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
IPR003139
3,139
Delta-retroviral matrix protein
D_retro_matrix
Domain
421
false
false
Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [ ]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into...
[ "GO:0005198", "GO:0019013" ]
[ "structural molecule activity", "viral nucleocapsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02228" ]
[ "Gag_p19" ]
[ 421 ]
1
[ "EC" ]
[ "3.4.23.-" ]
[ "EC:3.4.23.-" ]
1
[ "1jvr", "7m1w", "8pug", "8puh" ]
4
[ "PUB00014063", "PUB00016314", "PUB00016315", "PUB00055853" ]
[ "9657938", "9000634", "11752179", "18647839" ]
[ "Retroviral matrix proteins: a structural perspective.", "Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses.", "Intracellular distribution of human T-cell leukemia virus type 1 Gag proteins is indepen...
[ 1998, 1996, 2002, 2008 ]
4
[]
[]
0
0
null
[ "Deltaretrovirus" ]
[ 421 ]
1
[]
[]
0
true
Domain
Delta-retroviral matrix protein
Delta-retroviral matrix protein
D_retro_matrix
1
IPR003140
3,140
Phospholipase/carboxylesterase/thioesterase
PLipase/COase/thioEstase
Domain
35,538
false
false
This entry represents the α/β hydrolase domain found in phospholipases [ ], carboxylesterases [ ] and thioesterases.
[ "GO:0016787" ]
[ "hydrolase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02230" ]
[ "Abhydrolase_2" ]
[ 35538 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-203615", "R-DDI-9648002", "R-HSA-203615", "R-HSA-373760", "R-HSA-9648002", "R-MMU-203615", "R-MMU-373760", "R-MMU-9648002", "R-RNO-203615", "R-RNO-373760", "R-RNO-9648002", "R-SCE-203615", "R-SCE-9648002", "R-SPO-203615", "R-SPO-9648002" ]
[ "REACTOME:R-DDI-203615", "REACTOME:R-DDI-9648002", "REACTOME:R-HSA-203615", "REACTOME:R-HSA-373760", "REACTOME:R-HSA-9648002", "REACTOME:R-MMU-203615", "REACTOME:R-MMU-373760", "REACTOME:R-MMU-9648002", "REACTOME:R-RNO-203615", "REACTOME:R-RNO-373760", "REACTOME:R-RNO-9648002", "REACTOME:R-SCE...
15
[ "1auo", "1aur", "1fj2", "2h1i", "3cn7", "3cn9", "3doh", "3doi", "3u0v", "4f21", "4fhz", "4ftw", "4h0c", "5dwd", "5f2h", "5kre", "5sym", "5syn", "6avv", "6avw", "6avx", "6avy", "6bje", "6qgn", "6qgo", "6qgq", "6qgs" ]
27
[ "PUB00006398", "PUB00006496" ]
[ "9438866", "9644627" ]
[ "Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.", "cDNA cloning and expression of a novel family of enzymes with calcium-independent phospholipase A2 and lysophospholipase activities." ]
[ 1997, 1998 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Imitervirales", "Sym plasmid", "unclassified sequences" ]
[ 520, 18738, 15909, 18, 1, 352 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 50, 3, 9, 5, 1, 17, 10, 2, 18, 17, 1, 2, 48 ]
13
true
Domain
Phospholipase/carboxylesterase/thioesterase
Phospholipase/carboxylesterase/thioesterase
PLipase/COase/thioEstase
4
IPR003141
3,141
Polymerase/histidinol phosphatase, N-terminal
Pol/His_phosphatase_N
Domain
84,462
false
false
This domain is associated with the N terminus of members of the PHP superfamily, this includes: subunit of bacterial DNA polymerase III, eukaryotic DNA polymerase, X-family of DNA polymerases, histidinol phosphatases, and a number of uncharacterised protein families. In common for all PHP proteins is the presence of fo...
[]
[]
[]
0
[ "SMART" ]
[ "SM00481" ]
[ "POLIIIAc" ]
[ 84462 ]
1
[ "EC" ]
[ "2.7.7.7" ]
[ "EC:2.7.7.7" ]
1
[ "1m65", "1m68", "1pb0", "2anu", "2hnh", "2hpi", "2hpm", "2hqa", "2w9m", "2yb1", "2yb4", "2yxo", "2yz5", "2z4g", "3au2", "3au6", "3auo", "3b0x", "3b0y", "3e0d", "3e0f", "3e38", "3f2b", "3f2c", "3f2d", "3o0f", "4gc3", "4gk8", "4gx8", "4gx9", "4gyf", "4iqj"...
44
[ "PUB00027226" ]
[ "12661000" ]
[ "Crystal structure of the Escherichia coli YcdX protein reveals a trinuclear zinc active site." ]
[ 2003 ]
1
[ "IPR004013" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 2515, 79125, 1018, 321, 1483 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 3, 4, 4 ]
4
true
Domain
Polymerase/histidinol phosphatase, N-terminal
Polymerase/histidinol phosphatase, N-terminal
Pol/His_phosphatase_N
4
IPR003142
3,142
Biotin protein ligase, C-terminal
BPL_C
Domain
20,750
false
false
This C-terminal domain has an SH3-like barrel fold, the function of which is unknown. It is found associated with prokaryotic bifunctional transcriptional repressors [ ] and eukaryotic enzymes involved in biotin utilization [ , ].
[ "GO:0036211" ]
[ "protein modification process" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02237" ]
[ "BPL_C" ]
[ 20750 ]
1
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.4", "6.3.4.15", "R-HSA-196780", "R-HSA-3371599", "R-MMU-196780", "R-SPO-196780" ]
[ "EC:6.3.4", "EC:6.3.4.15", "REACTOME:R-HSA-196780", "REACTOME:R-HSA-3371599", "REACTOME:R-MMU-196780", "REACTOME:R-SPO-196780" ]
6
[ "1bia", "1bib", "1hxd", "1wnl", "1wpy", "1wq7", "1wqw", "1x01", "2cgh", "2deq", "2djz", "2dkg", "2dth", "2dti", "2dto", "2dve", "2dxt", "2dxu", "2dz9", "2dzc", "2e10", "2e1h", "2e41", "2e64", "2e65", "2eay", "2ej9", "2ejf", "2ejg", "2ewn", "2fyk", "2hni"...
74
[ "PUB00028009", "PUB00028010", "PUB00028011" ]
[ "2642476", "7842009", "9173880" ]
[ "Crystallization of the bifunctional biotin operon repressor.", "Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA.", "Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arabidopsis thaliana: subcellular fractionation studies and...
[ 1989, 1994, 1997 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 726, 18054, 1603, 367 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 8, 2, 4, 1, 2, 4, 5, 1, 2 ]
9
true
Domain
Biotin protein ligase, C-terminal
Biotin protein ligase, C-terminal
BPL_C
5
IPR003143
3,143
Cytochrome cd1-nitrite reductase, C-terminal domain superfamily
Cyt_cd1_C_sf
Homologous_superfamily
8,093
false
false
Cytochrome cd1 (cyt cd1) nitrite reductase is a dimeric enzyme of the bacterial periplasm that plays a key role in denitrification, the respiratory reduction of nitrite to nitric oxide in the nitrogen cycle. Each subunit of the cyt cd1 dimer contains one cytochrome c and one d1 haem group [ ]. The active site contains ...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.140.10.20" ]
[ "" ]
[ 8093 ]
1
[]
[]
[]
0
[ "1aof", "1aom", "1aoq", "1bl9", "1dy7", "1e2r", "1gjq", "1gq1", "1h9x", "1h9y", "1hcm", "1hj3", "1hj4", "1hj5", "1hzu", "1hzv", "1n15", "1n50", "1n90", "1nir", "1nno", "1qks", "5guw", "6rtd", "6rte", "6tpo", "6tsi", "6tv2", "6tv9" ]
29
[ "PUB00014166", "PUB00030289" ]
[ "12556530", "7736589" ]
[ "Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine.", "The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1." ]
[ 2003, 1995 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Opisthokonta", "unclassified sequences" ]
[ 29, 4596, 4, 3464 ]
4
[]
[]
0
true
Homologous_superfamily
Cytochrome cd1-nitrite reductase, C-terminal domain superfamily
Cytochrome cd1-nitrite reductase, C-terminal domain superfamily
Cyt_cd1_C_sf
5
IPR003146
3,146
Carboxypeptidase, activation peptide
M14A_act_pep
Domain
11,901
false
false
The peptidases are synthesised as inactive molecules, zymogens, with propeptides that must be removed by proteolytic cleavage to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended α-helix; this shields the catalytic site, wit...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02244" ]
[ "Propep_M14" ]
[ 11901 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.17", "R-BTA-2022377", "R-BTA-977606", "R-CEL-2022377", "R-DME-2022377", "R-HSA-2022377", "R-HSA-977606", "R-HSA-9925561", "R-MMU-2022377", "R-MMU-977606", "R-RNO-2022377", "R-RNO-977606" ]
[ "EC:3.4.17", "REACTOME:R-BTA-2022377", "REACTOME:R-BTA-977606", "REACTOME:R-CEL-2022377", "REACTOME:R-DME-2022377", "REACTOME:R-HSA-2022377", "REACTOME:R-HSA-977606", "REACTOME:R-HSA-9925561", "REACTOME:R-MMU-2022377", "REACTOME:R-MMU-977606", "REACTOME:R-RNO-2022377", "REACTOME:R-RNO-977606" ...
12
[ "1aye", "1jqg", "1kwm", "1nsa", "1o6x", "1pba", "1pca", "1pyt", "1vjq", "2boa", "2gjf", "3d66", "3d67", "3d68", "3dgv", "3glj", "3osl", "4p10", "5hvf", "5hvg", "5hvh", "5om9", "7eqx", "7nee", "7neu" ]
25
[ "PUB00003286", "PUB00003579", "PUB00011740", "PUB00011741" ]
[ "1548696", "7674922", "9384570", "12162965" ]
[ "Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.", "Evolutionary families of metallopeptidases.", "The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inh...
