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
IPR004183
4,183
Extradiol ring-cleavage dioxygenase, class III enzyme, subunit B
Xdiol_dOase_suB
Domain
27,486
false
false
Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms. Cleavage of aromatic rings is one of the most important functions of dioxygenases, which play key roles in the degradation of aromatic compounds. The substrates of ring-cleavage dioxygenases...
[ "GO:0008198", "GO:0016491" ]
[ "ferrous iron binding", "oxidoreductase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF02900" ]
[ "LigB" ]
[ 27486 ]
1
[ "EC", "GP", "GP", "METACYC" ]
[ "1.13.11.16", "GenProp1287", "GenProp1458", "PWY-6690" ]
[ "EC:1.13.11.16", "GP:GenProp1287", "GP:GenProp1458", "METACYC:PWY-6690" ]
4
[ "1b4u", "1bou", "2pw6", "3vsg", "3vsh", "3vsi", "3vsj", "3wku", "3wpm", "3wr3", "3wr4", "3wr8", "3wr9", "3wra", "3wrb", "3wrc", "5hee", "7txy", "8ihg", "8in2", "8iq8", "8k04", "9j2l", "9kti" ]
24
[ "PUB00011779", "PUB00015247", "PUB00015248", "PUB00015256" ]
[ "10467151", "15264822", "12728990", "10730195" ]
[ "Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions.", "Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases.", "Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carb...
[ 1999, 2004, 2003, 1999 ]
4
[]
[ "IPR034939" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences" ]
[ 218, 21569, 5381, 2, 316 ]
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", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 4, 2, 1, 8, 1, 10 ]
6
true
Domain
Extradiol ring-cleavage dioxygenase, class III enzyme, subunit B
Extradiol ring-cleavage dioxygenase, class III enzyme, subunit B
Xdiol_dOase_suB
6
IPR004184
4,184
Pyruvate formate lyase domain
PFL_dom
Domain
17,543
false
false
Pyruvate formate lyase (PFL) catalyses the non-oxidative conversion of pyruvate and CoA to formate and acetyl-CoA. Several other enzymes have been identified in the pyruvate formate lyase family: ketoacid formate lyase, glycerol dehydratase (GD), benzyl succinate synthetase and p-hydroxyphenylacetate decarboxylase [ , ...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02901", "PS51554" ]
[ "PFL-like", "PFL" ]
[ 17392, 17489 ]
2
[]
[]
[]
0
[ "1cm5", "1h16", "1h17", "1h18", "1mzo", "1qhm", "1r8w", "1r9d", "2f3o", "2pfl", "2y8n", "2yaj", "3pfl", "4mtj", "4pkc", "4pkf", "5a0u", "5a0z", "5bwd", "5bwe", "5fau", "5fav", "5faw", "5fay", "5i2a", "5i2g", "5kdp", "5ymr", "6lon", "6nd3", "6vue", "6vxc"...
53
[ "PUB00022521", "PUB00040523" ]
[ "10425676", "16414072" ]
[ "Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.", "Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus." ]
[ 1999, 2006 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 43, 16251, 323, 3, 923 ]
5
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Domain
Pyruvate formate lyase domain
Pyruvate formate lyase domain
PFL_dom
1
IPR004186
4,186
Epstein Barr virus nuclear antigen-1, DNA-binding
EBNA1_DNA-bd
Domain
673
false
false
The Epstein-Barr virus (strain GD1) nuclear antigen 1 (EBNA1) binds to and activates DNA replication from the latent origin of replication. The crystal structure of the DNA-binding and dimerization domains were solved [ ], and it was found that EBNA1 appears to bind DNA via two independent regions, the core and the fla...
[ "GO:0003677", "GO:0006275", "GO:0045893", "GO:0042025" ]
[ "DNA binding", "regulation of DNA replication", "positive regulation of DNA-templated transcription", "host cell nucleus" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PFAM" ]
[ "PF02905" ]
[ "EBV-NA1" ]
[ 673 ]
1
[ "EC" ]
[ "3.1.21.-" ]
[ "EC:3.1.21.-" ]
1
[ "1b3t", "1vhi", "5t7x", "5wmf", "6npi", "6npm", "6npp", "6pw2", "6vh6", "7u1t", "8dlf" ]
11
[ "PUB00007413" ]
[ "7553871" ]
[ "Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Lymphocryptovirus", "Thiocapsa imhoffii" ]
[ 672, 1 ]
2
[]
[]
0
true
Domain
Epstein Barr virus nuclear antigen-1, DNA-binding
Epstein Barr virus nuclear antigen-1, DNA-binding
EBNA1_DNA-bd
7
IPR004188
4,188
Phenylalanine-tRNA ligase, class II, N-terminal
Phe-tRNA_ligase_II_N
Domain
25,215
false
false
Phenylalanine-tRNA ligase (also known as phenylalanyl-tRNA synthetase) from Thermus thermophilus has an α2/β2 type quaternary structure and is one of the most complicated members of the ligase family. Identification of phenylalanine-tRNA ligase a member of class II aaRSs was based only on sequence alignment of the smal...
[ "GO:0000166", "GO:0004826", "GO:0005524", "GO:0006432", "GO:0005737" ]
[ "nucleotide binding", "phenylalanine-tRNA ligase activity", "ATP binding", "phenylalanyl-tRNA aminoacylation", "cytoplasm" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
5
[ "PFAM" ]
[ "PF02912" ]
[ "Phe_tRNA-synt_N" ]
[ 25215 ]
1
[ "EC" ]
[ "6.1.1.20" ]
[ "EC:6.1.1.20" ]
1
[ "1b70", "1b7y", "1eiy", "1jjc", "1pys", "2iy5", "3hfz", "3pco", "3teh", "4p71", "4p72", "4p73", "4p74", "4p75", "4tva", "6oz5", "6p24", "6p26", "6p8t", "7daw", "7db7", "7db8", "7k98", "7k9m", "7ka0", "7kab", "7n8y", "9drs", "9drt", "9drv", "9dsx", "9dtf"...
32
[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]
[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]
[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...
[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]
10
[]
[]
0
0
null
[ "Bacteria", "Candidatus Nitrosopumilus salarius BD31", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 24548, 1, 124, 1, 541 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Phenylalanine-tRNA ligase, class II, N-terminal
Phenylalanine-tRNA ligase, class II, N-terminal
Phe-tRNA_ligase_II_N
3
IPR004189
4,189
Bacteriophage Mu, transposase
Phage_Mu_transposase
Domain
701
false
false
This transposase is essential for integration, replication-transposition and excision of Bacteriophage Mu DNA. Transposition requires transposase and a transposition enhancer, and the DNA can be transposed into multiple sites in bacterial genomes. The crystal structure of the core domain of Mu transposase, MuA, has bee...
[ "GO:0003677", "GO:0004803", "GO:0006313", "GO:0015074" ]
[ "DNA binding", "transposase activity", "DNA transposition", "DNA integration" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "PFAM" ]
[ "PF02914" ]
[ "DDE_2" ]
[ 701 ]
1
[]
[]
[]
0
[ "1bcm", "1bco", "4fcy" ]
3
[ "PUB00007414" ]
[ "7628012" ]
[ "Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Effrenium voratum", "metagenomes" ]
[ 684, 13, 1, 3 ]
4
[]
[]
0
true
Domain
Bacteriophage Mu, transposase
Bacteriophage Mu, transposase
Phage_Mu_transposase
5
IPR004190
4,190
DNA polymerase processivity factor
DNA_pol_proc_fac
Domain
1,148
false
false
The DNA polymerase processivity factor is a replisome sliding clamp subunit, which is responsible for tethering the catalytic subunit of DNA polymerase to the DNA during high speed replication. The crystal structure of the Bacteriophage RB69 sliding clamp has been solved. It has shown that the peptide binds to the slid...
[ "GO:0006260" ]
[ "DNA replication" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02916" ]
[ "DNA_PPF" ]
[ 1148 ]
1
[]
[]
[]
0
[ "1b77", "1b8h", "1czd", "2xxp", "2xxq", "3tel", "3tep", "3tfl", "3u5z", "3u60", "3u61", "4de8", "6drt", "7d7d", "8uh7", "8uk9", "8unf", "8unh", "9qx1", "9qx2", "9qx5" ]
21
[ "PUB00007415" ]
[ "10535734" ]
[ "Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Bacteria", "Rhabditomorpha", "Viruses", "marine metagenome" ]
[ 817, 35, 294, 2 ]
4
[ "Caenorhabditis elegans" ]
[ 2 ]
1
true
Domain
DNA polymerase processivity factor
DNA polymerase processivity factor
DNA_pol_proc_fac
3
IPR004192
4,192
Cytochrome b-c1 complex subunit Rieske, transmembrane domain
Rieske_TM
Domain
4,756
false
false
The ubiquinol cytochrome c reductase (cytochrome bc1) complex is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The bc1 complex contains 11 subunits, 3 respiratory subunits (cytochrome B, cytochrome C1, Rieske protein), 2 core proteins and 6 low-molecular weight proteins [ ]. ...
[ "GO:0008121" ]
[ "quinol-cytochrome-c reductase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02921" ]
[ "UCR_TM" ]
[ 4756 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "RE...
[ "7.1.1.8", "PWY-3781", "PWY-6692", "PWY-7279", "R-BTA-611105", "R-BTA-9865881", "R-CEL-9865881", "R-DME-611105", "R-DME-9865881", "R-DRE-9865881", "R-GGA-611105", "R-GGA-9865881", "R-HSA-611105", "R-HSA-9865881", "R-MMU-611105", "R-MMU-9865881", "R-RNO-611105", "R-RNO-9865881", "...
[ "EC:7.1.1.8", "METACYC:PWY-3781", "METACYC:PWY-6692", "METACYC:PWY-7279", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9865881", "REACTOME:R-CEL-9865881", "REACTOME:R-DME-611105", "REACTOME:R-DME-9865881", "REACTOME:R-DRE-9865881", "REACTOME:R-GGA-611105", "REACTOME:R-GGA-9865881", "REACTOME:R-H...
24
[ "1bcc", "1be3", "1bgy", "1ezv", "1kb9", "1kyo", "1l0l", "1l0n", "1ntk", "1ntm", "1ntz", "1nu1", "1p84", "1pp9", "1ppj", "1qcr", "1sqb", "1sqp", "1sqq", "1sqv", "1sqx", "2a06", "2bcc", "2fyu", "2ibz", "2ybb", "3bcc", "3cwb", "3cx5", "3cxh", "3h1h", "3h1i"...
173
[ "PUB00006415" ]
[ "9651245" ]
[ "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Eukaryota", "viral metagenome" ]
[ 4755, 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...
[ 8, 1, 1, 3, 5, 1, 1, 6, 4, 1, 1, 12 ]
12
true
Domain
Cytochrome b-c1 complex subunit Rieske, transmembrane domain
Cytochrome b-c1 complex subunit Rieske, transmembrane domain
Rieske_TM
1
IPR004193
4,193
Glycoside hydrolase, family 13, N-terminal
Glyco_hydro_13_N
Domain
61,191
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02922" ]
[ "CBM_48" ]
[ 61191 ]
1
[ "CAZY", "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH13", "2.4.1.18", "GenProp1483", "GenProp1726", "PWY-5067", "PWY-622", "PWY-7900", "R-DDI-3322077", "R-HSA-3322077", "R-HSA-3878781", "R-MMU-3322077", "R-SCE-3322077" ]
[ "CAZY:GH13", "EC:2.4.1.18", "GP:GenProp1483", "GP:GenProp1726", "METACYC:PWY-5067", "METACYC:PWY-622", "METACYC:PWY-7900", "REACTOME:R-DDI-3322077", "REACTOME:R-HSA-3322077", "REACTOME:R-HSA-3878781", "REACTOME:R-MMU-3322077", "REACTOME:R-SCE-3322077" ]
12
[ "1bf2", "1m7x", "2bhu", "2bhy", "2bhz", "2bxy", "2bxz", "2by0", "2by1", "2by2", "2by3", "2e8y", "2e8z", "2e9b", "2fgz", "2fh6", "2fh8", "2fhb", "2fhc", "2fhf", "2vnc", "2vr5", "2vuy", "2wan", "2wsk", "2y4s", "2y5e", "2ya0", "2ya1", "2ya2", "2yoc", "3amk"...
115
[ "PUB00004870", "PUB00005266" ]
[ "7624375", "8535779" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1995, 1995 ]
2
[]
[ "IPR044143", "IPR044505" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Yasminevirus sp. GU-2018", "unclassified sequences" ]
[ 134, 51167, 9447, 1, 442 ]
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",...
[ 29, 2, 3, 2, 3, 4, 3, 1, 31, 7, 1, 85 ]
12
true
Domain
Glycoside hydrolase, family 13, N-terminal
Glycoside hydrolase, family 13, N-terminal
Glyco_hydro_13_N
4
IPR004194
4,194
Restriction endonuclease, type II, BamHI
Restrct_endonuc_II_BamHI
Family
130
false
false
This entry represents BamHI restriction endonucleases, which recognises the DNA sequence GGATCC and cleaves after G-1 [ , ]. The enzyme binds as a dimer to the symmetrical GGATCC sequence but it recognises this sequence in an asymmetric manner, in which the C-terminal arm of one BamHI subunit goes into the DNA minor gr...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF02923", "PIRSF009309" ]
[ "BamHI", "Restrict_endonuc_II_BamHI" ]
[ 130, 20 ]
2
[]
[]
[]
0
[ "1bam", "1bhm", "1esg", "2bam", "3bam", "3odh" ]
6
[ "PUB00007417", "PUB00022958", "PUB00024656", "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707", "PUB00110633" ]
[ "8145855", "9783752", "10882125", "15770420", "14576294", "11827971", "11557805", "15121719", "12665693", "20833632" ]
[ "Structure of restriction endonuclease BamHI and its relationship to EcoRI.", "The role of metals in catalysis by the restriction endonuclease BamHI.", "Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.", "Type II restriction endonucleases: structure and mechanism.", "Diversity of type I...
[ 1994, 1998, 2000, 2005, 2003, 2002, 2001, 2004, 2003, 2011 ]
10
[]
[]
0
0
null
[ "Bacteria", "Halobacteriales" ]
[ 125, 5 ]
2
[]
[]
0
true
Family
Restriction endonuclease, type II, BamHI
Restriction endonuclease, type II, BamHI
Restrct_endonuc_II_BamHI
3
IPR004195
4,195
Head decoration protein D
Head_decoration_D
Family
2,779
false
false
Bacteriophage lambda head decoration protein D stabilises the head shell after the rearrangement of GP7 subunits of the head shell lattice that accompanies expansion of the head. There are approximately 420 copies of protein D per mature phage.
[]
[]
[]
0
[ "PFAM" ]
[ "PF02924" ]
[ "HDPD" ]
[ 2779 ]
1
[]
[]
[]
0
[ "1c5e", "1tcz", "1td0", "1td3", "1td4", "1vd0", "5mfd", "6xgq", "7vii", "7vik", "8vji", "8w3p", "8xqb" ]
13
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1)", "Viruses", "unclassified sequences" ]
[ 2605, 17, 1, 140, 16 ]
5
[]
[]
0
true
Family
Head decoration protein D
Head decoration protein D
Head_decoration_D
6
IPR004196
4,196
Scaffold protein D
Scaffold_D
Family
328
false
false
The assembly of a macromolecular structure proceeds via a specific pathway of ordered events and occurs by changing of protein conformations as they join the assembly. The assembly process is aided by scaffolding proteins, which act as chaperones. In bacteriophages, scaffolding proteins B and D are responsible for proc...
[ "GO:0046797" ]
[ "viral procapsid maturation" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02925" ]
[ "gpD" ]
[ 328 ]
1
[]
[]
[]
0
[ "1al0", "1cd3", "1m0f", "1tx9" ]
4
[ "PUB00007418" ]
[ "9305849" ]
[ "Structure of a viral procapsid with molecular scaffolding." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Bacteria", "Candidatus Argoarchaeum ethanivorans", "Eukaryota", "Viruses" ]
[ 170, 1, 52, 105 ]
4
[]
[]
0
true
Family
Scaffold protein D
Scaffold protein D
Scaffold_D
1
IPR004197
4,197
Cellulase, Ig-like domain
Cellulase_Ig-like
Domain
5,895
false
false
Cellulases (Endoglucanases) catalyse the endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose. This is the N-terminal ig-like domain of cellulase, enzymes containing this domain belong to family 9 of the glycoside hydrolases ( ).
