BTA-9840373", "R-DRE-169911", "R-DRE-9840373", "R-HSA-169911", "R-HSA-9837999", "R-HSA-9840373", "R-MMU-169911", "R-MMU-9840373", "R-RNO-169911", "R-RNO-9840373", "R-SCE-169911", "R-SCE-9840373", "R-SPO-169911", "R-SPO-9840373" ]
[ "EC:3.4.24.-", "METACYC:PWY-8119", "REACTOME:R-BTA-169911", "REACTOME:R-BTA-9840373", "REACTOME:R-DRE-169911", "REACTOME:R-DRE-9840373", "REACTOME:R-HSA-169911", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9840373", "REACTOME:R-MMU-169911", "REACTOME:R-MMU-9840373", "REACTOME:R-RNO-169911", "R...
17
[ "2ypt", "3c37", "3cqb", "4aw6", "4il3", "5syt", "6ait", "6bh8", "6sar" ]
9
[ "PUB00075616", "PUB00075617" ]
[ "23539602", "23539603" ]
[ "Structure of the integral membrane protein CAAX protease Ste24p.", "The structural basis of ZMPSTE24-dependent laminopathies." ]
[ 2013, 2013 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2538, 72801, 11498, 16, 1180 ]
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",...
[ 17, 1, 3, 5, 4, 5, 3, 2, 9, 7, 2, 3, 41 ]
13
true
Domain
Peptidase M48
Peptidase M48
Peptidase_M48
1
IPR001916
1,916
Glycoside hydrolase, family 22
Glyco_hydro_22
Family
5,996
false
false
Glycoside hydrolase family 22 comprises enzymes with two known activities; lysozyme type C ( ) (also known as 1, 4-beta-N-acetylmuramidase or LYZ) and alpha-lactalbumins (also known as lactose synthase B protein or LA). Asp and/or the carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nuc...
[]
[]
[]
0
[ "PFAM", "PRINTS", "PROFILE", "PANTHER", "SMART" ]
[ "PF00062", "PR00135", "PS51348", "PTHR11407", "SM00263" ]
[ "Lys", "LYZLACT", "GLYCOSYL_HYDROL_F22_2", "", "LYZ1" ]
[ 5923, 5232, 5842, 5776, 5692 ]
5
[ "CAZY", "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH22", "3.2.1.17", "PDOC00119", "R-BTA-6798695", "R-BTA-6803157", "R-CFA-6798695", "R-CFA-6803157", "R-DME-5653890", "R-GGA-5653890", "R-GGA-6798695", "R-GGA-6803157", "R-HSA-5653890", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-977225", "R-MMU-5653890", "R-MMU-6798695", "R-MMU-68031...
[ "CAZY:GH22", "EC:3.2.1.17", "PROSITEDOC:PDOC00119", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6803157", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-6803157", "REACTOME:R-DME-5653890", "REACTOME:R-GGA-5653890", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-6803157", "REACTOME:R-HSA-5653890", "REACT...
23
[ "132l", "133l", "134l", "135l", "193l", "194l", "1a2y", "1a4v", "1aki", "1alc", "1at5", "1at6", "1azf", "1b0d", "1b2k", "1b5u", "1b5v", "1b5w", "1b5x", "1b5y", "1b5z", "1b7l", "1b7m", "1b7n", "1b7o", "1b7p", "1b7q", "1b7r", "1b7s", "1b9o", "1bb3", "1bb4"...
1,616
[ "PUB00001331", "PUB00001375", "PUB00001550", "PUB00002334", "PUB00002403", "PUB00002496", "PUB00003998", "PUB00004870", "PUB00005266", "PUB00071536" ]
[ "3104032", "2731545", "3666156", "3148618", "6715332", "2738070", "3785375", "7624375", "8535779", "12606493" ]
[ "Alpha-lactalbumin and related proteins: a versatile gene family with an interesting parentage.", "The evolution of lysozyme and alpha-lactalbumin.", "The calcium-binding property of equine lysozyme.", "Amino acid sequence of a lysozyme (B-enzyme) from Bacillus subtilis YT-25.", "Evolution of alpha-lactalbu...
[ 1986, 1989, 1987, 1988, 1984, 1989, 1986, 1995, 1995, 2003 ]
10
[]
[ "IPR000545", "IPR000974" ]
0
2
0
[ "Bacteria", "Caudoviricetes", "Eukaryota", "viral metagenome" ]
[ 13, 3, 5976, 4 ]
4
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 15, 22, 24, 23, 32 ]
5
true
Family
Glycoside hydrolase, family 22
Glycoside hydrolase, family 22
Glyco_hydro_22
7
IPR001917
1,917
Aminotransferase, class-II, pyridoxal-phosphate binding site
Aminotrans_II_pyridoxalP_BS
Binding_site
70,013
false
false
Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies. One of these, is called class-II. It consi...
[ "GO:0016740" ]
[ "transferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00599" ]
[ "AA_TRANSFER_CLASS_2" ]
[ 70013 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00518", "R-BTA-189451", "R-DRE-189451", "R-GGA-421984", "R-HSA-1660661", "R-HSA-189451", "R-HSA-1989781", "R-HSA-2151201", "R-HSA-9837999", "R-MMU-1660661", "R-MMU-189451", "R-MMU-9837999", "R-RNO-1660661", "R-RNO-189451", "R-RNO-9837999", "R-SCE-189451", "R-SPO-189451" ]
[ "PROSITEDOC:PDOC00518", "REACTOME:R-BTA-189451", "REACTOME:R-DRE-189451", "REACTOME:R-GGA-421984", "REACTOME:R-HSA-1660661", "REACTOME:R-HSA-189451", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-1660661", "REACTOME:R-MMU-189451", "REACTOME:R-MMU...
17
[ "1bs0", "1dj9", "1dje", "1fc4", "1fg3", "1fg7", "1gew", "1gex", "1gey", "1h1c", "1iji", "1uu0", "1uu1", "1uu2", "2bwn", "2bwo", "2bwp", "2f8j", "2g6w", "2jg2", "2jgt", "2w8j", "2w8t", "2w8u", "2w8v", "2w8w", "2x8u", "2xbn", "3a2b", "3hdo", "3tqx", "3wy7"...
119
[ "PUB00007901" ]
[ "11518529" ]
[ "Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 891, 53478, 14861, 4, 779 ]
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",...
[ 13, 2, 8, 3, 3, 12, 18, 2, 4, 20, 3, 3, 16 ]
13
true
Binding_site
Aminotransferase, class-II, pyridoxal-phosphate binding site
Aminotransferase, class-II, pyridoxal-phosphate binding site
Aminotrans_II_pyridoxalP_BS
5
IPR001919
1,919
Carbohydrate-binding type-2 domain
CBD2
Domain
27,537
false
false
The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) [ ]. Structurally, cellulases and xylanases generally consist of a catalytic domain and a conserved region of ~100 amino aci...
[ "GO:0004553", "GO:0030246", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate binding", "carbohydrate metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00553", "PS51173", "SM00637" ]
[ "CBM_2", "CBM2", "CBD_II" ]
[ 25965, 26655, 27108 ]
3
[ "EC", "GP", "PROSITEDOC" ]
[ "3.2.1", "GenProp1522", "PDOC00485" ]
[ "EC:3.2.1", "GP:GenProp1522", "PROSITEDOC:PDOC00485" ]
3
[ "1e5b", "1e5c", "1exg", "1exh", "1heh", "1hej", "1xbd", "2cwr", "2czn", "2rtt", "2xbd", "3ndy", "3ndz", "5dhd", "5dhe", "6bt9", "6f7e", "6qfs" ]
18
[ "PUB00000421", "PUB00003608", "PUB00005068", "PUB00032378", "PUB00033740" ]
[ "7766609", "1886523", "1812490", "10425686", "9662439" ]
[ "Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy.", "Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.", "Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides.", "A family ...
[ 1995, 1991, 1991, 1999, 1998 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Megaviricetes", "Thermococcaceae", "unclassified sequences" ]
[ 27033, 431, 21, 10, 42 ]
5
[]
[]
0
true
Domain
Carbohydrate-binding type-2 domain
Carbohydrate-binding type-2 domain
CBD2
5
IPR001920
1,920
Asp/Glu racemase
Asp/Glu_race
Homologous_superfamily
43,708
false
false
Aspartate racemase ( ) and glutamate racemase ( ) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [ ]. Glutamate racemase catalyses the interconversion of d-and l-glutamic acid and is the source of d-glutamate in most bacterial strains. d-Glutamic acid is an impo...
[ "GO:0016855" ]
[ "racemase and epimerase activity, acting on amino acids and derivatives" ]
[ "molecular_function" ]
1
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.40.50.1860", "SSF53681" ]
[ "", "" ]
[ 42670, 42171 ]
2
[ "EC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "5.1.1.3", "PWY-6386", "PWY-6387", "PDOC00714" ]
[ "EC:5.1.1.3", "METACYC:PWY-6386", "METACYC:PWY-6387", "PROSITEDOC:PDOC00714" ]
4
[ "1b73", "1b74", "1iu9", "1jfl", "1zuw", "2dgd", "2dwu", "2dx7", "2eq5", "2gzm", "2jfn", "2jfo", "2jfp", "2jfq", "2jfu", "2jfv", "2jfw", "2jfx", "2jfy", "2jfz", "2ohg", "2oho", "2ohv", "2vvt", "2w4i", "2zsk", "3hfr", "3ist", "3isv", "3ojc", "3out", "3s7z"...
60
[ "PUB00000380", "PUB00023532", "PUB00083403", "PUB00083404" ]
[ "8385993", "10331867", "10194325", "11371180" ]
[ "Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus.", "Structure and mechanism of glutamate racemase from Aquifex pyrophilus.", "Catalytic acid/base residues of glutamate racemase.", "Active site residues of glutamate racemase." ]
[ 1993, 1999, 1999, 2001 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 340, 40811, 1813, 2, 742 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 5, 3, 3, 1, 6 ]
5
true
Homologous_superfamily
Asp/Glu racemase
Asp/Glu racemase
Asp/Glu_race
2
IPR001921
1,921
Large ribosomal subunit protein eL8, eukaryota
Ribosomal_eL8_euk
Family
7,032
false
false
This family includes the large ribosomal subunit protein eL8 from human, which was formerly known as L7a, and its homologues [ , ]. The human gene resembles other mammalian ribosomal protein genes so far, as it contains a short first exon, a short 5' untranslated leader and its transcriptional start sites at C residues...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR00882" ]
[ "RIBOSOMALL7A" ]
[ 7032 ]
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-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706", "R-DDI-97595...
[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-9759...
64
[ "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "3jcs", "3jct", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u", "4u4y", "4u4z"...
586
[ "PUB00000574", "PUB00003742", "PUB00004372", "PUB00005644", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00101554" ]
[ "1756182", "2046660", "2183194", "2063628", "11297922", "11290319", "11114498", "32669547" ]
[ "The organization and expression of the human L7a ribosomal protein gene.", "The organization and expression of the Saccharomyces cerevisiae L4 ribosomal protein genes and their identification as the homologues of the mammalian ribosomal protein gene L7a.", "Ribosomal protein L4 of Saccharomyces cerevisiae: the...
[ 1991, 1991, 1990, 1991, 2001, 2001, 2000, 2020 ]
8
[ "IPR018492" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Natronococcus pandeyae" ]
[ 4, 7027, 1 ]
3
[ "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...
[ 8, 1, 1, 2, 4, 6, 1, 6, 33, 2, 1, 14 ]
12
true
Family
Large ribosomal subunit protein eL8, eukaryota
Large ribosomal subunit protein eL8, eukaryota
Ribosomal_eL8_euk
8
IPR001922
1,922
Dopamine D2 receptor
Dopamine_D2_rcpt
Family
1,126
false
false
Dopamine receptors are members of the rhodopsin-like G-protein coupled receptor family and are prominent in the vertebrate central nervous system (CNS). Dysfunction of dopaminergic neurotransmission in the CNS has been implicated in a variety of neuropsychiatric disorders [ ], including social phobia [ ], Tourette's sy...
[ "GO:0004952", "GO:0007195", "GO:0016020" ]
[ "dopamine neurotransmitter receptor activity", "adenylate cyclase-inhibiting dopamine receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00567" ]
[ "DOPAMINED2R" ]
[ 1126 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME" ]
[ "215", "R-HSA-390651", "R-MMU-390651", "R-RNO-390651" ]
[ "IUPHAR:215", "REACTOME:R-HSA-390651", "REACTOME:R-MMU-390651", "REACTOME:R-RNO-390651" ]
4
[ "7jvr", "8irs", "8tzq", "8u02", "9bs9", "9bsb" ]
6
[ "PUB00064281", "PUB00064282", "PUB00064283", "PUB00064284", "PUB00064285", "PUB00064286", "PUB00064287", "PUB00064288", "PUB00064289", "PUB00064290", "PUB00064291", "PUB00064292", "PUB00064293", "PUB00064301", "PUB00067001", "PUB00067006", "PUB00067007", "PUB00067008" ]
[ "15148138", "10698826", "16613557", "17017512", "12555236", "16961425", "11920678", "9633679", "16433053", "14060771", "1060115", "12836695", "9457173", "16968475", "16458973", "15671878", "9169514", "11303741" ]
[ "The neurobiology of dopamine signaling.", "Low dopamine D(2) receptor binding potential in social phobia.", "Dopamine and the diseased brain.", "The nigrostriatal DA pathway and Parkinson's disease.", "Relationship between functional dopamine D2 and D3 receptors gene polymorphisms and neuroleptic malignant...
[ 2004, 2000, 2006, 2006, 2003, 2006, 2002, 1998, 2005, 1963, 1975, 2003, 1998, 2006, 2006, 2005, 1997, 2001 ]
18
[ "IPR000929" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1126 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 4, 1, 3 ]
4
true
Family
Dopamine D2 receptor
Dopamine D2 receptor
Dopamine_D2_rcpt
3
IPR001925
1,925
Porin, eukaryotic type
Porin_Euk
Family
12,673
false
false
Eukaryotic mitochondrial porins are voltage-dependent anion-selective channels (VDAC) that behave as general diffusion pores for small hydrophilic molecules [ , , , ]. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The proteins are compo...
[ "GO:0008308", "GO:0098656", "GO:0005741" ]
[ "voltage-gated monoatomic anion channel activity", "monoatomic anion transmembrane transport", "mitochondrial outer membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PROSITE", "PANTHER", "CDD" ]
[ "PR00185", "PS00558", "PTHR11743", "cd07306" ]
[ "EUKARYTPORIN", "EUKARYOTIC_PORIN", "", "Porin3_VDAC" ]
[ 7008, 5291, 12531, 11350 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00483", "R-BTA-5205685", "R-BTA-5689880", "R-BTA-70268", "R-CEL-5205685", "R-CEL-5689880", "R-CEL-70268", "R-DDI-5205685", "R-DDI-70268", "R-DME-5205685", "R-DME-5689880", "R-DME-70268", "R-HSA-1268020", "R-HSA-5205685", "R-HSA-5689880", "R-HSA-70268", "R-HSA-8949215", "R-MMU-...
[ "PROSITEDOC:PDOC00483", "REACTOME:R-BTA-5205685", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-70268", "REACTOME:R-CEL-5205685", "REACTOME:R-CEL-5689880", "REACTOME:R-CEL-70268", "REACTOME:R-DDI-5205685", "REACTOME:R-DDI-70268", "REACTOME:R-DME-5205685", "REACTOME:R-DME-5689880", "REACTOME:R-DME-...
31
[ "2jk4", "2k4t", "3emn", "4bum", "4c69", "5jdp", "5xdn", "5xdo", "6g6u", "6g73", "6tiq", "6tir", "7kuh", "7nie", "7qi2", "7tcv", "8j0o", "9eih", "9eii", "9eij", "9gng", "9jvq" ]
22
[ "PUB00000661", "PUB00001485", "PUB00001974", "PUB00002365", "PUB00005391", "PUB00072140", "PUB00158948" ]
[ "8031826", "1689252", "8812436", "2442148", "1384178", "22020053", "31015432" ]
[ "Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins.", "The biogenesis and function of eukaryotic porins.", "A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8.", "Molecular genetics of the VDAC ion channel: structura...
[ 1994, 1990, 1996, 1987, 1992, 2012, 2019 ]
7
[ "IPR027246" ]
[]
1
0
1
[ "Actinomycetes", "Eukaryota", "bird metagenome" ]
[ 2, 12670, 1 ]
3
[ "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...
[ 25, 1, 13, 8, 18, 15, 1, 11, 14, 2, 1, 52 ]
12
true
Family
Porin, eukaryotic type
Porin, eukaryotic type
Porin_Euk
8
IPR001926
1,926
Tryptophan synthase beta chain-like, PALP domain
TrpB-like_PALP
Domain
236,235
false
false
This entry represents a domain found in a group of proteins of the PLP-dependent enzymes superfamily represented by the beta subunit of tryptophan synthase (TrpB) [ ]. This group of diverse proteins also include threonine dehydratase, cysteine synthase, threonine synthase and pyridoxal phosphate-dependent deaminase.
[]
[]
[]
0
[ "PFAM" ]
[ "PF00291" ]
[ "PALP" ]
[ 236235 ]
1
[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1223", "GenProp1274", "R-BTA-977347", "R-CEL-1614603", "R-DDI-1614603", "R-DDI-8849175", "R-DDI-977347", "R-HSA-1614603", "R-HSA-2408508", "R-HSA-8849175", "R-HSA-977347", "R-MMU-1614603", "R-MMU-8849175", "R-MMU-977347", "R-MTU-936654", "R-MTU-936721", "R-RNO-1614603", "R-...