[ 1992, 1995, 1997, 2002 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadota", "hydrothermal vent metagenome" ]
[ 11898, 2, 1 ]
3
[ "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" ]
[ 16, 10, 25, 27, 13, 1, 27 ]
7
true
Domain
Carboxypeptidase, activation peptide
Carboxypeptidase, activation peptide
M14A_act_pep
3
IPR003147
3,147
Protein L, Ig light chain-binding
B1_Ig_chn-bd
Repeat
7
false
false
Protein L is a bacterial protein with immunoglobulin (Ig) light chain-binding properties. It contains a number of homologous b1 repeats towards the N terminus. These repeats have been found to be responsible for the interaction of protein L with Ig light chains [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02246" ]
[ "B1" ]
[ 7 ]
1
[]
[]
[]
0
[ "1hez", "1hz5", "1hz6", "1jml", "1k50", "1k51", "1k52", "1k53", "1kh0", "1mhh", "1xcq", "1xct", "1xf5", "1ymh", "1ynt", "2jzp", "2kac", "2ptl", "4hjg", "4hkz", "4ioi", "5u3d", "5u5f", "5u5m", "5u6a", "6b9y", "6b9z", "6bae", "6bah" ]
29
[ "PUB00006277" ]
[ "1618782" ]
[ "Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Peptoniphilaceae" ]
[ 7 ]
1
[]
[]
0
true
Repeat
Protein L, Ig light chain-binding
Protein L, Ig light chain-binding
B1_Ig_chn-bd
7
IPR003148
3,148
Regulator of K+ conductance, N-terminal lobe
RCK_N
Domain
98,430
false
false
This entry represents the N-terminal lobe of the RCK domain. The regulator of K+ conductance (RCK) domain is found in many ligand-gated K+ channels, most often attached to the intracellular carboxy terminus. The domain is prevalent among prokaryotic K+ channels, and also found in eukaryotic, high-conductance Ca2+-activ...
[ "GO:0006813" ]
[ "potassium ion transport" ]
[ "biological_process" ]
1
[ "PFAM", "PFAM", "PROFILE" ]
[ "PF02254", "PF22614", "PS51201" ]
[ "TrkA_N", "Slo-like_RCK", "RCK_N" ]
[ 78768, 18213, 84061 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC51201", "R-BTA-1296052", "R-CEL-1300642", "R-DME-1300642", "R-GGA-1296052", "R-GGA-1300642", "R-HSA-1296052", "R-HSA-1300642", "R-HSA-418457", "R-HSA-9662360", "R-HSA-9667769", "R-MMU-1296052", "R-MMU-1300642", "R-PFA-5576890", "R-RNO-1296052", "R-RNO-1300642" ]
[ "PROSITEDOC:PDOC51201", "REACTOME:R-BTA-1296052", "REACTOME:R-CEL-1300642", "REACTOME:R-DME-1300642", "REACTOME:R-GGA-1296052", "REACTOME:R-GGA-1300642", "REACTOME:R-HSA-1296052", "REACTOME:R-HSA-1300642", "REACTOME:R-HSA-418457", "REACTOME:R-HSA-9662360", "REACTOME:R-HSA-9667769", "REACTOME:R...
16
[ "1id1", "1lnq", "1lss", "1lsu", "2aef", "2aej", "2aem", "2fy8", "2g1u", "2hms", "2hmt", "2hmu", "2hmv", "2hmw", "2ogu", "3c85", "3eyw", "3fwz", "3kxd", "3l4b", "3l9w", "3l9x", "3llv", "3mt5", "3naf", "3rbx", "3rbz", "3u6n", "4ei2", "4g65", "4gvl", "4gx0"...
155
[ "PUB00003847", "PUB00005478", "PUB00007364", "PUB00025981", "PUB00027068", "PUB00033755", "PUB00040861", "PUB00042190", "PUB00097335", "PUB00099198" ]
[ "8412700", "9478130", "11292341", "11301020", "12037559", "16227203", "16990139", "17287352", "17631529", "31992706" ]
[ "NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport.", "A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease.", "Regul...
[ 1993, 1998, 2001, 2001, 2002, 2005, 2006, 2007, 2007, 2020 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 5416, 70794, 20798, 1422 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 32, 21, 108, 18, 5, 79, 60, 18, 29, 73 ]
10
true
Domain
Regulator of K+ conductance, N-terminal lobe
Regulator of K+ conductance, N-terminal lobe
RCK_N
6
IPR003149
3,149
Iron hydrogenase, small subunit
Fe_hydrogenase_ssu
Domain
7,488
false
false
This family represents the small subunit of the Fe-only hydrogenases ( ). The subunit is comprised of alternating random coil and α-helical structures that encompasses the large subunit in a novel protein fold [ ].
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF02256", "SM00902" ]
[ "Fe_hyd_SSU", "Fe_hyd_SSU" ]
[ 7342, 7310 ]
2
[ "GP", "GP", "REACTOME" ]
[ "GenProp0914", "GenProp1353", "R-HSA-2564830" ]
[ "GP:GenProp0914", "GP:GenProp1353", "REACTOME:R-HSA-2564830" ]
3
[ "1c4a", "1c4c", "1e08", "1feh", "1gx7", "1hfe", "2n0s", "3c8y", "3lx4", "4r0v", "4xdc", "4xdd", "5byq", "5byr", "5bys", "5la3", "5oef", "6gl6", "6gly", "6glz", "6gm0", "6gm1", "6gm2", "6gm3", "6gm4", "6gm5", "6gm6", "6gm7", "6gm8", "6h63", "6n59", "6n6p"...
70
[ "PUB00006430" ]
[ "10368269" ]
[ "Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 4, 3900, 3489, 95 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 3, 3, 3, 5, 2, 4, 9, 8 ]
8
true
Domain
Iron hydrogenase, small subunit
Iron hydrogenase, small subunit
Fe_hydrogenase_ssu
4
IPR003150
3,150
DNA-binding RFX-type winged-helix domain
DNA-bd_RFX
Domain
15,903
false
false
The RFX family of transcription factors is characterised by a unique approximately 75-residue DNA-binding domain. RFX genes have been isolated in yeasts, nematode and vertebrates. The characteristic RFX-type HTH DNA binding domain has been recruited into otherwise very divergent regulatory factors functioning in a dive...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF02257", "PS51526" ]
[ "RFX_DNA_binding", "RFX_DBD" ]
[ 14057, 15674 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-210745", "R-HSA-3214858", "R-HSA-8939243", "R-HSA-9933939" ]
[ "REACTOME:R-HSA-210745", "REACTOME:R-HSA-3214858", "REACTOME:R-HSA-8939243", "REACTOME:R-HSA-9933939" ]
4
[ "1dp7", "6k15", "6kw3", "6kw4", "6kw5", "6tda", "6v8o", "6v92", "7vdv", "7y8r", "8zjr" ]
11
[ "PUB00024283", "PUB00057950", "PUB00057951" ]
[ "10706293", "8600444", "10767550" ]
[ "Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding.", "RFX proteins, a novel family of DNA binding proteins conserved in the eukaryotic kingdom.", "Cloning and characterization of dRFX, the Drosophila member of the RFX family of transcription factors." ]
[ 2000, 1996, 2000 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Tupanvirus", "marine sediment metagenome" ]
[ 26, 15867, 3, 2, 5 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 3, 42, 14, 39, 23, 2, 36, 2, 2 ]
9
true
Domain
DNA-binding RFX-type winged-helix domain
DNA-binding RFX-type winged-helix domain
DNA-bd_RFX
5
IPR003151
3,151
PIK-related kinase, FAT
PIK-rel_kinase_FAT
Domain
19,589
false
false
The FAT domain is a domain present in the PIK-related kinases. Members of the family of PIK-related kinases may act as intracellular sensors that govern radial and horizontal pathways [ ]. This domain shows an α-helical structure [ ].
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02259" ]
[ "FAT" ]
[ 19589 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.1", "R-CEL-1257604", "R-CEL-1632852", "R-CEL-165159", "R-CEL-166208", "R-CEL-3371571", "R-CEL-380972", "R-CEL-389357", "R-CEL-5218920", "R-CEL-5628897", "R-CEL-6804757", "R-CEL-8943724", "R-CEL-9639288", "R-CEL-9856530", "R-DDI-1257604", "R-DDI-1632852", "R-DDI-165159", "R-...
[ "EC:2.7.11.1", "REACTOME:R-CEL-1257604", "REACTOME:R-CEL-1632852", "REACTOME:R-CEL-165159", "REACTOME:R-CEL-166208", "REACTOME:R-CEL-3371571", "REACTOME:R-CEL-380972", "REACTOME:R-CEL-389357", "REACTOME:R-CEL-5218920", "REACTOME:R-CEL-5628897", "REACTOME:R-CEL-6804757", "REACTOME:R-CEL-8943724...
180
[ "3jbz", "4jsn", "4jsp", "4jsv", "4jsx", "4jt5", "4jt6", "5flc", "5fvm", "5h64", "5luq", "5np0", "5np1", "5oej", "5ojs", "5w1r", "5wbu", "5wby", "5x6o", "5y3r", "5y81", "5yz0", "5zcs", "6bcu", "6bcx", "6emk", "6ig9", "6k9k", "6k9l", "6sb0", "6sb2", "6sky"...
140
[ "PUB00006515", "PUB00103870" ]
[ "10782091", "27909983" ]
[ "FAT: a novel domain in PIK-related kinases.", "4.4 A Resolution Cryo-EM structure of human mTOR Complex 1." ]
[ 2000, 2016 ]
2
[ "IPR014009" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 16, 19571, 2 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 35, 3, 14, 8, 27, 15, 4, 7, 21, 4, 6, 44 ]
12
true
Domain
PIK-related kinase, FAT
PIK-related kinase, FAT
PIK-rel_kinase_FAT
2
IPR003152
3,152
FATC domain
FATC_dom
Domain
22,462
false
false
This entry represents the FATC domain in Serine/threonine-protein kinases and related proteins, including pseudo-kinases such as members of the SAGA and NuA4 complexes. The TOR1 FATC domain, in its oxidised form, consists of an α-helix and a well-structured COOH-terminal disulphide-bonded loop. Reduction of the disulph...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02260", "PS51190", "SM01343" ]
[ "FATC", "FATC", "FATC" ]
[ 19522, 22305, 21352 ]
3
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.1", "PDOC51189", "R-CEL-1257604", "R-CEL-1632852", "R-CEL-165159", "R-CEL-166208", "R-CEL-3371571", "R-CEL-380972", "R-CEL-389357", "R-CEL-5218920", "R-CEL-5628897", "R-CEL-5693607", "R-CEL-6804757", "R-CEL-8943724", "R-CEL-9639288", "R-CEL-975957", "R-CEL-9856530", "R-DDI-...