[ "GO:0008810", "GO:0005975" ]
[ "cellulase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "CDD" ]
[ "PF02927", "cd02850" ]
[ "CelD_N", "E_set_Cellulase_N" ]
[ 5717, 5841 ]
2
[ "CAZY", "EC", "METACYC" ]
[ "GH9", "3.2.1.4", "PWY-6788" ]
[ "CAZY:GH9", "EC:3.2.1.4", "METACYC:PWY-6788" ]
3
[ "1clc", "1rq5", "1ut9", "3ez8", "3gzk", "3h2w", "3h3k", "3h7l", "3k4z", "3rx5", "3rx7", "3rx8", "3x17", "4cj0", "4cj1", "5dgq", "5dgr", "5e2j", "5u0h", "5u2o", "6dht", "6fhj", "6fhn", "6gdt" ]
24
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]
[ 19, 5713, 105, 2, 56 ]
5
[]
[]
0
true
Domain
Cellulase, Ig-like domain
Cellulase, Ig-like domain
Cellulase_Ig-like
4
IPR004198
4,198
Zinc finger, C5HC2-type
Znf_C5HC2
Domain
14,202
false
false
This entry represents a predicted zinc finger with eight potential zinc ligand binding residues. This domain is found in proteins enconded by the Jumonji gene [ ], and may have a DNA binding function. The mouse jumonji protein is required for neural tube formation, and is essential for normal heart development. It also...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02928" ]
[ "zf-C5HC2" ]
[ 14202 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.11", "R-CEL-3214842", "R-DME-212300", "R-DME-8866911", "R-DRE-212300", "R-DRE-8866911", "R-GGA-8866911", "R-HSA-212300", "R-HSA-3214842", "R-HSA-8866911", "R-HSA-9821002", "R-MMU-212300", "R-MMU-3214842", "R-MMU-8866911", "R-SPO-3214842" ]
[ "EC:1.14.11", "REACTOME:R-CEL-3214842", "REACTOME:R-DME-212300", "REACTOME:R-DME-8866911", "REACTOME:R-DRE-212300", "REACTOME:R-DRE-8866911", "REACTOME:R-GGA-8866911", "REACTOME:R-HSA-212300", "REACTOME:R-HSA-3214842", "REACTOME:R-HSA-8866911", "REACTOME:R-HSA-9821002", "REACTOME:R-MMU-212300"...
15
[ "5a1f", "5a3n", "5a3p", "5a3t", "5a3w", "5ceh", "5fpl", "5fpu", "5fun", "5fup", "5fv3", "5fwj", "5fy4", "5fy5", "5fy9", "5fyb", "5fys", "5fyt", "5fyu", "5fyv", "5fyy", "5fyz", "5fz0", "5fz1", "5fz3", "5fz4", "5fz6", "5fz7", "5fz8", "5fz9", "5fza", "5fzb"...
66
[ "PUB00007419", "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]
[ "11165500", "12665246", "17210253", "15963892", "15718139", "10529348", "11179890" ]
[ "JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.", "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.", "...
[ 2001, 2002, 2007, 2005, 2005, 1999, 2001 ]
7
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 14201, 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", "Schizosaccharomyces pombe (stra...
[ 37, 2, 26, 3, 34, 6, 1, 12, 25, 3, 114 ]
11
true
Domain
Zinc finger, C5HC2-type
Zinc finger, C5HC2-type
Znf_C5HC2
4
IPR004199
4,199
Beta galactosidase small chain/ domain 5
B-gal_small/dom_5
Domain
16,702
false
false
This domain comprises the small chain of dimeric beta-galactosidases . This domain is also found in single chain beta-galactosidase, which is comprised of five domains, where it represents domain 5. It contains an N-terminal loop that swings towards the active site upon the deep binding of a ligand to produce a closed ...
[ "GO:0004565", "GO:0005975", "GO:0009341" ]
[ "beta-galactosidase activity", "carbohydrate metabolic process", "beta-galactosidase complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "SMART" ]
[ "PF02929", "SM01038" ]
[ "Bgal_small_N", "Bgal_small_N" ]
[ 16696, 15818 ]
2
[ "CAZY", "EC", "METACYC" ]
[ "GH42", "3.2.1.23", "PWY-6807" ]
[ "CAZY:GH42", "EC:3.2.1.23", "METACYC:PWY-6807" ]
3
[ "1dp0", "1f4a", "1f4h", "1hn1", "1jyn", "1jyv", "1jyw", "1jyx", "1jz2", "1jz3", "1jz4", "1jz5", "1jz6", "1jz7", "1jz8", "1px3", "1px4", "1yq2", "3bga", "3czj", "3dec", "3dym", "3dyo", "3dyp", "3e1f", "3i3b", "3i3d", "3i3e", "3iap", "3iaq", "3j7h", "3muy"...
103
[ "PUB00016274" ]
[ "11732897" ]
[ "A structural view of the action of Escherichia coli (lacZ) beta-galactosidase." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Heunggongvirae", "metagenomes" ]
[ 67, 13959, 2448, 4, 224 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Homo sapiens", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 9, 3, 1, 2, 3, 14 ]
6
true
Domain
Beta galactosidase small chain/ domain 5
Beta galactosidase small chain/ domain 5
B-gal_small/dom_5
3
IPR004201
4,201
CDC48, domain 2
Cdc48_dom2
Domain
15,323
false
false
The CDC48 N-terminal domain is a protein domain found in AAA ATPases including cell division protein 48 (CDC48), VCP-like ATPase (VAT) and N-ethylmaleimide sensitive fusion protein. It is a substrate recognition domain which binds polypeptides, prevents protein aggregation, and catalyses refolding of permissive substra...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF02933", "SM01072" ]
[ "CDC48_2", "CDC48_2" ]
[ 14311, 13489 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.6.4.6", "R-CEL-110320", "R-CEL-204005", "R-CEL-3371511", "R-CEL-382556", "R-CEL-532668", "R-CEL-5358346", "R-CEL-5689877", "R-CEL-6798695", "R-CEL-6807878", "R-CEL-6811434", "R-CEL-6811438", "R-CEL-6811440", "R-CEL-8876725", "R-CEL-8951664", "R-CEL-9013407", "R-CEL-9755511", "R-...
[ "EC:3.6.4.6", "REACTOME:R-CEL-110320", "REACTOME:R-CEL-204005", "REACTOME:R-CEL-3371511", "REACTOME:R-CEL-382556", "REACTOME:R-CEL-532668", "REACTOME:R-CEL-5358346", "REACTOME:R-CEL-5689877", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6807878", "REACTOME:R-CEL-6811434", "REACTOME:R-CEL-6811438"...
140
[ "1cr5", "1cz4", "1cz5", "1e32", "1qcs", "1qdn", "1r7r", "1s3s", "2jv2", "2m3x", "2pjh", "3cf1", "3cf2", "3cf3", "3hu1", "3hu2", "3hu3", "3j94", "3j95", "3j96", "3j97", "3j98", "3j99", "3qc8", "3qq7", "3qq8", "3qwz", "3tiw", "4kdi", "4kdl", "4kln", "4ko8"...
223
[ "PUB00007420" ]
[ "10531028" ]
[ "The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2271, 1468, 11513, 3, 68 ]
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...
[ 15, 4, 8, 7, 30, 4, 2, 7, 10, 2, 3, 46 ]
12
true
Domain
CDC48, domain 2
CDC48, domain 2
Cdc48_dom2
1
IPR004203
4,203
Cytochrome c oxidase subunit IV family
Cyt_c_oxidase_su4_fam
Family
4,789
false
false
Cytochrome c oxidase (CcO) ( ), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyses the reduction of O2 and simultaneously pumps protons across the membrane...
[ "GO:0006123" ]
[ "mitochondrial electron transport, cytochrome c to oxygen" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02936", "PTHR10707", "cd00922" ]
[ "COX4", "", "Cyt_c_Oxidase_IV" ]
[ 4724, 4462, 4217 ]
3
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1426", "R-BTA-5628897", "R-BTA-611105", "R-BTA-9707564", "R-BTA-9864848", "R-HSA-5628897", "R-HSA-611105", "R-HSA-9707564", "R-HSA-9837999", "R-HSA-9864848", "R-MMU-5628897", "R-MMU-611105", "R-MMU-9707564", "R-MMU-9864848", "R-RNO-5628897", "R-RNO-611105", "R-RNO-9707564", ...
[ "GP:GenProp1426", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9864848", "REACTOME:R-HSA-5628897", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-9707564", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9864848", "REACTOME:R-MMU-5628897", "REACTOME:R-MMU-61...
18
[ "1occ", "1oco", "1ocr", "1ocz", "1v54", "1v55", "2dyr", "2dys", "2eij", "2eik", "2eil", "2eim", "2ein", "2occ", "2y69", "2ybb", "2zxw", "3abk", "3abl", "3abm", "3ag1", "3ag2", "3ag3", "3ag4", "3asn", "3aso", "3wg7", "3x2q", "5b1a", "5b1b", "5b3s", "5gpn"...
130
[ "PUB00005218", "PUB00016470", "PUB00059200", "PUB00059303", "PUB00059304", "PUB00079537", "PUB00079538", "PUB00079539", "PUB00079540", "PUB00079541", "PUB00079542", "PUB00079543", "PUB00080111", "PUB00080112", "PUB00080113" ]
[ "8638158", "14562095", "18845848", "11311561", "2824989", "12909344", "11035249", "9752724", "16760263", "16631971", "16199211", "15598510", "16336199", "12973739", "12270909" ]
[ "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.", "Global analysis of protein localization in budding yeast.", "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae.", "Mammalian subun...
[ 1996, 2003, 2008, 2001, 1987, 2003, 2000, 1998, 2006, 2006, 2005, 2005, 2006, 2003, 2002 ]
15
[]
[ "IPR013288" ]
0
1
0
[ "Actinomycetes", "Eukaryota" ]
[ 2, 4787 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 1, 3, 3, 7, 4, 1, 9, 3, 1 ]
9
true
Family
Cytochrome c oxidase subunit IV family
Cytochrome c oxidase subunit IV family
Cyt_c_oxidase_su4_fam
2
IPR004204
4,204
Cytochrome c oxidase subunit 7e/7s
Cox7e/7s
Family
3
false
false
Cytochrome c oxidase (CcO; ), a 13 subunit complex, is the terminal oxidase in the mitochondrial electron transport chain. Cytochrome c oxidase is the component of the respiratory chain that catalyses the reduction of oxygen to water [ , ]. This entry contains the subunits 7e and 7s of cytochrome c oxidase (also known ...
[ "GO:0006123" ]
[ "mitochondrial electron transport, cytochrome c to oxygen" ]
[ "biological_process" ]
1
[ "CDD" ]
[ "cd00927" ]
[ "CcO_VIc-like" ]
[ 3 ]
1
[]
[]
[]
0
[]
0
[ "PUB00079538", "PUB00079540", "PUB00080112" ]
[ "11035249", "16760263", "12973739" ]
[ "Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase.", "Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process.", "Mitochondrial proteome: altered cytochrome c oxidase subunit levels in prostate cancer." ]
[ 2000, 2006, 2003 ]
3
[]
[]
0
0
null
[ "Dictyostelia" ]
[ 3 ]
1
[]
[]
0
true
Family
Cytochrome c oxidase subunit 7e/7s
Cytochrome c oxidase subunit 7e/7s
Cox7e/7s
9
IPR004205
4,205
Cytochrome b-c1 complex subunit 8
Cyt_bc1_su8
Family
3,260
false
false
The ubiquinol-cytochrome C reductase complex (cytochrome bc1 complex) is a respiratory multi-enzyme complex [ ], which recognises a mitochondrial targeting presequence. The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske protein), 2 core proteins and 6 low molecular weig...
[ "GO:0006122" ]
[ "mitochondrial electron transport, ubiquinol to cytochrome c" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02939", "PTHR12119" ]
[ "UcrQ", "" ]
[ 3260, 3047 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-611105", "R-DDI-9837999", "R-HSA-611105", "R-HSA-9837999", "R-HSA-9865881", "R-MMU-611105", "R-MMU-9837999", "R-MMU-9865881", "R-RNO-611105", "R-RNO-9837999", "R-RNO-9865881", "R-SCE-611105", "R-SCE-9837999", "R-SCE-9865878", "R-SPO-611105", "R-SPO-9837999" ]
[ "REACTOME:R-DDI-611105", "REACTOME:R-DDI-9837999", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9865881", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-9837999", "REACTOME:R-MMU-9865881", "REACTOME:R-RNO-611105", "REACTOME:R-RNO-9837999", "REACTOME:R-RNO-9865881", "REACTOME:R-...
16
[ "1bcc", "1be3", "1bgy", "1ezv", "1kb9", "1kyo", "1l0l", "1l0n", "1ntk", "1ntm", "1ntz", "1nu1", "1p84", "1pp9", "1ppj", "1qcr", "1sqb", "1sqp", "1sqq", "1sqv", "1sqx", "2a06", "2bcc", "2fyu", "2ibz", "2ybb", "3bcc", "3cwb", "3cx5", "3cxh", "3h1h", "3h1i"...
160
[ "PUB00006415", "PUB00059236" ]
[ "9651245", "12709789" ]
[ "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.", "A deletion in the human QP-C gene causes a complex III deficiency resulting in hypoglycaemia and lactic acidosis." ]
[ 1998, 2003 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3260 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 2, 1, 1, 2, 2, 1, 3, 1, 1 ]
9
true
Family
Cytochrome b-c1 complex subunit 8
Cytochrome b-c1 complex subunit 8
Cyt_bc1_su8
7
IPR004206
4,206
mRNA triphosphatase Cet1-like
mRNA_triPase_Cet1
Domain
2,309
false
false
The mRNA capping enzyme in yeast is composed of two subunits, alpha and beta. The alpha subunit has guanylyltransferase activity, whilst the beta subunit is an RNA 5'-triphosphatase (RTPase) [ ]. This entry represents a domain found in the mRNA capping enzyme beta subunit Cet1. RTPase catalyzes the first step in the mR...
[ "GO:0004651" ]
[ "polynucleotide 5'-phosphatase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "CDD" ]
[ "PF02940", "cd07470" ]
[ "mRNA_triPase", "CYTH-like_mRNA_RTPase" ]
[ 2272, 2090 ]
2
[ "EC", "GP", "METACYC" ]
[ "3.6.1.74", "GenProp1354", "PWY-7375" ]
[ "EC:3.6.1.74", "GP:GenProp1354", "METACYC:PWY-7375" ]
3
[ "1d8h", "1d8i", "3kyh", "4pn0", "4pn1", "6l7v", "6l7w", "6l7x", "6l7y" ]
9
[ "PUB00000015", "PUB00010433", "PUB00019882", "PUB00024132", "PUB00044682", "PUB00075584", "PUB00076463", "PUB00076464", "PUB00079677", "PUB00079678", "PUB00079679", "PUB00079680", "PUB00079681", "PUB00079682", "PUB00079683" ]
[ "8418825", "12456267", "9755857", "10589681", "9345280", "10219091", "16809816", "24021036", "12788946", "11279161", "11395522", "11279098", "9710603", "12762032", "11051760" ]
[ "Phylogeny of adenylyl cyclases.", "The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates.", "Isolation and characterization of the Candida albicans gene for mRNA 5'-triphosphatase: association of mRNA 5'-triphosphatase...
[ 1993, 2002, 1998, 1999, 1997, 1999, 2006, 2013, 2003, 2001, 2001, 2001, 1998, 2001, 2001 ]
15
[]
[]
0
0
null
[ "Eukaryota", "Viruses", "candidate division WWE3 bacterium", "metagenomes" ]
[ 2243, 50, 1, 15 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 2, 1 ]
3
true
Domain
mRNA triphosphatase Cet1-like
mRNA triphosphatase Cet1-like
mRNA_triPase_Cet1
4
IPR004207
4,207
Ferredoxin thioredoxin reductase, alpha chain
Fd_thioredoxin_Rdtase_alpha
Domain
1,144
false
false
Ferredoxin thioredoxin reductase is a [4FE-4S] protein which plays an important role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin), regulating enzymes by reduction of specific disulphide groups. It catalyses the light-dep...
[ "GO:0015979" ]
[ "photosynthesis" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02941" ]
[ "FeThRed_A" ]
[ 1144 ]
1
[]
[]
[]
0
[ "1dj7", "2pu9", "2puk", "2puo", "2pvd", "2pvg", "2pvo", "7c2b", "7c3f" ]
9
[ "PUB00010712", "PUB00095446" ]
[ "10649999", "8898896" ]
[ "Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.", "Amino acid sequence of the maize ferredoxin:thioredoxin reductase variable subunit." ]
[ 2000, 1996 ]
2
[]
[]
0
0
null
[ "Cyanobacteriota", "Eukaryota" ]
[ 332, 812 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 6, 6, 12 ]
3
true
Domain
Ferredoxin thioredoxin reductase, alpha chain
Ferredoxin thioredoxin reductase, alpha chain
Fd_thioredoxin_Rdtase_alpha
7
IPR004210
4,210
BESS motif
BESS_motif
Domain
7,327
false
false
The BESS domain has been named after the three proteins that originally defined the domain: BEAF (Boundary element associated factor 32) [ ], Suvar(3)7 [ ] and Stonewall [ ]). The BESS domain is 40 amino acid residues long and is predicted to be composed of three α helices, as such it might be related to the myb/SANT H...