[ "GP:GenProp1223", "GP:GenProp1274", "REACTOME:R-BTA-977347", "REACTOME:R-CEL-1614603", "REACTOME:R-DDI-1614603", "REACTOME:R-DDI-8849175", "REACTOME:R-DDI-977347", "REACTOME:R-HSA-1614603", "REACTOME:R-HSA-2408508", "REACTOME:R-HSA-8849175", "REACTOME:R-HSA-977347", "REACTOME:R-MMU-1614603", ...
23
[ "1a50", "1a5a", "1a5b", "1a5s", "1beu", "1bks", "1c29", "1c8v", "1c9d", "1cw2", "1cx9", "1d6s", "1e5x", "1f2d", "1fcj", "1fuy", "1j0a", "1j0b", "1j0c", "1j0d", "1j0e", "1jbq", "1k3u", "1k7e", "1k7f", "1k7x", "1k8x", "1k8y", "1k8z", "1kfb", "1kfc", "1kfe"...
443
[ "PUB00070977" ]
[ "10673430" ]
[ "The manifold of vitamin B6 dependent enzymes." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 5972, 180925, 45577, 31, 3730 ]
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",...
[ 94, 13, 12, 3, 9, 22, 14, 11, 59, 21, 9, 7, 125 ]
13
true
Domain
Tryptophan synthase beta chain-like, PALP domain
Tryptophan synthase beta chain-like, PALP domain
TrpB-like_PALP
6
IPR001927
1,927
Sodium:galactoside symporter
Na/Gal_symport
Domain
17,094
false
false
It has been shown [ ] that integral membrane proteins that mediate the intake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. This collection of sequences represents the...
[ "GO:0006814", "GO:0016020" ]
[ "sodium ion transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "NCBIFAM" ]
[ "TIGR00792" ]
[ "gph" ]
[ 17094 ]
1
[ "PROSITEDOC" ]
[ "PDOC00680" ]
[ "PROSITEDOC:PDOC00680" ]
1
[ "4m64", "7l16", "7l17", "8fq9", "8frh", "8t60" ]
6
[ "PUB00000660" ]
[ "8031825" ]
[ "A functional superfamily of sodium/solute symporters." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 17037, 10, 1, 46 ]
4
[ "Escherichia coli (strain K12)" ]
[ 7 ]
1
true
Domain
Sodium:galactoside symporter
Sodium:galactoside symporter
Na/Gal_symport
2
IPR001928
1,928
Endothelin-like toxin
Endothln-like_toxin
Domain
2,957
false
false
Endothelins (ET's) are the most potent vasoconstrictors known [ , , ]. They stimulate cardiac contraction, regulate release of vasoactive substances, and stimulate mitogenesis in blood vessels in primary culture. They also stimulate contraction in almost all other smooth muscles (e.g., uterus, bronchus, vas deferensa a...
[ "GO:0019229", "GO:0005576" ]
[ "regulation of vasoconstriction", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "SMART" ]
[ "PF00322", "SM00272" ]
[ "Endothelin", "END" ]
[ 2908, 2946 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00243", "R-BTA-375276", "R-BTA-416476", "R-CFA-375276", "R-CFA-416476", "R-HSA-375276", "R-HSA-416476", "R-HSA-9856649", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476", "R-SSC-375276", "R-SSC-416476" ]
[ "PROSITEDOC:PDOC00243", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-416476", "REACTOME:R-CFA-375276", "REACTOME:R-CFA-416476", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416...
14
[ "1edn", "1edp", "1srb", "1t7h", "1v6r", "2lde", "2ldf", "3cmh", "5glh", "6cmh", "6dk5", "6igk", "6igl", "6lry", "8hbd", "8hcq", "8hcx", "8iy5", "8iy6", "8xgr", "8xve", "8xvh", "8xvi", "8xwp", "8xwq", "8zrt" ]
26
[ "PUB00001506", "PUB00001510", "PUB00005372", "PUB00005552", "PUB00005553" ]
[ "2168326", "1916094", "1656557", "2549664", "2690429" ]
[ "Cellular signaling by peptides of the endothelin gene family.", "Endothelins.", "Endothelins and sarafotoxins: physiological regulation, receptor subtypes and transmembrane signaling.", "Similarities in mode and sites of action of sarafotoxins and endothelins.", "Molecular biology and biochemistry of the e...
[ 1990, 1991, 1991, 1989, 1989 ]
5
[]
[]
0
0
null
[ "Bacillati", "Bilateria", "Chordopoxvirinae" ]
[ 2, 2952, 3 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 8, 6, 9 ]
4
true
Domain
Endothelin-like toxin
Endothelin-like toxin
Endothln-like_toxin
1
IPR001932
1,932
PPM-type phosphatase-like domain
PPM-type_phosphatase-like_dom
Domain
234,626
false
false
Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg2- or Mn2-dependent (...
[]
[]
[]
0
[ "PFAM", "PFAM", "PFAM", "PROFILE", "SMART", "SMART", "CDD" ]
[ "PF00481", "PF07228", "PF13672", "PS51746", "SM00331", "SM00332", "cd00143" ]
[ "PP2C", "SpoIIE", "PP2C_2", "PPM_2", "PP2C_SIG", "PP2Cc", "PP2Cc" ]
[ 104387, 85290, 37744, 149655, 132803, 137910, 126810 ]
7
[ "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", "3.1.3.16", "R-BTA-1169408", "R-BTA-204174", "R-BTA-2173795", "R-BTA-380972", "R-BTA-70895", "R-CEL-1169408", "R-CEL-2173795", "R-CEL-380972", "R-DME-199418", "R-DME-6803207", "R-HSA-1169408", "R-HSA-1660661", "R-HSA-168638", "R-HSA-199418", "R-HSA-204174", "R-HSA-2173795"...
[ "EC:3.1.3", "EC:3.1.3.16", "REACTOME:R-BTA-1169408", "REACTOME:R-BTA-204174", "REACTOME:R-BTA-2173795", "REACTOME:R-BTA-380972", "REACTOME:R-BTA-70895", "REACTOME:R-CEL-1169408", "REACTOME:R-CEL-2173795", "REACTOME:R-CEL-380972", "REACTOME:R-DME-199418", "REACTOME:R-DME-6803207", "REACTOME:R...
66
[ "1a6q", "1txo", "2cm1", "2i0o", "2i44", "2iq1", "2irm", "2isn", "2j4o", "2j82", "2j86", "2jfr", "2jfs", "2jft", "2p8e", "2pk0", "2pnq", "2pom", "2pop", "2v06", "2xzv", "2y09", "3d8k", "3eq2", "3es2", "3f79", "3f7a", "3fxj", "3fxk", "3fxl", "3fxm", "3fxo"...
128
[ "PUB00001297", "PUB00056982", "PUB00074808", "PUB00074809", "PUB00101158" ]
[ "9003755", "22115775", "9869399", "22668558", "24518043" ]
[ "Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.", "Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis.", "Protein phosphatase 2C (PP2C) function in higher plants.", "Function analysis of conserved amino acid residues in a Mn(2+...
[ 1996, 2011, 1998, 2012, 2014 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 354, 120383, 112739, 96, 1054 ]
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",...
[ 350, 13, 57, 35, 1, 83, 56, 8, 200, 82, 8, 7, 810 ]
13
true
Domain
PPM-type phosphatase-like domain
PPM-type phosphatase-like domain
PPM-type_phosphatase-like_dom
9
IPR001933
1,933
Neuropeptide Y4 receptor
NPY4_rcpt
Family
659
false
false
Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit...
[ "GO:0004983", "GO:0007186", "GO:0016020" ]
[ "neuropeptide Y receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01015" ]
[ "NRPEPTIDEY4R" ]
[ 659 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "307", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "IUPHAR:307", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
7
[ "7x9c" ]
1
[ "PUB00002930", "PUB00063739", "PUB00063740", "PUB00063741", "PUB00063742", "PUB00063743", "PUB00063744", "PUB00063745", "PUB00063746", "PUB00063747", "PUB00063748", "PUB00063749", "PUB00063750", "PUB00063751", "PUB00063752", "PUB00063753", "PUB00063754", "PUB00063755", "PUB000637...
[ "7592911", "6549409", "16874931", "6547387", "6549039", "2821236", "8395947", "16190896", "7529442", "7644568", "15337373", "8685245", "8369959", "11287113", "7629398", "6133408", "3855566", "12678499", "17222466", "8013354", "9833945", "9389418", "9446690", "2453065", ...
[ "Cloning and functional expression of a human Y4 subtype receptor for pancreatic polypeptide, neuropeptide Y, and peptide YY.", "Neuropeptide Y: a potent inducer of consummatory behavior in rats.", "Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.", "Neuropeptide Y and human pancrea...
[ 1995, 1984, 2006, 1984, 1984, 1987, 1993, 2005, 1994, 1995, 2004, 1996, 1993, 2001, 1995, 1982, 1985, 2003, 2007, 1994, 1998, 1997, 1998, 1988, 1991, 1995, 2003, 2007, 1998, 2004, 2007, 2007, 2007, 2006, 2007, 2006, 2007, 2008, 1996, 1996...
42
[ "IPR000611" ]
[]
1
0
1
[ "Vertebrata" ]
[ 659 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 2, 2 ]
4
true
Family
Neuropeptide Y4 receptor
Neuropeptide Y4 receptor
NPY4_rcpt
2
IPR001936
1,936
Ras GTPase-activating domain
RasGAP_dom
Domain
35,943
false
false
This entry represents a conserved domain in the RasGAPs (Ras GTPase-activating proteins). This domain is also known as the RasGAP domain. Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP [ ]. This intrinsic GTPase activity of Ras is regulated by a family of p...
[ "GO:0043087" ]
[ "regulation of GTPase activity" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00616", "PS50018", "SM00323" ]
[ "RasGAP", "RAS_GTPASE_ACTIV_2", "RasGAP" ]
[ 34566, 35799, 31427 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00438", "R-BTA-8856828", "R-BTA-8876198", "R-CEL-8856828", "R-CEL-8876198", "R-DDI-5626467", "R-DDI-5658442", "R-DDI-6798695", "R-DDI-9013149", "R-DDI-9013404", "R-DDI-9013406", "R-DDI-9013408", "R-DDI-9013420", "R-DDI-9013424", "R-DME-5658442", "R-DME-8856828", "R-DME-8876198",...
[ "PROSITEDOC:PDOC00438", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8876198", "REACTOME:R-CEL-8856828", "REACTOME:R-CEL-8876198", "REACTOME:R-DDI-5626467", "REACTOME:R-DDI-5658442", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9013149", "REACTOME:R-DDI-9013404", "REACTOME:R-DDI-9013406", "REACTOME:...
88
[ "1nf1", "1wer", "1wq1", "3bxj", "3fay", "5cjp", "6ob2", "6ob3", "6v65", "6v6f", "7moc", "7mp5", "7mp6", "7pgp", "7pgq", "7pgr", "7pgs", "7pgt", "7pgu", "7r03", "7r04", "8bos", "8e20", "8edl", "8edm", "8edn", "8edo", "8eoz", "9bz4" ]
29
[ "PUB00000726", "PUB00000983", "PUB00004087", "PUB00004162" ]
[ "7945277", "1883874", "1898771", "8259209" ]
[ "Regulation of the Ras signalling network.", "sar1, a gene from Schizosaccharomyces pombe encoding a protein that regulates ras1.", "The GTPase superfamily: conserved structure and molecular mechanism.", "Proteins regulating Ras and its relatives." ]
[ 1994, 1991, 1991, 1993 ]
4
[]
[ "IPR037776" ]
0
1
0
[ "Bacteria", "Eukaryota", "Halopenitus persicus", "Marseillevirus LCMAC101", "ecological metagenomes" ]
[ 48, 35891, 1, 1, 2 ]
5
[ "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...
[ 5, 151, 22, 72, 55, 4, 83, 4, 2 ]
9
true
Domain
Ras GTPase-activating domain
Ras GTPase-activating domain
RasGAP_dom
2
IPR001937
1,937
Galactose-1-phosphate uridyl transferase, class I
GalP_UDPtransf1
Family
14,240
false
false
Galactose-1-phosphate uridyl transferase (GalT) catalyses the transfer of an uridyldiphosphate group on galactose (or glucose) 1-phosphate. During the reaction, the uridyl moiety links to a histidine residue. In the Escherichia coli enzyme, it has been shown [ ] that two histidine residues separated by a single proline...
[ "GO:0008108", "GO:0008270", "GO:0006012" ]
[ "UDP-glucose:hexose-1-phosphate uridylyltransferase activity", "zinc ion binding", "galactose metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "PIRSF000808", "PTHR11943", "TIGR00209", "cd00608" ]
[ "GalT", "", "galT_1", "GalT" ]
[ 12808, 12079, 12520, 7747 ]
4
[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.7.12", "GenProp0143", "GenProp1310", "GenProp1661", "PWY-6317", "PWY-6527", "PDOC00108", "R-CEL-70370", "R-DME-70370", "R-HSA-5609978", "R-HSA-70370", "R-MMU-70370", "R-RNO-70370" ]
[ "EC:2.7.7.12", "GP:GenProp0143", "GP:GenProp1310", "GP:GenProp1661", "METACYC:PWY-6317", "METACYC:PWY-6527", "PROSITEDOC:PDOC00108", "REACTOME:R-CEL-70370", "REACTOME:R-DME-70370", "REACTOME:R-HSA-5609978", "REACTOME:R-HSA-70370", "REACTOME:R-MMU-70370", "REACTOME:R-RNO-70370" ]
13
[ "1gup", "1guq", "1hxp", "1hxq", "1z84", "1zwj", "2h39", "2q4h", "2q4l", "4qvu", "5in3", "6gqd", "6k5z", "6k9z" ]
14
[ "PUB00002146", "PUB00004352" ]
[ "2066342", "2845364" ]
[ "Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes.", "Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implication...
[ 1991, 1988 ]
2
[]
[ "IPR012361", "IPR043576" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 239, 9528, 4205, 268 ]
4
[ "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",...
[ 4, 1, 4, 2, 1, 28, 9, 1, 1, 4, 1, 1, 4 ]
13
true
Family
Galactose-1-phosphate uridyl transferase, class I
Galactose-1-phosphate uridyl transferase, class I
GalP_UDPtransf1
5
IPR001938
1,938
Thaumatin family
Thaumatin
Family
21,535
false
false
Thaumatin [ ] is an intensely sweet-tasting protein, 100 000 times sweeter than sucrose on a molar basis [ ], found in berries from Thaumatococcus daniellii, a tropical flowering plant known as Katemfe. It is induced by attack by viroids, which are single-stranded unencapsulated RNA molecules that do not code for prote...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PRINTS", "PROFILE", "PANTHER", "SMART" ]
[ "PF00314", "PIRSF002703", "PR00347", "PS51367", "PTHR31048", "SM00205" ]
[ "Thaumatin", "Thaumatin", "THAUMATIN", "THAUMATIN_2", "", "THN" ]
[ 20323, 14005, 16847, 20903, 17892, 20587 ]
6
[ "PROSITEDOC" ]
[ "PDOC00286" ]
[ "PROSITEDOC:PDOC00286" ]
1
[ "1aun", "1du5", "1lr2", "1lr3", "1lxz", "1ly0", "1pcv", "1pp3", "1rqw", "1thi", "1thu", "1thv", "1thw", "1z3q", "2a7i", "2ahn", "2blr", "2blu", "2d8o", "2d8p", "2g4y", "2i0w", "2oqn", "2pe7", "2vhk", "2vhr", "2vi1", "2vi2", "2vi3", "2vi4", "2vu6", "2vu7"...
215
[ "PUB00001747", "PUB00004543", "PUB00004556", "PUB00004580", "PUB00004582", "PUB00043682", "PUB00088725" ]
[ "7049841", "1650615", "1463856", "7846159", "7630973", "16666857", "8637920" ]
[ "Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli.", "A wheat glutathione-S-transferase gene with transposon-like sequences in the promoter region.", "Nucleotide sequence of an osmotin-like cDNA induced in tomato during viroid infection.", "Characteriza...
[ 1982, 1991, 1992, 1994, 1995, 1989, 1996 ]
7
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 454, 21048, 29, 4 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 136, 5, 1, 142, 163 ]
5
true
Family
Thaumatin family
Thaumatin family
Thaumatin
8
IPR001940
1,940
Peptidase S1C
Peptidase_S1C
Family
86,468
false
false
This group of serine peptidases and non-peptidase homologues belong to the MEROPS peptidase family S1, subfamily S1C (protease Do subfamily, clan PS(S)). A type example is the protease Do from Escherichia coli. This entry also includes the membrane transporter protein MamO and the magnetosome formation protease MamE. M...
[ "GO:0004252", "GO:0006508" ]
[ "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00834" ]
[ "PROTEASES2C" ]
[ 86468 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21", "R-BTA-9837999", "R-DME-9837999", "R-HSA-1474228", "R-HSA-9760173", "R-HSA-9837999", "R-HSA-9841251", "R-MMU-1474228", "R-MMU-9837999", "R-RNO-1474228" ]
[ "EC:3.4.21", "REACTOME:R-BTA-9837999", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-9760173", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9841251", "REACTOME:R-MMU-1474228", "REACTOME:R-MMU-9837999", "REACTOME:R-RNO-1474228" ]
10
[ "1ky9", "1l1j", "1lcy", "1sot", "1soz", "1te0", "1vcw", "1y8t", "2qf0", "2qf3", "2qgr", "2r3u", "2r3y", "2rce", "2z9i", "2zle", "3b8j", "3cs0", "3gcn", "3gco", "3gds", "3gdu", "3gdv", "3k6y", "3k6z", "3lgi", "3lgt", "3lgu", "3lgv", "3lgw", "3lgy", "3lh1"...