[ "EC:2.7.11.1", "PROSITEDOC:PDOC51189", "REACTOME:R-CEL-1257604", "REACTOME:R-CEL-1632852", "REACTOME:R-CEL-165159", "REACTOME:R-CEL-166208", "REACTOME:R-CEL-3371571", "REACTOME:R-CEL-380972", "REACTOME:R-CEL-389357", "REACTOME:R-CEL-5218920", "REACTOME:R-CEL-5628897", "REACTOME:R-CEL-5693607",...
198
[ "1w1n", "2kio", "2kit", "3jbz", "4jsn", "4jsp", "4jsv", "4jsx", "4jt5", "4jt6", "5flc", "5fvm", "5h64", "5luq", "5np0", "5np1", "5oej", "5ojs", "5w1r", "5wbu", "5wby", "5x6o", "5y3r", "5y81", "5yz0", "5zcs", "6bcu", "6bcx", "6emk", "6hka", "6ig9", "6jxa"...
157
[ "PUB00006515", "PUB00021047", "PUB00033610" ]
[ "10782091", "15772072", "7569949" ]
[ "FAT: a novel domain in PIK-related kinases.", "The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability.", "PIK-related kinases: DNA repair, recombination, and cell cycle checkpoints." ]
[ 2000, 2005, 1995 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 22462 ]
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...
[ 32, 6, 17, 12, 16, 17, 4, 15, 24, 5, 6, 66 ]
12
true
Domain
FATC domain
FATC domain
FATC_dom
8
IPR003153
3,153
Adaptor protein Cbl, N-terminal helical
Adaptor_Cbl_N_hlx
Domain
4,312
false
false
This entry represents the N-terminal four-helical bundle domain. Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface. The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) dom...
[ "GO:0007166" ]
[ "cell surface receptor signaling pathway" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02262" ]
[ "Cbl_N" ]
[ 4312 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "2.3.2.27", "PWY-7511", "R-HSA-1059683", "R-HSA-1236382", "R-HSA-1295596", "R-HSA-1433559", "R-HSA-182971", "R-HSA-2173789", "R-HSA-5637810", "R-HSA-5654726", "R-HSA-5654727", "R-HSA-5654732", "R-HSA-5654733", "R-HSA-6807004", "R-HSA-8849469", "R-HSA-8856825", "R-HSA-8856828", "R-H...
[ "EC:2.3.2.27", "METACYC:PWY-7511", "REACTOME:R-HSA-1059683", "REACTOME:R-HSA-1236382", "REACTOME:R-HSA-1295596", "REACTOME:R-HSA-1433559", "REACTOME:R-HSA-182971", "REACTOME:R-HSA-2173789", "REACTOME:R-HSA-5637810", "REACTOME:R-HSA-5654726", "REACTOME:R-HSA-5654727", "REACTOME:R-HSA-5654732", ...
41
[ "1b47", "1fbv", "1yvh", "2cbl", "2y1m", "2y1n", "3bum", "3bun", "3buo", "3buw", "3bux", "3ob1", "3ob2", "3op0", "3pfv", "3plf", "3vgo", "3vrn", "3vro", "3vrp", "3vrq", "3vrr", "3zni", "4a4b", "4a4c", "4gpl", "5axi", "5hkw", "5hkx", "5hky", "5hkz", "5hl0"...
54
[ "PUB00019259", "PUB00055526" ]
[ "10078535", "18840649" ]
[ "Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.", "A Dictyostelium homologue of the metazoan Cbl proteins regulates STAT signalling." ]
[ 1999, 2008 ]
2
[]
[]
0
0
null
[ "Cas-NS-1 murine leukemia virus", "Opisthokonta" ]
[ 1, 4311 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 11, 3, 19, 11, 19 ]
6
true
Domain
Adaptor protein Cbl, N-terminal helical
Adaptor protein Cbl, N-terminal helical
Adaptor_Cbl_N_hlx
2
IPR003154
3,154
S1/P1 nuclease
S1/P1nuclease
Family
10,118
false
false
This family summarizes both S1 and P1 nucleases ( ) which cleave RNA and single stranded DNA with no base specificity [ ]. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups [ ]. Although its primary substrate is single-stranded, it may...
[ "GO:0003676", "GO:0004519", "GO:0006308" ]
[ "nucleic acid binding", "endonuclease activity", "DNA catabolic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02265", "PTHR33146", "cd11010" ]
[ "S1-P1_nuclease", "", "S1-P1_nuclease" ]
[ 10096, 9542, 9081 ]
3
[ "EC" ]
[ "3.1.30.1" ]
[ "EC:3.1.30.1" ]
1
[ "1ak0", "3sng", "3w52", "4cwm", "4cxo", "4cxp", "4cxv", "4dj4", "4jdg", "5fb9", "5fba", "5fbb", "5fbc", "5fbd", "5fbf", "5fbg", "7qta", "7qtb", "8qjl", "8qjm", "8qjn", "8qjo", "8qjp", "8qjq", "9emg" ]
25
[ "PUB00020287", "PUB00080593", "PUB00080594" ]
[ "9726413", "12586391", "6101052" ]
[ "Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs.", "Single-strand-specific nucleases.", "S1 nuclease of Aspergillus oryzae." ]
[ 1998, 2003, 1981 ]
3
[]
[]
0
0
null
[ "Ascovirus", "Bacteria", "Eukaryota", "metagenomes" ]
[ 8, 3990, 6067, 53 ]
4
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 28, 2, 14, 25 ]
4
true
Family
S1/P1 nuclease
S1/P1 nuclease
S1/P1nuclease
2
IPR003156
3,156
DHHA1 domain
DHHA1_dom
Domain
76,968
false
false
This domain is often found adjacent to the DHH domain ( ), and is called DHHA1 for DHH associated domain. DHHA1 is diagnostic of DHH subfamily 1 members [ ]. This domain is also found in alanyl tRNA synthetase (e.g., ), suggesting that it may have an RNA binding function. The domain is about 60 residues long and contai...
[ "GO:0003676" ]
[ "nucleic acid binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02272" ]
[ "DHHA1" ]
[ 76968 ]
1
[ "EC", "REACTOME" ]
[ "6.1.1.7", "R-HSA-379716" ]
[ "EC:6.1.1.7", "REACTOME:R-HSA-379716" ]
2
[ "1ir6", "2zvf", "2zxo", "2zxp", "2zxr", "3dev", "3g98", "3w5w", "3wqy", "3wqz", "4ls9", "4py9", "5cet", "5f54", "5f55", "5f56", "5ghr", "5ghs", "5ght", "5ipp", "5iuf", "5izo", "5j21", "5jju", "5o1u", "5o25", "5o4z", "5o58", "5o70", "5o7f", "5t5s", "5t76"...
55
[ "PUB00005478" ]
[ "9478130" ]
[ "A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3572, 66685, 5371, 45, 1295 ]
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",...
[ 11, 1, 2, 3, 2, 8, 6, 1, 5, 1, 1, 1, 20 ]
13
true
Domain
DHHA1 domain
DHHA1 domain
DHHA1_dom
4
IPR003157
3,157
Acyl transferase, LuxD
LuxD
Family
154
false
false
LuxD proteins are bacterial acyl transferases. Together with an acyl-protein synthetase (LuxE) and reductase (LuxC), they form a multienzyme complex. This complex channels activated fatty acids into the aldehyde substrate for the luciferase-catalyzed bacterial bioluminescence reaction [ , ].
[ "GO:0016746", "GO:0006631" ]
[ "acyltransferase activity", "fatty acid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF" ]
[ "MF_00774", "PF02273", "PIRSF009416" ]
[ "LuxD", "Acyl_transf_2", "LuxD" ]
[ 106, 154, 99 ]
3
[ "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"...
[ "2.3.1.-", "PWY-3602", "PWY-361", "PWY-4801", "PWY-4922", "PWY-5048", "PWY-5139", "PWY-5268", "PWY-5284", "PWY-5292", "PWY-5307", "PWY-5313", "PWY-5317", "PWY-5318", "PWY-5353", "PWY-5400", "PWY-5473", "PWY-5475", "PWY-5477", "PWY-5660", "PWY-5679", "PWY-5710", "PWY-5794"...
[ "EC:2.3.1.-", "METACYC:PWY-3602", "METACYC:PWY-361", "METACYC:PWY-4801", "METACYC:PWY-4922", "METACYC:PWY-5048", "METACYC:PWY-5139", "METACYC:PWY-5268", "METACYC:PWY-5284", "METACYC:PWY-5292", "METACYC:PWY-5307", "METACYC:PWY-5313", "METACYC:PWY-5317", "METACYC:PWY-5318", "METACYC:PWY-53...
219
[ "1tht" ]
1
[ "PUB00019098", "PUB00027988" ]
[ "8472957", "11018714" ]
[ "Sequence of the luxD gene encoding acyltransferase of the lux operon from Photobacterium leiognathi.", "Hyperactivity and interactions of a chimeric myristoryl-ACP thioesterase from the lux system of luminescent bacteria." ]
[ 1993, 2000 ]
2
[]
[]
0
0
null
[ "Bacteria" ]
[ 154 ]
1
[]
[]
0
true
Family
Acyl transferase, LuxD
Acyl transferase, LuxD
LuxD
5
IPR003158
3,158
Photosynthetic reaction centre, cytochrome c subunit
Photosyn_RC_cyt_c-su
Family
937
false
false
The photosynthetic apparatus in non-oxygenic bacteria consists of light-harvesting (LH) protein-pigment complexes LH1 and LH2, which use carotenoid and bacteriochlorophyll as primary donors [ ]. LH1 acts as the energy collection hub, temporarily storing it before its transfer to the photosynthetic reaction centre (RC) ...
[ "GO:0005506", "GO:0009055", "GO:0020037", "GO:0019684", "GO:0030077" ]
[ "iron ion binding", "electron transfer activity", "heme binding", "photosynthesis, light reaction", "plasma membrane light-harvesting complex" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
5
[ "NCBIFAM", "PFAM", "PIRSF", "CDD" ]
[ "NF040706", "PF02276", "PIRSF000017", "cd09224" ]
[ "photo_cyt_PufC", "CytoC_RC", "RC_cytochrome", "CytoC_RC" ]
[ 472, 937, 437, 488 ]
4
[]
[]
[]
0
[ "1dxr", "1eys", "1prc", "1r2c", "1vrn", "2i5n", "2jbl", "2prc", "2wjm", "2wjn", "2x5u", "2x5v", "3d38", "3g7f", "3prc", "3t6d", "3t6e", "3wmm", "4ac5", "4cas", "4v8k", "5b5m", "5b5n", "5m7j", "5m7k", "5m7l", "5nj4", "5o4c", "5o64", "5prc", "5y5s", "5yq7"...