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02944", "PS51031" ]
[ "BESS", "BESS" ]
[ 5539, 6955 ]
2
[ "PROSITEDOC" ]
[ "PDOC51031" ]
[ "PROSITEDOC:PDOC51031" ]
1
[]
0
[ "PUB00007422", "PUB00007423", "PUB00007424", "PUB00018477", "PUB00018478", "PUB00018479", "PUB00018480" ]
[ "7781065", "2107402", "8631271", "1731341", "9528796", "12459265", "11902679" ]
[ "Visualization of chromosomal domains with boundary element-associated factor BEAF-32.", "Dependence of position-effect variegation in Drosophila on dose of a gene encoding an unusual zinc-finger protein.", "The Drosophila stonewall gene encodes a putative transcription factor essential for germ cell developmen...
[ 1995, 1990, 1996, 1992, 1998, 2002, 2002 ]
7
[]
[]
0
0
null
[ "Acinetobacter haemolyticus", "Eukaryota", "Mythimna separata entomopoxvirus 'L'" ]
[ 1, 7325, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster" ]
[ 2, 14, 76 ]
3
true
Domain
BESS motif
BESS motif
BESS_motif
7
IPR004211
4,211
Recombination endonuclease VII
Endonuclease_7
Family
4,037
false
false
This family of proteins which includes Bacteriophage T4 endonuclease VII, Mycobacteriophage D29 gene 59, and other as yet uncharacterised proteins. The T4 endonuclease VII (Endo VII) recognises a broad spectrum of DNA substrates ranging from branched DNAs to single base mismatches. The structure of this enzyme has been...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02945" ]
[ "Endonuclease_7" ]
[ 4037 ]
1
[]
[]
[]
0
[ "1e7d", "1e7l", "1en7", "2qnc", "2qnf", "3fc3", "3gox" ]
7
[ "PUB00007425" ]
[ "10075917" ]
[ "X-ray structure of T4 endonuclease VII: a DNA junction resolvase with a novel fold and unusual domain-swapped dimer architecture." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 6, 1407, 907, 1528, 189 ]
5
[]
[]
0
true
Family
Recombination endonuclease VII
Recombination endonuclease VII
Endonuclease_7
4
IPR004212
4,212
GTF2I-like repeat
GTF2I
Repeat
3,572
false
false
This region of sequence similarity is found up to six times in a variety of proteins including general transcription factor II-I (GTF2I). It has been suggested that this may be a DNA binding domain [ , ].
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF02946", "PS51139" ]
[ "GTF2I", "GTF2I" ]
[ 3394, 3532 ]
2
[ "PROSITEDOC" ]
[ "PDOC51139" ]
[ "PROSITEDOC:PDOC51139" ]
1
[ "1q60", "2d99", "2d9b", "2dn4", "2dn5", "2dzq", "2dzr", "2e3l", "2ed2", "2eje", "8iuf", "8j9h", "8j9i", "8j9j" ]
14
[ "PUB00007426", "PUB00007427" ]
[ "9774679", "10198167" ]
[ "Identification of a novel slow-muscle-fiber enhancer binding protein, MusTRD1.", "Identification of a putative transcription factor gene (WBSCR11) that is commonly deleted in Williams-Beuren syndrome." ]
[ 1998, 1999 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "Myoviridae sp. ctX172", "ecological metagenomes" ]
[ 108, 1, 3459, 1, 3 ]
5
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 16, 30, 26, 32 ]
4
true
Repeat
GTF2I-like repeat
GTF2I-like repeat
GTF2I
2
IPR004213
4,213
Flt3 ligand
Flt3_lig
Family
467
false
false
The flt3 (fms-related tyrosine kinase 3) ligand is a short chain cytokine with a 4 helical bundle fold. It is a type I membrane protein which stimulates the proliferation of of early hematopoeitic cells, and synergises well with other colony stimulating factors and interleukins.
[ "GO:0005125", "GO:0016020" ]
[ "cytokine activity", "membrane" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF02947", "PTHR11032" ]
[ "Flt3_lig", "" ]
[ 461, 463 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-109704", "R-HSA-1257604", "R-HSA-2219530", "R-HSA-5673001", "R-HSA-6811558", "R-HSA-9607240", "R-HSA-9645135", "R-HSA-9706369", "R-HSA-9706374", "R-HSA-9706377", "R-MMU-109704", "R-MMU-1257604", "R-MMU-5673001", "R-MMU-6811558", "R-MMU-9607240", "R-MMU-9706369", "R-MMU-9706374...
[ "REACTOME:R-HSA-109704", "REACTOME:R-HSA-1257604", "REACTOME:R-HSA-2219530", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-6811558", "REACTOME:R-HSA-9607240", "REACTOME:R-HSA-9645135", "REACTOME:R-HSA-9706369", "REACTOME:R-HSA-9706374", "REACTOME:R-HSA-9706377", "REACTOME:R-MMU-109704", "REACTOME:...
17
[ "1ete", "3qs7", "3qs9", "7nbi", "7qdp", "7qwq", "7qwr", "7qws", "7zv9" ]
9
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 467 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 7, 10 ]
3
true
Family
Flt3 ligand
Flt3 ligand
Flt3_lig
4
IPR004214
4,214
Conotoxin
Conotoxin
Family
2,428
false
false
Cone snail toxins, conotoxins, are small neurotoxic peptides with disulphide connectivity that target ion-channels or G-protein coupled receptors. Based on the number and pattern of disulphide bonds and biological activities, conotoxins can be classified into several families [ ]. Omega, delta and kappa families of con...
[ "GO:0008200", "GO:0005576" ]
[ "ion channel inhibitor activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02950" ]
[ "Conotoxin" ]
[ 2428 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016617", "PUB00016622", "PUB00017021", "PUB00017022", "PUB00096619" ]
[ "11478951", "10988292", "2410412", "1390774", "26817840" ]
[ "Cone venom--from accidental stings to deliberate injection.", "lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus.", "Conus geographus toxins that discriminate between neuronal and muscle sodium chann...
[ 2001, 2000, 1985, 1992, 2016 ]
5
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 2425, 3 ]
2
[]
[]
0
true
Family
Conotoxin
Conotoxin
Conotoxin
4
IPR004215
4,215
Prokaryotic glutathione synthetase, N-terminal
GSHS_N
Domain
11,084
false
false
Prokaryotic glutathione synthetase (glutathione synthase) catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to orthophosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis. The enzyme is inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim. This d...
[ "GO:0004363", "GO:0006750" ]
[ "glutathione synthase activity", "glutathione biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02951" ]
[ "GSH-S_N" ]
[ 11084 ]
1
[ "EC", "METACYC" ]
[ "6.3.2.3", "PWY-8043" ]
[ "EC:6.3.2.3", "METACYC:PWY-8043" ]
2
[ "1glv", "1gsa", "1gsh", "2glt" ]
4
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10917, 24, 143 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Prokaryotic glutathione synthetase, N-terminal
Prokaryotic glutathione synthetase, N-terminal
GSHS_N
1
IPR004216
4,216
L-fucose/L-arabinose isomerase, C-terminal
Fuc/Ara_isomerase_C
Homologous_superfamily
11,125
false
false
L-fucose isomerase ( ) converts the aldose L-fucose into the corresponding ketose L-fuculose during the first step in fucose metabolism using Mn2+ as a cofactor. The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The...
[]
[]
[]
0
[ "SSF" ]
[ "SSF50443" ]
[ "" ]
[ 11125 ]
1
[ "EC" ]
[ "5.3.1.4" ]
[ "EC:5.3.1.4" ]
1
[ "1fui", "2ajt", "2hxg", "3a9r", "3a9s", "3a9t", "4c20", "4c21", "4c22", "4f2d", "4lql", "4r1o", "4r1p", "4r1q", "6k1f", "6k1g", "7ch3", "7chl", "7cwv", "7cx7", "7cxo", "7cyy" ]
22
[ "PUB00007428", "PUB00008241", "PUB00039308" ]
[ "9367760", "9084180", "16756997" ]
[ "Structure and mechanism of L-fucose isomerase from Escherichia coli.", "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression.", "Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production." ]
[ 1997, 1997, 2006 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 23, 10878, 24, 200 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Homologous_superfamily
L-fucose/L-arabinose isomerase, C-terminal
L-fucose/L-arabinose isomerase, C-terminal
Fuc/Ara_isomerase_C
3
IPR004217
4,217
Tim10-like
Tim10-like
Domain
17,698
false
false
This domain has four conserved cysteine residues. It is found in proteins Tim8, Tim9, Tim10 and Tim13, which are involved in mitochondrial protein import [ ] and seem to be localised to the mitochondrial intermembrane space. The Tim8-Tim13 complex has a complex architecture, similar to the Tim9-Tim10 complex, composed ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02953" ]
[ "zf-Tim10_DDP" ]
[ 17698 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1268020", "R-DDI-1268020", "R-DME-1268020", "R-GGA-1268020", "R-HSA-1268020", "R-HSA-9837999", "R-SCE-1268020", "R-SPO-1268020" ]
[ "REACTOME:R-BTA-1268020", "REACTOME:R-DDI-1268020", "REACTOME:R-DME-1268020", "REACTOME:R-GGA-1268020", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-9837999", "REACTOME:R-SCE-1268020", "REACTOME:R-SPO-1268020" ]
8
[ "2bsk", "3cjh", "3dxr", "6lo8", "7cgp", "7w5z", "8b6h", "8bqs", "8gym", "8gzu" ]
10
[ "PUB00007429", "PUB00039744", "PUB00051023" ]
[ "11101512", "16387659", "18706423" ]
[ "The role of the TIM8-13 complex in the import of Tim23 into mitochondria.", "Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller.", "The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23." ]
[ 2000, 2006, 2008 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 17698 ]
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...
[ 12, 5, 8, 12, 14, 15, 4, 20, 17, 5, 4, 28 ]
12
true
Domain
Tim10-like
Tim10-like
Tim10-like
4
IPR004218
4,218
Prokaryotic glutathione synthetase, ATP-binding
GSHS_ATP-bd
Domain
12,337
false
false
Prokaryotic glutathione synthetase (glutathione synthase) catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to orthophosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis. The enzyme is inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim. This i...
[ "GO:0004363", "GO:0005524", "GO:0006750" ]
[ "glutathione synthase activity", "ATP binding", "glutathione biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF02955" ]
[ "GSH-S_ATP" ]
[ 12337 ]
1
[ "EC", "METACYC" ]
[ "6.3.2.3", "PWY-8043" ]
[ "EC:6.3.2.3", "METACYC:PWY-8043" ]
2
[ "1glv", "1gsa", "1gsh", "2glt", "7m4s" ]
5
[]
[]
[]
[]
0
[ "IPR011761" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10, 12103, 54, 170 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Prokaryotic glutathione synthetase, ATP-binding
Prokaryotic glutathione synthetase, ATP-binding
GSHS_ATP-bd
3
IPR004219
4,219
TT viral protein of unknown function
TTvirus_Unk
Family
5,678
false
false
Torque teno virus, isolated initially from a Japanese patient with hepatitis of unknown aetiology, has since been found to infect both healthy and diseased individuals and numerous prevalence studies have raised questions about its role in unexplained hepatitis. ORF1 is a large 750 residue protein.
[]
[]
[]
0
[ "PFAM" ]
[ "PF02956" ]
[ "TT_ORF1" ]
[ 5678 ]
1
[]
[]
[]
0
[ "8cyg", "8v7x" ]
2
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Anaerotruncus colihominis", "Viruses" ]
[ 1, 5677 ]
2
[]
[]
0
true
Family
TT viral protein of unknown function
TT viral protein of unknown function
TTvirus_Unk
7
IPR004220
4,220
5-carboxymethyl-2-hydroxymuconate isomerase
5-COMe_2-OHmuconate_Isoase
Family
5,819
false
false
5-carboxymethyl-2-hydroxymuconate isomerase transforms 5-carboxymethyl-2-hydroxy-muconic acid into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid during the third step of the homoprotocatechuate catabolic pathway [ ]. Homoprotocatechuate (HPC; 3,4-dihydroxyphenylacetate) is catabolized to Krebs cycle intermediates via extra...
[ "GO:0008704", "GO:0009056" ]
[ "5-carboxymethyl-2-hydroxymuconate delta-isomerase activity", "catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02962", "PTHR37950", "cd00580" ]
[ "CHMI", "", "CHMI" ]
[ 5703, 5701, 4797 ]
3
[ "GP" ]
[ "GenProp0231" ]
[ "GP:GenProp0231" ]
1
[ "1otg", "3e6q", "4jcu", "4jj9", "4nwp", "4nwq", "6c9i", "6c9k", "6nht", "6nhv", "8vdz" ]
11
[ "PUB00001446", "PUB00035626", "PUB00043417" ]
[ "8223600", "2194841", "8384293" ]
[ "Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C.", "Purification, some properties and nucleotide sequence of 5-carboxymethyl-2-hydroxymuconate isomerase of Escherichia coli C.", "The Escherich...
[ 1993, 1990, 1993 ]
3
[]
[]
0
0
null
[ "Bacteria", "Sar", "unclassified sequences" ]
[ 5790, 2, 27 ]
3
[]
[]
0
true
Family
5-carboxymethyl-2-hydroxymuconate isomerase
5-carboxymethyl-2-hydroxymuconate isomerase
5-COMe_2-OHmuconate_Isoase
2
IPR004222
4,222
Methane monooxygenase, gamma chain
Me_mOase_g
Family
60
false
false
Methane monooxygenases ( ) catalyse the oxidation of methane to methanol in the presence of oxygen and NADH in methanotrophs. It has a broad specificity, hydroxylating many alkanes, and converting alkenes into the corresponding epoxides. In additional reactions, CO is oxidized to CO2, ammonia is oxidized to hydroxylami...
[ "GO:0015049", "GO:0015947" ]
[ "methane monooxygenase [NAD(P)H] activity", "methane metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF" ]
[ "PF02964", "PIRSF018503" ]
[ "MeMO_Hyd_G", "Me_mOase_g" ]
[ 60, 45 ]
2
[]
[]
[]
0
[ "1fyz", "1fz0", "1fz1", "1fz2", "1fz3", "1fz4", "1fz5", "1fz6", "1fz7", "1fz8", "1fz9", "1fzh", "1fzi", "1mhy", "1mhz", "1mmo", "1mty", "1xmf", "1xmg", "1xmh", "1xu3", "1xu5", "1xvb", "1xvc", "1xvd", "1xve", "1xvf", "1xvg", "4gam", "6d7k", "6vk4", "6vk5"...
50
[ "PUB00021642", "PUB00036067" ]
[ "11456616", "9329079" ]
[ "Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.", "Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating ...
[ 2001, 1997 ]
2
[]
[]
0
0
null
[ "Bacteria" ]
[ 60 ]
1
[]
[]
0
true
Family
Methane monooxygenase, gamma chain
Methane monooxygenase, gamma chain
Me_mOase_g
6
IPR004223
4,223
Vitamin B12-dependent methionine synthase, activation domain
VitB12-dep_Met_synth_activ_dom
Domain
21,135
false
false
Vitamin B12 dependent methionine synthase (5-methyltetrahydrofolate--homocysteine S-methyltransferase) catalyses the conversion of 5-methyltetrahydrofolate and L-homocysteine to tetrahydrofolate and L-methionine as the final step in de novo methionine biosynthesis. The enzyme requires methylcobalamin as a cofactor. In ...
[ "GO:0008705" ]
[ "methionine synthase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02965", "PS50974" ]
[ "Met_synt_B12", "ADOMET_ACTIVATION" ]
[ 20982, 20448 ]
2
[ "EC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.1.1.13", "PWY-2201", "PWY-3841", "PDOC50974", "R-CEL-156581", "R-CEL-1614635", "R-CEL-9013407", "R-CEL-9759218", "R-DDI-156581", "R-DDI-1614635", "R-DDI-9013407", "R-DDI-9759218", "R-HSA-156581", "R-HSA-1614635", "R-HSA-3359467", "R-HSA-3359469", "R-HSA-9013407", "R-HSA-9759218"...
[ "EC:2.1.1.13", "METACYC:PWY-2201", "METACYC:PWY-3841", "PROSITEDOC:PDOC50974", "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9013407", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-156581", "REACTOME:R-DDI-1614635", "REACTOME:R-DDI-9013407", "REACTOME:R-DDI-9759218", "REACTO...
26
[ "1k7y", "1k98", "1msk", "2o2k", "3bul", "3iv9", "3iva", "6bdy", "6bm5", "6bm6", "8g3h", "8ssc", "8ssd", "8sse", "9ssp", "9ssq", "9ssr", "9sss", "9sst", "9ssu", "9ssv" ]
21
[ "PUB00014004" ]
[ "11731805" ]
[ "Domain alternation switches B(12)-dependent methionine synthase to the activation conformation." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 41, 18230, 2392, 472 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 1, 9, 2, 5 ]
6
true
Domain
Vitamin B12-dependent methionine synthase, activation domain
Vitamin B12-dependent methionine synthase, activation domain
VitB12-dep_Met_synth_activ_dom
9
IPR004224
4,224
Fumarate reductase type B, transmembrane subunit
Fum_red_B_TM
Family
721
false
false
Quinol:fumarate reductase (QFR) couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinone oxidoreductase (SQR). QFR and SQR complexes are collectively referred to as succinate:quinone oxidoreductases and are pr...