137
[ "PUB00002101", "PUB00002289", "PUB00004344", "PUB00009824", "PUB00093597", "PUB00093599" ]
[ "2180903", "8576051", "3057437", "12408815", "26981620", "21414040" ]
[ "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase.", "Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease.", "Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mecha...
[ 1990, 1996, 1988, 2002, 2016, 2011 ]
6
[]
[ "IPR011782", "IPR011783", "IPR047680" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 735, 70574, 13760, 28, 1371 ]
5
[ "Arabidopsis thaliana", "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", "Saccharomyces cerevisiae...
[ 59, 68, 2, 3, 15, 14, 1, 27, 16, 1, 1, 60 ]
12
true
Family
Peptidase S1C
Peptidase S1C
Peptidase_S1C
5
IPR001941
1,941
Pro-opiomelanocortin
PMOC
Family
5,375
false
false
Pro-opiomelanocortin is present in high levels in the pituitary and is processed into 3 major peptide families: adrenocorticotrophin (ACTH); alpha-, beta- and gamma-melanocyte- stimulating hormones (MSH); and beta-endorphin [ ]. ACTH regulates the synthesis and release of glucocorticoids and, to some extent, aldosteron...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00383" ]
[ "MELANOCORTIN" ]
[ 5375 ]
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-111885", "R-BTA-193048", "R-BTA-194002", "R-BTA-202040", "R-BTA-209952", "R-BTA-211976", "R-BTA-375276", "R-BTA-418555", "R-BTA-418594", "R-HSA-111885", "R-HSA-193048", "R-HSA-194002", "R-HSA-202040", "R-HSA-209952", "R-HSA-211976", "R-HSA-375276", "R-HSA-418555", "R-HSA-418...
[ "REACTOME:R-BTA-111885", "REACTOME:R-BTA-193048", "REACTOME:R-BTA-194002", "REACTOME:R-BTA-202040", "REACTOME:R-BTA-209952", "REACTOME:R-BTA-211976", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-418594", "REACTOME:R-HSA-111885", "REACTOME:R-HSA-193048", "REACTOME:R-HSA-194...
39
[ "8gy7" ]
1
[ "PUB00000465", "PUB00002596" ]
[ "2839146", "2266117" ]
[ "Alpha-amidated peptides derived from pro-opiomelanocortin in normal human pituitary.", "Post-translational modification of bovine pro-opiomelanocortin. Tyrosine sulfation and pyroglutamate formation, a mass spectrometric study." ]
[ 1988, 1990 ]
2
[]
[]
0
0
null
[ "Vertebrata" ]
[ 5375 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 12, 1, 4 ]
4
true
Family
Pro-opiomelanocortin
Pro-opiomelanocortin
PMOC
5
IPR001943
1,943
UVR domain
UVR_dom
Domain
82,001
false
false
During the process of Escherichia coli nucleotide excision repair, DNA damage recognition and processing are achieved by the action of the uvrA, uvrB, and uvrC gene products [ ]. UvrB and UvrC share a common domain of around 35 amino acids, the so called UVR domain. This domain in UvrB can interact with the homologous ...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02151", "PS50151" ]
[ "UVR", "UVR" ]
[ 59795, 79291 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50151", "R-HSA-8980692", "R-HSA-9013026", "R-HSA-9013106", "R-MMU-8980692", "R-MMU-9013026", "R-MMU-9013106", "R-RNO-8980692", "R-RNO-9013026" ]
[ "PROSITEDOC:PDOC50151", "REACTOME:R-HSA-8980692", "REACTOME:R-HSA-9013026", "REACTOME:R-HSA-9013106", "REACTOME:R-MMU-8980692", "REACTOME:R-MMU-9013026", "REACTOME:R-MMU-9013106", "REACTOME:R-RNO-8980692", "REACTOME:R-RNO-9013026" ]
9
[ "1c4o", "1d2m", "1d9x", "1d9z", "1e52", "1qoj", "1t5l", "2d7d", "2fdc", "2nmv", "3j3r", "3j3s", "3j3t", "3j3u", "3pxg", "3pxi", "3uwx", "3v4r", "6em8", "6em9", "6emw", "6lsy", "6lt4", "7abr", "8a8u", "8a8v", "8a8w", "8wtb", "8wtc", "8xon", "8xoo", "8ycx"...
43
[ "PUB00006064", "PUB00006065", "PUB00057847" ]
[ "8466476", "8530482", "15554981" ]
[ "Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem.", "The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision.", "Clp ATPases are req...
[ 1993, 1995, 2004 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1220, 72453, 6717, 7, 1604 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 32, 1, 2, 2, 2, 21, 5, 46 ]
8
true
Domain
UVR domain
UVR domain
UVR_dom
9
IPR001944
1,944
Glycoside hydrolase, family 35
Glycoside_Hdrlase_35
Family
33,285
false
false
Glycoside hydrolase family 35 ( ) comprises enzymes with only one known activity: beta-galactosidase ( ). Mammalian beta-galactosidase is a lysosomal enzyme (gene GLB1 ) that cleaves the terminal galactose from gangliosides, glycoproteins, and glycosaminoglycans and whose deficiency is the cause of the genetic disease ...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS", "PANTHER" ]
[ "PR00742", "PTHR23421" ]
[ "GLHYDRLASE35", "" ]
[ 30558, 33052 ]
2
[ "CAZY", "EC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "RE...
[ "GH35", "3.2.1.23", "PWY-6807", "PDOC00910", "R-CFA-2022857", "R-CFA-2024101", "R-CFA-4085001", "R-CFA-6798695", "R-CFA-9840310", "R-DDI-2022857", "R-DDI-2024101", "R-DDI-6798695", "R-DDI-9840310", "R-HSA-2022857", "R-HSA-2024101", "R-HSA-2206308", "R-HSA-4085001", "R-HSA-4341670",...
[ "CAZY:GH35", "EC:3.2.1.23", "METACYC:PWY-6807", "PROSITEDOC:PDOC00910", "REACTOME:R-CFA-2022857", "REACTOME:R-CFA-2024101", "REACTOME:R-CFA-4085001", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-9840310", "REACTOME:R-DDI-2022857", "REACTOME:R-DDI-2024101", "REACTOME:R-DDI-6798695", "REACTOME:R-...
29
[ "1tg7", "1xc6", "3d3a", "3og2", "3ogr", "3ogs", "3ogv", "3thc", "3thd", "3w5f", "3w5g", "3wez", "3wf0", "3wf1", "3wf2", "3wf3", "3wf4", "4e8c", "4e8d", "4iug", "4mad", "5gsl", "5gsm", "5ifp", "5ift", "5ihr", "5juv", "5mgc", "5mgd", "6eon", "6ik5", "6ik6"...
57
[ "PUB00004870", "PUB00005266", "PUB00160296" ]
[ "7624375", "8535779", "35065074" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages." ]
[ 1995, 1995, 2022 ]
3
[]
[ "IPR026283" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 44, 7948, 25255, 38 ]
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", "Zea mays" ]
[ 107, 2, 10, 3, 21, 22, 2, 51, 27, 233 ]
10
true
Family
Glycoside hydrolase, family 35
Glycoside hydrolase, family 35
Glycoside_Hdrlase_35
8
IPR001945
1,945
RAD3/XPD
RAD3/XPD
Family
4,487
false
false
Xeroderma pigmentosum (XP) [ ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. People's skin cells with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genetic comp...
[ "GO:0003677", "GO:0003678", "GO:0005524", "GO:0016818", "GO:0006289", "GO:0005634" ]
[ "DNA binding", "DNA helicase activity", "ATP binding", "hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides", "nucleotide-excision repair", "nucleus" ]
[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR00852" ]
[ "XRODRMPGMNTD" ]
[ 4487 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "5.6.2.3", "GenProp2048", "R-BTA-113418", "R-BTA-5696395", "R-BTA-5696400", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-72086", "R-BTA-73762", "R-BTA-73772", "R-BTA-73776", "R-BTA-73779", "R-BTA-73863", "R-BTA-75953", "R-BTA-75955", ...
[ "EC:5.6.2.3", "GP:GenProp2048", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5696395", "REACTOME:R-BTA-5696400", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-72086", "REACTOME:R-BTA-73762", "REACT...
111
[ "5fmf", "5ivw", "5iy6", "5iy7", "5iy8", "5iy9", "5of4", "5oqj", "5oqm", "5sva", "6gym", "6nmi", "6o9l", "6o9m", "6ro4", "6tun", "7ad8", "7egb", "7egc", "7ena", "7enc", "7k01", "7k04", "7lbm", "7m2u", "7ml0", "7ml1", "7ml2", "7ml3", "7ml4", "7nvr", "7nvw"...
72
[ "PUB00002008", "PUB00002851", "PUB00003894", "PUB00004160", "PUB00004189", "PUB00004395", "PUB00004415", "PUB00005433", "PUB00097845", "PUB00154490" ]
[ "9101292", "8206890", "7920640", "8247134", "8090225", "1956796", "8464724", "8160271", "32821917", "31253769" ]
[ "Mutations in the XPD gene leading to xeroderma pigmentosum symptoms.", "Isolation of active recombinant XPG protein, a human DNA repair endonuclease.", "Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy.", "Yeast excision repair gene RAD2 encode...
[ 1997, 1994, 1994, 1993, 1994, 1991, 1993, 1994, 2020, 2019 ]
10
[ "IPR013020" ]
[]
1
0
1
[ "Eukaryota", "bird metagenome" ]
[ 4486, 1 ]
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...
[ 4, 1, 1, 7, 7, 5, 1, 2, 4, 1, 1, 7 ]
12
true
Family
RAD3/XPD
RAD3/XPD
RAD3/XPD
5
IPR001946
1,946
Alpha 2A adrenoceptor
ADRA2A_rcpt
Family
230
false
false
This entry represents the alpha 2A adrenoceptor. It is expressed at high levels in the CNS, and in peripheral tissues such as kidney, aorta, skeletal muscle, spleen and lung [ , , , ]. The adrenoceptors (or adrenergic receptors) are rhodopsin-like G protein-coupled receptors that are targets of the catecholamines, espe...
[ "GO:0004938", "GO:0006940", "GO:0007186", "GO:0019229", "GO:0030168", "GO:0016020" ]
[ "alpha2-adrenergic receptor activity", "regulation of smooth muscle contraction", "G protein-coupled receptor signaling pathway", "regulation of vasoconstriction", "platelet activation", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR00558" ]
[ "ADRENRGCA2AR" ]
[ 230 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "25", "R-BTA-390696", "R-BTA-392023", "R-BTA-400042", "R-BTA-418594", "R-BTA-418597", "R-BTA-5683826", "R-HSA-390696", "R-HSA-392023", "R-HSA-400042", "R-HSA-418594", "R-HSA-418597", "R-HSA-5683826", "R-MMU-390696", "R-MMU-392023", "R-MMU-400042", "R-MMU-418594", "R-MMU-418597", ...
[ "IUPHAR:25", "REACTOME:R-BTA-390696", "REACTOME:R-BTA-392023", "REACTOME:R-BTA-400042", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-418597", "REACTOME:R-BTA-5683826", "REACTOME:R-HSA-390696", "REACTOME:R-HSA-392023", "REACTOME:R-HSA-400042", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-418597", "RE...
31
[ "6kux", "6kuy", "7ej0", "7ej8", "7eja", "7ejk", "7w6p", "7w7e", "9pln", "9plo", "9pqd" ]
11
[ "PUB00066376", "PUB00066377", "PUB00066395", "PUB00066396", "PUB00066462", "PUB00066463", "PUB00066464", "PUB00066465", "PUB00066466", "PUB00066467", "PUB00066468", "PUB00066469", "PUB00066470", "PUB00066471", "PUB00066472" ]
[ "18882199", "2855960", "2887122", "9280371", "9605427", "9760042", "9824686", "8670422", "15684247", "2574568", "10215710", "7688069", "1334200", "7812219", "7684725" ]
[ "A study of the adrenotropic receptors.", "Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.", "Coronary vasoconstriction mediated by alpha 1- and alpha 2-adrenoceptors in conscious dogs.", "Alpha-adrenoceptors in equine digital veins: evidence for the presence of ...
[ 1948, 1988, 1987, 1997, 1998, 1998, 1998, 1996, 2004, 1989, 1999, 1993, 1992, 1994, 1993 ]
15
[ "IPR002233" ]
[]
1
0
1
[ "Eukaryota", "Streptomyces" ]
[ 228, 2 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 2 ]
3
true
Family
Alpha 2A adrenoceptor
Alpha 2A adrenoceptor
ADRA2A_rcpt
4
IPR001947
1,947
Scorpion short chain toxin, potassium channel inhibitor
Scorpion_toxinS_K_inh
Family
254
false
false
Scorpion venoms contain a variety of peptides toxic to mammals, insects and crustaceans. Among these peptides there is a family of short toxins (30 to 40 residues) [ , ]. This entry represents members of this family with potassium channel blocking activity [ ]. KTX 12 Sp2 toxin from Scorpiops pococki has shown a strong...
[ "GO:0008200", "GO:0005576" ]
[ "ion channel inhibitor activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS" ]
[ "PF00451", "PR00286" ]
[ "Toxin_2", "CHARYBDTOXIN" ]
[ 254, 139 ]
2
[ "PROSITEDOC" ]
[ "PDOC00875" ]
[ "PROSITEDOC:PDOC00875" ]
1
[ "1agt", "1bah", "1big", "1bkt", "1c49", "1c55", "1c56", "1cmr", "1hly", "1hp2", "1j5j", "1ktx", "1lgl", "1lir", "1m2s", "1mtx", "1n8m", "1pjv", "1pnh", "1q2k", "1qky", "1quz", "1r1g", "1sco", "1scy", "1sxm", "1tsk", "1txm", "1wmt", "1wpd", "1wt7", "1wz5"...
83
[ "PUB00000410", "PUB00000536", "PUB00030001", "PUB00095583", "PUB00097194", "PUB00097857" ]
[ "7819188", "7998956", "15146482", "31890149", "32602722", "33466524" ]
[ "NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.", "Novel K(+)-channel-blocking toxins from the venom of the scorpion Centruroides limpidus limpidus Karsch.", "Solution structure of BmKK2, a new potassium channel blocker from the venom of c...
[ 1995, 1994, 2004, 2019, 2020, 2021 ]
6
[]
[]
0
0
null
[ "Corallococcus sicarius", "Eukaryota" ]
[ 1, 253 ]
2
[]
[]
0
true
Family
Scorpion short chain toxin, potassium channel inhibitor
Scorpion short chain toxin, potassium channel inhibitor
Scorpion_toxinS_K_inh
5
IPR001948
1,948
Peptidase M18
Peptidase_M18
Family
16,090
false
false
This group of metallopeptidases belong to the MEROPS peptidase family M18, (clan MH). The proteins have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the release of an N-terminal aminoacid, usually neutral or hydrophobic, from a polypeptide [ ]....
[ "GO:0004177", "GO:0008270", "GO:0006508" ]
[ "aminopeptidase activity", "zinc ion binding", "proteolysis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF02127", "PR00932", "PTHR28570" ]
[ "Peptidase_M18", "AMINO1PTASE", "" ]
[ 16084, 15532, 15980 ]
3
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "3.4.11.-", "PWY-6423", "PWY-7694", "PWY-7954" ]
[ "EC:3.4.11.-", "METACYC:PWY-6423", "METACYC:PWY-7694", "METACYC:PWY-7954" ]
4
[ "1y7e", "2glf", "2glj", "2ijz", "3var", "3vat", "3wt4", "4dyo", "4eme", "4njq", "4njr", "4oid", "4oiw", "4r8f", "5jgf", "5jh9", "5jm6", "5jm9", "6pev", "7dde", "7u5h" ]
21
[ "PUB00002544", "PUB00003579" ]
[ "2651436", "7674922" ]
[ "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae.", "Evolutionary families of metallopeptidases." ]
[ 1989, 1995 ]
2
[]
[ "IPR022983", "IPR022984" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 22, 8721, 7194, 153 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "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)", "S...
[ 9, 2, 2, 16, 11, 2, 5, 10, 2, 1, 10 ]
11
true
Family
Peptidase M18
Peptidase M18
Peptidase_M18
1
IPR001949
1,949
NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
NADH-UbQ_OxRdtase_51kDa_CS
Conserved_site
28,332
false
false
Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 51kDa (in mammals), which is the second largest subunit of complex I and is a component of the iron-sulphur (IP) fragment of the enzyme. It seems to bind to NAD, FMN, and a 2Fe-2S cluster. The 51kDa subunit and the bacte...
[ "GO:0008137", "GO:0010181", "GO:0051539" ]
[ "NADH dehydrogenase (ubiquinone) activity", "FMN binding", "4 iron, 4 sulfur cluster binding" ]
[ "molecular_function", "molecular_function", "molecular_function" ]
3
[ "PROSITE", "PROSITE" ]
[ "PS00644", "PS00645" ]
[ "COMPLEX1_51K_1", "COMPLEX1_51K_2" ]
[ 18989, 27899 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "7.1.1.-", "PDOC00555", "R-DDI-6799198", "R-DDI-9837999", "R-HSA-611105", "R-HSA-6799198", "R-HSA-9837999", "R-MMU-611105", "R-MMU-6799198", "R-MMU-9837999" ]
[ "EC:7.1.1.-", "PROSITEDOC:PDOC00555", "REACTOME:R-DDI-6799198", "REACTOME:R-DDI-9837999", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-6799198", "REACTOME:R-MMU-9837999" ]
10
[ "2fug", "2ybb", "3i9v", "3iam", "3ias", "3m9s", "4hea", "5gpn", "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xf9", "5xfa", "5xtb", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6gcs", "6hl2", "6hl3", "6hl4", "6hla", "6hli", "6hlj", "6hlm", "6i0d", "6i1p"...