75
[ "PUB00014111", "PUB00014116", "PUB00015279", "PUB00015395", "PUB00034760", "PUB00034761", "PUB00034762", "PUB00034765" ]
[ "11095707", "11005826", "2676514", "12872158", "15329728", "16931113", "8027023", "15155756" ]
[ "Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.", "Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described...
[ 2000, 2000, 1989, 2003, 2004, 2006, 1994, 2004 ]
8
[]
[]
0
0
null
[ "Bacteria", "Oesophagostomum dentatum", "ecological metagenomes" ]
[ 916, 2, 19 ]
3
[]
[]
0
true
Family
Photosynthetic reaction centre, cytochrome c subunit
Photosynthetic reaction centre, cytochrome c subunit
Photosyn_RC_cyt_c-su
3
IPR003159
3,159
Polysaccharide lyase family 8, central domain
Lyase_8_central_dom
Domain
5,811
false
false
Proteins containing this central domain consist of a group of secreted bacterial lyase enzymes capable of acting on a variety of substrates. One such enzyme is hyaluronate lyase, a Streptococcal surface enzyme that degrades hyaluronan and chondroitin, thereby helping to spread the bacteria throughout host tissues [ ]. ...
[ "GO:0016829", "GO:0005576" ]
[ "lyase activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02278" ]
[ "Lyase_8" ]
[ 5811 ]
1
[ "EC" ]
[ "4.2.2" ]
[ "EC:4.2.2" ]
1
[ "1c82", "1cb8", "1egu", "1f1s", "1f9g", "1hm2", "1hm3", "1hmu", "1hmw", "1hn0", "1i8q", "1j0m", "1j0n", "1loh", "1lxk", "1lxm", "1n7n", "1n7o", "1n7p", "1n7q", "1n7r", "1ojm", "1ojn", "1ojo", "1ojp", "1rw9", "1rwa", "1rwc", "1rwf", "1rwg", "1rwh", "1w3y"...
54
[ "PUB00014309", "PUB00014311", "PUB00014313", "PUB00014314" ]
[ "14523022", "10329169", "12706721", "12475987" ]
[ "Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action.", "Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.", "Crystal structure ...
[ 2003, 1999, 2003, 2003 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halomicrobium mukohataei", "Medusavirus stheno T3", "metagenomes" ]
[ 4847, 934, 3, 1, 26 ]
5
[]
[]
0
true
Domain
Polysaccharide lyase family 8, central domain
Polysaccharide lyase family 8, central domain
Lyase_8_central_dom
1
IPR003162
3,162
Transcription initiation factor TAFII31
TFIID-31
Family
5,450
false
false
Human transcription initiation factor TFIID is composed of the TATA-binding polypeptide (TBP) and at least 13 TBP-associated factors (TAFs) that collectively or individually are involved in activator-dependent transcription [ , , ]. This entry represents the N terminus of the 31kDa subunit (42kDa in Drosophila) of tran...
[ "GO:0006352" ]
[ "DNA-templated transcription initiation" ]
[ "biological_process" ]
1
[ "PFAM", "CDD" ]
[ "PF02291", "cd07979" ]
[ "TFIID-31kDa", "HFD_TAF9" ]
[ 5450, 5120 ]
2
[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "GenProp2052", "GenProp2054", "R-BTA-674695", "R-BTA-6804756", "R-BTA-6807505", "R-BTA-73776", "R-BTA-73779", "R-BTA-75953", "R-BTA-76042", "R-CEL-674695", "R-CEL-6807505", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953", "R-CEL-76042", "R-DME-5689880", "R-DME-674695", "R-DME-6804756",...
[ "GP:GenProp2052", "GP:GenProp2054", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6804756", "REACTOME:R-BTA-6807505", "REACTOME:R-BTA-73776", "REACTOME:R-BTA-73779", "REACTOME:R-BTA-75953", "REACTOME:R-BTA-76042", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6807505", "REACTOME:R-CEL-73776", "REACTOM...
65
[ "1taf", "6f3t", "6hqa", "6mzc", "6mzd", "6mzl", "6mzm", "6t9i", "6t9k", "6tb4", "6tbm", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7egd", "7ege", "7egf", "7egg", "7egi", "7egj", "7ena", "7enc", "7ktr", "7kts", "8gxq", "8gxs", "8h7g", "8wak"...
39
[ "PUB00006329", "PUB00014354", "PUB00020401", "PUB00079479", "PUB00079480", "PUB00079481", "PUB00079569" ]
[ "7667268", "11963920", "8598927", "19308322", "11295558", "10664584", "15899866" ]
[ "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors.", "A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription...
[ 1995, 2002, 1996, 2009, 2001, 2000, 2005 ]
7
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5450 ]
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...
[ 2, 1, 1, 2, 8, 7, 1, 6, 10, 1, 1, 9 ]
12
true
Family
Transcription initiation factor TAFII31
Transcription initiation factor TAFII31
TFIID-31
3
IPR003163
3,163
Transcription regulator HTH, APSES-type DNA-binding domain
Tscrpt_reg_HTH_APSES-type
Domain
8,775
false
false
The APSES domain, named after five founding members (ASM-1, Phd1, StuA, EFG1 and Sok2), is a sequence-specific DNA-binding domain of approximately 110 residues found in a family of fungal transcription factors and other DNA-binding proteins. This domain is often found in association with ankyrin repeats (see ) and a he...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51299" ]
[ "HTH_APSES" ]
[ 8775 ]
1
[]
[]
[]
0
[ "1bm8", "1l3g", "1mb1", "4ux5", "5ybx", "5yc2", "5yca", "6a6w" ]
8
[ "PUB00019159", "PUB00021230", "PUB00026907", "PUB00043683", "PUB00043684", "PUB00087159" ]
[ "9299332", "9083114", "12564929", "8913744", "9312029", "19948484" ]
[ "The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution.", "Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis.", "NMR structure of the DNA-binding domain o...
[ 1997, 1997, 2003, 1996, 1997, 2009 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 7, 8768 ]
2
[ "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)" ]
[ 5, 5, 4 ]
3
true
Domain
Transcription regulator HTH, APSES-type DNA-binding domain
Transcription regulator HTH, APSES-type DNA-binding domain
Tscrpt_reg_HTH_APSES-type
1
IPR003164
3,164
Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain
Clathrin_a-adaptin_app_sub_C
Domain
6,103
false
false
Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ...
[ "GO:0006886", "GO:0016192", "GO:0030131" ]
[ "intracellular protein transport", "vesicle-mediated transport", "clathrin adaptor complex" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF02296" ]
[ "Alpha_adaptin_C" ]
[ 6103 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-177504", "R-BTA-2132295", "R-BTA-416993", "R-BTA-437239", "R-BTA-5099900", "R-BTA-5140745", "R-BTA-6798695", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8866427", "R-BTA-8964038", "R-DDI-437239", "R-DDI-6798695", "R-DDI-8856825", "R-DDI-8856828", "R-DDI-8866427", "R-DDI-8964038",...
[ "REACTOME:R-BTA-177504", "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-416993", "REACTOME:R-BTA-437239", "REACTOME:R-BTA-5099900", "REACTOME:R-BTA-5140745", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8866427", "REACTOME:R-BTA-8964038", "REACTOME:R...
71
[ "1b9k", "1ky6", "1ky7", "1kyd", "1kyf", "1kyu", "1qtp", "1qts", "1w80", "2vj0", "3hs8", "6owt", "7ohi" ]
13
[ "PUB00010644", "PUB00011752", "PUB00011791", "PUB00035753", "PUB00035754", "PUB00035755", "PUB00035756", "PUB00035757", "PUB00035765", "PUB00035769" ]
[ "11080148", "12057195", "10430869", "17449236", "15107467", "12952931", "16542748", "17254016", "11598180", "15261670" ]
[ "Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.", "Accessory protein recruitment motifs in clathrin-mediated endocytosis.", "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.", "Do different en...
[ 2000, 2002, 1999, 2007, 2004, 2003, 2006, 2007, 2001, 2004 ]
10
[]
[]
0
0
null
[ "Eukaryota" ]
[ 6103 ]
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", "Schizosaccharomyces pombe (stra...
[ 9, 1, 6, 2, 7, 6, 1, 4, 11, 1, 45 ]
11
true
Domain
Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain
Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain
Clathrin_a-adaptin_app_sub_C
8
IPR003165
3,165
Piwi domain
Piwi
Domain
36,746
false
false
The Piwi domain [ ] is a protein domain found in piwi proteins and a large number of related nucleic acid-binding proteins, especially those that bind and cleave RNA. The function of the domain is double stranded-RNA-guided hydrolysis of single stranded-RNA, as has been determined in the argonaute family of related pro...
[ "GO:0003676" ]
[ "nucleic acid binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02171", "PS50822", "SM00950" ]
[ "Piwi", "PIWI", "Piwi" ]
[ 36137, 34974, 33572 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50822", "R-CEL-203927", "R-CEL-426486", "R-CEL-5578749", "R-DME-203927", "R-DME-426486", "R-DME-426496", "R-DME-5578749", "R-GGA-203927", "R-GGA-426486", "R-GGA-426496", "R-HSA-1912408", "R-HSA-203927", "R-HSA-2559580", "R-HSA-2559585", "R-HSA-4086398", "R-HSA-426486", "R-HSA-...
[ "PROSITEDOC:PDOC50822", "REACTOME:R-CEL-203927", "REACTOME:R-CEL-426486", "REACTOME:R-CEL-5578749", "REACTOME:R-DME-203927", "REACTOME:R-DME-426486", "REACTOME:R-DME-426496", "REACTOME:R-DME-5578749", "REACTOME:R-GGA-203927", "REACTOME:R-GGA-426486", "REACTOME:R-GGA-426496", "REACTOME:R-HSA-19...
54
[ "1u04", "1w9h", "1ytu", "1yvu", "1z25", "1z26", "2bgg", "2f8s", "2f8t", "2nub", "2w42", "2xdy", "2yha", "2yhb", "3dlb", "3dlh", "3f73", "3hjf", "3hk2", "3hm9", "3ho1", "3hvr", "3hxm", "3luc", "3lud", "3lug", "3luh", "3luj", "3luk", "3qx8", "3qx9", "3vna"...