[ "GO:0006099" ]
[ "tricarboxylic acid cycle" ]
[ "biological_process" ]
1
[ "NCBIFAM", "PIRSF", "CDD" ]
[ "NF010072", "PIRSF000177", "cd00581" ]
[ "PRK13553.1", "Fumar_rd_cyt_b", "QFR_TypeB_TM" ]
[ 561, 706, 493 ]
3
[]
[]
[]
0
[ "1e7p", "1qlb", "2bs2", "2bs3", "2bs4", "5xmj" ]
6
[ "PUB00007431", "PUB00015792" ]
[ "10586875", "9210286" ]
[ "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution.", "Succinate: quinone oxidoreductases. Variations on a conserved theme." ]
[ 1999, 1997 ]
2
[ "IPR000701" ]
[]
1
0
1
[ "Bacteria", "ecological metagenomes" ]
[ 710, 11 ]
2
[]
[]
0
true
Family
Fumarate reductase type B, transmembrane subunit
Fumarate reductase type B, transmembrane subunit
Fum_red_B_TM
9
IPR004226
4,226
Tubulin binding cofactor A
TBCA
Family
4,394
false
false
The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin p...
[ "GO:0048487", "GO:0007021", "GO:0007023" ]
[ "beta-tubulin binding", "tubulin complex assembly", "post-chaperonin tubulin folding pathway" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PANTHER" ]
[ "PF02970", "PTHR21500" ]
[ "TBCA", "" ]
[ 4378, 4217 ]
2
[ "REACTOME" ]
[ "R-HSA-389977" ]
[ "REACTOME:R-HSA-389977" ]
1
[ "1h7c", "1qsd", "3mxz", "4cqi" ]
4
[ "PUB00025558", "PUB00074025", "PUB00077898", "PUB00077901" ]
[ "12054808", "11739729", "23973072", "15321725" ]
[ "Three-dimensional structure of human tubulin chaperone cofactor A.", "Protection from free beta-tubulin by the beta-tubulin binding protein Rbl2p.", "Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.", "Model for the yeast cofactor A-beta-tubulin complex based...
[ 2002, 2002, 2013, 2004 ]
4
[]
[]
0
0
null
[ "Eukaryota", "viral metagenome" ]
[ 4391, 3 ]
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...
[ 3, 1, 1, 2, 7, 3, 1, 3, 6, 1, 1, 3 ]
12
true
Family
Tubulin binding cofactor A
Tubulin binding cofactor A
TBCA
8
IPR004227
4,227
Formiminotransferase catalytic domain
Formiminotransferase_cat
Domain
3,110
false
false
This entry represents the formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD), which forms a homodimer, with each protomer being comprised of two subdomains. Each subdomain has the structure consisting of an α/β sandwich with antiparallel β-sheet in the form (β-α-β)x2. Tetrahydrofolate (THF)-...
[ "GO:0005542", "GO:0016740" ]
[ "folic acid binding", "transferase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "NCBIFAM" ]
[ "TIGR02024" ]
[ "FtcD" ]
[ 3110 ]
1
[ "EC", "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.2.5", "4.3.1.4", "PWY-5030", "PWY-5497", "R-DDI-70921", "R-HSA-70921", "R-MMU-70921", "R-RNO-70921" ]
[ "EC:2.1.2.5", "EC:4.3.1.4", "METACYC:PWY-5030", "METACYC:PWY-5497", "REACTOME:R-DDI-70921", "REACTOME:R-HSA-70921", "REACTOME:R-MMU-70921", "REACTOME:R-RNO-70921" ]
8
[ "1qd1", "1tt9", "2pfd" ]
3
[ "PUB00007432", "PUB00015609" ]
[ "10673422", "12815595" ]
[ "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.", "The molecular basis of glutamate formiminotransferase deficiency." ]
[ 2000, 2003 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 37, 1677, 1310, 86 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 1, 2 ]
4
true
Domain
Formiminotransferase catalytic domain
Formiminotransferase catalytic domain
Formiminotransferase_cat
3
IPR004229
4,229
Methylamine dehydrogenase light chain
MeN_DH_Ltc
Family
135
false
false
This family consists of the light chain (small subunit) of methylamine dehydrogenase, a periplasmic enzyme. This subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group derived from Trp-114 and Trp-165 of the precursor, numbered according to the sequence from Paracoccus denitrificans [ , ]. The enzyme fo...
[ "GO:0052876", "GO:0030288" ]
[ "methylamine dehydrogenase (amicyanin) activity", "outer membrane-bounded periplasmic space" ]
[ "molecular_function", "cellular_component" ]
2
[ "NCBIFAM" ]
[ "TIGR02659" ]
[ "TTQ_MADH_Lt" ]
[ 135 ]
1
[ "EC", "GP", "METACYC" ]
[ "1.4.9.1", "GenProp0860", "PWY-6967" ]
[ "EC:1.4.9.1", "GP:GenProp0860", "METACYC:PWY-6967" ]
3
[ "1mae", "1maf", "1mda", "1mg2", "1mg3", "2bbk", "2gc4", "2gc7", "2j55", "2j56", "2j57", "2mad", "2mta", "3c75", "3l4m", "3l4o", "3orv", "3pxs", "3pxt", "3pxw", "3rlm", "3rmz", "3rn0", "3rn1", "3sjl", "3sle", "3svw", "3sws", "3sxt", "4fa1", "4fa4", "4fa5"...
42
[ "PUB00021028", "PUB00065256" ]
[ "15734739", "23487750" ]
[ "Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.", "Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis." ]
[ 2005, 2013 ]
2
[ "IPR016008" ]
[]
1
0
1
[ "Pseudomonadota", "marine sediment metagenome" ]
[ 134, 1 ]
2
[]
[]
0
true
Family
Methylamine dehydrogenase light chain
Methylamine dehydrogenase light chain
MeN_DH_Ltc
4
IPR004230
4,230
DNA mismatch repair protein MutH
DNA_mismatch_repair_MutH
Family
2,496
false
false
MutS, MutL and MutH are the three essential proteins for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH req...
[ "GO:0003677", "GO:0004519", "GO:0006304" ]
[ "DNA binding", "endonuclease activity", "DNA modification" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_00759", "TIGR02248" ]
[ "MutH", "mutH_TIGR" ]
[ 2494, 2453 ]
2
[ "GP" ]
[ "GenProp0225" ]
[ "GP:GenProp0225" ]
1
[ "1azo", "2aoq", "2aor", "2azo" ]
4
[ "PUB00007435" ]
[ "9482749" ]
[ "Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Bacteria", "Beauveria bassiana D1-5", "ecological metagenomes" ]
[ 2486, 1, 9 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
DNA mismatch repair protein MutH
DNA mismatch repair protein MutH
DNA_mismatch_repair_MutH
1
IPR004231
4,231
Carboxypeptidase A inhibitor-like
COpept_A_inh-like
Domain
180
false
false
In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well-characterised metallocarboxypeptidase A inhibitor (MCPI) from potatoes, which belongs to the MEROPS inhibitor family I37, clan IE. It inhibits metallopeptidases belonging to MEROPS peptidase family M14...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02977" ]
[ "CarbpepA_inh" ]
[ 180 ]
1
[]
[]
[]
0
[ "1h20", "2hlg", "4cpa", "6jic", "7eqz", "8sdm", "8sdp", "8se7", "8se8" ]
9
[ "PUB00063032" ]
[ "1715974" ]
[ "Regulation of metallocarboxypeptidase inhibitor gene expression in tomato." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Solanaceae" ]
[ 180 ]
1
[]
[]
0
true
Domain
Carboxypeptidase A inhibitor-like
Carboxypeptidase A inhibitor-like
COpept_A_inh-like
2
IPR004232
4,232
Nitrile hydratase alpha/Thiocyanate hydrolase gamma
CN_Hdrtase_a/SCN_Hdrlase_g
Domain
3,476
false
false
Nitrile hydratases ( ) are bacterial enzymes that catalyse the hydration of nitrile compounds to the corresponding amides. They are used as biocatalysts in acrylamide production, one of the few commercial scale bioprocesses, as well as in environmental remediation for the removal of nitriles from waste streams. Nitrile...
[ "GO:0003824", "GO:0046914" ]
[ "catalytic activity", "transition metal ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF02979" ]
[ "NHase_alpha" ]
[ 3476 ]
1
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "4.2.1.84", "PWY-5025", "PWY-581", "PWY-7308" ]
[ "EC:4.2.1.84", "METACYC:PWY-5025", "METACYC:PWY-581", "METACYC:PWY-7308" ]
4
[ "1ahj", "1ire", "1ugp", "1ugq", "1ugr", "1ugs", "1v29", "2ahj", "2cyz", "2cz0", "2cz1", "2cz6", "2cz7", "2d0q", "2dd4", "2dd5", "2dpp", "2dxb", "2dxc", "2qdy", "2zcf", "2zpb", "2zpe", "2zpf", "2zpg", "2zph", "2zpi", "2zzd", "3a8g", "3a8h", "3a8l", "3a8m"...
74
[ "PUB00006378", "PUB00019922", "PUB00031767", "PUB00035663", "PUB00044782", "PUB00044783" ]
[ "9195885", "9586994", "14717710", "17267045", "16417356", "9573140" ]
[ "Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold.", "Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms.", "Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding.", "Influence of cobalt subst...
[ 1997, 1998, 2004, 2007, 2006, 1998 ]
6
[]
[ "IPR022513" ]
0
1
0
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "unclassified sequences" ]
[ 3277, 135, 21, 43 ]
4
[]
[]
0
true
Domain
Nitrile hydratase alpha/Thiocyanate hydrolase gamma
Nitrile hydratase alpha/Thiocyanate hydrolase gamma
CN_Hdrtase_a/SCN_Hdrlase_g
1
IPR004233
4,233
FokI, recognition domain, subdomain 2
FokI_D2
Domain
87
false
false
Type IIS restriction endonuclease FokI ( ) is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [ , ]. FokI contains amino- an...
[ "GO:0003677", "GO:0009307" ]
[ "DNA binding", "DNA restriction-modification system" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02980" ]
[ "FokI_dom_2" ]
[ 87 ]
1
[]
[]
[]
0
[ "1fok", "2fok" ]
2
[ "PUB00007438", "PUB00010506", "PUB00019577" ]
[ "9214510", "12093751", "9724743" ]
[ "Structure of the multimodular endonuclease FokI bound to DNA.", "Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I.", "Structure of FokI has implications for DNA cleavage." ]
[ 1997, 2002, 1998 ]
3
[]
[]
0
0
null
[ "Bacteria" ]
[ 87 ]
1
[]
[]
0
true
Domain
FokI, recognition domain, subdomain 2
FokI, recognition domain, subdomain 2
FokI_D2
6
IPR004234
4,234
FokI, recognition domain, subdomain 1
FokI_D1
Domain
88
false
false
Type IIS restriction endonuclease FokI ( ) is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [ , ]. FokI contains amino- an...
[ "GO:0003677", "GO:0009307" ]
[ "DNA binding", "DNA restriction-modification system" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02981" ]
[ "FokI_D1" ]
[ 88 ]
1
[]
[]
[]
0
[ "1fok", "2fok" ]
2
[ "PUB00007438", "PUB00010506", "PUB00019577" ]
[ "9214510", "12093751", "9724743" ]
[ "Structure of the multimodular endonuclease FokI bound to DNA.", "Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I.", "Structure of FokI has implications for DNA cleavage." ]
[ 1997, 2002, 1998 ]
3
[]
[]
0
0
null
[ "Bacteria" ]
[ 88 ]
1
[]
[]
0
true
Domain
FokI, recognition domain, subdomain 1
FokI, recognition domain, subdomain 1
FokI_D1
2
IPR004235
4,235
Scytalone dehydratase
Scytalone_dehydratase
Family
936
false
false
This entry represents Scytalone dehydratase (SDH) and similar proteins mainly found in the fungi Accomycota. SDH is a member of the group of enzymes involved in fungal melanin biosynthesis [ , ]. It was first identified in a phytopathogenic fungus, Magnaporthe grisea (Rice blast fungus), which causes rice blast disease...
[ "GO:0030411", "GO:0006582" ]
[ "scytalone dehydratase activity", "melanin metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF" ]
[ "PIRSF024851" ]
[ "SCD1" ]
[ 936 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "4.2.1.-", "PWY-2229", "PWY-2467", "PWY-5061", "PWY-5367", "PWY-5408", "PWY-5409", "PWY-5410", "PWY-5644", "PWY-5780", "PWY-5793", "PWY-5979", "PWY-6322", "PWY-6602", "PWY-6627", "PWY-6672", "PWY-6679", "PWY-6721", "PWY-6749", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948...
[ "EC:4.2.1.-", "METACYC:PWY-2229", "METACYC:PWY-2467", "METACYC:PWY-5061", "METACYC:PWY-5367", "METACYC:PWY-5408", "METACYC:PWY-5409", "METACYC:PWY-5410", "METACYC:PWY-5644", "METACYC:PWY-5780", "METACYC:PWY-5793", "METACYC:PWY-5979", "METACYC:PWY-6322", "METACYC:PWY-6602", "METACYC:PWY-6...
53
[ "1idp", "1std", "2std", "3std", "4std", "5std", "6std", "7std" ]
8
[ "PUB00007439", "PUB00016790", "PUB00020316", "PUB00022713", "PUB00099644", "PUB00099645" ]
[ "9922139", "14716498", "9665698", "7866745", "31116900", "33255939" ]
[ "Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site.", "Cloning, functional analysis and expression of a scytalone dehydratase gene ( SCD1) involved in melanin biosynthesis of the phytopathogenic fungus Bipolaris oryzae.", "Cryogenic X-ray...
[ 1998, 2004, 1998, 1994, 2019, 2020 ]
6
[]
[]
0
0
null
[ "Eukaryota" ]
[ 936 ]
1
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Scytalone dehydratase
Scytalone dehydratase
Scytalone_dehydratase
1
IPR004237
4,237
Fibronectin binding repeat
Fibron_repeat-bd
Repeat
646
false
false
The ability of bacteria to bind fibronectin is thought to enable the colonisation of wound tissue and blood clots. The fibronectin binding repeat is found in bacterial fibronectin binding proteins and serum opacity factor. Each fibronectin binding repeat is an array of short motifs that bind to fibronectin type I domai...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02986" ]
[ "Fn_bind" ]
[ 646 ]
1
[]
[]
[]
0
[ "1o9a", "3zrz" ]
2
[ "PUB00029354", "PUB00044984" ]
[ "12736686", "15247227" ]
[ "Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper.", "High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules." ]
[ 2003, 2004 ]
2
[]
[]
0
0
null
[ "Bacillati" ]
[ 646 ]
1
[]
[]
0
true
Repeat
Fibronectin binding repeat
Fibronectin binding repeat
Fibron_repeat-bd
9
IPR004238
4,238
Late embryogenesis abundant protein ECP63-like domain
ECP63-like_dom
Domain
520
false
false
This entry represents a domain found in Late embryogenesis abundant protein ECP63 from Arabidopsis thaliana and similar plant proteins. ECP63, a member of the LEA family, is though to be involved in the BHLH109-mediated regulation of somatic embryogenesis [ ]. LEA (late embryogenesis abundant) proteins were first ident...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02987" ]
[ "LEA_4" ]
[ 520 ]
1
[]
[]
[]
0
[]
0
[ "PUB00009713", "PUB00019786", "PUB00055586", "PUB00083904", "PUB00088595", "PUB00088596", "PUB00096344" ]
[ "10681550", "7630968", "9218720", "25809152", "18318901", "21034219", "26973252" ]
[ "Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit.", "Sequence and regulation of a late embryogenesis abundant group 3 protein of maize.", "A group 3 LEA cDNA of rice, responsive to abscisic acid, but not to jasmonic acid, shows variety-specific differences...
[ 2000, 1995, 1997, 2015, 2008, 2011, 2016 ]
7
[]
[]
0
0
null
[ "Exercitatus varius", "Spermatophyta" ]
[ 2, 518 ]
2
[ "Arabidopsis thaliana" ]
[ 14 ]
1
true
Domain
Late embryogenesis abundant protein ECP63-like domain
Late embryogenesis abundant protein ECP63-like domain
ECP63-like_dom
3
IPR004239
4,239
Protein of unknown function DUF228
DUF228
Family
431
false
false
This group comprises proteins of unknown function from Borrelia burgdorferi, the causitive organism of Lyme disease.
[]
[]
[]
0
[ "PFAM" ]
[ "PF02989" ]
[ "DUF228" ]
[ 431 ]
1
[]
[]
[]
0
[ "8phq", "8phr", "8phs", "8phu", "8pkh", "8qo0", "8qo1" ]
7
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Borreliaceae" ]
[ 431 ]
1
[]
[]
0
true
Family
Protein of unknown function DUF228
Protein of unknown function DUF228
DUF228
3
IPR004240
4,240
Nonaspanin (TM9SF)
EMP70
Family
23,853
false
false
The transmembrane 9 superfamily protein (TM9SF) may function as a channel or small molecule transporter. Proteins in this group are endosomal integral membrane proteins.
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02990", "PTHR10766" ]
[ "EMP70", "" ]
[ 23766, 23507 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota", "Pectobacterium polaris" ]
[ 23852, 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...