369
[ "PUB00005074", "PUB00043561", "PUB00045437" ]
[ "1470679", "10940377", "18394423" ]
[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.", "Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." ]
[ 1992, 2000, 2008 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 65, 22666, 4888, 713 ]
4
[ "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",...
[ 2, 1, 1, 4, 1, 9, 4, 1, 5, 4, 10 ]
11
true
Conserved_site
NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
NADH-UbQ_OxRdtase_51kDa_CS
8
IPR001950
1,950
SUI1 domain
SUI1
Domain
25,141
false
false
In budding yeast (Saccharomyces cerevisiae), SUI1 is a translation initiation factor that functions in concert with eIF-2 and the initiator tRNA-Met in directing the ribosome to the proper start site of translation [ ]. SUI1 is a protein of 108 residues. Close homologues of SUI1 have been found [ ] in mammals, insects ...
[ "GO:0003743", "GO:0006413" ]
[ "translation initiation factor activity", "translational initiation" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF01253", "PS50296" ]
[ "SUI1", "SUI1" ]
[ 25019, 25014 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00862", "R-DME-5389840", "R-DME-5419276", "R-DME-9937383" ]
[ "PROSITEDOC:PDOC00862", "REACTOME:R-DME-5389840", "REACTOME:R-DME-5419276", "REACTOME:R-DME-9937383" ]
4
[ "1d1r", "2if1", "2ogh", "2rvh", "3j80", "3j81", "3jam", "3jap", "4bts", "4kzx", "4kzy", "4mo0", "4uer", "4v5o", "5jb3", "5jbh", "5oa3", "5oa9", "5vyc", "5w2f", "5zcy", "6gsm", "6gsn", "6vpq", "6vpr", "6ybw", "6zce", "6zmw", "6zp4", "6zvj", "7a09", "7ase"...
43
[ "PUB00000232", "PUB00003679" ]
[ "7904817", "1729602" ]
[ "Expressed sequence tags identify a human isolog of the suil translation initiation factor.", "The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon." ]
[ 1994, 1992 ]
2
[]
[ "IPR039759", "IPR046447" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]
[ 1121, 7190, 16632, 43, 155 ]
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",...
[ 21, 3, 5, 7, 1, 11, 12, 2, 19, 21, 3, 2, 48 ]
13
true
Domain
SUI1 domain
SUI1 domain
SUI1
9
IPR001951
1,951
Histone H4
Histone_H4
Family
13,871
false
false
Histone H4 is one of the five histones, along with H1/H5, H2A, H2B and H3. Two copies of each of the H2A, H2B, H3, and H4 histones ensemble to form the core of the nucleosome [ ]. The nucleosome forms octameric structure that wraps DNA in a left-handed manner. H3 is a highly conserved protein of 135 amino acid residues...
[ "GO:0003677", "GO:0030527" ]
[ "DNA binding", "structural constituent of chromatin" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS", "PANTHER", "SMART", "CDD" ]
[ "PR00623", "PTHR10484", "SM00417", "cd22912" ]
[ "HISTONEH4", "", "H4", "HFD_H4" ]
[ 13151, 13126, 13034, 13007 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00046", "R-BTA-110330", "R-BTA-110331", "R-BTA-171306", "R-BTA-201722", "R-BTA-212300", "R-BTA-2299718", "R-BTA-2559580", "R-BTA-2559582", "R-BTA-2559586", "R-BTA-3214815", "R-BTA-3214841", "R-BTA-3214842", "R-BTA-3214847", "R-BTA-3214858", "R-BTA-427359", "R-BTA-427413", "R-B...
[ "PROSITEDOC:PDOC00046", "REACTOME:R-BTA-110330", "REACTOME:R-BTA-110331", "REACTOME:R-BTA-171306", "REACTOME:R-BTA-201722", "REACTOME:R-BTA-212300", "REACTOME:R-BTA-2299718", "REACTOME:R-BTA-2559580", "REACTOME:R-BTA-2559582", "REACTOME:R-BTA-2559586", "REACTOME:R-BTA-3214815", "REACTOME:R-BTA...
279
[ "1aoi", "1eqz", "1f66", "1hio", "1hq3", "1id3", "1kx3", "1kx4", "1kx5", "1m18", "1m19", "1m1a", "1p34", "1p3a", "1p3b", "1p3f", "1p3g", "1p3i", "1p3k", "1p3l", "1p3m", "1p3o", "1p3p", "1s32", "1tzy", "1u35", "1zbb", "1zla", "2aro", "2cv5", "2f8n", "2fj7"...
971
[ "PUB00003642", "PUB00004015", "PUB00004388", "PUB00004448", "PUB00040100", "PUB00056944", "PUB00061022", "PUB00066796", "PUB00095672", "PUB00100973", "PUB00150375", "PUB00156085", "PUB00157111", "PUB00157117", "PUB00157122", "PUB00157123", "PUB00157124", "PUB00157125", "PUB001571...
[ "6808351", "3340182", "2041803", "8121801", "15951514", "21812398", "20498094", "16472024", "30886146", "31353180", "29280735", "24251097", "31542297", "27016736", "26607036", "32327602", "6314274", "27105115", "27105113" ]
[ "Acetylation of histones in nucleosomes.", "A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA.", "Histone and histone gene compilation and alignment update.", "Phylogenetic analysis of the core histones H2A, H2B, H3, and H4.", "Alteration of the nucleosomal DNA path in the...
[ 1982, 1988, 1991, 1994, 2005, 2011, 2010, 2006, 2019, 2019, 2017, 2013, 2019, 2016, 2015, 2020, 1983, 2016, 2016 ]
19
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "organismal metagenomes" ]
[ 5, 4, 13749, 110, 3 ]
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", "Saccharomyces cerevisiae (strai...
[ 5, 1, 7, 2, 5, 4, 2, 6, 2, 1, 1, 44 ]
12
true
Family
Histone H4
Histone H4
Histone_H4
4
IPR001952
1,952
Alkaline phosphatase
Alkaline_phosphatase
Family
23,211
false
false
This entry represents alkaline phosphatases ( ) (ALP), which act as non-specific phosphomonoesterases to hydrolyse phosphate esters, optimally at high pH. The reaction mechanism involves the attack of a serine alkoxide on a phosphorus of the substrate to form a transient covalent enzyme-phosphate complex, followed by t...
[ "GO:0016791" ]
[ "phosphatase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PANTHER", "SMART", "CDD" ]
[ "PF00245", "PR00113", "PTHR11596", "SM00098", "cd16012" ]
[ "Alk_phosphatase", "ALKPHPHTASE", "", "alkPPc", "ALP" ]
[ 23202, 21403, 22971, 21963, 21217 ]
5
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.3.1", "GenProp1255", "GenProp1407", "GenProp1411", "GenProp1630", "PWY-5491", "PDOC00113", "R-BTA-163125", "R-DME-1483166", "R-DME-6811438", "R-DME-8935690", "R-HSA-1483166", "R-HSA-163125", "R-HSA-6811438", "R-HSA-8935690", "R-MMU-163125", "R-MMU-6811438", "R-RNO-1483166", ...
[ "EC:3.1.3.1", "GP:GenProp1255", "GP:GenProp1407", "GP:GenProp1411", "GP:GenProp1630", "METACYC:PWY-5491", "PROSITEDOC:PDOC00113", "REACTOME:R-BTA-163125", "REACTOME:R-DME-1483166", "REACTOME:R-DME-6811438", "REACTOME:R-DME-8935690", "REACTOME:R-HSA-1483166", "REACTOME:R-HSA-163125", "REACT...
21
[ "1aja", "1ajb", "1ajc", "1ajd", "1alh", "1ali", "1alj", "1alk", "1ani", "1anj", "1b8j", "1ed8", "1ed9", "1elx", "1ely", "1elz", "1ew2", "1ew8", "1ew9", "1hjk", "1hqa", "1k7h", "1kh4", "1kh5", "1kh7", "1kh9", "1khj", "1khk", "1khl", "1khn", "1shn", "1shq"...
86
[ "PUB00003744", "PUB00024691", "PUB00038439", "PUB00038859", "PUB00042958", "PUB00042959", "PUB00042960", "PUB00042961" ]
[ "1654502", "11124260", "15938627", "15946677", "11910033", "17520090", "18292227", "17719863" ]
[ "Genetics of streptomycin production in Streptomyces griseus: nucleotide sequence of five genes, strFGHIK, including a phosphatase gene.", "Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity.", "Metal specificity is correlated with two cruc...
[ 1991, 2001, 2005, 2005, 2002, 2007, 2008, 2007 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 89, 11445, 11523, 1, 153 ]
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", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe...
[ 7, 16, 2, 12, 17, 3, 18, 1, 1, 1 ]
10
true
Family
Alkaline phosphatase
Alkaline phosphatase
Alkaline_phosphatase
2
IPR001953
1,953
Sodium/hydrogen exchanger 2/4
NHE-2/4
Family
851
false
false
Sodium proton exchangers (NHEs) constitute a large family of integral membrane protein transporters that are responsible for the counter-transport of protons and sodium ions across lipid bilayers [ , ]. These proteins are found in organisms across all domains of life. In archaea, bacteria, yeast and plants, these excha...
[ "GO:0015385", "GO:0006814", "GO:0006885", "GO:0016020" ]
[ "sodium:proton antiporter activity", "sodium ion transport", "regulation of pH", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01086" ]
[ "NAHEXCHNGR2" ]
[ 851 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-425986", "R-MMU-425986", "R-RNO-425986" ]
[ "REACTOME:R-HSA-425986", "REACTOME:R-MMU-425986", "REACTOME:R-RNO-425986" ]
3
[]
0
[ "PUB00001715", "PUB00002996", "PUB00003039", "PUB00044828", "PUB00044829", "PUB00044830", "PUB00044831", "PUB00044832", "PUB00044833", "PUB00044834", "PUB00100472", "PUB00100473", "PUB00100474", "PUB00100475", "PUB00100476", "PUB00100477" ]
[ "9537504", "9278382", "9507001", "12027219", "12502567", "16734752", "17071327", "16513813", "11187762", "17218973", "19458287", "7961960", "9038815", "17943310", "26350456", "34785669" ]
[ "Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?", "Na+/H+ exchangers of mammalian cells.", "Identification of a mitochondrial Na+/H+ exchanger.", "The Na+/H+ exchanger gene family.", "Multiple modes of regulation of Na+/H+ exchangers.", "Na+/H+ exchangers and the...
[ 1998, 1997, 1998, 2002, 2002, 2006, 2006, 2006, 2000, 2006, 2009, 1994, 1997, 2008, 2015, 2021 ]
16
[ "IPR004709" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 851 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 9 ]
3
true
Family
Sodium/hydrogen exchanger 2/4
Sodium/hydrogen exchanger 2/4
NHE-2/4
2
IPR001954
1,954
Gliadin/LMW glutenin
Glia_glutenin
Family
5,019
false
false
Gluten is the protein component of Triticum aestivum (Wheat) flour. It consists of numerous proteins, which are of 2 different types responsible for different physical properties of dough: the glutenins, which are primarily responsible for the elasticity, and the gliadins, which contribute to the extensibility. The glu...
[ "GO:0045735" ]
[ "nutrient reservoir activity" ]
[ "molecular_function" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00208", "PTHR33454" ]
[ "GLIADGLUTEN", "" ]
[ 4030, 4999 ]
2
[]
[]
[]
0
[]
0
[ "PUB00001754", "PUB00002416", "PUB00004336", "PUB00004360", "PUB00082623" ]
[ "3017812", "2989281", "3840588", "2563152", "27503660" ]
[ "Structure of wheat gamma-gliadin genes.", "Evolution and heterogeneity of the alpha-/beta-type and gamma-type gliadin DNA sequences.", "Nucleotide sequence of a gene from chromosome 1D of wheat encoding a HMW-glutenin subunit.", "Nucleotide sequences of the two high-molecular-weight glutenin genes from the D...
[ 1986, 1985, 1985, 1989, 2016 ]
5
[]
[]
0
0
null
[ "Mesangiospermae", "Pseudomonadati" ]
[ 5006, 13 ]
2
[ "Oryza sativa subsp. japonica", "Zea mays" ]
[ 60, 39 ]
2
true
Family
Gliadin/LMW glutenin
Gliadin/LMW glutenin
Glia_glutenin
7
IPR001956
1,956
Carbohydrate-binding module 3
CBM3
Domain
3,351
false
false
Carbohydrate-binding modules (CBM) have been classified into more than 40 families according to sequence homology. Several cellulolytic enzymes share a conserved region of about 150 amino acid residues, the CBM3 domain [ ]. It has been classified in three different subtypes, termed family IIIa, IIIb and IIIc. The famil...
[ "GO:0030248", "GO:0005975" ]
[ "cellulose binding", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00942", "PS51172", "SM01067" ]
[ "CBM_3", "CBM3", "CBM_3" ]
[ 3340, 3281, 3141 ]
3
[ "EC", "METACYC", "PROSITEDOC" ]
[ "3.2.1.4", "PWY-6788", "PDOC51172" ]
[ "EC:3.2.1.4", "METACYC:PWY-6788", "PROSITEDOC:PDOC51172" ]
3
[ "1g43", "1g87", "1ga2", "1js4", "1k72", "1kfg", "1nbc", "1tf4", "2l8a", "2wnx", "2wo4", "2wob", "2xbt", "2xfg", "2ylk", "3tf4", "3zqw", "3zqx", "3zu8", "3zuc", "4b96", "4b97", "4b9c", "4b9f", "4b9p", "4c8x", "4jo5", "4tf4", "5gxx", "5gxy", "5gxz", "5gy0"...
42
[ "PUB00001296", "PUB00001730", "PUB00025133", "PUB00033741", "PUB00033742" ]
[ "8918451", "1490597", "11092922", "9537366", "9055408" ]
[ "Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose.", "Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS.", "Structure of a family IIIa scaffoldin CBD from the cellulosome of Clostridi...
[ 1996, 1992, 2000, 1998, 1997 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Haloarculaceae", "bioreactor metagenome" ]
[ 3323, 22, 5, 1 ]
4
[]
[]
0
true
Domain
Carbohydrate-binding module 3
Carbohydrate-binding module 3
CBM3
3
IPR001957
1,957
Chromosomal replication control, initiator DnaA
Chromosome_initiator_DnaA
Family
25,509
false
false
The bacterial DnaA protein [ , , ] plays an important role in initiating and regulating chromosomal replication. DnaA is an ATP- and DNA-binding protein. It binds specifically to 9 bp nucleotide repeats known as dnaA boxes which are found in the chromosome origin of replication (oriC). DnaA contains two conserved regio...
[ "GO:0003677", "GO:0003688", "GO:0005524", "GO:0006270", "GO:0006275" ]
[ "DNA binding", "DNA replication origin binding", "ATP binding", "DNA replication initiation", "regulation of DNA replication" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "biological_process" ]
5
[ "HAMAP", "NCBIFAM" ]
[ "MF_00377", "TIGR00362" ]
[ "DnaA_bact", "DnaA" ]
[ 25049, 25455 ]
2
[ "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC" ]
[ "GenProp0806", "GenProp1113", "GenProp1152", "GenProp1186", "GenProp1195", "GenProp1200", "GenProp1207", "GenProp1210", "PDOC00771" ]
[ "GP:GenProp0806", "GP:GenProp1113", "GP:GenProp1152", "GP:GenProp1186", "GP:GenProp1195", "GP:GenProp1200", "GP:GenProp1207", "GP:GenProp1210", "PROSITEDOC:PDOC00771" ]
9
[ "1l8q", "2hcb", "2z4r", "2z4s", "3r8f", "8btg", "8bv3" ]
7
[ "PUB00000665", "PUB00001793", "PUB00003815", "PUB00005517" ]
[ "8110826", "2172087", "1779750", "2558436" ]
[ "The initiator protein DnaA: evolution, properties and function.", "Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli.", "Structure and function of DnaA and the DnaA-box in eubacteria: evolutionary relationships of bacterial re...
[ 1994, 1990, 1991, 1989 ]
4
[ "IPR020591" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Microviridae sp. ctNWS1", "unclassified sequences" ]
[ 25017, 40, 2, 1, 449 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Chromosomal replication control, initiator DnaA
Chromosomal replication control, initiator DnaA
Chromosome_initiator_DnaA
7
IPR001959
1,959
Probable transposase, IS891/IS1136/IS1341
Transposase
Domain
32,776
false
false
This entry represents a conserved region of a probable transposase family, which is found in a number prokaryotic and viral proteins, including the insertion sequence (IS)-like element of the Bacillus PS3 (Thermophilic bacterium PS-3) that promotes expression of the alanine carrier protein-encoding gene [ ] and IS1136 ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01385" ]
[ "OrfB_IS605" ]
[ 32776 ]
1
[]
[]
[]
0
[ "8bf8", "8ex9", "8exa", "8h1j", "8iaz", "9b0l", "9j09", "9udi" ]
8
[ "PUB00001825", "PUB00001858", "PUB00002091", "PUB00100808", "PUB00100809" ]
[ "8386127", "7557457", "2553665", "34619744", "20090938" ]
[ "IS1136, an insertion element in the erythromycin gene cluster of Saccharopolyspora erythraea.", "A novel insertion sequence (IS)-like element of the thermophilic bacterium PS3 promotes expression of the alanine carrier protein-encoding gene.", "Characterization of an insertion sequence (IS891) of novel structu...