175
[ "PUB00018283", "PUB00020128" ]
[ "11050429", "15284453" ]
[ "Domains in gene silencing and cell differentiation proteins: the novel PAZ domain and redefinition of the Piwi domain.", "Crystal structure of Argonaute and its implications for RISC slicer activity." ]
[ 2000, 2004 ]
2
[]
[ "IPR045246", "IPR057272" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 119, 971, 35644, 12 ]
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", "Schizosaccharomyces pombe (stra...
[ 48, 31, 22, 21, 25, 25, 3, 55, 30, 1, 280 ]
11
true
Domain
Piwi domain
Piwi domain
Piwi
1
IPR003166
3,166
Transcription factor TFIIE beta subunit, DNA-binding domain
TFIIE_bsu_DNA-bd
Domain
4,247
false
false
This entry represents the central core DNA-binding domain of the TFIIE beta subunit. Initiation of eukaryotic mRNA transcription requires melting of promoter DNA with the help of the general transcription factors TFIIE and TFIIH. In higher eukaryotes, the general transcription factor TFIIE consists of two subunits: the...
[ "GO:0006367" ]
[ "transcription initiation at RNA polymerase II promoter" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE", "CDD" ]
[ "PF02186", "PS51351", "cd07977" ]
[ "TFIIE_beta", "TFIIE_BETA_C", "TFIIE_beta_winged_helix" ]
[ 3586, 4178, 2254 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-DDI-674695", "R-DDI-6807505", "R-DDI-73776", "R-DDI-73779", "R-DDI-75953", "R-DDI-76042", "R-HSA-167161", "R-HSA-167162", "R-HSA-167172", "R-HSA-674695", "R-HSA-6807505", "R-HSA-73776", "R-HSA-73779", "R-HSA-75953", "R-HSA-76042", "R-MMU-674695", "R-MMU-6807505", "R-MMU-73776", ...
[ "REACTOME:R-DDI-674695", "REACTOME:R-DDI-6807505", "REACTOME:R-DDI-73776", "REACTOME:R-DDI-73779", "REACTOME:R-DDI-75953", "REACTOME:R-DDI-76042", "REACTOME:R-HSA-167161", "REACTOME:R-HSA-167162", "REACTOME:R-HSA-167172", "REACTOME:R-HSA-674695", "REACTOME:R-HSA-6807505", "REACTOME:R-HSA-73776...
33
[ "1d8j", "1d8k", "5fmf", "5fyw", "5fz5", "5iy6", "5iy7", "5iy8", "5iy9", "5iya", "5iyb", "5iyc", "5iyd", "5oqj", "5oqm", "5sva", "6gyl", "6gym", "6o9l", "7eg9", "7ega", "7egb", "7egc", "7ena", "7enc", "7lbm", "7ml0", "7ml1", "7ml2", "7ml4", "7nvr", "7nvs"...
69
[ "PUB00006521", "PUB00016689", "PUB00079518", "PUB00079519" ]
[ "10716934", "15808743", "19210545", "9348072" ]
[ "Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.", "The many faces of the helix-turn-helix domain: transcription regulation and beyond.", "Central forkhead domain of human TFIIE beta plays a primary role in binding double-stranded DNA at transcription initiati...
[ 2000, 2005, 2009, 1997 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "environmental samples" ]
[ 49, 4193, 5 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 7, 1, 1, 2, 3, 4, 1, 7, 3, 1, 1, 5 ]
12
true
Domain
Transcription factor TFIIE beta subunit, DNA-binding domain
Transcription factor TFIIE beta subunit, DNA-binding domain
TFIIE_bsu_DNA-bd
9
IPR003169
3,169
GYF domain
GYF
Domain
15,428
false
false
The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino acid domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic re...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF02213", "PS50829", "SM00444", "cd00072" ]
[ "GYF", "GYF", "GYF", "GYF" ]
[ 14276, 15299, 12996, 8084 ]
4
[ "PROSITEDOC" ]
[ "PDOC50829" ]
[ "PROSITEDOC:PDOC50829" ]
1
[ "1gyf", "1l2z", "1syx", "1wh2", "3fma", "3k3v", "4bws", "7rup", "7ruq", "8q7q", "8q7v", "8q7w", "8q7x", "8q91", "8rc0" ]
15
[ "PUB00011823", "PUB00011824", "PUB00011825" ]
[ "9843987", "10404223", "12426371" ]
[ "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation.", "The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences.", "Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules."...
[ 1998, 1999, 2002 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 31, 15394, 3 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 67, 6, 45, 2, 16, 12, 2, 18, 12, 3, 2, 157 ]
12
true
Domain
GYF domain
GYF domain
GYF
4
IPR003170
3,170
UDP-N-acetylenolpyruvoylglucosamine reductase
MurB
Family
28,129
false
false
Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes, which are also called UDP-N-acetylmuramate dehydrogenases. This enzyme is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis and consequently provides an attractive target for the design of antib...
[ "GO:0008762" ]
[ "UDP-N-acetylmuramate dehydrogenase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00037", "PTHR21071", "TIGR00179" ]
[ "MurB", "", "murB" ]
[ 27911, 27994, 25288 ]
3
[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC" ]
[ "1.3.1.98", "GenProp1448", "GenProp1623", "PWY-6386", "PWY-6387", "PWY-7953" ]
[ "EC:1.3.1.98", "GP:GenProp1448", "GP:GenProp1623", "METACYC:PWY-6386", "METACYC:PWY-6387", "METACYC:PWY-7953" ]
6
[ "1hsk", "1mbb", "1mbt", "1uxy", "2gqt", "2gqu", "2mbr", "2q85", "3i99", "3tx1", "4jay", "4jb1", "4pyt", "5jzx", "7or2", "7orz", "7osq", "9dtk" ]
18
[ "PUB00028012" ]
[ "7552726" ]
[ "An enzyme-substrate complex involved in bacterial cell wall biosynthesis." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 14, 27076, 421, 618 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
UDP-N-acetylenolpyruvoylglucosamine reductase
UDP-N-acetylenolpyruvoylglucosamine reductase
MurB
7
IPR003171
3,171
Methylenetetrahydrofolate reductase-like, catalytic domain
Mehydrof_redctse-like
Domain
32,802
false
false
This represents the catalytic domain of 5,10-methylenetetrahydrofolate reductase from prokaryotes and methylenetetrahydrofolate reductase (MTHFR) from eukaryotes ( ). Both generate 5-methyltetrahydrofolate from 5,10-methylenetetrahydrofolate. Mammalian and yeast MTHFRs are homodimers in which each subunit contains an N...
[ "GO:0004489", "GO:0006555" ]
[ "methylenetetrahydrofolate reductase [NAD(P)H] activity", "methionine metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "CDD" ]
[ "PF02219", "cd00537" ]
[ "MTHFR", "MTHFR" ]
[ 32777, 29037 ]
2
[ "EC", "EC", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.5.1", "1.5.1.54", "GenProp1356", "PWY-2201", "PWY-3841", "R-CEL-196757", "R-HSA-196757", "R-MMU-196757", "R-SCE-196757", "R-SPO-196757" ]
[ "EC:1.5.1", "EC:1.5.1.54", "GP:GenProp1356", "METACYC:PWY-2201", "METACYC:PWY-3841", "REACTOME:R-CEL-196757", "REACTOME:R-HSA-196757", "REACTOME:R-MMU-196757", "REACTOME:R-SCE-196757", "REACTOME:R-SPO-196757" ]
10
[ "1b5t", "1v93", "1zp3", "1zp4", "1zpt", "1zrq", "2fmn", "2fmo", "3apt", "3apy", "3fst", "3fsu", "3ijd", "5ume", "6fcx", "6fnu", "6pey", "7rml", "7th4", "7th5", "7xg9", "7xlf", "8eac", "8qa4", "8qa5", "8qa6", "8uy1", "8uy2" ]
28
[ "PUB00006438", "PUB00052921" ]
[ "10201405", "19610625" ]
[ "The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.", "Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli." ]
[ 1999, 2009 ]
2
[]
[ "IPR004621" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 238, 24647, 7198, 719 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 8, 1, 1, 1, 1, 15, 7, 2, 4, 8, 2, 2, 11 ]
13
true
Domain
Methylenetetrahydrofolate reductase-like, catalytic domain
Methylenetetrahydrofolate reductase-like, catalytic domain
Mehydrof_redctse-like
7
IPR003172
3,172
MD-2-related lipid-recognition domain
ML_dom
Domain
13,137
false
false
The MD-2-related lipid-recognition (ML) domain is implicated in lipid recognition, particularly in the recognition of pathogen related products. It has an immunoglobulin-like β-sandwich fold similar to that of E-set Ig domains. This domain is present in proteins from plants, animals and fungi, including the following p...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF02221", "SM00737" ]
[ "E1_DerP2_DerF2", "ML" ]
[ 12681, 11017 ]
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-6798695", "R-BTA-8964038", "R-CEL-6798695", "R-CEL-8964038", "R-DDI-6798695", "R-DDI-8964038", "R-DME-6798695", "R-DME-8964038", "R-DRE-6798695", "R-DRE-8964038", "R-HSA-1236974", "R-HSA-140534", "R-HSA-166016", "R-HSA-166058", "R-HSA-166166", "R-HSA-2562578", "R-HSA-5602498",...
[ "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8964038", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8964038", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-8964038", "REACTOME:R-DME-6798695", "REACTOME:R-DME-8964038", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-8964038", "REACTOME:R-HSA-1236974", "REACTOM...
50
[ "1a9v", "1ahk", "1ahm", "1g13", "1ktj", "1nep", "1pu5", "1pub", "1tjj", "1wrf", "1xwv", "2af9", "2ag2", "2ag4", "2ag9", "2agc", "2e56", "2e59", "2f08", "2hka", "2z64", "2z65", "3b2d", "3fxi", "3m7o", "3mtx", "3mu3", "3rg1", "3t6q", "3ula", "3vq1", "3vq2"...