[ 51, 8, 9, 3, 32, 23, 2, 63, 22, 3, 1, 128 ]
12
true
Family
Nonaspanin (TM9SF)
Nonaspanin (TM9SF)
EMP70
9
IPR004241
4,241
Autophagy protein Atg8 ubiquitin-like
Atg8-like
Family
14,423
false
false
A number of autophagy-related proteins have been identified in yeast, including the key autophagic protein Atg8, which is a ubiquitin-like protein with a structure consisting of two amino-terminal α-helices and a ubiquitin-like core [ , ]. Many other eukaryotes contain multiple Atg8 orthologues. Atg8 genes of multicell...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02991", "PTHR10969" ]
[ "ATG8", "" ]
[ 14410, 13930 ]
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-1632852", "R-BTA-5205685", "R-BTA-8854214", "R-BTA-8934903", "R-BTA-9664873", "R-BTA-9755511", "R-CEL-1632852", "R-CEL-5205685", "R-CEL-8934903", "R-CEL-9755511", "R-DDI-1632852", "R-DDI-5205685", "R-DDI-8854214", "R-DDI-8934903", "R-DDI-9664873", "R-DDI-9755511", "R-HSA-16328...
[ "REACTOME:R-BTA-1632852", "REACTOME:R-BTA-5205685", "REACTOME:R-BTA-8854214", "REACTOME:R-BTA-8934903", "REACTOME:R-BTA-9664873", "REACTOME:R-BTA-9755511", "REACTOME:R-CEL-1632852", "REACTOME:R-CEL-5205685", "REACTOME:R-CEL-8934903", "REACTOME:R-CEL-9755511", "REACTOME:R-DDI-1632852", "REACTOM...
45
[ "1eo6", "1gnu", "1kjt", "1klv", "1km7", "1kot", "1ugm", "1v49", "2k6q", "2kq7", "2kwc", "2l8j", "2li5", "2lue", "2n9x", "2ncn", "2r2q", "2z0d", "2z0e", "2zjd", "2zpn", "2zzp", "3d32", "3dow", "3eci", "3h9d", "3m95", "3rui", "3vh3", "3vh4", "3vtu", "3vtv"...
174
[ "PUB00007445", "PUB00031766", "PUB00066985", "PUB00066992", "PUB00066993" ]
[ "7908909", "15265004", "21867568", "18508918", "20562859" ]
[ "Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B.", "The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8.", "Atg8: an autophagy-related ubiquitin-like protein family.", "Atg8 controls phagop...
[ 1994, 2004, 2011, 2008, 2010 ]
5
[]
[ "IPR027731" ]
0
1
0
[ "Eukaryota", "Symploca sp. SIO1C4", "Viruses", "metagenomes" ]
[ 14301, 1, 37, 84 ]
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...
[ 27, 3, 11, 5, 22, 10, 1, 9, 29, 1, 1, 20 ]
12
true
Family
Autophagy protein Atg8 ubiquitin-like
Autophagy protein Atg8 ubiquitin-like
Atg8-like
1
IPR004242
4,242
Transposon, En/Spm-like
Transposase_21
Family
15,404
false
false
This family includes a En/Spm-like transposable element, Tdc1 from carrot [ ]. The function of these proteins is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF02992" ]
[ "Transposase_21" ]
[ 15404 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007446" ]
[ "9180694" ]
[ "Somatic variation during long-term subculturing of plant cells caused by insertion of a transposable element in a phenylalanine ammonia-lyase (PAL) gene." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "invertebrate metagenome" ]
[ 8, 15395, 1 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 41, 640, 10 ]
3
true
Family
Transposon, En/Spm-like
Transposon, En/Spm-like
Transposase_21
5
IPR004243
4,243
Minor capsid protein VI
McpVI
Family
472
false
false
Protein VI is a structural protein of the adenoviral capsid. It shuttles between the nucleus and the cytoplasm and links hexon to the nuclear import machinery via an importin alpha/beta-dependent mechanism [ ]. It also mediates adenovirus endosome penetration during cell entry [ , ].
[ "GO:0039664", "GO:0019028" ]
[ "lysis of host organelle involved in viral entry into host cell", "viral capsid" ]
[ "biological_process", "cellular_component" ]
2
[ "HAMAP", "PFAM" ]
[ "MF_04048", "PF02993" ]
[ "ADV_CAP6", "MCPVI" ]
[ 340, 472 ]
2
[]
[]
[]
0
[ "6b1t", "6yba", "6z7n", "7rd1", "7s78", "7tau", "9lr9" ]
7
[ "PUB00087146", "PUB00087147", "PUB00087149" ]
[ "14633984", "22516138", "2040956" ]
[ "Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals.", "Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis.", "Excystation of Giardia muris induced by a phosphate-bicarbonate medium: localizatio...
[ 2003, 2012, 1991 ]
3
[]
[]
0
0
null
[ "Adenoviridae", "Mycobacterium simiae" ]
[ 471, 1 ]
2
[]
[]
0
true
Family
Minor capsid protein VI
Minor capsid protein VI
McpVI
7
IPR004244
4,244
Transposase, L1
Transposase_22
Family
16,631
false
false
Many human L1 elements are capable of retrotransposition. Some of these have been shown to exhibit reverse transcriptase (RT) activity [ ]. This entry includes L1RE1 and L1TD1 from human. L1RE1 is essential for retrotransposition of LINE-1 elements in the genome. It functions as a nucleic acid chaperone binding its own...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11505" ]
[ "" ]
[ 16631 ]
1
[]
[]
[]
0
[ "2jrb", "2ldy", "2lr6", "2w7a", "2yko", "2ykp", "2ykq", "3soo", "6fia" ]
9
[ "PUB00007448", "PUB00153048", "PUB00153049", "PUB00153050", "PUB00153051", "PUB00153052" ]
[ "9140393", "21559406", "21937507", "22162396", "28806172", "30122351" ]
[ "Many human L1 elements are capable of retrotransposition.", "L1TD1 is a marker for undifferentiated human embryonic stem cells.", "Polymerization and nucleic acid-binding properties of human L1 ORF1 protein.", "RNA-binding protein L1TD1 interacts with LIN28 via RNA and is required for human embryonic stem ce...
[ 1997, 2011, 2012, 2012, 2017, 2018 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "invertebrate metagenome" ]
[ 17, 16613, 1 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 25, 16, 104 ]
4
true
Family
Transposase, L1
Transposase, L1
Transposase_22
2
IPR004245
4,245
Protein of unknown function DUF229
DUF229
Family
6,979
false
false
Members of this family are uncharacterised with a long conserved region that may contain several domains.
[]
[]
[]
0
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02995", "PTHR10974", "cd16021" ]
[ "DUF229", "", "ALP_like" ]
[ 6873, 6835, 4363 ]
3
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota" ]
[ 6979 ]
1
[ "Caenorhabditis elegans", "Drosophila melanogaster" ]
[ 17, 36 ]
2
true
Family
Protein of unknown function DUF229
Protein of unknown function DUF229
DUF229
4
IPR004247
4,247
Lentiviral Vpr-like protein
Lentiviral_Vpr-like
Family
82
false
false
This family consists of Vpr-like accessory proteins from maedi-visna and caprine/ovine lentivirus. This small open reading frame (ORF) in maedi-visna virus (MVV) and caprine arthritis encephalitis virus (CAEV) was initially named "tat" by analogy with a similarly placed ORF in the primate lentiviruses [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02998" ]
[ "Lentiviral_Tat" ]
[ 82 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007449", "PUB00076653" ]
[ "2536163", "12915575" ]
[ "Characterization of a cDNA clone encoding the visna virus transactivating protein.", "Maedi-visna virus and caprine arthritis encephalitis virus genomes encode a Vpr-like but no Tat protein." ]
[ 1989, 2003 ]
2
[]
[]
0
0
null
[ "Lentivirus" ]
[ 82 ]
1
[]
[]
0
true
Family
Lentiviral Vpr-like protein
Lentiviral Vpr-like protein
Lentiviral_Vpr-like
4
IPR004248
4,248
Borrelia plasmid, OrfD
Borrelia_plasmid_OrfD
Family
239
false
false
Borrelia burgdorferi supercoiled plasmids encode multicopy tandem open reading frames called OrfA, OrfB, OrfC and OrfD. This entry represents the protein encoded by OrfD, known as Outer membrane lipoprotein BBA14, which could act as a component of a potential toxin-antitoxin system in this organism and serve as a plasm...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02999" ]
[ "Borrelia_orfD" ]
[ 239 ]
1
[]
[]
[]
0
[ "7qdv", "7zjc" ]
2
[ "PUB00007450", "PUB00100746" ]
[ "8655511", "35215098" ]
[ "Borrelia burgdorferi supercoiled plasmids encode multicopy tandem open reading frames and a lipoprotein gene family.", "Structural Analysis of the Outer Membrane Lipoprotein BBA14 (OrfD) and the Corresponding Paralogous Gene Family 143 (PFam143) from <i>Borrelia burgdorferi</i>." ]
[ 1996, 2022 ]
2
[]
[]
0
0
null
[ "Borreliaceae" ]
[ 239 ]
1
[]
[]
0
true
Family
Borrelia plasmid, OrfD
Borrelia plasmid, OrfD
Borrelia_plasmid_OrfD
2
IPR004250
4,250
Somatostatin
Somatostatin
Family
1,908
false
false
Somatostatin (SST) also known as somatotropin release-inhibiting factor (SRIF), is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Somatostatin, acting through the 5 somatostatin receptors, it has been found to regulate the secretion of various hormones such as pituitary gro...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PIRSF", "PANTHER" ]
[ "PIRSF001814", "PTHR10558" ]
[ "Somatostatin", "" ]
[ 1540, 1876 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-375276", "R-CFA-418594", "R-GGA-375276", "R-GGA-418594", "R-HSA-375276", "R-HSA-418594", "R-HSA-9022702", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594", "R-SSC-375276", "R-SSC-418594" ]
[ "REACTOME:R-CFA-375276", "REACTOME:R-CFA-418594", "REACTOME:R-GGA-375276", "REACTOME:R-GGA-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-9022702", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594", "REACTOME:R-SSC-37...
13
[]
0
[ "PUB00013316", "PUB00063571", "PUB00063573", "PUB00063574", "PUB00063590", "PUB00063609", "PUB00063610", "PUB00063615", "PUB00063616", "PUB00063617" ]
[ "14507421", "4879544", "15056499", "15533778", "7792934", "12511609", "10614629", "210185", "12354575", "11897621" ]
[ "Somatostatin receptors.", "Stimulatory and inhibitory effects of purified hypothalamic extracts on growth hormone release from rat pituitary in vitro.", "Somatostatin analogues: multiple roles in cellular proliferation, neoplasia, and angiogenesis.", "Clinical endocrinology and metabolism. The somatostatin n...
[ 2003, 1968, 2004, 2004, 1995, 2003, 2000, 1978, 2002, 2002 ]
10
[]
[]
0
0
null
[ "Vertebrata" ]
[ 1908 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 4, 3, 4 ]
4
true
Family
Somatostatin
Somatostatin
Somatostatin
8
IPR004251
4,251
Pox virus entry-fusion-complex G9/A16
Pox_virus_G9/A16
Family
531
false
false
This family includes two of the eight entry-fusion complex proteins of pox viruses. The viral fusion proteins are components of the mature virion, MV, membrane. Extracellular enveloped virions (EVs), the infecting particles, are MVs with an additional membrane that is opened or removed prior to the fusion of the MV and...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03003" ]
[ "Pox_G9-A16" ]
[ 531 ]
1
[]
[]
[]
0
[ "8gp6", "8wt5", "9hbk", "9hls", "9hng", "9hpa", "9r09", "9r0b", "9r0j", "9rdh" ]
10
[ "PUB00078710" ]
[ "18353946" ]
[ "Vaccinia virus A56/K2 fusion regulatory protein interacts with the A16 and G9 subunits of the entry fusion complex." ]
[ 2008 ]
1
[]
[]
0
0
null
[ "Nucleocytoviricota", "seawater metagenome" ]
[ 530, 1 ]
2
[]
[]
0
true
Family
Pox virus entry-fusion-complex G9/A16
Pox virus entry-fusion-complex G9/A16
Pox_virus_G9/A16
7
IPR004252
4,252
Probable transposase, Ptta/En/Spm, plant
Probable_transposase_24
Family
21,026
false
false
Transposase proteins are necessary for efficient DNA transposition. This family includes various probable plant transposases from the Ptta and En/Spm families [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03004" ]
[ "Transposase_24" ]
[ 21026 ]
1
[]
[]
[]
0
[]
0
[ "PUB00034639", "PUB00066989" ]
[ "16297077", "15957213" ]
[ "Efficient insertional mutagenesis in rice using the maize En/Spm elements.", "Molecular analysis of the En/Spm transposable element system of Zea mays." ]
[ 2005, 1986 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 21026 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 158, 141, 145 ]
3
true
Family
Probable transposase, Ptta/En/Spm, plant
Probable transposase, Ptta/En/Spm, plant
Probable_transposase_24
5
IPR004254
4,254
AdipoR/Haemolysin-III-related
AdipoR/HlyIII-related
Family
43,806
false
false
Members of this family are integral membrane proteins. This family includes a protein with hemolytic activity from Bacillus cereus [ ]. YOL002c (AdipoR-like receptor IZH2) from Saccharomyces cerevisiae encodes a protein that plays a key role in metabolic pathways that regulate lipid and phosphate metabolism [ , ]. In e...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF03006", "PTHR20855" ]
[ "HlyIII", "" ]
[ 43388, 42781 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-163680", "R-HSA-5675221", "R-MMU-163680", "R-MMU-5675221" ]
[ "REACTOME:R-HSA-163680", "REACTOME:R-HSA-5675221", "REACTOME:R-MMU-163680", "REACTOME:R-MMU-5675221" ]
4
[ "5lwy", "5lx9", "5lxa", "5lxg", "6krz", "6ks0", "6ks1", "6yx9", "6yxd", "6yxf", "6yxg" ]
11
[ "PUB00019707", "PUB00019708", "PUB00071573", "PUB00071574", "PUB00071575" ]
[ "7495855", "11916977", "16044242", "17082257", "15664187" ]
[ "Cloning and primary structure of a new hemolysin gene from Bacillus cereus.", "Multiple regulatory roles of a novel Saccharomyces cerevisiae protein, encoded by YOL002c, in lipid and phosphate metabolism.", "PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif.", "...
[ 1995, 2002, 2005, 2007, 2005 ]
5
[]
[ "IPR005744" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 8, 18235, 25223, 3, 337 ]
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",...
[ 27, 9, 60, 14, 1, 33, 30, 2, 16, 39, 4, 2, 28 ]
13
true
Family
AdipoR/Haemolysin-III-related
AdipoR/Haemolysin-III-related
AdipoR/HlyIII-related
3
IPR004255
4,255
O-acyltransferase, WSD1-like, N-terminal
O-acyltransferase_WSD1_N
Domain
18,205
false
false
This entry represents the N-terminal catalytic domain of a number of wax ester synthase/diacylglycerol acyltransferases (WS/DGATs), predominantly from bacteria and plants. They catalyse the condensation of a fatty alcohol and a fatty acyl-Coenzyme A (acyl-CoA) and they can also catalyse the transesterification of acyl-...
[ "GO:0004144", "GO:0045017" ]
[ "diacylglycerol O-acyltransferase activity", "glycerolipid biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03007" ]
[ "WS_DGAT_cat" ]
[ 18205 ]
1
[ "EC" ]
[ "2.3.1.20" ]
[ "EC:2.3.1.20" ]
1
[ "6chj", "7nxg" ]
2
[ "PUB00053680", "PUB00100087" ]
[ "18621978", "31559109" ]
[ "Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis.", "Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters." ]
[ 2008, 2018 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteria", "metagenomes" ]
[ 12363, 5711, 8, 123 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 61, 12, 6 ]
3
true
Domain
O-acyltransferase, WSD1-like, N-terminal
O-acyltransferase, WSD1-like, N-terminal
O-acyltransferase_WSD1_N
8
IPR004256
4,256
Domain of unknown function DUF234
DUF234
Domain
4,303
false
false
This entry represents a domain of unknown function found in bacterial and archaeal sequences. In some instances it is fused to a prokaryotic putative DEXX-box ATPase domain, found at its C-terminal ( ) [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03008" ]
[ "DUF234" ]
[ 4303 ]
1
[]
[]
[]
0
[]
0
[ "PUB00016655" ]
[ "9045616" ]
[ "Evidence for a family of archaeal ATPases." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 1009, 3189, 105 ]
3
[]
[]
0
true
Domain
Domain of unknown function DUF234
Domain of unknown function DUF234
DUF234
9
IPR004257
4,257
Equine arteritis virus (EAV), glycoprotein 4
Equine_arteritis_virus_Gp4
Family
123
false
false
This family contains a predicted structural envelope protein Gp4 from Equine arteritis virus (EAV).