[ 1993, 1995, 1989, 2021, 2010 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3771, 28281, 84, 256, 384 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Probable transposase, IS891/IS1136/IS1341
Probable transposase, IS891/IS1136/IS1341
Transposase
7
IPR001962
1,962
Asparagine synthase
Asn_synthase
Domain
51,348
false
false
Most family members that contain this domain catalyse the conversion of aspartate to asparagine. Asparagine synthetase [glutamine-hydrolyzing] (ASNS, ) catalyses the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine [ , , ]. The three-dimensional architecture of the N-terminal domain of asparagine synthet...
[]
[]
[]
0
[ "PFAM", "CDD" ]
[ "PF00733", "cd01991" ]
[ "Asn_synthase", "Asn_synthase_B_C" ]
[ 50927, 42837 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.5.4", "R-BTA-8963693", "R-DDI-8963693", "R-HSA-380994", "R-HSA-8963693", "R-HSA-9633012", "R-HSA-9648895", "R-MMU-8963693", "R-RNO-8963693", "R-SCE-8963693", "R-SPO-8963693" ]
[ "EC:6.3.5.4", "REACTOME:R-BTA-8963693", "REACTOME:R-DDI-8963693", "REACTOME:R-HSA-380994", "REACTOME:R-HSA-8963693", "REACTOME:R-HSA-9633012", "REACTOME:R-HSA-9648895", "REACTOME:R-MMU-8963693", "REACTOME:R-RNO-8963693", "REACTOME:R-SCE-8963693", "REACTOME:R-SPO-8963693" ]
11
[ "1ct9", "1jgt", "1m1z", "1mb9", "1mbz", "1mc1", "1q15", "1q19", "6gq3", "7ylz", "8sue", "9b6c" ]
12
[ "PUB00002540", "PUB00006460", "PUB00043790", "PUB00080257", "PUB00161693" ]
[ "2564390", "10587437", "2573597", "11551215", "32638637" ]
[ "Expression of human asparagine synthetase in Escherichia coli.", "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.", "The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity.", "Characterization of...
[ 1989, 1999, 1989, 2001, 2020 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1747, 36337, 12286, 76, 902 ]
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",...
[ 19, 3, 3, 2, 1, 7, 5, 2, 7, 7, 3, 2, 49 ]
13
true
Domain
Asparagine synthase
Asparagine synthase
Asn_synthase
9
IPR001964
1,964
Luteovirus VPG protein
Luteo_VPG
Family
1,510
false
false
The nucleotide sequence of the RNA of Potato leafroll virus (PLrV) has been determined [ , ]. The sequence contains six large ORFs. The 3' coding region encodes three polypeptides: a 23K coat protein, a 17K polypeptide encoded in a different frame, and a 53K polypeptide, immediately following the coat protein sequence ...
[]
[]
[]
0
[ "PFAM", "PRINTS" ]
[ "PF01659", "PR00912" ]
[ "Luteo_Vpg", "LVIRUSORF5" ]
[ 1510, 1266 ]
2
[]
[]
[]
0
[]
0
[ "PUB00001567", "PUB00003126" ]
[ "2466700", "2732710" ]
[ "Nucleotide sequence and organization of potato leafroll virus genomic RNA.", "Nucleotide sequence of potato leafroll luteovirus RNA." ]
[ 1989, 1989 ]
2
[]
[]
0
0
null
[ "Viruses" ]
[ 1510 ]
1
[]
[]
0
true
Family
Luteovirus VPG protein
Luteovirus VPG protein
Luteo_VPG
9
IPR001965
1,965
Zinc finger, PHD-type
Znf_PHD
Domain
240,751
false
false
This entry represents the PHD (homeodomain) zinc finger domain [ ], which is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of, but distinct from the C3HC4 type RING finger. The function of this domain...
[]
[]
[]
0
[ "SMART" ]
[ "SM00249" ]
[ "PHD" ]
[ 240751 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50016", "R-BTA-6807505", "R-BTA-9772755", "R-CEL-114608", "R-CEL-2299718", "R-CEL-3214842", "R-CEL-3214847", "R-CEL-4551638", "R-CEL-6804758", "R-CEL-9031628", "R-DME-114608", "R-DME-201722", "R-DME-209407", "R-DME-209421", "R-DME-3214815", "R-DME-6804758", "R-DME-6807505", "R...
[ "PROSITEDOC:PDOC50016", "REACTOME:R-BTA-6807505", "REACTOME:R-BTA-9772755", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-2299718", "REACTOME:R-CEL-3214842", "REACTOME:R-CEL-3214847", "REACTOME:R-CEL-4551638", "REACTOME:R-CEL-6804758", "REACTOME:R-CEL-9031628", "REACTOME:R-DME-114608", "REACTOME:R-...
172
[ "1f62", "1fp0", "1mm2", "1mm3", "1we9", "1wee", "1wem", "1wen", "1wep", "1wes", "1weu", "1wev", "1wew", "1x4i", "1xwh", "2dx8", "2e6r", "2e6s", "2f6j", "2f6n", "2fsa", "2fui", "2fuu", "2g6q", "2jmi", "2jmj", "2k16", "2k17", "2k1j", "2ke1", "2kft", "2kgg"...
465
[ "PUB00005446", "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]
[ "7701562", "12665246", "17210253", "15963892", "15718139", "10529348", "11179890" ]
[ "The PHD finger: implications for chromatin-mediated transcriptional regulation.", "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", "Zinc f...
[ 1995, 2002, 2007, 2005, 2005, 1999, 2001 ]
7
[]
[ "IPR019787", "IPR034732", "IPR039095", "IPR042015", "IPR042017", "IPR043319", "IPR047010", "IPR047432", "IPR047442", "IPR047458", "IPR047527", "IPR055197", "IPR055198", "IPR059102" ]
0
14
0
[ "Bacteria", "Eukaryota", "Haloarculaceae", "metagenomes", "unclassified Marseilleviridae" ]
[ 2, 240725, 9, 13, 2 ]
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", "Saccharomyces cerevisiae (strai...
[ 707, 61, 680, 103, 463, 298, 21, 203, 399, 15, 17, 1070 ]
12
true
Domain
Zinc finger, PHD-type
Zinc finger, PHD-type
Znf_PHD
3
IPR001966
1,966
Gastrin-releasing peptide receptor
Gastrin_pep_rcpt
Family
652
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:0008528", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled peptide receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00640" ]
[ "GASTRINRELPR" ]
[ 652 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]
[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]
6
[ "8h0q" ]
1
[ "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
[ "IPR001556" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 652 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 1, 1 ]
4
true
Family
Gastrin-releasing peptide receptor
Gastrin-releasing peptide receptor
Gastrin_pep_rcpt
1
IPR001967
1,967
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
Peptidase_S11_N
Domain
49,799
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[ "GO:0009002", "GO:0006508" ]
[ "serine-type D-Ala-D-Ala carboxypeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF00768" ]
[ "Peptidase_S11" ]
[ 49799 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "3.4.16.4", "PWY-5265", "PWY-6471" ]
[ "EC:3.4.16.4", "METACYC:PWY-5265", "METACYC:PWY-6471" ]
3
[ "1es2", "1es3", "1es4", "1es5", "1esi", "1hd8", "1j9m", "1nj4", "1nzo", "1nzu", "1sdn", "1skf", "1tvf", "1xp4", "1z6f", "3a3j", "3beb", "3bec", "3hum", "3hun", "3it9", "3ita", "3itb", "3mfd", "3mzd", "3mze", "3mzf", "4drt", "4k91", "4p0m", "4ppr", "4rye"...
57
[ "PUB00000120", "PUB00000499", "PUB00000522", "PUB00003576" ]
[ "1741619", "1930140", "8439290", "7845208" ]
[ "Serine beta-lactamases and penicillin-binding proteins.", "Amino acid sequence of the penicillin-binding protein/DD-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A.", "Evolutionary families of peptidases.", "Families of serine peptidases." ]
[ 1991, 1991, 1993, 1994 ]
4
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 49135, 10, 272, 382 ]
4
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Domain
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
Peptidase_S11_N
2
IPR001969
1,969
Aspartic peptidase, active site
Aspartic_peptidase_AS
Active_site
456,804
false
false
This signature contains the active site residues which are conserved in eukaryotic and viral aspartyl proteases. Aspartic peptidase, also known as aspartyl proteases ([ec:3.4.23.-]) are a widely distributed family of proteolytic enzymes [ , , ] known to exist in vertebrates, fungi, plants, retroviruses and some plant v...
[ "GO:0004190", "GO:0006508" ]
[ "aspartic-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00141" ]
[ "ASP_PROTEASE" ]
[ 456804 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.4.23", "PDOC00128", "R-CEL-2022377", "R-CEL-5683826", "R-CFA-1442490", "R-CFA-2022377", "R-CFA-2132295", "R-CFA-5683826", "R-CFA-6798695", "R-CFA-77387", "R-DDI-2132295", "R-DDI-5683826", "R-DDI-6798695", "R-GGA-2022377", "R-GGA-2132295", "R-GGA-6798695", "R-GGA-77387", "R-HSA-1...
[ "EC:3.4.23", "PROSITEDOC:PDOC00128", "REACTOME:R-CEL-2022377", "REACTOME:R-CEL-5683826", "REACTOME:R-CFA-1442490", "REACTOME:R-CFA-2022377", "REACTOME:R-CFA-2132295", "REACTOME:R-CFA-5683826", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-77387", "REACTOME:R-DDI-2132295", "REACTOME:R-DDI-5683826",...
52
[ "1a30", "1a8g", "1a8k", "1a94", "1a9m", "1aaq", "1aid", "1ajv", "1ajx", "1am5", "1apt", "1apu", "1apv", "1apw", "1avf", "1axa", "1az5", "1b11", "1b5f", "1b6j", "1b6k", "1b6l", "1b6m", "1b6p", "1bai", "1bbs", "1bdl", "1bdq", "1bdr", "1bil", "1bim", "1bv7"...
2,554
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00042504", "PUB00065205", "PUB00066803", "PUB00076784", "PUB00076785", "PUB00076786" ]
[ "2194475", "1851433", "8439290", "6795036", "10331925", "11566868", "10864493", "2682266", "23254940", "21765428", "4912600", "10497172", "21751400" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Crystal structure of the hy...
[ 1990, 1991, 1993, 1981, 1999, 2001, 2000, 1989, 2013, 2011, 1970, 1999, 2011 ]
13
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 122, 10774, 93792, 351957, 159 ]
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", "Saccharomyces cerevisiae (strai...
[ 224, 14, 80, 23, 68, 62, 11, 458, 33, 38, 14, 240 ]
12
true
Active_site
Aspartic peptidase, active site
Aspartic peptidase, active site
Aspartic_peptidase_AS
9
IPR001971
1,971
Small ribosomal subunit protein uS11
Ribosomal_uS11
Family
49,734
false
false
Small ribosomal subunit protein uS11, previously known as Ribosomal protein S11 [ ], plays an essential role in selecting the correct tRNA in protein biosynthesis. It is located on the large lobe of the small ribosomal subunit. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. ...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PIRSF", "PANTHER" ]
[ "MF_01310", "PF00411", "PIRSF002131", "PTHR11759" ]
[ "Ribosomal_uS11", "Ribosomal_S11", "Ribosomal_S11", "" ]
[ 47818, 49316, 43809, 48937 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00053", "R-CEL-156827", "R-CEL-1799339", "R-CEL-6791226", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-6791226", "R-DDI-72689", "R-DDI-72695", "R-DDI-72702", "R-DDI-72706", ...
[ "PROSITEDOC:PDOC00053", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-6791226", "REACTOME:R-CEL-72649", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-72695", "REACTOME:R-CEL-72702", "REACTOME:R-CEL-72706", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-156827"...
86
[ "1fjg", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1x18", "1xmo", "1xmq", "1xnq", "1xnr", "2e5l"...
1,906
[ "PUB00001562", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00086615" ]
[ "3191988", "11297922", "11290319", "11114498", "14568531" ]
[ "Amino acid sequences of ribosomal proteins S11 from Bacillus stearothermophilus and S19 from Halobacterium marismortui. Comparison of the ribosomal protein S11 family.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal pr...
[ 1988, 2001, 2001, 2000, 2003 ]
5
[]
[ "IPR019961", "IPR019981" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 903, 23063, 25275, 493 ]
4
[ "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, 2, 2, 5, 1, 7, 9, 2, 18, 9, 3, 3, 43 ]
13
true
Family
Small ribosomal subunit protein uS11
Small ribosomal subunit protein uS11
Ribosomal_uS11
6
IPR001972
1,972
Stomatin/HflK family
Stomatin_HflK_fam
Family
46,946
false
false
This entry includes human Stomatin, bacterial HflK and similar proteins from all cellular organisms. The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain. The exact function of the band-7 dom...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00721" ]
[ "STOMATIN" ]
[ 46946 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00977", "R-CEL-2672351", "R-CEL-373753", "R-CEL-6798695", "R-CEL-8980692", "R-CEL-9013026", "R-CEL-9013406", "R-CEL-9013407", "R-DME-2672351", "R-DME-373753", "R-DME-6798695", "R-DME-8980692", "R-DME-9013026", "R-DME-9013406", "R-DME-9013407", "R-HSA-2672351", "R-HSA-373753", ...
[ "PROSITEDOC:PDOC00977", "REACTOME:R-CEL-2672351", "REACTOME:R-CEL-373753", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8980692", "REACTOME:R-CEL-9013026", "REACTOME:R-CEL-9013406", "REACTOME:R-CEL-9013407", "REACTOME:R-DME-2672351", "REACTOME:R-DME-373753", "REACTOME:R-DME-6798695", "REACTOME:R-...
40
[ "2rpb", "3bk6", "4fvf", "4fvg", "4fvj", "7vhp", "7vhq", "7wh3", "7wi3", "8gn9", "8z5g", "9cz1", "9cz2", "9oh9" ]
14
[ "PUB00002046", "PUB00068598", "PUB00068600", "PUB00068627", "PUB00076124", "PUB00093790", "PUB00093791" ]
[ "9147127", "15471860", "12239636", "21501885", "24782879", "28575093", "19684140" ]
[ "Stomatin.", "Stomatin modulates gating of acid-sensing ion channels.", "Cloning and characterization of SLP3: a novel member of the stomatin family expressed by olfactory receptor neurons.", "Stomatin-domain proteins.", "Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?", "S...
[ 1997, 2004, 2003, 2012, 2014, 2017, 2009 ]
7
[]
[ "IPR043202" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]
[ 1221, 30187, 15032, 26, 480 ]
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",...
[ 9, 33, 16, 20, 2, 16, 18, 2, 4, 14, 1, 5 ]
12
true
Family
Stomatin/HflK family
Stomatin/HflK family
Stomatin_HflK_fam
6
IPR001973
1,973
P2Y6 purinoceptor
P2Y6_rcpt
Family
207
false
false
There are three distinct families of extracellular receptors for purine and pyrimidine nucleotides [ ], known as P1, P2X and P2Y purinoceptors [ ]. These receptors induce a wide variety of biological effects and are involved in many different cellular functions [ , , ]. P2X receptors are ligand-gated ion channels, wher...
[ "GO:0045028", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled purinergic nucleotide receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01068" ]
[ "P2Y6PRNOCPTR" ]
[ 207 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "326", "R-HSA-416476", "R-HSA-417957", "R-MMU-416476", "R-MMU-417957", "R-RNO-416476", "R-RNO-417957" ]
[ "IUPHAR:326", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-417957", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-417957", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-417957" ]
7
[]
0
[ "PUB00002928", "PUB00007054", "PUB00028347", "PUB00033968", "PUB00066193", "PUB00066194", "PUB00066195", "PUB00066196", "PUB00066197", "PUB00066198", "PUB00066203", "PUB00066204", "PUB00066205", "PUB00066206", "PUB00066207", "PUB00066208", "PUB00066209", "PUB00066210", "PUB000662...
[ "7592819", "12270951", "8872457", "11111826", "10629443", "20471713", "11099464", "19921464", "11734617", "16257449", "9364468", "7724657", "16968944", "8508924", "19386608", "8921391", "8702478", "12724320", "18404483", "9755289", "11794691", "16914897", "16934527", "1...
[ "Molecular cloning and functional analysis of a novel P2 nucleotide receptor.", "Molecular physiology of P2X receptors.", "Modelling the P2Y purinoceptor using rhodopsin as template.", "Molecular pharmacology of P2Y-receptors.", "Renal vascular reactivity to P(2)-purinoceptor activation in spontaneously hyp...
[ 1995, 2002, 1995, 2000, 2000, 2011, 2000, 2010, 2001, 2006, 1997, 1994, 2006, 1993, 2009, 1996, 1996, 2003, 2006, 1998, 2001, 2006, 2006, 2000, 2001, 1996, 1996, 1997, 2008, 2008 ]
30
[ "IPR000276" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 207 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 2, 2 ]
3
true
Family
P2Y6 purinoceptor
P2Y6 purinoceptor
P2Y6_rcpt
3
IPR001975
1,975
Large ribosomal subunit protein eL40 domain
Ribosomal_eL40_dom
Domain
5,524
false
false
This entry represents the L40 ribosomal domain from both archaea and eukaryotes. In eukaryotes, L40 is fused to ubiquitin moieties, and this fusion protein is known as Ubiquitin-ribosomal protein eL40 fusion protein or UBL40 [ , ]. Specific endopeptidases cleave these precursor molecules to release ubiquitin moieties [...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "SMART" ]
[ "PF01020", "SM01377" ]
[ "Ribosomal_L40e", "Ribosomal_L40e" ]
[ 5344, 5200 ]
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-110312", "R-BTA-110314", "R-BTA-110320", "R-BTA-1169091", "R-BTA-1234176", "R-BTA-1253288", "R-BTA-1295596", "R-BTA-1358803", "R-BTA-156827", "R-BTA-168638", "R-BTA-174048", "R-BTA-174084", "R-BTA-174113", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-179409", "R-BT...