52
[ "PUB00029036", "PUB00032538" ]
[ "12591954", "15710415" ]
[ "Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease.", "Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity." ]
[ 2003, 2005 ]
2
[]
[ "IPR033916", "IPR033917" ]
0
2
0
[ "Actinomycetes", "Eukaryota", "metagenomes" ]
[ 13, 13107, 17 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 42, 1, 7, 13, 18, 11, 1, 6, 13, 1, 1, 14 ]
12
true
Domain
MD-2-related lipid-recognition domain
MD-2-related lipid-recognition domain
ML_dom
3
IPR003173
3,173
Transcriptional coactivator p15 (PC4), C-terminal
PC4_C
Domain
9,084
false
false
This entry represents a ssDNA binding domain found at the C-terminal end of YdbC from Lactococcus lactis, Activated RNA polymerase II transcriptional coactivator p15 from humans and other PC4 family members. YdbC, which adopts a dimeric fold, shows a concave four-stranded antiparallel sheet followed by a C-terminal hel...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02229" ]
[ "PC4" ]
[ 9084 ]
1
[]
[]
[]
0
[ "1pcf", "2c62", "2l3a", "2ltd", "2ltt", "2phe", "3obh", "3pm7", "4agh", "4bg7", "4bhm", "4g06", "4usg", "5a4n", "5a4o", "5zg9", "5zkl", "5zkm", "6jip", "6jiq", "6ycs", "7e4w" ]
22
[ "PUB00006308", "PUB00011851", "PUB00063943", "PUB00100871" ]
[ "8062392", "9360603", "23303792", "34534740" ]
[ "A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators.", "C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site.", "Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain fam...
[ 1994, 1997, 2013, 2021 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "unclassified sequences" ]
[ 2283, 6478, 23, 209, 91 ]
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...
[ 18, 1, 3, 2, 5, 1, 1, 6, 3, 1, 1, 12 ]
12
true
Domain
Transcriptional coactivator p15 (PC4), C-terminal
Transcriptional coactivator p15 (PC4), C-terminal
PC4_C
5
IPR003174
3,174
Alpha trans-inducing protein (Alpha-TIF)
Alpha_TIF
Family
205
false
false
Alpha-TIF (VP16) from Herpes Simplex virus is an essential tegument protein involved in the transcriptional activation of viral immediate early (IE) promoters (alpha genes) during the lytic phase of viral infection. VP16 associates with cellular transcription factors to enhance transcription rates, including the genera...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "SMART" ]
[ "PF02232", "SM00814" ]
[ "Alpha_TIF", "Alpha_TIF" ]
[ 205, 204 ]
2
[]
[]
[]
0
[ "16vp" ]
1
[ "PUB00014315", "PUB00016635" ]
[ "12826401", "15654739" ]
[ "The herpes simplex virus VP16-induced complex: the makings of a regulatory switch.", "Structural properties of the promiscuous VP16 activation domain." ]
[ 2003, 2005 ]
2
[]
[]
0
0
null
[ "Gallus gallus", "Herpesvirales" ]
[ 1, 204 ]
2
[]
[]
0
true
Family
Alpha trans-inducing protein (Alpha-TIF)
Alpha trans-inducing protein (Alpha-TIF)
Alpha_TIF
6
IPR003175
3,175
Cyclin-dependent kinase inhibitor domain
CDI_dom
Domain
7,269
false
false
Cell cycle progression is negatively controlled by cyclin-dependent kinases inhibitors (CDIs). CDIs are involved in cell cycle arrest at the G1 phase. This entry represents a domain found in CDIs [ ].
[ "GO:0004861", "GO:0051726", "GO:0005634" ]
[ "cyclin-dependent protein serine/threonine kinase inhibitor activity", "regulation of cell cycle", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF02234" ]
[ "CDI" ]
[ 7269 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-HSA-187577", "R-HSA-198323", "R-HSA-2559582", "R-HSA-2559586", "R-HSA-5625900", "R-HSA-5674400", "R-HSA-6785807", "R-HSA-6804116", "R-HSA-69202", "R-HSA-69231", "R-HSA-69563", "R-HSA-69656", "R-HSA-69895", "R-HSA-8849470", "R-HSA-8852276", "R-HSA-8866911", "R-HSA-8878166", "R-HS...
[ "REACTOME:R-HSA-187577", "REACTOME:R-HSA-198323", "REACTOME:R-HSA-2559582", "REACTOME:R-HSA-2559586", "REACTOME:R-HSA-5625900", "REACTOME:R-HSA-5674400", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6804116", "REACTOME:R-HSA-69202", "REACTOME:R-HSA-69231", "REACTOME:R-HSA-69563", "REACTOME:R-HSA-...
43
[ "1jsu", "5uq3", "6ath", "6p8e", "6p8f", "6p8g", "6p8h", "7b5l", "7b5m", "7b5r", "8bya", "8byl", "8bzo" ]
13
[ "PUB00019281" ]
[ "7729683" ]
[ "Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 7269 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 31, 4, 8, 3, 19, 8, 11, 15, 24 ]
9
true
Domain
Cyclin-dependent kinase inhibitor domain
Cyclin-dependent kinase inhibitor domain
CDI_dom
1
IPR003176
3,176
Adenovirus DNA-binding, all-alpha domain
Adenovirus_DNA-bd_a
Domain
485
false
false
This entry represents a domain of the viral DNA-binding protein, a multi functional protein involved in DNA replication and transcription control [ ].
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02236" ]
[ "Viral_DNA_bi" ]
[ 485 ]
1
[]
[]
[]
0
[ "1adu", "1adv", "1anv", "2waz", "2wb0" ]
5
[ "PUB00007753" ]
[ "8039495" ]
[ "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Adenoviridae", "Streptomyces sioyaensis" ]
[ 484, 1 ]
2
[]
[]
0
true
Domain
Adenovirus DNA-binding, all-alpha domain
Adenovirus DNA-binding, all-alpha domain
Adenovirus_DNA-bd_a
5
IPR003177
3,177
Cytochrome c oxidase subunit VIIa, metazoa
Cytc_oxidase_su7a_met
Family
3,177
false
false
Cytochrome c oxidase ( ) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ ]. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plas...
[ "GO:0006123" ]
[ "mitochondrial electron transport, cytochrome c to oxygen" ]
[ "biological_process" ]
1
[ "PANTHER", "CDD" ]
[ "PTHR10510", "cd00928" ]
[ "", "Cyt_c_Oxidase_VIIa" ]
[ 3141, 2642 ]
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-5628897", "R-BTA-611105", "R-BTA-9707564", "R-BTA-9864848", "R-DME-5628897", "R-DME-611105", "R-DME-9707564", "R-DME-9864848", "R-DRE-5628897", "R-DRE-611105", "R-DRE-9707564", "R-HSA-5628897", "R-HSA-611105", "R-HSA-9707564", "R-HSA-9844594", "R-HSA-9864848", "R-MMU-5628897",...
[ "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9864848", "REACTOME:R-DME-5628897", "REACTOME:R-DME-611105", "REACTOME:R-DME-9707564", "REACTOME:R-DME-9864848", "REACTOME:R-DRE-5628897", "REACTOME:R-DRE-611105", "REACTOME:R-DRE-9707564", "REACTOME:R...
27
[ "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"...
109
[ "PUB00000581", "PUB00079539" ]
[ "6307356", "9752724" ]
[ "Structure of cytochrome c oxidase.", "Structural organization and transcription regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex." ]
[ 1983, 1998 ]
2
[ "IPR039297" ]
[ "IPR017267" ]
1
1
0
[ "Eumetazoa", "Pantoea vagans" ]
[ 3176, 1 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 5, 15, 9, 19 ]
5
true
Family
Cytochrome c oxidase subunit VIIa, metazoa
Cytochrome c oxidase subunit VIIa, metazoa
Cytc_oxidase_su7a_met
5
IPR003178
3,178
Methyl-coenzyme M reductase, gamma subunit
Me_CoM_Rdtase_gsu
Family
337
false
false
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-...
[ "GO:0050524", "GO:0015948" ]
[ "coenzyme-B sulfoethylthiotransferase activity", "methanogenesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "NCBIFAM", "CDD" ]
[ "PF02240", "PIRSF000264", "TIGR03259", "cd00539" ]
[ "MCR_gamma", "Meth_CoM_rd_gama", "met_CoM_red_gam", "MCR_gamma" ]
[ 337, 285, 336, 114 ]
4
[ "EC", "GP", "GP" ]
[ "2.8.4.1", "GenProp0719", "GenProp0722" ]
[ "EC:2.8.4.1", "GP:GenProp0719", "GP:GenProp0722" ]
3
[ "1e6v", "1e6y", "1hbm", "1hbn", "1hbo", "1hbu", "1mro", "3m1v", "3m2r", "3m2u", "3m2v", "3m30", "3m32", "3pot", "3sqg", "5a0y", "5a8k", "5a8r", "5a8w", "5g0r", "5n1q", "5n28", "5n2a", "7b1s", "7b2c", "7b2h", "7nkg", "7suc", "7sxm", "8gf5", "8gf6", "8s7v"...
39
[ "PUB00006391", "PUB00010614", "PUB00035993", "PUB00035994" ]
[ "9367957", "11491299", "16260307", "16234924" ]
[ "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.", "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.", "Methyl-coenzyme M reductase genes: unique functional ma...
[ 1997, 2001, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "ecological metagenomes" ]
[ 331, 6 ]
2
[]
[]
0
true
Family
Methyl-coenzyme M reductase, gamma subunit
Methyl-coenzyme M reductase, gamma subunit
Me_CoM_Rdtase_gsu
5
IPR003179
3,179
Methyl-coenzyme M reductase, beta subunit
Me_CoM_Rdtase_bsu
Family
307
false
false
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-...
[ "GO:0050524", "GO:0015948" ]
[ "coenzyme-B sulfoethylthiotransferase activity", "methanogenesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "NCBIFAM" ]
[ "PIRSF000263", "TIGR03257" ]
[ "Meth_CoM_rd_beta", "met_CoM_red_bet" ]
[ 274, 306 ]
2
[ "EC", "GP", "GP" ]
[ "2.8.4.1", "GenProp0719", "GenProp0722" ]
[ "EC:2.8.4.1", "GP:GenProp0719", "GP:GenProp0722" ]
3
[ "1e6v", "1e6y", "1hbm", "1hbn", "1hbo", "1hbu", "1mro", "3m1v", "3m2r", "3m2u", "3m2v", "3m30", "3m32", "3pot", "3sqg", "5a0y", "5a8k", "5a8r", "5a8w", "5g0r", "5n1q", "5n28", "5n2a", "7b2h", "7nkg", "7suc", "7sxm", "8gf5", "8gf6", "8s7v", "8s7x", "9ecn"...