[]
[]
[]
0
[ "PFAM" ]
[ "PF03010" ]
[ "GP4" ]
[ 123 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Equine arteritis virus" ]
[ 123 ]
1
[]
[]
0
true
Family
Equine arteritis virus (EAV), glycoprotein 4
Equine arteritis virus (EAV), glycoprotein 4
Equine_arteritis_virus_Gp4
5
IPR004258
4,258
Duffy-binding-like domain
DBL
Domain
2,515
false
false
Plasmodium Duffy Binding-Like (DBL) domains mediate diverse receptor-ligand interactions critical for invasion, cytoadherence, sequestration and the pathogenesis of malaria [ ]. Members of the erythrocyte binding-like (EBL) superfamily contain one or two extracellular cysteine-rich DBL domains.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03011" ]
[ "PFEMP" ]
[ 2515 ]
1
[]
[]
[]
0
[ "2yk0", "3c64", "3cml", "3cpz", "4p1t", "4v3d", "4v3e", "5lgd", "5x6n", "7fap", "7fas", "7jgg", "7jgh", "7y0j", "8c3y", "8c44", "8vdf", "8vdg", "8vdl", "9bhb", "9naq" ]
21
[ "PUB00059017" ]
[ "21743458" ]
[ "Dimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARC." ]
[ 2011 ]
1
[]
[]
0
0
null
[ "Massilia haematophila", "Plasmodium" ]
[ 1, 2514 ]
2
[]
[]
0
true
Domain
Duffy-binding-like domain
Duffy-binding-like domain
DBL
3
IPR004259
4,259
Phosphoprotein M1-like
PP_M1-like
Family
1,911
false
false
This family includes the M1 phosphoprotein non-structural RNA polymerase alpha subunit ( ) from various strains of Rabies virus [ ]. The M1 phosphoprotein is thought to be a component of the active polymerase, and may be involved in template binding.
[ "GO:0003968", "GO:0019083" ]
[ "RNA-directed RNA polymerase activity", "viral transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03012" ]
[ "PP_M1" ]
[ 1911 ]
1
[]
[]
[]
0
[ "1vyi", "2wzl", "3l32", "3oa1", "6ueb", "7c20", "7c21", "7t5g", "7t5h", "8b8v", "8fuq", "8fwl", "8u0a", "8u0b" ]
14
[ "PUB00007455" ]
[ "2148206" ]
[ "Nucleotide and deduced amino acid sequences of the nominal nonstructural phosphoprotein of the ERA, PM and CVS-11 strains of rabies virus." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Alpharhabdovirinae", "Glomus cerebriforme" ]
[ 1910, 1 ]
2
[]
[]
0
true
Family
Phosphoprotein M1-like
Phosphoprotein M1-like
PP_M1-like
6
IPR004260
4,260
Pyrimidine dimer DNA glycosylase
Pyr-dimer_DNA_glycosylase
Family
4,083
false
false
Pyrimidine dimer DNA glycosylases are enzymes responsible for initiating the base excision repair pathway, excising pyrimidine dimers by hydrolysis of the glycosylic bond of the 5' pyrimidine, followed by the intra-pyrimidine phosphodiester bond [ ]. One such enzyme is T4 endonuclease V, an enzyme responsible for the f...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF03013", "PIRSF001000" ]
[ "Pyr_excise", "PDG_ENDV" ]
[ 4083, 476 ]
2
[]
[]
[]
0
[ "1eni", "1enj", "1enk", "1vas", "2end", "2fcc" ]
6
[ "PUB00007456", "PUB00015082" ]
[ "2067549", "11148051" ]
[ "Site-directed deletion mutagenesis within the T4 endonuclease V gene: dispensable sequences within putative loop regions.", "The reaction mechanism of DNA glycosylase/AP lyases at abasic sites." ]
[ 1991, 2001 ]
2
[]
[ "IPR012650", "IPR021143" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 180, 3350, 55, 457, 41 ]
5
[]
[]
0
true
Family
Pyrimidine dimer DNA glycosylase
Pyrimidine dimer DNA glycosylase
Pyr-dimer_DNA_glycosylase
1
IPR004261
4,261
Hepatitis E virus structural protein 2, N-terminal domain
SP2_N
Domain
8,284
false
false
This entry represents the N-terminal domain of structural protein 2 of the hepatitis E virus. The high basic amino acid content of this protein has lead to the suggestion of a role in viral genomic RNA encapsidation. The Hepatitis E virus (HEV) structural protein 2 (also known as ORF2) is a major viral capsid protein t...
[ "GO:0003723", "GO:0005198" ]
[ "RNA binding", "structural molecule activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF03014" ]
[ "SP2" ]
[ 8284 ]
1
[]
[]
[]
0
[ "2ztn", "2zzq", "3hag", "3iyo", "6lat", "6lb0", "9fns", "9fnt", "9fq3" ]
9
[ "PUB00090971", "PUB00090972" ]
[ "14671114", "29669922" ]
[ "The ORF2 protein of hepatitis E virus binds the 5' region of viral RNA.", "Origin, antigenicity, and function of a secreted form of ORF2 in hepatitis E virus infection." ]
[ 2004, 2018 ]
2
[]
[]
0
0
null
[ "Viruses" ]
[ 8284 ]
1
[]
[]
0
true
Domain
Hepatitis E virus structural protein 2, N-terminal domain
Hepatitis E virus structural protein 2, N-terminal domain
SP2_N
6
IPR004263
4,263
Exostosin-like
Exostosin
Family
34,854
false
false
There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors [ ]. They are glycosyltransferases required for the biosynthesis of heparan sulfate. Hereditary multiple exostoses (EXT) is an autosomal dominant d...
[ "GO:0016757", "GO:0009101" ]
[ "glycosyltransferase activity", "glycoprotein biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "PANTHER" ]
[ "PTHR11062", "PTHR48261" ]
[ "", "" ]
[ 25829, 9025 ]
2
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1595", "R-BTA-2022928", "R-CEL-2022928", "R-DME-2022928", "R-DRE-2022928", "R-HSA-2022928", "R-HSA-3656237", "R-HSA-3656253", "R-HSA-381038", "R-MMU-2022928" ]
[ "GP:GenProp1595", "REACTOME:R-BTA-2022928", "REACTOME:R-CEL-2022928", "REACTOME:R-DME-2022928", "REACTOME:R-DRE-2022928", "REACTOME:R-HSA-2022928", "REACTOME:R-HSA-3656237", "REACTOME:R-HSA-3656253", "REACTOME:R-HSA-381038", "REACTOME:R-MMU-2022928" ]
10
[ "7au2", "7aua", "7sch", "7scj", "7sck", "7uqx", "7uqy", "7zay", "8og1", "8og4" ]
10
[ "PUB00007458", "PUB00007459", "PUB00066948", "PUB00076678", "PUB00076679" ]
[ "9473480", "9756849", "17237233", "12837954", "14998928" ]
[ "Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family.", "The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate.", "Expression of rib-1, a Caenorhabditis elegans homolog of t...
[ 1998, 1998, 2007, 2003, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halapricum salinum", "Viruses", "metagenomes" ]
[ 305, 34505, 1, 5, 38 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 203, 2, 20, 6, 24, 20, 120, 14, 216 ]
9
true
Family
Exostosin-like
Exostosin-like
Exostosin
3
IPR004264
4,264
Transposase, Tnp1/En/Spm-like
Transposase_23
Domain
1,075
false
false
Proteins in this group are TNP1/EN/SPM-like transposon proteins with no known function from plants [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03017" ]
[ "Transposase_23" ]
[ 1075 ]
1
[]
[]
[]
0
[]
0
[ "PUB00034639" ]
[ "16297077" ]
[ "Efficient insertional mutagenesis in rice using the maize En/Spm elements." ]
[ 2005 ]
1
[]
[]
0
0
null
[ "Embryophyta" ]
[ 1075 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 37, 79 ]
3
true
Domain
Transposase, Tnp1/En/Spm-like
Transposase, Tnp1/En/Spm-like
Transposase_23
2
IPR004265
4,265
Dirigent protein
Dirigent
Family
17,448
false
false
Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism [ , ]. This family also includes homolo...
[]
[]
[]
0
[ "PFAM", "PANTHER", "PANTHER", "PANTHER" ]
[ "PF03018", "PTHR21495", "PTHR46215", "PTHR46442" ]
[ "Dirigent", "", "", "" ]
[ 17326, 11707, 2493, 1813 ]
4
[]
[]
[]
0
[ "4rev", "5lal", "6ooc", "6ood", "7r5z", "7ywe", "7ywf", "8th2" ]
8
[ "PUB00085026", "PUB00085027", "PUB00085029" ]
[ "27756822", "19946920", "25457488" ]
[ "Dirigent Protein Mode of Action Revealed by the Crystal Structure of AtDIR6.", "An enantiocomplementary dirigent protein for the enantioselective laccase-catalyzed oxidative coupling of phenols.", "Non-host disease resistance response in pea (Pisum sativum) pods: Biochemical function of DRR206 and phytoalexin ...
[ 2016, 2010, 2015 ]
3
[]
[]
0
0
null
[ "Bacteria", "Streptophyta", "hydrothermal vent metagenome" ]
[ 33, 17413, 2 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 91, 166, 151 ]
3
true
Family
Dirigent protein
Dirigent protein
Dirigent
8
IPR004267
4,267
Influenza C virus M2 protein
CM2
Family
319
false
false
This family represents the matrix protein, M2, of Influenza C virus. The M1 protein is the product of a spliced mRNA (see ). Small quantities of the unspliced mRNA are found in the cell additionally encoding the M2 protein.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03021" ]
[ "CM2" ]
[ 319 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Orthomyxoviridae" ]
[ 319 ]
1
[]
[]
0
true
Family
Influenza C virus M2 protein
Influenza C virus M2 protein
CM2
9
IPR004269
4,269
Folate receptor
Folate_rcpt
Family
3,486
false
false
Folic acid and its reduced derivatives are transported via two widely expressed transporters, the reduced folate carrier (RFC) and the proton-coupled folate transporter (PCFT), and via a family of glycosyl-phosphatidylinositol (GPI)-anchored receptors with limited expression profiles known as folate receptors (FRs) [ ]...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10517" ]
[ "" ]
[ 3486 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-163125", "R-HSA-196757", "R-HSA-204005", "R-HSA-5694530", "R-HSA-6798695", "R-HSA-6807878", "R-MMU-163125", "R-MMU-196757", "R-MMU-204005", "R-MMU-5694530", "R-MMU-6798695", "R-MMU-6807878", "R-RNO-163125" ]
[ "REACTOME:R-HSA-163125", "REACTOME:R-HSA-196757", "REACTOME:R-HSA-204005", "REACTOME:R-HSA-5694530", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6807878", "REACTOME:R-MMU-163125", "REACTOME:R-MMU-196757", "REACTOME:R-MMU-204005", "REACTOME:R-MMU-5694530", "REACTOME:R-MMU-6798695", "REACTOME:R-MM...
13
[ "4km6", "4km7", "4kmx", "4kmy", "4kmz", "4kn0", "4kn1", "4kn2", "4lrh", "5ejn", "5f4e", "5f4q", "5izq", "5jka", "5jkb", "5jkc", "5jkd", "5jke", "5jyj", "6hce" ]
20
[ "PUB00088696", "PUB00088697" ]
[ "8839936", "23934049" ]
[ "Folate receptors.", "Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition." ]
[ 1996, 2013 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3486 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 29, 20, 13 ]
4
true
Family
Folate receptor
Folate receptor
Folate_rcpt
6
IPR004270
4,270
Papillomavirus E5, alphapapillomavirus
Papilloma_E5_alpha
Family
1,286
false
false
The E5 protein from papillomaviruses is about 80 amino acids long and contain three regions that have been predicted to be transmembrane α helices. The function of this protein is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03025" ]
[ "Papilloma_E5" ]
[ 1286 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Homo sapiens", "Papillomaviridae" ]
[ 1, 1285 ]
2
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Papillomavirus E5, alphapapillomavirus
Papillomavirus E5, alphapapillomavirus
Papilloma_E5_alpha
5
IPR004271
4,271
Influenza C virus M1 protein
CM1
Family
347
false
false
This family represents the matrix protein, M1, of Influenza C virus. The M1 protein is the product of a spliced mRNA. Small quantities of the unspliced mRNA are found in the cell additionally encoding the M2 protein (see ).
[ "GO:0019028" ]
[ "viral capsid" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF03026" ]
[ "CM1" ]
[ 347 ]
1
[]
[]
[]
0
[ "5m1m" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Orthomyxoviridae" ]
[ 347 ]
1
[]
[]
0
true
Family
Influenza C virus M1 protein
Influenza C virus M1 protein
CM1
3
IPR004273
4,273
Dynein heavy chain, D6 P-loop domain
Dhc_D6_P-loop
Domain
29,237
false
false
This entry represents the C-terminal region of dynein heavy chain. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained [ ]. Dyneins are motor proteins of eukaryotic cells that conver...
[ "GO:0008569", "GO:0007018", "GO:0030286" ]
[ "minus-end-directed microtubule motor activity", "microtubule-based movement", "dynein complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF03028" ]
[ "Dynein_heavy" ]
[ 29237 ]
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-CEL-5620924", "R-CEL-6798695", "R-CEL-6807878", "R-CEL-6811436", "R-CEL-9646399", "R-DDI-6798695", "R-DDI-6807878", "R-DDI-9646399", "R-DME-3371497", "R-DME-6798695", "R-DME-6807878", "R-DME-6811436", "R-DME-9646399", "R-HSA-141444", "R-HSA-2132295", "R-HSA-2467813", "R-HSA-250025...
[ "REACTOME:R-CEL-5620924", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6807878", "REACTOME:R-CEL-6811436", "REACTOME:R-CEL-9646399", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-6807878", "REACTOME:R-DDI-9646399", "REACTOME:R-DME-3371497", "REACTOME:R-DME-6798695", "REACTOME:R-DME-6807878", "REACTOM...
82
[ "3j67", "3j68", "3qmz", "3vkg", "3vkh", "4ai6", "4akg", "4akh", "4aki", "4rh7", "4w8f", "5nug", "5vh9", "5vlj", "6rla", "6rlb", "6sc2", "6zyw", "6zyx", "6zyy", "7k58", "7k5b", "7kek", "7kzm", "7kzn", "7kzo", "7mgm", "7mi1", "7mi3", "7mi6", "7mi8", "7moq"...
151
[ "PUB00005841", "PUB00019481", "PUB00028625", "PUB00033356", "PUB00061850", "PUB00062447", "PUB00097475", "PUB00097476", "PUB00097477", "PUB00097478", "PUB00097479", "PUB00163363", "PUB00163364" ]
[ "9927482", "7866389", "11250194", "15661525", "8666668", "22398446", "9242627", "15880123", "9403697", "12610617", "19203583", "16061793", "16229832" ]
[ "AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.", "Molecular characterization of a cytoplasmic dynein from Dictyostelium.", "Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases.", ...
[ 1999, 1994, 2001, 2005, 1996, 2012, 1997, 2005, 1997, 2003, 2009, 2005, 2005 ]
13
[]
[]
0
0
null
[ "Eukaryota" ]
[ 29237 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 3, 35, 34, 59, 39, 1, 52, 1, 1 ]
9
true
Domain
Dynein heavy chain, D6 P-loop domain
Dynein heavy chain, D6 P-loop domain
Dhc_D6_P-loop
9
IPR004274
4,274
FCP1 homology domain
FCP1_dom
Domain
42,877
false
false
Yeast FCP1 is an essential protein serine phosphatase ( ) that dephosphorylates the C-terminal domain (CTD) of RNA polymerase II. FCP1 orthologs are present in all known eukaryote proteomes. The N-terminal domain of FCP1 corresponds to the catalytic unit of the phosphatase and has been refered to as the FCP1 homology d...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF03031", "PS50969", "SM00577" ]
[ "NIF", "FCP1", "CPDc" ]
[ 42352, 41542, 40345 ]
3
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.1.3", "PDOC50969", "R-BTA-4419969", "R-CEL-112382", "R-CEL-113418", "R-CEL-4419969", "R-CEL-674695", "R-CEL-6796648", "R-CEL-75955", "R-DME-4419969", "R-HSA-112382", "R-HSA-113418", "R-HSA-1268020", "R-HSA-167152", "R-HSA-167158", "R-HSA-167200", "R-HSA-167238", "R-HSA-167242", ...
[ "EC:3.1.3", "PROSITEDOC:PDOC50969", "REACTOME:R-BTA-4419969", "REACTOME:R-CEL-112382", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-4419969", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6796648", "REACTOME:R-CEL-75955", "REACTOME:R-DME-4419969", "REACTOME:R-HSA-112382", "REACTOME:R-HSA-113418", "RE...
42
[ "1t9z", "1ta0", "2ghq", "2ght", "2hhl", "2q5e", "3ef0", "3ef1", "3l0b", "3l0c", "3l0y", "3pgl", "3qle", "3shq", "4qqf", "4xpz", "4xq0", "4ygy", "4yh1", "6du2", "6du3", "8ujl", "8ujm" ]
23
[ "PUB00018438", "PUB00018439", "PUB00018440", "PUB00018441" ]
[ "9405607", "10445027", "12556522", "10385623" ]
[ "An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae.", "An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae.", "Defining the active site of Schizosacch...