[ "REACTOME:R-BTA-110312", "REACTOME:R-BTA-110314", "REACTOME:R-BTA-110320", "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1253288", "REACTOME:R-BTA-1295596", "REACTOME:R-BTA-1358803", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-168638", "REACTOME:R-BTA-174048", "REACTOME:R-BT...
792
[ "2ayj", "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "4adx", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u", "4u4y", "4u4z"...
483
[ "PUB00000250", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00083511", "PUB00083514", "PUB00083520", "PUB00083521", "PUB00101554", "PUB00151163", "PUB00151164" ]
[ "7488009", "11297922", "11290319", "11114498", "15571815", "16185873", "22297692", "25208476", "32669547", "35613268", "23169626" ]
[ "The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27a and L40.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins.", "Mechanism and function of deubiquitinating enzymes.", "...
[ 1995, 2001, 2001, 2000, 2004, 2005, 2012, 2014, 2020, 2022, 2013 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 784, 6, 4713, 2, 19 ]
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", "Saccharomyces cerevisiae (strai...
[ 4, 1, 1, 2, 4, 4, 2, 20, 5, 2, 2, 10 ]
12
true
Domain
Large ribosomal subunit protein eL40 domain
Large ribosomal subunit protein eL40 domain
Ribosomal_eL40_dom
2
IPR001977
1,977
Dephospho-CoA kinase
Depp_CoAkinase
Family
32,347
false
false
This family contains Dephospho-coenzyme A kinase (DPCK, ), which catalyzes the final step in dephosphocoenzyme A (dCoA) biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. The crystal structures of a number of the proteins in this entry have been determined, including th...
[ "GO:0004140", "GO:0005524", "GO:0015937" ]
[ "dephospho-CoA kinase activity", "ATP binding", "coenzyme A biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM", "PROFILE", "NCBIFAM" ]
[ "MF_00376", "PF01121", "PS51219", "TIGR00152" ]
[ "Dephospho_CoA_kinase", "CoaE", "DPCK", "" ]
[ 30613, 32138, 32211, 31402 ]
4
[ "EC", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1.24", "GenProp0171", "PWY-7851", "PDOC00996", "R-CEL-196783", "R-DRE-196783", "R-HSA-196783", "R-MMU-196783", "R-RNO-196783", "R-SCE-196783", "R-SPO-196783", "R-SSC-196783", "R-XTR-196783" ]
[ "EC:2.7.1.24", "GP:GenProp0171", "METACYC:PWY-7851", "PROSITEDOC:PDOC00996", "REACTOME:R-CEL-196783", "REACTOME:R-DRE-196783", "REACTOME:R-HSA-196783", "REACTOME:R-MMU-196783", "REACTOME:R-RNO-196783", "REACTOME:R-SCE-196783", "REACTOME:R-SPO-196783", "REACTOME:R-SSC-196783", "REACTOME:R-XTR...
13
[ "1jjv", "1n3b", "1t3h", "1uf9", "1vhl", "1vht", "1viy", "2f6r", "2grj", "2if2", "4i1u", "4i1v", "4ttp", "4ttq", "4ttr", "4zo4", "6ari", "6n39", "8dv0", "8sbn", "8sbo", "8u94", "8u96", "8u97", "9bkz", "9dug" ]
26
[ "PUB00026419" ]
[ "11886213" ]
[ "Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 10, 25076, 6586, 4, 671 ]
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",...
[ 5, 5, 3, 4, 1, 7, 5, 1, 2, 6, 1, 1, 10 ]
13
true
Family
Dephospho-CoA kinase
Dephospho-CoA kinase
Depp_CoAkinase
8
IPR001978
1,978
Troponin
Troponin
Family
16,040
false
false
The troponin (Tn) complex regulates Ca 2+ induced muscle contraction. Tn contains three subunits, Ca 2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin [ , , ].
[ "GO:0005861" ]
[ "troponin complex" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF00992" ]
[ "Troponin" ]
[ 16040 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-390522", "R-CEL-5578775", "R-CFA-390522", "R-CFA-5578775", "R-DME-5578775", "R-HSA-390522", "R-HSA-5578775", "R-MMU-390522", "R-MMU-5578775", "R-RNO-390522", "R-RNO-5578775", "R-SSC-390522" ]
[ "REACTOME:R-BTA-390522", "REACTOME:R-CEL-5578775", "REACTOME:R-CFA-390522", "REACTOME:R-CFA-5578775", "REACTOME:R-DME-5578775", "REACTOME:R-HSA-390522", "REACTOME:R-HSA-5578775", "REACTOME:R-MMU-390522", "REACTOME:R-MMU-5578775", "REACTOME:R-RNO-390522", "REACTOME:R-RNO-5578775", "REACTOME:R-S...
12
[ "1a2x", "1j1d", "1j1e", "1ytz", "1yv0", "2mzp", "2n7l", "2w49", "2w4u", "2z5h", "4y99", "5vln", "5w88", "5wcl", "6klt", "6klu", "6kn7", "6kn8", "6mv3", "7jgi", "7kaa", "7ko4", "7ko5", "7ko7", "7kon", "7kor", "7sc2", "7sc3", "7sup", "7svc", "7swg", "7swi"...
80
[ "PUB00001531", "PUB00002926", "PUB00004000" ]
[ "7601340", "7852318", "3102969" ]
[ "The troponin complex and regulation of muscle contraction.", "A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction.", "Structure of co-crystals of tropomyosin and troponin." ]
[ 1995, 1995, 1987 ]
3
[]
[ "IPR027707" ]
0
1
0
[ "Bacteria", "Eukaryota", "Lightbulbvirus", "bird metagenome" ]
[ 15, 16019, 5, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 12, 85, 17, 58, 49, 46 ]
6
true
Family
Troponin
Troponin
Troponin
9
IPR001980
1,980
Phosphopantetheine adenylyltransferase
PPAT
Family
24,591
false
false
Phosphopantetheine adenylyltransferase (PPAT; ) is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis: catalysis of the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine to give dephospho-CoA (DPCOA) and pyrophosphate in the fourt...
[ "GO:0004595", "GO:0015937" ]
[ "pantetheine-phosphate adenylyltransferase activity", "coenzyme A biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PRINTS", "NCBIFAM", "CDD" ]
[ "MF_00151", "PR01020", "TIGR01510", "cd02163" ]
[ "PPAT_bact", "LPSBIOSNTHSS", "coaD_prev_kdtB", "PPAT" ]
[ 24058, 24470, 24219, 21738 ]
4
[ "EC", "GP", "METACYC", "METACYC" ]
[ "2.7.7.3", "GenProp0171", "PWY-7851", "PWY-8342" ]
[ "EC:2.7.7.3", "GP:GenProp0171", "METACYC:PWY-7851", "METACYC:PWY-8342" ]
4
[ "1b6t", "1gn8", "1h1t", "1o6b", "1od6", "1qjc", "1tfu", "1vlh", "3f3m", "3k9w", "3l92", "3l93", "3lcj", "3nba", "3nbk", "3nd5", "3nd6", "3nd7", "3nv7", "3otw", "3pnb", "3pxu", "3rba", "3rff", "3rhs", "3uc5", "3x1j", "3x1k", "3x1m", "4e1a", "4f3r", "4nah"...
118
[ "PUB00000266", "PUB00002701", "PUB00015594", "PUB00023529", "PUB00036800", "PUB00080721" ]
[ "10208837", "2033061", "10480925", "10205156", "11812124", "17873050" ]
[ "CTP:phosphocholine cytidylyltransferase: insights into regulatory mechanisms and novel functions.", "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing.", "Purification and characterization of phosphopantetheine adenylyltransfera...
[ 1999, 1991, 1999, 1999, 2002, 2007 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 18, 23863, 94, 12, 604 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Phosphopantetheine adenylyltransferase
Phosphopantetheine adenylyltransferase
PPAT
6
IPR001981
1,981
Colipase
Colipase
Family
1,421
false
false
Colipase [ , ] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. Efficient absorption of dietary fats is dependent on the action of pan...
[ "GO:0008047", "GO:0007586", "GO:0016042", "GO:0005576" ]
[ "enzyme activator activity", "digestion", "lipid catabolic process", "extracellular region" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS", "PROFILE", "PANTHER", "SMART" ]
[ "PR00128", "PS51342", "PTHR10041", "SM00023" ]
[ "COLIPASE", "COLIPASE_2", "", "COLIPASE" ]
[ 769, 965, 1269, 767 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00111", "R-BTA-192456", "R-BTA-975634", "R-HSA-192456", "R-HSA-975634", "R-MMU-192456", "R-MMU-975634", "R-RNO-192456", "R-RNO-975634", "R-SSC-192456", "R-SSC-975634", "R-XTR-192456", "R-XTR-975634" ]
[ "PROSITEDOC:PDOC00111", "REACTOME:R-BTA-192456", "REACTOME:R-BTA-975634", "REACTOME:R-HSA-192456", "REACTOME:R-HSA-975634", "REACTOME:R-MMU-192456", "REACTOME:R-MMU-975634", "REACTOME:R-RNO-192456", "REACTOME:R-RNO-975634", "REACTOME:R-SSC-192456", "REACTOME:R-SSC-975634", "REACTOME:R-XTR-1924...
13
[ "1eth", "1lpa", "1lpb", "1n8s", "1pcn", "1pco" ]
6
[ "PUB00000630", "PUB00000684", "PUB00006457", "PUB00006494" ]
[ "1567900", "3147715", "10570245", "9240923" ]
[ "Pancreatic colipase. Structural and physiological aspects.", "Minireview on pancreatic lipase and colipase.", "Colipase: structure and interaction with pancreatic lipase.", "Structure and function of pancreatic lipase and colipase." ]
[ 1992, 1988, 1999, 1997 ]
4
[]
[ "IPR047576" ]
0
1
0
[ "Enterobacteriaceae", "Eukaryota" ]
[ 2, 1419 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 5, 8 ]
3
true
Family
Colipase
Colipase
Colipase
8
IPR001985
1,985
S-adenosylmethionine decarboxylase, eukaryotes
S-AdoMet_decarboxylase_euk
Family
5,525
false
false
This entry includes S-adenosylmethionine decarboxylases from eukaryotes. S-adenosylmethionine decarboxylase (AdoMetDC) [ ] catalyses the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines ...
[ "GO:0004014", "GO:0006597", "GO:0008295" ]
[ "adenosylmethionine decarboxylase activity", "spermine biosynthetic process", "spermidine biosynthetic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PIRSF", "NCBIFAM" ]
[ "PIRSF001355", "TIGR00535" ]
[ "S-AdenosylMet_decarboxylase", "SAM_DCase" ]
[ 3763, 5251 ]
2
[ "EC", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.1.1.50", "GenProp1571", "PWY-6834", "PDOC01038", "R-BTA-351202", "R-CEL-351202", "R-DDI-351202", "R-DME-351202", "R-HSA-351202", "R-MMU-351202", "R-RNO-351202", "R-SCE-351202", "R-SPO-351202" ]
[ "EC:4.1.1.50", "GP:GenProp1571", "METACYC:PWY-6834", "PROSITEDOC:PDOC01038", "REACTOME:R-BTA-351202", "REACTOME:R-CEL-351202", "REACTOME:R-DDI-351202", "REACTOME:R-DME-351202", "REACTOME:R-HSA-351202", "REACTOME:R-MMU-351202", "REACTOME:R-RNO-351202", "REACTOME:R-SCE-351202", "REACTOME:R-SPO...
13
[ "1i72", "1i79", "1i7b", "1i7c", "1i7m", "1jen", "1jl0", "1mhm", "1msv", "3dz2", "3dz3", "3dz4", "3dz5", "3dz6", "3dz7", "3ep3", "3ep4", "3ep5", "3ep6", "3ep7", "3ep8", "3ep9", "3epa", "3epb", "3h0v", "3h0w", "9p1h", "9p7q", "9pbb" ]
29
[ "PUB00006224" ]
[ "10378277" ]
[ "The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold." ]
[ 1999 ]
1
[ "IPR048283" ]
[]
1
0
1
[ "Eukaryota", "Pseudomonadati" ]
[ 5520, 5 ]
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...
[ 13, 1, 1, 2, 5, 3, 1, 12, 4, 1, 1, 13 ]
12
true
Family
S-adenosylmethionine decarboxylase, eukaryotes
S-adenosylmethionine decarboxylase, eukaryotes
S-AdoMet_decarboxylase_euk
3
IPR001986
1,986
Enolpyruvate transferase domain
Enolpyruvate_Tfrase_dom
Domain
66,279
false
false
This entry represents the core domain of 3-phosphoshikimate 1-carboxyvinyltransferase and UDP-N-acetylglucosamine 1-carboxyvinyltransferase. These proteins transfer enolpryruvate from phosphoenolpyruvate to 3-phosphoshikimate and UDP-N-acetyl-alpha-D-glucosamine respectively [ , ]. The domain can also be found in the f...
[ "GO:0016765" ]
[ "transferase activity, transferring alkyl or aryl (other than methyl) groups" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00275" ]
[ "EPSP_synthase" ]
[ 66279 ]
1
[ "EC", "PROSITEDOC", "REACTOME" ]
[ "2.5.1", "PDOC00097", "R-MTU-964903" ]
[ "EC:2.5.1", "PROSITEDOC:PDOC00097", "REACTOME:R-MTU-964903" ]
3
[ "1a2n", "1dlg", "1ejc", "1ejd", "1eps", "1eyn", "1g6s", "1g6t", "1mi4", "1naw", "1p88", "1p89", "1q36", "1q3g", "1rf4", "1rf5", "1rf6", "1ryw", "1uae", "1x8r", "1x8t", "1ybg", "2aa9", "2aay", "2bjb", "2gg4", "2gg6", "2gga", "2ggd", "2o0b", "2o0d", "2o0e"...
123
[ "PUB00024300", "PUB00031046", "PUB00099962", "PUB00099963" ]
[ "9685163", "15103156", "28064057", "28830812" ]
[ "Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.", "Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.", "UDP-N-Acetylglucosamine enolpyruvyl transferase (MurA) of Acinetoba...
[ 1998, 2004, 2017, 2017 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 882, 59903, 3985, 2, 1507 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 12, 2, 1, 6, 1, 1, 12 ]
7
true
Domain
Enolpyruvate transferase domain
Enolpyruvate transferase domain
Enolpyruvate_Tfrase_dom
7
IPR001989
1,989
Radical-activating enzyme, conserved site
Radical_activat_CS
Conserved_site
19,474
false
false
In Escherichia coli and related bacteria, the pflA protein (or act) [ ] is involved ( ) in the activation of pyruvate formate-lyase (gene pflB) under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. The activi...
[ "GO:0016491", "GO:0051539" ]
[ "oxidoreductase activity", "4 iron, 4 sulfur cluster binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PROSITE" ]
[ "PS01087" ]
[ "RADICAL_ACTIVATING" ]
[ 19474 ]
1
[ "EC", "PROSITEDOC" ]
[ "1.97.1", "PDOC00834" ]
[ "EC:1.97.1", "PROSITEDOC:PDOC00834" ]
2
[ "3c8f", "3cb8", "8fo0", "8fol", "8fsi" ]
5
[ "PUB00001367", "PUB00002923", "PUB00003594" ]
[ "3053170", "7852304", "7773398" ]
[ "Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences.", "Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme.", "Novel phosphotransferase...
[ 1988, 1995, 1995 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 85, 18723, 121, 411, 134 ]
5
[ "Escherichia coli (strain K12)" ]
[ 5 ]
1
true
Conserved_site
Radical-activating enzyme, conserved site
Radical-activating enzyme, conserved site
Radical_activat_CS
7
IPR001990
1,990
Chromogranin A/B/C
Granin
Family
2,752
false
false
Granins (chromogranins or secretogranins) [ ] are a family of acidic proteins present in the secretory granules of a wide variety of endocrine and neuro-endocrine cells. The exact function(s) of these proteins is not yet known but they seem to be the precursors of biologically active peptides and/or they may act as hel...
[ "GO:0030141" ]
[ "secretory granule" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF01271" ]
[ "Granin" ]
[ 2752 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00365", "R-BTA-381426", "R-BTA-8957275", "R-HSA-381426", "R-HSA-6803157", "R-HSA-8957275", "R-MMU-381426", "R-MMU-6803157", "R-MMU-8957275", "R-RNO-381426", "R-RNO-6803157", "R-RNO-8957275", "R-SSC-381426", "R-SSC-8957275" ]
[ "PROSITEDOC:PDOC00365", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-8957275", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-6803157", "REACTOME:R-MMU-8957275", "REACTOME:R-RNO-381426", "REACTOME:R-RNO-6803157", "REACTOME:R-RN...
14
[]
0
[ "PUB00005374" ]
[ "2053134" ]
[ "The granin (chromogranin/secretogranin) family." ]
[ 1991 ]
1
[]
[ "IPR001819", "IPR038858" ]
0
2
0
[ "Vertebrata" ]
[ 2752 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 11, 10, 23 ]
4
true
Family
Chromogranin A/B/C
Chromogranin A/B/C
Granin
8
IPR001991
1,991
Sodium:dicarboxylate symporter
Na-dicarboxylate_symporter
Family
71,445
false
false
It has been shown [ ] that integral membrane proteins that mediate the uptake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. One of these families is known as the sodiu...
[ "GO:0015293", "GO:0016020" ]
[ "symporter activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00375", "PTHR42865" ]
[ "SDF", "" ]
[ 71423, 52207 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00591", "R-BTA-210455", "R-BTA-210500", "R-BTA-352230", "R-BTA-425393", "R-BTA-9013149", "R-BTA-9013406", "R-BTA-9013407", "R-BTA-9013423", "R-CEL-210455", "R-CEL-210500", "R-CEL-352230", "R-CEL-425393", "R-CEL-9013149", "R-CEL-9013406", "R-CEL-9013407", "R-CEL-9013423", "R-HS...