37
[ "PUB00006391", "PUB00010614", "PUB00035993", "PUB00035994" ]
[ "9367957", "11491299", "16260307", "16234924" ]
[ "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.", "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.", "Methyl-coenzyme M reductase genes: unique functional ma...
[ 1997, 2001, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "ecological metagenomes" ]
[ 301, 6 ]
2
[]
[]
0
true
Family
Methyl-coenzyme M reductase, beta subunit
Methyl-coenzyme M reductase, beta subunit
Me_CoM_Rdtase_bsu
1
IPR003180
3,180
Methylpurine-DNA glycosylase
MPG
Family
13,768
false
false
Methylpurine-DNA glycosylase (MPG, or alkyladenine DNA glycosylase (AAG)) is a base excision-repair protein, catalyzing the first step in base excision repair by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. MPG bends DNA by intercalating between the base pairs, causing the damaged ba...
[ "GO:0003677", "GO:0003905", "GO:0006284" ]
[ "DNA binding", "alkylbase DNA N-glycosylase activity", "base-excision repair" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00527", "PF02245", "PTHR10429", "TIGR00567", "cd00540" ]
[ "3MGH", "Pur_DNA_glyco", "", "3mg", "AAG" ]
[ 13273, 13751, 13661, 12224, 12677 ]
5
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.2.2.-", "PWY-2681", "PWY-5316", "PWY-5381", "PWY-7342", "PWY-7564", "PWY-8106", "R-HSA-110330", "R-HSA-110331", "R-HSA-110357", "R-MMU-110331", "R-MMU-110357", "R-RNO-110331", "R-RNO-110357" ]
[ "EC:3.2.2.-", "METACYC:PWY-2681", "METACYC:PWY-5316", "METACYC:PWY-5381", "METACYC:PWY-7342", "METACYC:PWY-7564", "METACYC:PWY-8106", "REACTOME:R-HSA-110330", "REACTOME:R-HSA-110331", "REACTOME:R-HSA-110357", "REACTOME:R-MMU-110331", "REACTOME:R-MMU-110357", "REACTOME:R-RNO-110331", "REACT...
14
[ "1bnk", "1ewn", "1f4r", "1f6o", "3qi5", "3uby", "7xfh", "7xfj", "7xfm" ]
9
[ "PUB00014119", "PUB00016253", "PUB00020209", "PUB00043337", "PUB00043338", "PUB00043339", "PUB00079895", "PUB00079896", "PUB00079897", "PUB00079898", "PUB00079899", "PUB00079900", "PUB00079901" ]
[ "11106395", "11554308", "9790531", "18191412", "17768096", "17716976", "10440863", "14567703", "14688248", "15990363", "12077143", "14555760", "12323378" ]
[ "Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG.", "Crystallizing thoughts about DNA base excision repair.", "Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision.", "Expr...
[ 2000, 2001, 1998, 2008, 2008, 2007, 1999, 2003, 2004, 2005, 2002, 2003, 2002 ]
13
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Yasminevirus sp. GU-2018", "metagenomes" ]
[ 147, 11394, 2095, 1, 131 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 5, 2, 3, 3, 4, 5, 4 ]
7
true
Family
Methylpurine-DNA glycosylase
Methylpurine-DNA glycosylase
MPG
2
IPR003181
3,181
Large coat protein
Como_LCP
Family
327
false
false
The virus capsid is composed 60 icosahedral units, each of which is composed of one copy of each of the two coat proteins. This family contains the large coat protein (LCP) [ ] of the comoviridae viral family.
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02247" ]
[ "Como_LCP" ]
[ 327 ]
1
[]
[]
[]
0
[ "1bmv", "1ny7", "1pgl", "1pgw", "2bfu", "5a32", "5a33", "5fmo", "5ms1", "5msh", "6qcc", "6qoz" ]
12
[ "PUB00006271" ]
[ "1546463" ]
[ "Nucleotide sequence and genetic map of cowpea severe mosaic virus RNA 2 and comparisons with RNA 2 of other comoviruses." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Arthrobacter bussei", "Cuscuta campestris", "Viruses" ]
[ 1, 1, 325 ]
3
[]
[]
0
true
Family
Large coat protein
Large coat protein
Como_LCP
4
IPR003182
3,182
RNA2 polyprotein
RNA2_polyprotein
Family
257
false
false
RNA2 is a polyprotein movement protein: transports viral genome to neighbouring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. It acts by forming a tubular structure at the host plasmodesmata, enl...
[ "GO:0046740", "GO:0019028", "GO:0044219" ]
[ "transport of virus in host, cell to cell", "viral capsid", "host cell plasmodesma" ]
[ "biological_process", "cellular_component", "cellular_component" ]
3
[ "PFAM" ]
[ "PF02248" ]
[ "Como_SCP" ]
[ 257 ]
1
[]
[]
[]
0
[ "1bmv", "1ny7", "1pgl", "1pgw", "2bfu", "5a32", "5a33", "5fmo", "5ms1", "5msh", "6qcc", "6qoz" ]
12
[ "PUB00066849", "PUB00066850", "PUB00066851" ]
[ "10049828", "15483261", "14722313" ]
[ "The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation.", "Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing.", "The movement protein of cowpea mosaic virus binds GTP and s...
[ 1999, 2004, 2004 ]
3
[]
[]
0
0
null
[ "Arthrobacter bussei", "Comovirinae" ]
[ 1, 256 ]
2
[]
[]
0
true
Family
RNA2 polyprotein
RNA2 polyprotein
RNA2_polyprotein
5
IPR003183
3,183
Methyl-coenzyme M reductase, alpha subunit, N-terminal
Me_CoM_Rdtase_asu_N
Domain
1,870
false
false
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-...
[ "GO:0050524", "GO:0015948" ]
[ "coenzyme-B sulfoethylthiotransferase activity", "methanogenesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02745" ]
[ "MCR_alpha_N" ]
[ 1870 ]
1
[ "EC" ]
[ "2.8.4.1" ]
[ "EC:2.8.4.1" ]
1
[ "1e6v", "1e6y", "1hbm", "1hbn", "1hbo", "1hbu", "1mro", "3m1v", "3m2r", "3m2u", "3m2v", "3m30", "3m32", "3pot", "3sqg", "5a0y", "5a8k", "5a8r", "5a8w", "5g0r", "5n1q", "5n28", "5n2a", "7b1s", "7b2c", "7b2h", "7nkg", "7suc", "7sxm", "8gf5", "8gf6", "8s7v"...
39
[ "PUB00006391", "PUB00010614", "PUB00035993", "PUB00035994" ]
[ "9367957", "11491299", "16260307", "16234924" ]
[ "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.", "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.", "Methyl-coenzyme M reductase genes: unique functional ma...
[ 1997, 2001, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "unclassified sequences", "uncultured rumen bacterium" ]
[ 1720, 133, 17 ]
3
[]
[]
0
true
Domain
Methyl-coenzyme M reductase, alpha subunit, N-terminal
Methyl-coenzyme M reductase, alpha subunit, N-terminal
Me_CoM_Rdtase_asu_N
6
IPR003184
3,184
Viral chemokine binding protein
Orthopox_35kDa
Family
410
false
false
This entry represents a family of proteins from poxviruses, including Protein OPG170 from Vaccinia virus (also known as A41) and Protein T1 from Rabbit fibroma virus. These secreted proteins interact with members of both the CC and CXC superfamilies of chemokines [ ]. It has been suggested that these secreted proteins ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02250" ]
[ "Orthopox_35kD" ]
[ 410 ]
1
[]
[]
[]
0
[ "1cq3", "2ffk", "2fin", "2grk", "2vga", "4p5i", "4zk9", "4zkb", "4zkc", "5d28", "8jc6" ]
11
[ "PUB00006369", "PUB00049719" ]
[ "9123853", "18208323" ]
[ "The T1/35kDa family of poxvirus-secreted proteins bind chemokines and modulate leukocyte influx into virus-infected tissues.", "Structure and function of A41, a vaccinia virus chemokine binding protein." ]
[ 1997, 2008 ]
2
[]
[ "IPR009173" ]
0
1
0
[ "Chordopoxvirinae" ]
[ 410 ]
1
[]
[]
0
true
Family
Viral chemokine binding protein
Viral chemokine binding protein
Orthopox_35kDa
2
IPR003185
3,185
Proteasome activator PA28, N-terminal domain
Proteasome_activ_PA28_N
Domain
3,628
false
false
The specificity of the 20S proteasome, which degrades many intracellular proteins, is regulated by protein complexes that bind to one or both ends of the cylindrical proteasome structure. Proteasome activator 28 (PA28), also known as 11S regulator or REG, is one of these complexes. PA28 binds to the 20S proteasome and ...
[ "GO:0008537" ]
[ "proteasome activator complex" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF02251" ]
[ "PA28_N" ]
[ 3628 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1236974", "R-BTA-1236978", "R-BTA-9907900", "R-BTA-9912633", "R-GGA-9907900", "R-HSA-1236974", "R-HSA-1236978", "R-HSA-8950505", "R-HSA-9907900", "R-HSA-9912633", "R-MMU-1236974", "R-MMU-1236978", "R-MMU-9907900", "R-MMU-9912633", "R-RNO-1236974", "R-RNO-1236978", "R-RNO-99079...
[ "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-9907900", "REACTOME:R-BTA-9912633", "REACTOME:R-GGA-9907900", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1236978", "REACTOME:R-HSA-8950505", "REACTOME:R-HSA-9907900", "REACTOME:R-HSA-9912633", "REACTOME:R-MMU-1236974", "REACTOM...
22
[ "1avo", "5msj", "5msk", "5mx5", "7dr6", "7drw", "7nao", "7nap", "7yqc", "7yqd", "8cxb" ]
11
[ "PUB00013234", "PUB00033208", "PUB00033209" ]
[ "9403698", "11147828", "9346951" ]
[ "Structure of the proteasome activator REGalpha (PA28alpha).", "Properties of the beta subunit of the proteasome activator PA28 (11S REG).", "Relative functions of the alpha and beta subunits of the proteasome activator, PA28." ]
[ 1997, 2000, 1997 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3628 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 1, 16, 14, 22 ]
6
true
Domain
Proteasome activator PA28, N-terminal domain
Proteasome activator PA28, N-terminal domain
Proteasome_activ_PA28_N
6
IPR003186
3,186
Proteasome activator PA28, C-terminal domain
PA28_C
Domain
4,890
false
false
The specificity of the 20S proteasome, which degrades many intracellular proteins, is regulated by protein complexes that bind to one or both ends of the cylindrical proteasome structure. Proteasome activator 28 (PA28), also known as 11S regulator or REG, is one of these complexes. PA28 binds to the 20S proteasome and ...