[ 1997, 1999, 2003, 1999 ]
4
[]
[ "IPR011943", "IPR011947", "IPR011948" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 24, 465, 42168, 135, 85 ]
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...
[ 129, 7, 27, 16, 35, 15, 6, 64, 33, 5, 5, 140 ]
12
true
Domain
FCP1 homology domain
FCP1 homology domain
FCP1_dom
3
IPR004275
4,275
Frog antimicrobial peptide, propeptide
Frog_antimicrobial_propeptide
Domain
2,184
false
false
In addition to the highly specific cell-mediated immune system, vertebrates possess an efficient host-defence mechanism against invading microorganisms which involves the synthesis of highly potent antimicrobial peptides with a large spectrum of activity. This entry represents the signal peptide and propeptide regions ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03032" ]
[ "FSAP_sig_propep" ]
[ 2184 ]
1
[]
[]
[]
0
[]
0
[ "PUB00076491", "PUB00076492" ]
[ "19272309", "18983817" ]
[ "Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?", "Antimicrobial peptides from the skins of North American frogs." ]
[ 2009, 2009 ]
2
[]
[]
0
0
null
[ "Bilateria", "Rufibacter" ]
[ 2181, 3 ]
2
[]
[]
0
true
Domain
Frog antimicrobial peptide, propeptide
Frog antimicrobial peptide, propeptide
Frog_antimicrobial_propeptide
6
IPR004276
4,276
Glycosyltransferase family 28, N-terminal domain
GlycoTrans_28_N
Domain
44,088
false
false
Glycosyltransferase family 28 comprises enzymes with a number of known activities; 1,2-diacylglycerol 3-beta-galactosyltransferase ( ); 1,2-diacylglycerol 3-beta-glucosyltransferase ( ); beta-N-acetylglucosamine transferase ( ). The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action...
[ "GO:0016758", "GO:0005975" ]
[ "hexosyltransferase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03033" ]
[ "Glyco_transf_28" ]
[ 44088 ]
1
[ "CAZY", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "GT28", "2.4.1", "2.4.1.227", "PWY-5265", "PWY-6385", "PWY-6470", "PWY-6471" ]
[ "CAZY:GT28", "EC:2.4.1", "EC:2.4.1.227", "METACYC:PWY-5265", "METACYC:PWY-6385", "METACYC:PWY-6470", "METACYC:PWY-6471" ]
7
[ "1f0k", "1iir", "1nlm", "1pn3", "1pnv", "1rrv", "3h4i", "3h4t", "3s2u", "5gl5", "5xvm", "7d1i" ]
12
[ "PUB00009409" ]
[ "9334165" ]
[ "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Alphaendornavirus", "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 8, 48, 33103, 10343, 586 ]
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)", "Zea mays" ]
[ 15, 1, 3, 13, 1, 51 ]
6
true
Domain
Glycosyltransferase family 28, N-terminal domain
Glycosyltransferase family 28, N-terminal domain
GlycoTrans_28_N
5
IPR004278
4,278
Minor capsid protein VP2
VP2
Family
2,837
false
false
This entry represents Minor capsid protein VP2 from Caliciviruses. VP2 is a minor structural protein that forms a portal-like structure at a unique three-fold axis of symmetry, following binding to the host receptor [ ]. This structure contains twelve copies of VP2, arranged with their hydrophobic N termini pointing aw...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03035" ]
[ "RNA_capsid" ]
[ 2837 ]
1
[]
[]
[]
0
[]
0
[ "PUB00097361", "PUB00153756" ]
[ "30626974", "15767403" ]
[ "Calicivirus VP2 forms a portal-like assembly following receptor engagement.", "Feline calicivirus VP2 is essential for the production of infectious virions." ]
[ 2019, 2005 ]
2
[]
[]
0
0
null
[ "Caliciviridae" ]
[ 2837 ]
1
[]
[]
0
true
Family
Minor capsid protein VP2
Minor capsid protein VP2
VP2
1
IPR004279
4,279
Perilipin
Perilipin
Family
7,154
false
false
The perilipin family includes lipid droplet-associated protein (perilipin) and adipose differentiation-related protein (adipophilin). Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis are involved in the development and maintenance of adipose tissue. The relative expression of these proteins and ...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF03036", "PIRSF036881" ]
[ "Perilipin", "PAT" ]
[ 7154, 3625 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-6811440", "R-DME-9706019", "R-HSA-163560", "R-HSA-1989781", "R-HSA-381340", "R-HSA-6811440", "R-HSA-9031528", "R-HSA-9613354", "R-HSA-9613829", "R-HSA-9615710", "R-HSA-9706019", "R-HSA-9841922", "R-MMU-6811440", "R-MMU-9706019" ]
[ "REACTOME:R-DME-6811440", "REACTOME:R-DME-9706019", "REACTOME:R-HSA-163560", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-6811440", "REACTOME:R-HSA-9031528", "REACTOME:R-HSA-9613354", "REACTOME:R-HSA-9613829", "REACTOME:R-HSA-9615710", "REACTOME:R-HSA-9706019", "REACTOME:...
14
[ "1szi" ]
1
[ "PUB00007460", "PUB00027935", "PUB00094348", "PUB00094349" ]
[ "9590177", "15242596", "26357594", "28754637" ]
[ "TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking.", "Structure of a lipid droplet protein; the PAT family member TIP47.", "Perilipin-related protein regulates lipid metabolism in C. elegans.", "The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis....
[ 1998, 2004, 2015, 2017 ]
4
[]
[ "IPR042998" ]
0
1
0
[ "Eukaryota", "bird metagenome" ]
[ 7152, 2 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 14, 8, 18, 19, 27 ]
6
true
Family
Perilipin
Perilipin
Perilipin
5
IPR004280
4,280
Herpesvirus UL95
Herpes_UL95
Family
253
false
false
Members of this family are functionally uncharacterised proteins from herpesviruses.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03038" ]
[ "Herpes_UL95" ]
[ 253 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-9609690", "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9610379" ]
2
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Homo sapiens", "Orthoherpesviridae", "Salmonella enterica" ]
[ 1, 251, 1 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Herpesvirus UL95
Herpesvirus UL95
Herpes_UL95
4
IPR004281
4,281
Interleukin-12 alpha
IL-12_alpha
Family
754
false
false
Interleukin 12 (IL-12) is a disulphide-bonded heterodimer consisting of a 35kDa alpha subunit and a 40kDa beta subunit. It is involved in the stimulation and maintenance of Th1 cellular immune responses, including the normal host defence against various intracellular pathogens, such as Leishmania, Toxoplasma, Measles v...
[ "GO:0005143", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "interleukin-12 receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM" ]
[ "PF03039" ]
[ "IL12" ]
[ 754 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-8984722", "R-BTA-9020591", "R-HSA-6783783", "R-HSA-6785807", "R-HSA-8984722", "R-HSA-9020591", "R-MMU-8984722", "R-MMU-9020591", "R-RNO-8984722", "R-RNO-9020591" ]
[ "REACTOME:R-BTA-8984722", "REACTOME:R-BTA-9020591", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-8984722", "REACTOME:R-HSA-9020591", "REACTOME:R-MMU-8984722", "REACTOME:R-MMU-9020591", "REACTOME:R-RNO-8984722", "REACTOME:R-RNO-9020591" ]
10
[ "1f45", "3hmx", "8cr6", "8odz", "8oe0", "8pb1", "8xrp", "8yi7" ]
8
[ "PUB00007461", "PUB00007462" ]
[ "11422900", "9597139" ]
[ "Il-12: keeping cell-mediated immunity alive.", "The interleukin-12/interleukin-12-receptor system: role in normal and pathologic immune responses." ]
[ 2001, 1998 ]
2
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 754 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 4, 3 ]
4
true
Family
Interleukin-12 alpha
Interleukin-12 alpha
IL-12_alpha
3
IPR004283
4,283
Late expression factor 2
Lef-2
Family
179
false
false
The late expression factor 2 (lef-2) protein from Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV) is required for expression of late genes. The lef-2 protein has been shown to be specifically required for expression from the vp39 and polh promoters [ ].
[ "GO:0019083" ]
[ "viral transcription" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF03041" ]
[ "Baculo_LEF-2" ]
[ 179 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007464" ]
[ "8445724" ]
[ "Three baculovirus genes involved in late and very late gene expression: ie-1, ie-n, and lef-2." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Baculoviridae" ]
[ 179 ]
1
[]
[]
0
true
Family
Late expression factor 2
Late expression factor 2
Lef-2
9
IPR004284
4,284
Birnavirus VP5 protein
Birna_VP5
Family
177
false
false
Birnaviruses are ds RNA viruses. Non structural protein VP5 is found in RNA segment A. The function of this small viral protein is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03042" ]
[ "Birna_VP5" ]
[ 177 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Birnaviridae" ]
[ 177 ]
1
[]
[]
0
true
Family
Birnavirus VP5 protein
Birnavirus VP5 protein
Birna_VP5
5
IPR004285
4,285
Herpesvirus UL87, C-terminal
Herpes_UL87_C
Domain
316
false
false
This entry represents the C-terminal domain found in protein UL87 from human cytomegalovirus and related proteins members of herpesviridae UL87 family. The function of this domain is unknown. It is also found in Epstein-Barr virus (EBV) early protein BcRF1 that is a viral factor crucial for the activation of late gene ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03043" ]
[ "Herpes_UL87" ]
[ 316 ]
1
[ "REACTOME" ]
[ "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9610379" ]
1
[]
0
[ "PUB00103928" ]
[ "22457524" ]
[ "The Epstein-Barr virus BcRF1 gene product is a TBP-like protein with an essential role in late gene expression." ]
[ 2012 ]
1
[]
[]
0
0
null
[ "Homo sapiens", "Neisseria elongata subsp. glycolytica ATCC 29315", "Orthoherpesviridae" ]
[ 1, 1, 314 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Domain
Herpesvirus UL87, C-terminal
Herpesvirus UL87, C-terminal
Herpes_UL87_C
5
IPR004286
4,286
Herpesvirus UL16/UL94
Herpes_UL16/UL94
Family
517
false
false
UL16 protein (also known as cytoplasmic envelopment protein 2) plays a role in capsid maturation including DNA packaging/cleavage [ ]. In immunofluorescence studies [ ], UL16 was localised to the nucleus of infected cells in areas containing high concentrations of Human herpesvirus 2 (Herpes simplex virus 2) capsid pro...
[]
[]
[]
0
[ "HAMAP", "PFAM" ]
[ "MF_04039", "PF03044" ]
[ "HSV_CEP2", "Herpes_UL16" ]
[ 233, 517 ]
2
[ "REACTOME", "REACTOME" ]
[ "R-HSA-9609690", "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9610379" ]
2
[]
0
[ "PUB00007465", "PUB00007466", "PUB00007467", "PUB00082621" ]
[ "9645194", "8955043", "8676489", "22171267" ]
[ "Characterization of the UL16 gene product of herpes simplex virus type 2.", "The UL 16 gene product of herpes simplex virus 1 is a virion protein that colocalizes with intranuclear capsid proteins.", "Assemblons: nuclear structures defined by aggregation of immature capsids and some tegument proteins of herpes...
[ 1998, 1996, 1996, 2012 ]
4
[]
[]
0
0
null
[ "Herpesvirales", "Homo sapiens", "Salmonella enterica" ]
[ 515, 1, 1 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Herpesvirus UL16/UL94
Herpesvirus UL16/UL94
Herpes_UL16/UL94
8
IPR004288
4,288
Competence protein, ComC
Competence_ComC
Family
487
false
false
Competence is the ability of a cell to take up exogenous DNA from its environment, resulting in transformation. It is widespread among bacteria and is probably an important mechanism for the horizontal transfer of genes. DNA usually becomes available by the death and lysis of other cells. Competent bacteria use compone...
[ "GO:0005186" ]
[ "pheromone activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03047" ]
[ "ComC" ]
[ 487 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007468", "PUB00007469", "PUB00016384", "PUB00052316" ]
[ "9352904", "7479953", "10858242", "8901420" ]
[ "Natural competence in the genus Streptococcus: evidence that streptococci can change pherotype by interspecies recombinational exchanges.", "An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae.", "Genetic locus for streptolysin S production by grou...
[ 1997, 1995, 2000, 1996 ]
4
[]
[]
0
0
null
[ "Bacteria", "Oesophagostomum dentatum", "human gut metagenome" ]
[ 485, 1, 1 ]
3
[]
[]
0
true
Family
Competence protein, ComC
Competence protein, ComC
Competence_ComC
3
IPR004289
4,289
Herpesvirus UL92
Herpes_UL92
Family
461
false
false
Members of this family are functionally uncharacterised proteins from herpesviruses. The N terminus of these proteins contain 6 conserved cysteines and histidines that might form a zinc binding domain.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03048" ]
[ "Herpes_UL92" ]
[ 461 ]
1
[ "REACTOME" ]
[ "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9610379" ]
1
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Heunggongvirae" ]
[ 5, 297, 159 ]
3
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Herpesvirus UL92
Herpesvirus UL92
Herpes_UL92
5
IPR004290
4,290
Herpesvirus UL79
Herpes_UL79
Family
236
false
false
Members of the herpesvirus UL79 family also contain proteins such as U52 and gene 18 protein. UL79 plays a role in the expression of late transcripts bridging viral DNA replication and late gene expression during infection [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03049" ]
[ "Herpes_UL79" ]
[ 236 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-9609690", "R-HSA-9610379" ]
[ "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-9610379" ]
2
[]
0
[ "PUB00077060" ]
[ "21367901" ]
[ "The human cytomegalovirus gene UL79 is required for the accumulation of late viral transcripts." ]
[ 2011 ]
1
[]
[]
0
0
null
[ "Herpesvirales", "Homo sapiens" ]
[ 235, 1 ]
2
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Herpesvirus UL79
Herpesvirus UL79
Herpes_UL79
6
IPR004291
4,291
Transposase IS66, central domain
Transposase_IS66_central
Domain
23,706
false
false
This domain can be found in transposase IS66 from Agrobacterium tumefaciens [ ]. Transposases are necessary for efficient DNA transposition. IS66 may cause genetic and structural variations of the T region and the vir region of the octopine Ti plasmids [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03050" ]
[ "DDE_Tnp_IS66" ]
[ 23706 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007470" ]
[ "6095299" ]
[ "Nucleotide sequence of the insertion sequence found in the T-DNA region of mutant Ti plasmid pTiA66 and distribution of its homologues in octopine Ti plasmid." ]
[ 1984 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Plasmid Ti", "Viruses", "metagenomes" ]
[ 595, 22368, 112, 1, 9, 621 ]
6
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Transposase IS66, central domain
Transposase IS66, central domain
Transposase_IS66_central
1
IPR004293
4,293
Coronavirus Orf3a/b
Coronavirus_Orf3a/b
Family
1,322
false
false
Members of this family are non-structural proteins that are found in alphacoronavirus, including Transmissible gastroenteritis virus (TGEV) and Porcine respiratory coronavirus (PRCV). These proteins are found on the same mRNA as another product, designated ORF3a and they are referred to as 3a-like accessory proteins fo...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03053" ]
[ "Corona_NS3b" ]
[ 1322 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007472", "PUB00007473", "PUB00100945" ]
[ "10948987", "10365166", "33154751" ]
[ "Molecular characterization and pathogenesis of transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCV) field isolates co-circulating in a swine herd.", "Characterisation of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a.", "Coronavir...
[ 2000, 1999, 2020 ]
3
[]
[]
0
0
null
[ "Coronaviridae" ]
[ 1322 ]
1
[]
[]
0
true
Family
Coronavirus Orf3a/b
Coronavirus Orf3a/b
Coronavirus_Orf3a/b
2
IPR004294
4,294
Carotenoid oxygenase
Carotenoid_Oase
Family
27,470
false
false
This entry represents a number of enzymes with oxidoreductase activity, many of which acting on carotenoids. They fold into a seven-bladed β-propeller and require Fe2+ for activity. Carotenoids such as β-carotene, lycopene, lutein and beta-cryptoxanthine are produced in plants and certain bacteria, algae and fungi, whe...
[ "GO:0016702" ]
[ "oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF03055", "PTHR10543" ]
[ "RPE65", "" ]
[ 27458, 26800 ]
2
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.13.11", "GenProp1703", "R-BTA-2453902", "R-DME-2453902", "R-DME-975634", "R-DRE-2453902", "R-GGA-975634", "R-HSA-2453902", "R-HSA-975634", "R-MMU-2453902", "R-MMU-975634", "R-RNO-2453902", "R-RNO-975634" ]
[ "EC:1.13.11", "GP:GenProp1703", "REACTOME:R-BTA-2453902", "REACTOME:R-DME-2453902", "REACTOME:R-DME-975634", "REACTOME:R-DRE-2453902", "REACTOME:R-GGA-975634", "REACTOME:R-HSA-2453902", "REACTOME:R-HSA-975634", "REACTOME:R-MMU-2453902", "REACTOME:R-MMU-975634", "REACTOME:R-RNO-2453902", "REA...