[ "PROSITEDOC:PDOC00591", "REACTOME:R-BTA-210455", "REACTOME:R-BTA-210500", "REACTOME:R-BTA-352230", "REACTOME:R-BTA-425393", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013407", "REACTOME:R-BTA-9013423", "REACTOME:R-CEL-210455", "REACTOME:R-CEL-210500", "REACTOME:R-CEL-...
43
[ "1xfh", "2nwl", "2nww", "2nwx", "3kbc", "3v8f", "3v8g", "4izm", "4ky0", "4oye", "4oyf", "4p19", "4p1a", "4p3j", "4p6h", "4x2s", "5cfy", "5dwy", "5e9s", "5llm", "5llu", "5lm4", "5mju", "6bat", "6bau", "6bav", "6bmi", "6ctf", "6gct", "6mp6", "6mpb", "6r7r"...
125
[ "PUB00000660", "PUB00004137", "PUB00004138", "PUB00004767" ]
[ "8031825", "1448170", "1280334", "1279699" ]
[ "A functional superfamily of sodium/solute symporters.", "Cloning and expression of a rat brain L-glutamate transporter.", "Primary structure and functional characterization of a high-affinity glutamate transporter.", "Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate tra...
[ 1994, 1992, 1992, 1992 ]
4
[]
[ "IPR023025", "IPR023954", "IPR034703" ]
0
3
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 373, 53449, 3, 17187, 433 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 32, 8, 4, 69, 40, 55 ]
7
true
Family
Sodium:dicarboxylate symporter
Sodium:dicarboxylate symporter
Na-dicarboxylate_symporter
8
IPR001992
1,992
T2SS_GspF/T4SS_PilC conserved site
T2SS_GspF/T4SS_PilC_CS
Conserved_site
12,070
false
false
GspF is the inner membrane component of the type II secretion system (T2SS). It interacts with GspE, a cytoplasmic hexameric ATPase of the T2SS [ ]. It shows considerable sequence similarity to PilC, which is required for the formation of type IV pili [ ]. The type II secretion system (T2SS) is one of several extracell...
[ "GO:0009306", "GO:0016020" ]
[ "protein secretion", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PROSITE" ]
[ "PS00874" ]
[ "T2SP_F" ]
[ 12070 ]
1
[ "PROSITEDOC" ]
[ "PDOC00682" ]
[ "PROSITEDOC:PDOC00682" ]
1
[]
0
[ "PUB00051842", "PUB00093998", "PUB00094002", "PUB00094004", "PUB00094010" ]
[ "19217396", "30767847", "28258547", "22523076", "17464073" ]
[ "Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.", "Architecture, Function, and Substrates of the Type II Secretion System.", "1H, 15N and 13C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxyt...
[ 2009, 2019, 2017, 2012, 2007 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 11820, 22, 228 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Conserved_site
T2SS_GspF/T4SS_PilC conserved site
T2SS_GspF/T4SS_PilC conserved site
T2SS_GspF/T4SS_PilC_CS
2
IPR001995
1,995
Peptidase A2A, retrovirus, catalytic
Peptidase_A2_cat
Domain
384,106
false
false
This group of aspartic peptidases belong to the peptidase clan AA. The clan includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses) which are active as homodimers. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C...
[ "GO:0004190", "GO:0006508" ]
[ "aspartic-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PROFILE" ]
[ "PS50175" ]
[ "ASP_PROT_RETROV" ]
[ 384106 ]
1
[ "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME",...
[ "2.7.7.-", "2.7.7.49", "2.7.7.7", "3.1.26", "3.4.23", "PWY-6322", "PWY-6626", "PWY-6749", "PWY-6955", "PWY-6998", "PWY-7127", "PWY-7419", "PWY-7529", "PWY-7706", "PWY-7719", "PWY-7735", "PWY-7737", "PWY-7769", "PWY-7888", "PWY-7904", "PWY-8117", "PWY-8179", "PDOC00128", ...
[ "EC:2.7.7.-", "EC:2.7.7.49", "EC:2.7.7.7", "EC:3.1.26", "EC:3.4.23", "METACYC:PWY-6322", "METACYC:PWY-6626", "METACYC:PWY-6749", "METACYC:PWY-6955", "METACYC:PWY-6998", "METACYC:PWY-7127", "METACYC:PWY-7419", "METACYC:PWY-7529", "METACYC:PWY-7706", "METACYC:PWY-7719", "METACYC:PWY-7735...
36
[ "1a30", "1a8g", "1a8k", "1a94", "1a9m", "1aaq", "1aid", "1ajv", "1ajx", "1axa", "1az5", "1b11", "1b6j", "1b6k", "1b6l", "1b6m", "1b6p", "1bai", "1bdl", "1bdq", "1bdr", "1bv7", "1bv9", "1bve", "1bvg", "1bwa", "1bwb", "1c6x", "1c6y", "1c6z", "1c70", "1cpi"...
963
[ "PUB00000093", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00032703", "PUB00041573", "PUB00042504", "PUB00048142", "PUB00065205", "PUB00066803", "PUB00076754", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076788", "PUB000767...
[ "2194475", "1851433", "8439290", "6795036", "10331925", "11566868", "10864493", "8841139", "17010377", "2682266", "18597783", "23254940", "21765428", "16395329", "4912600", "10497172", "21751400", "15831103", "9311808" ]
[ "The structure and function of the aspartic proteinases.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptidases.", "Gastric proteinases--structure, function, evolution and mechanism of action.", "Crystal structure of the hy...
[ 1990, 1991, 1993, 1981, 1999, 2001, 2000, 1996, 2006, 1989, 2008, 2013, 2011, 2006, 1970, 1999, 2011, 2005, 1997 ]
19
[]
[ "IPR018061" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 118, 4156, 18451, 361315, 66 ]
5
[ "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)", "...
[ 4, 17, 8, 21, 19, 1, 31, 1, 1, 1 ]
10
true
Domain
Peptidase A2A, retrovirus, catalytic
Peptidase A2A, retrovirus, catalytic
Peptidase_A2_cat
8
IPR001996
1,996
Phosphotransferase system, IIB component, type 1
PTS_IIB_1
Domain
44,446
false
false
This entry represents the component IIB of the glucose family of PTS systems (type 1). Several PTS permease families are currently recognised, namely, the (i) glucose (including glucoside), (ii) fructose (including mannitol), (iii) lactose (including N,N-diacetylchitobiose), (iv) galactitol, (v) glucitol, (vi) mannose,...
[ "GO:0008982", "GO:0009401" ]
[ "protein-N(PI)-phosphohistidine-sugar phosphotransferase activity", "phosphoenolpyruvate-dependent sugar phosphotransferase system" ]
[ "molecular_function", "biological_process" ]
2
[ "PROFILE", "NCBIFAM" ]
[ "PS51098", "TIGR00826" ]
[ "PTS_EIIB_TYPE_1", "EIIB_glc" ]
[ 44425, 27199 ]
2
[ "EC", "GP", "PROSITEDOC" ]
[ "2.7.1", "GenProp0119", "PDOC00795" ]
[ "EC:2.7.1", "GP:GenProp0119", "PROSITEDOC:PDOC00795" ]
3
[ "1iba", "1o2f", "3bp3", "3bp8", "3ipj", "8qsr", "8qst", "9hnp" ]
8
[ "PUB00000073", "PUB00002162", "PUB00003612", "PUB00070132" ]
[ "2197982", "1537788", "8246840", "16339738" ]
[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.", "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "Comparative genomic...
[ 1990, 1992, 1993, 2005 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 44330, 41, 75 ]
3
[ "Escherichia coli (strain K12)" ]
[ 8 ]
1
true
Domain
Phosphotransferase system, IIB component, type 1
Phosphotransferase system, IIB component, type 1
PTS_IIB_1
4
IPR001997
1,997
Calponin/LIMCH1
Calponin/LIMCH1
Family
5,206
false
false
Calponin is a smooth muscle-specific, actin-, tropomyosin- and calmodulin-binding protein believed to be involved in regulation or modulation of contraction [ , ]. Interaction of the protein with actin inhibits actomyosin MgATPase activity. Multiple isoforms are found in smooth muscle [ ]. Calponin is a basic protein o...
[ "GO:0003779", "GO:0031032" ]
[ "actin binding", "actomyosin structure organization" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00889" ]
[ "CALPONIN" ]
[ 5206 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6798695", "R-HSA-6798695", "R-HSA-8950505", "R-HSA-9927432", "R-MMU-6798695" ]
[ "REACTOME:R-BTA-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-8950505", "REACTOME:R-HSA-9927432", "REACTOME:R-MMU-6798695" ]
5
[ "1h67", "1wyn", "1wyp" ]
3
[ "PUB00001664", "PUB00002836", "PUB00002979" ]
[ "8370452", "8144658", "8550594" ]
[ "Mammalian calponin. Identification and expression of genetic variants.", "Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle.", "Developmental pattern of expression and genomic organization of the calponin-h1 gene. A contractile smooth muscle cell marker." ]
[ 1993, 1994, 1996 ]
3
[ "IPR003096" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "bird metagenome" ]
[ 2, 5203, 1 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 20, 1, 26, 18, 21 ]
5
true
Family
Calponin/LIMCH1
Calponin/LIMCH1
Calponin/LIMCH1
5
IPR001998
1,998
Xylose isomerase
Xylose_isomerase
Family
13,237
false
false
Xylose isomerase ( ) [ ] is an enzyme found in microorganisms which catalyzes the interconversion of D-xylose to D-xylulose. It can also isomerize D-ribose to D-ribulose and D-glucose to D-fructose. The enzyme is a homotetramer, which is stabilised by cobalt, and requires magnesium for its catalytic activity. Each subu...
[ "GO:0009045", "GO:0005975" ]
[ "xylose isomerase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PRINTS", "PROFILE", "PANTHER" ]
[ "MF_00455", "PR00688", "PS51415", "PTHR48408" ]
[ "Xylose_isom_A", "XYLOSISMRASE", "XYLOSE_ISOMERASE", "" ]
[ 11189, 12282, 13173, 11689 ]
4
[ "EC", "PROSITEDOC" ]
[ "5.3.1.5", "PDOC00156" ]
[ "EC:5.3.1.5", "PROSITEDOC:PDOC00156" ]
2
[ "1a0c", "1a0d", "1a0e", "1bhw", "1bxb", "1bxc", "1clk", "1did", "1die", "1dxi", "1gw9", "1mnz", "1muw", "1o1h", "1oad", "1qt1", "1s5m", "1s5n", "1xib", "1xic", "1xid", "1xie", "1xif", "1xig", "1xih", "1xii", "1xij", "1xim", "1xin", "1xis", "1xla", "1xlb"...
208
[ "PUB00001465", "PUB00001569", "PUB00003247" ]
[ "8620879", "2651156", "2769749" ]
[ "Protein purification, and cloning and characterization of the cDNA and gene for xylose isomerase of barley.", "Crystallisation and preliminary analysis of glucose isomerase from Streptomyces albus.", "Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbit...
[ 1996, 1989, 1989 ]
3
[]
[ "IPR013452", "IPR013453" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 14, 11548, 1494, 181 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 9, 1, 4, 42 ]
4
true
Family
Xylose isomerase
Xylose isomerase
Xylose_isomerase
2
IPR001999
1,999
Osteonectin-like, conserved site
Osteonectin_CS
Conserved_site
2,659
false
false
The osteonectin like domain, of unknown function, is found in extracellular proteins strongly expressed in tissues undergoing morphogenesis. It is a 240 amino acids domain, highly conserved, localised in the C-terminal part of the protein [ ]. This domain has a N-terminal section of about 90 residues that contains 11 c...
[ "GO:0005615" ]
[ "extracellular space" ]
[ "cellular_component" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00612", "PS00613" ]
[ "OSTEONECTIN_1", "OSTEONECTIN_2" ]
[ 2094, 2596 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00535", "R-BTA-114608", "R-BTA-3000178", "R-BTA-3000497", "R-CEL-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-8957275", "R-HSA-114608", "R-HSA-1251985", "R-HSA-3000178", "R-HSA-3000497", "R-HSA-381426", "R-HSA-8957275", "R-MMU-114608", "R-MMU-3000178", "R-MMU-3000497", "R-...
[ "PROSITEDOC:PDOC00535", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-3000497", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-3000178", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-8957275", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-1251985", "REACTOME:R-HSA-3000178", "REACTOME:R-HS...
27
[ "1bmo", "1nub", "1sra", "2v53", "7kbu" ]
5
[ "PUB00001526", "PUB00003931" ]
[ "8119487", "8548457" ]
[ "The biology of SPARC, a protein that modulates cell-matrix interactions.", "Structure of a novel extracellular Ca(2+)-binding module in BM-40." ]
[ 1994, 1996 ]
2
[]
[]
0
0
null
[ "Kangiella spongicola", "Opisthokonta" ]
[ 1, 2658 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 1, 14, 9, 12 ]
6
true
Conserved_site
Osteonectin-like, conserved site
Osteonectin-like, conserved site
Osteonectin_CS
6
IPR002000
2,000
Lysosome-associated membrane glycoprotein
Lysosome-assoc_membr_glycop
Family
6,740
false
false
Lysosome-associated membrane glycoproteins (lamp) [ ] are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal ext...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS", "PROFILE", "PANTHER" ]
[ "PR00336", "PS51407", "PTHR11506" ]
[ "LYSASSOCTDMP", "LAMP_3", "" ]
[ 3722, 5267, 6632 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00280", "R-BTA-6798695", "R-CEL-114608", "R-CEL-6798695", "R-HSA-114608", "R-HSA-6798695", "R-HSA-9613829", "R-MMU-114608", "R-MMU-6798695", "R-RNO-114608", "R-RNO-6798695" ]
[ "PROSITEDOC:PDOC00280", "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-6798695", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9613829", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-6798695" ]
11
[ "4akm", "5gv0", "5gv3", "8ath", "8fy5", "8fyf" ]
6
[ "PUB00002666", "PUB00002833", "PUB00052605", "PUB00052606" ]
[ "1939168", "8486654", "9768752", "10862717" ]
[ "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking.", "Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp/lgp family.", "A novel lysosome-associated membrane glycoprotein, DC-LAMP, induced upon DC maturation, is transiently expressed in MHC cl...
[ 1991, 1993, 1998, 2000 ]
4
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 6740 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 16, 7, 22, 17, 29 ]
6
true
Family
Lysosome-associated membrane glycoprotein
Lysosome-associated membrane glycoprotein
Lysosome-assoc_membr_glycop
7
IPR002001
2,001
GPCR, family 2, diuretic hormone receptor
GPCR_2_diuretic_rcpt
Family
691
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:0008036", "GO:0016020" ]
[ "diuretic hormone receptor activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01127" ]
[ "DIUHORMONER" ]
[ 691 ]
1
[]
[]
[]
0
[]
0
[ "PUB00001208", "PUB00002036", "PUB00002894", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "1646711", "8673074", "8276884", "1314625", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Molecular cloning and function expression of a diuretic hormone receptor from the house cricket, Acheta domesticus.", "Expression cloning of an insect diuretic hormone receptor. A member of the calcitonin/secretin receptor family.", ...
[ 1991, 1996, 1994, 1992, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]
13
[ "IPR000832" ]
[]
1
0
1
[ "Bilateria" ]
[ 691 ]
1
[ "Drosophila melanogaster" ]
[ 4 ]
1
true
Family
GPCR, family 2, diuretic hormone receptor
GPCR, family 2, diuretic hormone receptor
GPCR_2_diuretic_rcpt
3
IPR002002
2,002
Octopamine receptor
Octopmn_rcpt
Family
652
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:0004989", "GO:0007186", "GO:0016020" ]
[ "octopamine receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00664" ]
[ "OCTOPAMINER" ]
[ 652 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-390696", "R-CEL-392023", "R-CEL-400042", "R-CEL-418594", "R-CEL-418597", "R-DME-390696", "R-DME-392023", "R-DME-400042", "R-DME-418594", "R-DME-418597" ]
[ "REACTOME:R-CEL-390696", "REACTOME:R-CEL-392023", "REACTOME:R-CEL-400042", "REACTOME:R-CEL-418594", "REACTOME:R-CEL-418597", "REACTOME:R-DME-390696", "REACTOME:R-DME-392023", "REACTOME:R-DME-400042", "REACTOME:R-DME-418594", "REACTOME:R-DME-418597" ]
10
[]
0
[ "PUB00000131", "PUB00001197", "PUB00002477", "PUB00004304", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "2111655", "2170118", "2830256", "2156539", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "G proteins in signal transduction.", "Cloning and characterization of a Drosophila tyramine receptor.", "G protein involvement in receptor-effector coupling.", "Cloning, localization, and permanent expression of a Drosophila octopamine receptor.", "Design of a discriminating fingerprint for G-protein-coupl...
[ 1990, 1990, 1988, 1990, 1993, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
12
[ "IPR000276" ]
[]
1
0
1
[ "Bilateria" ]
[ 652 ]
1
[ "Caenorhabditis elegans", "Drosophila melanogaster" ]
[ 4, 2 ]
2
true
Family
Octopamine receptor
Octopamine receptor
Octopmn_rcpt
6
IPR002003
2,003
Gas vesicle protein GvpC
Gas-vesicle_GvpC
Repeat
228
false
false
Gas vesicles are small, hollow, gas filled protein structures found in several cyanobacterial and archaebacterial microorganisms [ ]. They allow the positioning of the bacteria at the favorable depth for growth. Gas vesicles are hollow cylindrical tubes, closed by a hollow, conical cap at each end. Both the conical end...
[ "GO:0031412", "GO:0031411" ]
[ "gas vesicle organization", "gas vesicle" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "NCBIFAM" ]
[ "PF01304", "TIGR02641" ]
[ "Gas_vesicle_C", "gvpC_cyan_rpt" ]
[ 153, 228 ]
2
[ "GP", "PROSITEDOC" ]
[ "GenProp0460", "PDOC00208" ]
[ "GP:GenProp0460", "PROSITEDOC:PDOC00208" ]
2
[]
0
[ "PUB00000481" ]
[ "2513809" ]
[ "Gas vesicle proteins." ]
[ 1989 ]
1
[]
[]
0
0
null
[ "Bacteria", "marine metagenome" ]
[ 227, 1 ]
2
[]
[]
0
true
Repeat
Gas vesicle protein GvpC
Gas vesicle protein GvpC
Gas-vesicle_GvpC
9
IPR002004
2,004
Polyadenylate-binding protein/Hyperplastic disc protein, C-terminal
PABP_HYD_C
Domain
15,966
false
false
The polyadenylate-binding protein (PABP) has a conserved C-terminal domain (PABC), which is also found in the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains ( ) [ ]. PABP recognises the 3' mRNA poly(A) tail and plays an essential role in eukaryotic translation initiation and mRNA...
[ "GO:0003723" ]
[ "RNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00658", "PS51309", "SM00517" ]
[ "MLLE", "PABC", "PolyA" ]
[ 15784, 15562, 15457 ]
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-156827", "R-BTA-429947", "R-BTA-450408", "R-BTA-72649", "R-BTA-975956", "R-BTA-975957", "R-DDI-156827", "R-DDI-450408", "R-DDI-975956", "R-DDI-975957", "R-DRE-156827", "R-DRE-450408", "R-DRE-975956", "R-DRE-975957", "R-HSA-156827", "R-HSA-429947", "R-HSA-450408", "R-HSA-7264...
[ "REACTOME:R-BTA-156827", "REACTOME:R-BTA-429947", "REACTOME:R-BTA-450408", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-450408", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-975957", "REACTOME:R-DRE-156827", "REACTOME:R-DRE-4504...
35
[ "1g9l", "1i2t", "1ifw", "1jgn", "1jh4", "1nmr", "2dyd", "2rqg", "2rqh", "2x04", "3ktp", "3ktr", "3kui", "3kuj", "3kur", "3kus", "3kut", "3ntw", "3pkn", "3pth", "4ive", "6h7a", "6h7b", "6r5k", "7bn3", "7pze", "8bja", "8c06", "8c07", "8d4x", "8e0q", "8ewi"...
38
[ "PUB00015091", "PUB00015092" ]
[ "11287654", "11940585" ]
[ "X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein.", "Solution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein." ]
[ 2001, 2002 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 11, 15944, 11 ]
3
[ "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...
[ 28, 4, 42, 5, 41, 21, 1, 22, 20, 1, 1, 42 ]
12
true
Domain
Polyadenylate-binding protein/Hyperplastic disc protein, C-terminal
Polyadenylate-binding protein/Hyperplastic disc protein, C-terminal
PABP_HYD_C
7
IPR002006
2,006
Hepatitis core antigen
Hepatitis_core
Family
24,018
false
false
This entry represent the core antigen of the viral capsid (HBcAg) from various Hepatitis B virus (HBV), which is a major human pathogen. The virus is composed of an outer envelope of host-derived lipid containing the surface proteins, and an inner protein capsid that contains genomic DNA. The capsid is composed of a si...
[ "GO:0005198" ]
[ "structural molecule activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM" ]
[ "MF_04076", "PF00906" ]
[ "HBV_HBEAG", "Hepatitis_core" ]
[ 8178, 24018 ]
2
[]
[]
[]
0
[ "1qgt", "2g33", "2g34", "2qij", "3j2v", "3kxs", "3v6z", "4bmg", "4g93", "5d7y", "5e0i", "5gmz", "5t2p", "5wre", "5wtw", "6bvf", "6bvn", "6cvk", "6cwd", "6cwt", "6ecs", "6edj", "6htx", "6hu4", "6hu7", "6j10", "6t36", "6tik", "6ui6", "6ui7", "6vzp", "6w0k"...
86
[ "PUB00030260" ]
[ "10394365" ]
[ "The crystal structure of the human hepatitis B virus capsid." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Hepadnaviridae", "Opisthokonta" ]
[ 24014, 4 ]
2
[]
[]
0
true
Family
Hepatitis core antigen
Hepatitis core antigen
Hepatitis_core
6
IPR002008
2,008
DNA polymerase family X, beta-like
DNA_pol_X_beta-like
Family
10,052
false
false
DNA carries the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA-polymerases, which add nucleotide triphosphate (dNTP) residues to the 3'-end of the growing ...
[ "GO:0003677", "GO:0006281" ]
[ "DNA binding", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00870" ]
[ "DNAPOLXBETA" ]
[ 10052 ]
1
[ "EC", "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTO...
[ "2.7.7.7", "4.2.99.-", "PWY-5397", "R-BTA-110362", "R-BTA-110373", "R-BTA-110381", "R-BTA-5649702", "R-BTA-5651801", "R-BTA-5689880", "R-BTA-73930", "R-DRE-110362", "R-DRE-110373", "R-DRE-5649702", "R-DRE-73930", "R-HSA-110362", "R-HSA-110373", "R-HSA-110381", "R-HSA-5649702", "R...
[ "EC:2.7.7.7", "EC:4.2.99.-", "METACYC:PWY-5397", "REACTOME:R-BTA-110362", "REACTOME:R-BTA-110373", "REACTOME:R-BTA-110381", "REACTOME:R-BTA-5649702", "REACTOME:R-BTA-5651801", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-73930", "REACTOME:R-DRE-110362", "REACTOME:R-DRE-110373", "REACTOME:R-DRE-...
38
[ "1bpb", "1bpd", "1bpe", "1bpx", "1bpy", "1bpz", "1huo", "1huz", "1jn3", "1mq2", "1mq3", "1nom", "1rpl", "1rzt", "1tv9", "1tva", "1xsl", "1xsn", "1xsp", "1zjm", "1zjn", "1zqa", "1zqb", "1zqc", "1zqd", "1zqe", "1zqf", "1zqg", "1zqh", "1zqi", "1zqj", "1zqk"...
547
[ "PUB00004647", "PUB00004955" ]
[ "3479792", "2196557" ]
[ "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.", "An attempt to unify the structure of polymerases." ]
[ 1987, 1990 ]
2
[ "IPR022312" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 490, 2649, 6618, 66, 229 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "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)", "Schizosaccharomyces pombe (st...
[ 5, 3, 22, 2, 2, 2, 7, 1, 1, 8 ]
10
true
Family
DNA polymerase family X, beta-like
DNA polymerase family X, beta-like
DNA_pol_X_beta-like
4
IPR002009
2,009
Bromovirus coat protein
Bromo_CP
Family
24
false
false
null
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01318" ]
[ "Bromo_coat" ]
[ 24 ]
1
[]
[]
[]
0
[ "1cwp", "1js9", "1yc6", "1za7", "3j7l", "3j7m", "3j7n", "6voc", "7pe1", "7pe2", "8bi4", "8c38", "8cpy" ]
13
[ "PUB00005263" ]
[ "7743132" ]
[ "Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Bromovirus" ]
[ 24 ]
1
[]
[]
0
true
Family
Bromovirus coat protein
Bromovirus coat protein
Bromo_CP
1
IPR002010
2,010
Type III secretion system inner membrane R protein
T3SS_IM_R
Family
17,407
false
false
Secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior [ ]. There have been four secretion systems described in animal enteropathogens such as Salmonella and Yersinia, with further sequence similarities in plant pathogens like Rals...
[ "GO:0006605", "GO:0016020" ]
[ "protein targeting", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01311", "PR00953", "PTHR30065" ]
[ "Bac_export_1", "TYPE3IMRPROT", "" ]
[ 17403, 16913, 17120 ]
3
[]
[]
[]
0
[ "6f2d", "6pem", "6pep", "6q14", "6q15", "6q16", "6r69", "6r6b", "6rwy", "6s3l", "6s3r", "6s3s", "7agx", "7ah9", "7ahi", "7bin", "7cgo", "7e80", "7nvg", "8axk", "8wk3", "8wkk", "8wkq", "8wl2", "8wlh", "8wln", "8wlq", "8wlt", "8wo5", "8woe", "8z5s", "8z5u"...
35
[ "PUB00003585", "PUB00007583", "PUB00007897", "PUB00007898" ]
[ "9618447", "10564516", "8969244", "10334981" ]
[ "Type III protein secretion systems in bacterial pathogens of animals and plants.", "Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium.", "Molecular mechanisms of bacterial virulence: type III secretion and pathogeni...
[ 1998, 1999, 1996, 1999 ]
4
[]
[ "IPR006303", "IPR006304" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 17208, 18, 181 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Type III secretion system inner membrane R protein
Type III secretion system inner membrane R protein
T3SS_IM_R
4
IPR002011
2,011
Tyrosine-protein kinase, receptor class II, conserved site
Tyr_kinase_rcpt_2_CS
Conserved_site
17,564
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:0004714", "GO:0005524", "GO:0006468", "GO:0007169", "GO:0016020" ]
[ "transmembrane receptor protein tyrosine kinase activity", "ATP binding", "protein phosphorylation", "cell surface receptor protein tyrosine kinase signaling pathway", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]
5
[ "PROSITE" ]
[ "PS00239" ]
[ "RECEPTOR_TYR_KIN_II" ]
[ 17564 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.10.1", "PDOC00212", "R-DME-110478", "R-DME-5140745", "R-DME-77387", "R-DME-9009391", "R-DRE-201556", "R-DRE-9842663", "R-DRE-9851151", "R-GGA-1257604", "R-GGA-388844", "R-GGA-6811558", "R-GGA-9026527", "R-GGA-9028731", "R-GGA-9032759", "R-GGA-9034013", "R-GGA-9034793", "R-GGA-...
[ "EC:2.7.10.1", "PROSITEDOC:PDOC00212", "REACTOME:R-DME-110478", "REACTOME:R-DME-5140745", "REACTOME:R-DME-77387", "REACTOME:R-DME-9009391", "REACTOME:R-DRE-201556", "REACTOME:R-DRE-9842663", "REACTOME:R-DRE-9851151", "REACTOME:R-GGA-1257604", "REACTOME:R-GGA-388844", "REACTOME:R-GGA-6811558", ...
122
[ "1g1f", "1gag", "1i44", "1ir3", "1irk", "1jqh", "1k3a", "1m7n", "1p14", "1p4o", "1rqq", "2auh", "2b4s", "2oj9", "2xb7", "2xba", "2xp2", "2yfx", "2yhv", "2yjr", "2yjs", "2z8c", "2zm3", "3aox", "3bu3", "3bu5", "3bu6", "3d94", "3ekk", "3ekn", "3eta", "3f5p"...
265
[ "PUB00000055", "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00052410", "PUB00052411", "PUB00052412" ]
[ "3052279", "3291115", "12368087", "12471243", "15078142", "15320712", "19275641", "16700535", "15845350" ]
[ "Growth factor receptor tyrosine kinases.", "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery...
[ 1988, 1988, 2002, 2002, 2004, 2004, 2009, 2006, 2005 ]
9
[]
[]
0
0
null
[ "Archaeoglobus fulgidus", "Bacteria", "Eukaryota", "UR2 avian sarcoma virus" ]
[ 3, 12, 17548, 1 ]
4
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 77, 42, 89, 25, 40 ]
5
true
Conserved_site
Tyrosine-protein kinase, receptor class II, conserved site
Tyrosine-protein kinase, receptor class II, conserved site
Tyr_kinase_rcpt_2_CS
9
IPR002013
2,013
SAC domain
SAC_dom
Domain
28,957
false
false
The Sac domain is a region of homology between the N terminus of synaptojanin and the otherwise unrelated yeast protein Sac1p. The Sac domain is approximately 400 residues in length, and proteins containing this domain show approximately 35% identity with other Sac domains throughout this region. The Sac domain exhibit...
[ "GO:0016791" ]
[ "phosphatase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02383", "PS50275" ]
[ "Syja_N", "SAC" ]
[ 28058, 27505 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.1.3", "GenProp1229", "GenProp1395", "GenProp1509", "GenProp1605", "GenProp1758", "PDOC50275", "R-BTA-1483248", "R-BTA-1660514", "R-CEL-1660499", "R-CEL-1855183", "R-CEL-1855204", "R-CEL-8856828", "R-DDI-1483248", "R-DDI-1660514", "R-DDI-1660516", "R-DME-1483248", "R-DME-1660514"...
[ "EC:3.1.3", "GP:GenProp1229", "GP:GenProp1395", "GP:GenProp1509", "GP:GenProp1605", "GP:GenProp1758", "PROSITEDOC:PDOC50275", "REACTOME:R-BTA-1483248", "REACTOME:R-BTA-1660514", "REACTOME:R-CEL-1660499", "REACTOME:R-CEL-1855183", "REACTOME:R-CEL-1855204", "REACTOME:R-CEL-8856828", "REACTOM...
54
[ "3lwt", "4tu3", "7k1w", "8c81" ]
4
[ "PUB00018232" ]
[ "11413010" ]
[ "The Sac phosphatase domain." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanocrinis", "marine sediment metagenome" ]
[ 37, 28917, 2, 1 ]
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...
[ 49, 5, 60, 11, 65, 22, 4, 37, 40, 5, 5, 169 ]
12
true
Domain
SAC domain
SAC domain
SAC_dom
8
IPR002014
2,014
VHS domain
VHS_dom
Domain
33,042
false
false
The VHS domain is an about 150 residues long domain, whose name is derived from its occurrence in VPS-27, Hrs and STAM. The VHS domain is found at the N- termini of proteins associated with endocytocis and/or vesicular trafficking, often in association with other domains like FYVE, SH3 or TAM [ , ]. The VHS domain of H...
[ "GO:0035091", "GO:0043130" ]
[ "phosphatidylinositol binding", "ubiquitin binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00790", "PS50179", "SM00288" ]
[ "VHS", "VHS", "VHS" ]
[ 29574, 32957, 29177 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50179", "R-BTA-182971", "R-BTA-432720", "R-BTA-5689880", "R-BTA-6807004", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-9013420", "R-BTA-917729", "R-BTA-9706019", "R-CEL-182971", "R-CEL-6807004", "R-CEL-8856825", "R-CEL-8856828", "R-CEL-9013420", "R-CEL-917729", "R-DME-182971", "R-...
[ "PROSITEDOC:PDOC50179", "REACTOME:R-BTA-182971", "REACTOME:R-BTA-432720", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-6807004", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-9013420", "REACTOME:R-BTA-917729", "REACTOME:R-BTA-9706019", "REACTOME:R-CEL-182971", "REACTOME:R-CE...
67
[ "1dvp", "1elk", "1jpl", "1juq", "1jwf", "1jwg", "1lf8", "1mhq", "1py1", "1ujj", "1ujk", "1vdy", "1x5b", "2dcp", "2l0t", "3g2s", "3g2t", "3g2u", "3g2v", "3g2w", "3ldz", "3rru", "3zyq", "4avx", "9rdc" ]
25
[ "PUB00008037", "PUB00008038", "PUB00018177", "PUB00018178" ]
[ "10985773", "10693761", "9600884", "9872381" ]
[ "Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes.", "Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction.", "SMART, a simple modular architecture research tool: identif...
[ 2000, 2000, 1998, 1998 ]
4
[]
[ "IPR027429", "IPR046996", "IPR047013", "IPR047493", "IPR047528" ]
0
5
0
[ "Bacteria", "Eukaryota", "Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)", "Pithovirus LCPAC001", "uncultured organism MedDCM-OCT-S01-C7" ]
[ 65, 32974, 1, 1, 1 ]
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", "Saccharomyces cerevisiae (strai...
[ 45, 5, 31, 8, 93, 35, 6, 31, 48, 4, 5, 101 ]
12
true
Domain
VHS domain
VHS domain
VHS_dom
8
IPR002015
2,015
Proteasome/cyclosome repeat
Proteasome/cyclosome_rpt
Repeat
12,638
false
false
A weakly conserved repeat module of unknown function, which occurs in two regulatory subunits of the 26S-proteasome and in one subunit of the anaphase-promoting complex [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF01851" ]
[ "PC_rep" ]
[ 12638 ]
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-1169091", "R-BTA-1234176", "R-BTA-1236978", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-187577", "R-BTA-195253", "R-BTA-202424", "R-BTA-2467813", "R-BTA-2871837", "R-BTA-349425", "R-BTA-350562", "R-BTA-382556", "R-BTA-450408", "R-BTA-4608870", "R-B...
[ "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA-187577", "REACTOME:R-BTA-195253", "REACTOME:R-BTA-202424", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA...
355
[ "2n3t", "2n3u", "2n3v", "2n3w", "2nbw", "3jco", "3jcp", "4ady", "4cr2", "4cr3", "4cr4", "5a5b", "5gjq", "5gjr", "5l4k", "5ln3", "5m32", "5mpb", "5mpc", "5mpd", "5mpe", "5t0c", "5t0g", "5t0h", "5t0i", "5t0j", "5vfp", "5vfq", "5vfr", "5vfs", "5vft", "5vfu"...
126
[ "PUB00005789" ]
[ "9204704" ]
[ "A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (anaphase-promoting complex)." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 12638 ]
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...
[ 13, 2, 3, 4, 22, 18, 2, 23, 12, 2, 2, 37 ]
12
true
Repeat
Proteasome/cyclosome repeat
Proteasome/cyclosome repeat
Proteasome/cyclosome_rpt
4