13
[ "2biw", "2bix", "3fsn", "3kvc", "3npe", "4f2z", "4f30", "4f3a", "4f3d", "4ou8", "4ou9", "4rsc", "4rse", "4ryx", "4ryy", "4ryz", "4zhk", "5j53", "5j54", "5j55", "5kja", "5kjb", "5kjd", "5kk0", "5u8x", "5u8y", "5u8z", "5u90", "5u97", "5ul5", "5ulg", "5v2d"...
71
[ "PUB00016926", "PUB00016927", "PUB00016929", "PUB00016930", "PUB00100266", "PUB00100267", "PUB00100268", "PUB00100269", "PUB00100270" ]
[ "14704328", "12834401", "15821095", "14532273", "21106934", "17848510", "28874556", "1278918", "20635095" ]
[ "Carotene oxygenases: a new family of double bond cleavage enzymes.", "Molecular characterization of the Arabidopsis 9-cis epoxycarotenoid dioxygenase gene family.", "The structure of a retinal-forming carotenoid oxygenase.", "Rpe65 is a retinyl ester binding protein that presents insoluble substrate to the i...
[ 2004, 2003, 2005, 2004, 2011, 2007, 2017, 1976, 2010 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Pithovirus LCPAC202", "metagenomes" ]
[ 175, 6516, 20596, 1, 182 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 41, 4, 18, 2, 15, 8, 2, 36, 12, 75 ]
10
true
Family
Carotenoid oxygenase
Carotenoid oxygenase
Carotenoid_Oase
2
IPR004296
4,296
DUF236 repeat
DUF236
Repeat
693
false
false
This family represents a short repeat region found a number of C. elegans proteins of unknown function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03057" ]
[ "DUF236" ]
[ 693 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Rhabditida" ]
[ 693 ]
1
[ "Caenorhabditis elegans" ]
[ 14 ]
1
true
Repeat
DUF236 repeat
DUF236 repeat
DUF236
1
IPR004297
4,297
Systemic acquired resistance protein SAR
Sar8_2
Family
53
false
false
Members of this family are found in Solanaceae spp. plants, a taxonomic group (family) that includes pepper and tobacco plant species. Synthesis of these proteins is induced by Tobacco mosaic virus and salicylic acid [ ]; indeed they are thought to be involved in the development of systemic acquired resistance (SAR) af...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03058" ]
[ "Sar8_2" ]
[ 53 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007474", "PUB00007475" ]
[ "1477404", "10888849" ]
[ "A new multigene family inducible by tobacco mosaic virus or salicylic acid in tobacco.", "Overproduction of salicylic acid in plants by bacterial transgenes enhances pathogen resistance." ]
[ 1992, 2000 ]
2
[]
[]
0
0
null
[ "lamiids" ]
[ 53 ]
1
[]
[]
0
true
Family
Systemic acquired resistance protein SAR
Systemic acquired resistance protein SAR
Sar8_2
4
IPR004298
4,298
Nicotianamine synthase
Nicotian_synth
Family
2,958
false
false
Nicotianamine synthase catalyzes the trimerization of S-adenosylmethionine to yield one molecule of nicotianamine. Nicotianamine has an important role in plant iron uptake mechanisms. Plants adopt two strategies (termed I and II) of iron acquisition. Strategy I is adopted by all higher plants except graminaceous plants...
[ "GO:0030410", "GO:0030418" ]
[ "nicotianamine synthase activity", "nicotianamine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "PANTHER" ]
[ "PF03059", "PS51142", "PTHR32266" ]
[ "NAS", "NAS", "" ]
[ 2797, 2554, 2877 ]
3
[ "EC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "2.5.1.43", "PWY-5912", "PWY-5957", "PDOC51142" ]
[ "EC:2.5.1.43", "METACYC:PWY-5912", "METACYC:PWY-5957", "PROSITEDOC:PDOC51142" ]
4
[ "3fpe", "3fpf", "3fpg", "3fph", "3fpj", "3o31", "7c7m", "7c9k", "7c9m", "8zx0" ]
10
[ "PUB00007476", "PUB00007477", "PUB00054692" ]
[ "10359845", "9952442", "19805277" ]
[ "Map-based cloning of chloronerva, a gene involved in iron uptake of higher plants encoding nicotianamine synthase.", "Cloning of nicotianamine synthase genes, novel genes involved in the biosynthesis of phytosiderophores.", "Crystallographic snapshots of iterative substrate translocations during nicotianamine ...
[ 1999, 1999, 2009 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "bioreactor metagenome" ]
[ 117, 564, 2276, 1 ]
4
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 17, 1, 8, 29 ]
4
true
Family
Nicotianamine synthase
Nicotianamine synthase
Nicotian_synth
1
IPR004299
4,299
Membrane bound O-acyl transferase, MBOAT
MBOAT_fam
Family
46,414
false
false
The MBOAT (membrane bound O-acyl transferase) family of membrane proteins contains a variety of acyltransferase enzymes. A conserved histidine has been suggested to be the active site residue [ ]. The structure of MBOAT has been revealed [ ]. This family includes Diacylglycerol O-acyltransferase 1 (DGAT1) and Lysophosp...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03062" ]
[ "MBOAT" ]
[ 46414 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "2.3.1", "GenProp1316", "GenProp1398", "GenProp1558", "GenProp1575", "GenProp1718", "GenProp1761", "R-BTA-1482922", "R-CEL-1482788", "R-CEL-1482801", "R-CEL-1482839", "R-CEL-1482922", "R-DDI-1482883", "R-DDI-6798695", "R-DDI-75109", "R-DME-1482788", "R-DME-1482801", "R-DME-1482839"...
[ "EC:2.3.1", "GP:GenProp1316", "GP:GenProp1398", "GP:GenProp1558", "GP:GenProp1575", "GP:GenProp1718", "GP:GenProp1761", "REACTOME:R-BTA-1482922", "REACTOME:R-CEL-1482788", "REACTOME:R-CEL-1482801", "REACTOME:R-CEL-1482839", "REACTOME:R-CEL-1482922", "REACTOME:R-DDI-1482883", "REACTOME:R-DD...
64
[ "6bug", "6buh", "6bui", "6l47", "6l48", "6p2j", "6p2p", "6vp0", "6vum", "6vyi", "6vz1", "7ewt", "7f3x", "7f40", "7mhy", "7mhz", "7n6q", "7n6r", "7q1u", "7q6z", "7ura", "7urc", "7urd", "7ure", "7urf", "8erc", "8esm", "8etm", "8jem", "8jes", "8jf2", "9vjm"...
35
[ "PUB00007478", "PUB00095085", "PUB00099654", "PUB00099655" ]
[ "10694878", "30283133", "32253259", "16214399" ]
[ "A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling.", "Crystal structure of a membrane-bound O-acyltransferase.", "LPIAT1/MBOAT7 depletion increases triglyceride synthesis fueled by high phosphatidylinositol turnover.", "Acyl coenzyme A dependent retinol esterification by ...
[ 2000, 2018, 2021, 2005 ]
4
[]
[ "IPR014371", "IPR024194", "IPR049941" ]
0
3
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 20, 16529, 2, 29648, 215 ]
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...
[ 16, 12, 43, 11, 31, 19, 6, 10, 49, 5, 4, 30 ]
12
true
Family
Membrane bound O-acyl transferase, MBOAT
Membrane bound O-acyl transferase, MBOAT
MBOAT_fam
5
IPR004300
4,300
Glycoside hydrolase family 57, N-terminal domain
Glyco_hydro_57_N
Domain
7,619
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0003824", "GO:0005975" ]
[ "catalytic activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03065" ]
[ "Glyco_hydro_57" ]
[ 7619 ]
1
[ "CAZY" ]
[ "GH57" ]
[ "CAZY:GH57" ]
1
[ "1k1w", "1k1x", "1k1y", "1ufa", "2b5d", "3n8t", "3n92", "3n98", "3p0b", "5wu7", "7e1y", "8zyi", "9iht", "9ihu", "9ihv", "9ihw", "9ihx", "9ii0", "9ii1", "9jlq", "9jlr", "9jls", "9jlt", "9jlu", "9jlv", "9jlw", "9k7c", "9k7d", "9kyp", "9kyq", "9kyr" ]
31
[ "PUB00004870", "PUB00005266" ]
[ "7624375", "8535779" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1995, 1995 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 708, 6628, 15, 268 ]
4
[]
[]
0
true
Domain
Glycoside hydrolase family 57, N-terminal domain
Glycoside hydrolase family 57, N-terminal domain
Glyco_hydro_57_N
3
IPR004301
4,301
Nucleoplasmin family
Nucleoplasmin
Family
4,206
false
false
The nucleoplasmin family includes nucleophosmin, nucleoplasmin and nucleoplasmin-like proteins. Nucleophosmin (also known as NPM1/B23) is a multifunctional protein that is involved in a number of cellular activities, such as ribosome maturatation and export, centrosome duplication, and response to stress stimuli [ ]. N...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR22747" ]
[ "" ]
[ 4206 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-DME-3899300", "R-DME-8869496", "R-DME-9833482", "R-HSA-180746", "R-HSA-3899300", "R-HSA-606279", "R-HSA-6804115", "R-HSA-8869496", "R-HSA-9692914", "R-HSA-9700645", "R-HSA-9725370", "R-HSA-9725371", "R-HSA-9821993", "R-HSA-9833482", "R-MMU-3899300", "R-MMU-606279", "R-MMU-6804115"...
[ "REACTOME:R-DME-3899300", "REACTOME:R-DME-8869496", "REACTOME:R-DME-9833482", "REACTOME:R-HSA-180746", "REACTOME:R-HSA-3899300", "REACTOME:R-HSA-606279", "REACTOME:R-HSA-6804115", "REACTOME:R-HSA-8869496", "REACTOME:R-HSA-9692914", "REACTOME:R-HSA-9700645", "REACTOME:R-HSA-9725370", "REACTOME:...
24
[ "1k5j", "1nlq", "1xb9", "1xe0", "2llh", "2p1b", "2vtx", "3t30", "4n8m", "5ehd", "8as5", "8vhi", "8vhj", "8vhk" ]
14
[ "PUB00066091", "PUB00076527", "PUB00076530" ]
[ "22707729", "16794633", "25772360" ]
[ "Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter.", "Nucleophosmin and cancer.", "Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition." ]
[ 2012, 2006, 2015 ]
3
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 4205, 1 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 4, 23, 16, 14 ]
5
true
Family
Nucleoplasmin family
Nucleoplasmin family
Nucleoplasmin
6
IPR004302
4,302
Cellulose/chitin-binding protein, N-terminal
Cellulose/chitin-bd_N
Domain
15,879
false
false
This domain is found in a variety of cellulose- and chitin-binding proteins [ , ]. This domain is also found in baculoviral spheroidins and spindolins [ ], and in bacterial GlcNAc-binding protein A (gbpA) [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03067" ]
[ "LPMO_10" ]
[ 15879 ]
1
[]
[]
[]
0
[ "2bem", "2ben", "2lhs", "2xwx", "2yow", "2yox", "2yoy", "3uam", "4a02", "4alc", "4ale", "4alq", "4alr", "4als", "4alt", "4opb", "4ow5", "4oy6", "4oy7", "4oy8", "4x27", "4x29", "4yn1", "4yn2", "5aa7", "5fjq", "5ftz", "5iju", "5l2v", "5lsv", "5lw4", "5msz"...
61
[ "PUB00019304", "PUB00056779", "PUB00078764", "PUB00084309" ]
[ "7815940", "16341015", "8376960", "10671445" ]
[ "The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline alpha-chitin of fungi and other organisms.", "A colonization factor links Vibrio cholerae environmental survival and human infection.", "A gene encoding a highly expressed...
[ 1994, 2005, 1993, 2000 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "Viruses", "ecological metagenomes" ]
[ 10621, 5092, 5, 155, 6 ]
5
[ "Drosophila melanogaster", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 9, 1 ]
2
true
Domain
Cellulose/chitin-binding protein, N-terminal
Cellulose/chitin-binding protein, N-terminal
Cellulose/chitin-bd_N
2
IPR004303
4,303
Protein-arginine deiminase
PAD
Family
4,478
false
false
In the presence of calcium ions, Protein-arginine deiminase (PAD) enzymes catalyse the post-translational modification reaction responsible for the formation of citrulline residues from protein-bound arginine residues [ ]. Four PAD isotypes of PAD have been identified in mammals, a fifth may also exist. Non-mammalian v...
[ "GO:0004668" ]
[ "protein-arginine deiminase activity" ]
[ "molecular_function" ]
1
[ "PIRSF", "PANTHER" ]
[ "PIRSF001247", "PTHR10837" ]
[ "Protein-arginine_deiminase", "" ]
[ 1980, 4478 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.3.15", "PWY-4921", "R-HSA-3247509", "R-HSA-6798695", "R-MMU-3247509", "R-MMU-6798695", "R-RNO-3247509", "R-RNO-6798695" ]
[ "EC:3.5.3.15", "METACYC:PWY-4921", "REACTOME:R-HSA-3247509", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-3247509", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-3247509", "REACTOME:R-RNO-6798695" ]
8
[ "1wd8", "1wd9", "1wda", "2dew", "2dex", "2dey", "2dw5", "3apm", "3apn", "3b1t", "3b1u", "4dkt", "4n20", "4n22", "4n24", "4n25", "4n26", "4n28", "4n2a", "4n2b", "4n2c", "4n2d", "4n2e", "4n2f", "4n2g", "4n2h", "4n2i", "4n2k", "4n2l", "4n2m", "4n2n", "4x8c"...
62
[ "PUB00007480", "PUB00100949", "PUB00100950", "PUB00100951", "PUB00100952", "PUB00100953", "PUB00100954" ]
[ "10092850", "27545678", "28549415", "30044909", "34116679", "35079870", "31952341" ]
[ "Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse.", "Mutations in PADI6 Cause Female Infertility Characterized by Early Embryonic Arrest.", "Role of peptidylarginine deiminase 2 (PAD2) in mammary carcinoma cell migration....
[ 1999, 2016, 2017, 2018, 2021, 2022, 2020 ]
7
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 442, 4032, 4 ]
3
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 20, 12, 20 ]
4
true
Family
Protein-arginine deiminase
Protein-arginine deiminase
PAD
4
IPR004304
4,304
Acetamidase/Formamidase
FmdA_AmdA
Family
14,119
false
false
This family includes amidohydrolases of formamide [ ] and acetamide [ , ]. The formamidase from Methylophilus methylotrophus (Bacterium W3A1) forms a homotrimer suggesting that this may be a common property of other members of this family.
[ "GO:0016811" ]
[ "hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF03069", "PTHR31891" ]
[ "FmdA_AmdA", "" ]
[ 14041, 13965 ]
2
[]
[]
[]
0
[ "2f4l", "2ii1", "2wkn", "3b9t", "3tkk", "5ubu" ]
6
[ "PUB00020777", "PUB00070856", "PUB00070857" ]
[ "8841393", "6030461", "8473863" ]
[ "Molecular characterisation of formamidase from Methylophilus methylotrophus.", "The aliphatic acylamide amidohydrolase of Mycobacterium smegmatis: its inducible nature and relation to acyl-transfer to hydroxylamine.", "Cloning and sequencing of the gene which encodes the highly inducible acetamidase of Mycobac...
[ 1996, 1967, 1993 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Catovirus CTV1", "Eukaryota", "unclassified sequences" ]
[ 631, 10048, 1, 3211, 228 ]
5
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 23, 2, 3, 1, 41 ]
5
true
Family
Acetamidase/Formamidase
Acetamidase/Formamidase
FmdA_AmdA
1
IPR004305
4,305
Thiaminase-2/PQQC
Thiaminase-2/PQQC
Domain
20,226
false
false
Proteins containing this domain are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TenA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase [ ] and has been identi...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03070" ]
[ "TENA_THI-4" ]
[ 20226 ]
1
[ "EC", "GP" ]
[ "1.3.3", "GenProp0253" ]
[ "EC:1.3.3", "GP:GenProp0253" ]
2
[ "1otv", "1otw", "1rcw", "1rtw", "1to9", "1tyh", "1udd", "1yaf", "1yak", "1z72", "2a6b", "2f2g", "2gm7", "2gm8", "2q4x", "2qcx", "2qzc", "2rd3", "3hlx", "3hml", "3hnh", "3ibx", "3mvu", "3no6", "3rm5", "4fn6", "4lqx", "4ny7", "5vrc", "5vrd", "8va9", "8vab"...
34
[ "PUB00007481", "PUB00007482", "PUB00010477", "PUB00032610" ]
[ "1898926", "8662211", "12437981", "15709744" ]
[ "Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis.", "Molecular cloning of thi-4, a gene necessary for the biosynthesis of thiamine in Neurospora crassa.", "PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone....
[ 1991, 1996, 2002, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 658, 14592, 4852, 124 ]
4
[ "Arabidopsis thaliana", "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" ]
[ 4, 3, 7, 4, 2, 13 ]
6
true
Domain
Thiaminase-2/PQQC
Thiaminase-2/PQQC
Thiaminase-2/PQQC
2