[ "GO:0008537" ]
[ "proteasome activator complex" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF02252" ]
[ "PA28_C" ]
[ 4890 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1236974", "R-BTA-1236978", "R-BTA-9907900", "R-BTA-9912633", "R-DDI-1236974", "R-DDI-1236978", "R-DDI-9907900", "R-DDI-9912633", "R-GGA-9907900", "R-HSA-1236974", "R-HSA-1236978", "R-HSA-8950505", "R-HSA-9907900", "R-HSA-9912633", "R-MMU-1236974", "R-MMU-1236978", "R-MMU-99079...
[ "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-9907900", "REACTOME:R-BTA-9912633", "REACTOME:R-DDI-1236974", "REACTOME:R-DDI-1236978", "REACTOME:R-DDI-9907900", "REACTOME:R-DDI-9912633", "REACTOME:R-GGA-9907900", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1236978", "REACTOM...
26
[ "1avo", "1fnt", "1ya7", "1yar", "1yau", "1z7q", "3ipm", "3jrm", "3jse", "3jtl", "5msj", "5msk", "5mx5", "6dfk", "6muv", "6mux", "6utg", "6uth", "6utj", "6xmj", "7dr6", "7drw", "7nao", "7nap", "7yqc", "7yqd", "8cxb" ]
27
[ "PUB00013234", "PUB00033208", "PUB00033209" ]
[ "9403698", "11147828", "9346951" ]
[ "Structure of the proteasome activator REGalpha (PA28alpha).", "Properties of the beta subunit of the proteasome activator PA28 (11S REG).", "Relative functions of the alpha and beta subunits of the proteasome activator, PA28." ]
[ 1997, 2000, 1997 ]
3
[]
[]
0
0
null
[ "Eukaryota", "Rhodobacter flavimaris" ]
[ 4889, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 1, 25, 16, 24 ]
6
true
Domain
Proteasome activator PA28, C-terminal domain
Proteasome activator PA28, C-terminal domain
PA28_C
5
IPR003187
3,187
Phospholipase A1
PLipase_A1
Family
5,500
false
false
Outer membrane phospholipase A (OMPLA) is an integral membrane phospholipase, which is present in many Gram-negative bacteria and has a broad substrate specificity . The role of OMPLA has been most thoroughly studied in Escherichia coli, where it participates in the secretion of bacteriocins. Bacteriocin release is tri...
[ "GO:0004620", "GO:0006629", "GO:0016020" ]
[ "glycerophospholipase activity", "lipid metabolic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PANTHER", "CDD" ]
[ "PF02253", "PR01486", "PTHR40457", "cd00541" ]
[ "PLA1", "PHPHLIPASEA1", "", "OMPLA" ]
[ 5496, 5387, 5476, 3902 ]
4
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "3.1.1.32", "3.1.1.4", "PWY-6803", "PWY-7409", "PWY-7416", "PWY-7417", "PWY-7783", "PWY-8051", "PWY-8053", "PWY-8355", "PWY-8356", "PWY-8357", "PWY-8395", "PWY-8396", "PWY-8397", "PWY-8398", "PWY-8399", "PWY-8400", "PWY-8410", "PWY-8411", "PWY-8412", "PWY-8413" ]
[ "EC:3.1.1.32", "EC:3.1.1.4", "METACYC:PWY-6803", "METACYC:PWY-7409", "METACYC:PWY-7416", "METACYC:PWY-7417", "METACYC:PWY-7783", "METACYC:PWY-8051", "METACYC:PWY-8053", "METACYC:PWY-8355", "METACYC:PWY-8356", "METACYC:PWY-8357", "METACYC:PWY-8395", "METACYC:PWY-8396", "METACYC:PWY-8397",...
22
[ "1fw2", "1fw3", "1ild", "1ilz", "1im0", "1qd5", "1qd6", "7ezz" ]
8
[ "PUB00011129", "PUB00018812", "PUB00079628" ]
[ "12615538", "11080680", "10322034" ]
[ "Detergent organisation in crystals of monomeric outer membrane phospholipase A.", "Bacterial phospholipase A: structure and function of an integral membrane phospholipase.", "Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo." ]
[ 2003, 2000, 1999 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 5446, 9, 45 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Phospholipase A1
Phospholipase A1
PLipase_A1
6
IPR003188
3,188
Phosphotransferase system, lactose/cellobiose-type IIA subunit
PTS_IIA_lac/cel
Family
9,313
false
false
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars...
[ "GO:0009401" ]
[ "phosphoenolpyruvate-dependent sugar phosphotransferase system" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF", "PROFILE", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF02255", "PIRSF000699", "PS51095", "PTHR34382", "TIGR00823", "cd00215" ]
[ "PTS_IIA", "PTS_IILac_III", "PTS_EIIA_TYPE_3", "", "EIIA-LAC", "PTS_IIA_lac" ]
[ 9309, 8919, 9128, 9250, 613, 7387 ]
6
[ "GP", "PROSITEDOC" ]
[ "GenProp0119", "PDOC00528" ]
[ "GP:GenProp0119", "PROSITEDOC:PDOC00528" ]
2
[ "1e2a", "1wcr", "2e2a", "2lrk", "2lrl", "2wwv", "2wy2", "3k1s", "3l8r" ]
9
[ "PUB00000073", "PUB00002162", "PUB00003612", "PUB00006380", "PUB00017027", "PUB00017028" ]
[ "2197982", "1537788", "8246840", "9261069", "7815935", "11361063" ]
[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.", "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "The structure of en...
[ 1990, 1992, 1993, 1997, 1994, 2001 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanosarcina mazei", "unclassified sequences" ]
[ 9280, 7, 1, 25 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Phosphotransferase system, lactose/cellobiose-type IIA subunit
Phosphotransferase system, lactose/cellobiose-type IIA subunit
PTS_IIA_lac/cel
6
IPR003189
3,189
Shiga-like toxin, beta subunit
SLT_beta
Family
273
false
false
This family represents the B subunit of shiga-like toxin (SLT or verotoxin) produced by some strains of Escherichia coli associated with hemorrhagic colitis and hemolytic uremic syndrome. SLT s are composed of one enzymatic A subunit and five cell binding B subunits [ ].
[ "GO:0019836", "GO:0005576" ]
[ "symbiont-mediated hemolysis of host erythrocyte", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02258" ]
[ "SLT_beta" ]
[ 273 ]
1
[]
[]
[]
0
[ "1bos", "1c48", "1c4q", "1cqf", "1czg", "1czw", "1d1i", "1d1k", "1dm0", "1qnu", "1qoh", "1r4p", "1r4q", "2bos", "2c5c", "2ga4", "2xsc", "3mxg", "4m1u", "4p2c", "4ull", "6fe4", "6u3u", "6x6h", "7d6q", "7d6r", "7u6v", "7ujj", "7vhc", "7vhd", "7vhe", "7vhf"...
34
[ "PUB00020348" ]
[ "10745005" ]
[ "A mutant Shiga-like toxin IIe bound to its receptor Gb(3): structure of a group II Shiga-like toxin with altered binding specificity." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Gammaproteobacteria", "Viruses" ]
[ 175, 98 ]
2
[]
[]
0
true
Family
Shiga-like toxin, beta subunit
Shiga-like toxin, beta subunit
SLT_beta
3
IPR003190
3,190
Aspartate decarboxylase
Asp_decarbox
Family
14,737
false
false
Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme L-aspartate decarboxylase (ADC, ). Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The enzyme is translated as an inactive proenzyme...
[ "GO:0004068", "GO:0006523" ]
[ "aspartate 1-decarboxylase activity", "alanine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00446", "PF02261", "PIRSF006246", "PTHR21012", "TIGR00223", "cd06919" ]
[ "PanD", "Asp_decarbox", "Asp_decarbox", "", "panD", "Asp_decarbox" ]
[ 14610, 14737, 13397, 14704, 14444, 14436 ]
6
[ "EC", "GP", "GP", "METACYC" ]
[ "4.1.1.11", "GenProp0124", "GenProp1601", "PWY-5155" ]
[ "EC:4.1.1.11", "GP:GenProp0124", "GP:GenProp1601", "METACYC:PWY-5155" ]
4
[ "1aw8", "1ppy", "1pqe", "1pqf", "1pqh", "1pt0", "1pt1", "1pyq", "1pyu", "1uhd", "1uhe", "1vc3", "2c45", "2eeo", "3oug", "3plx", "3tm7", "4aok", "4aon", "4azd", "4cry", "4crz", "4cs0", "4d7z", "5ls7", "6oyy", "6oz8", "6p02", "6p1y", "6rxh", "7a8y" ]
31
[ "PUB00011777", "PUB00019168", "PUB00022472", "PUB00031775", "PUB00039881", "PUB00070769", "PUB00079743" ]
[ "10368289", "9546220", "14633979", "15184017", "17001646", "9169598", "3003510" ]
[ "A six-stranded double-psi beta barrel is shared by several protein superfamilies.", "Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.", "Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.", "Crystal ...
[ 1999, 1998, 2003, 2004, 2006, 1997, 1985 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Gordonia phage Jace", "unclassified sequences" ]
[ 28, 14446, 26, 1, 236 ]
5
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 1, 1 ]
2
true
Family
Aspartate decarboxylase
Aspartate decarboxylase
Asp_decarbox
2
IPR003191
3,191
Guanylate-binding protein/Atlastin, C-terminal
Guanylate-bd/ATL_C
Domain
10,438
false
false
Guanylate-binding protein is a GTPase that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-kd GTPases, the Mx proteins, and the large 65- to 67-kd GTPases. Guanylate-...
[ "GO:0003924", "GO:0005525" ]
[ "GTPase activity", "GTP binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF02841" ]
[ "GBP_C" ]
[ 10438 ]
1
[ "EC", "REACTOME", "REACTOME" ]
[ "3.6.5.-", "R-HSA-877300", "R-HSA-909733" ]
[ "EC:3.6.5.-", "REACTOME:R-HSA-877300", "REACTOME:R-HSA-909733" ]
3
[ "1dg3", "1f5n", "2b8w", "2b92", "2bc9", "2d4h", "5vgr", "6k1z", "6k2d", "6loj", "6vkj", "7ckf", "7e58", "7e59", "7e5a", "7m1s", "8cqb", "8q4l", "8r1a" ]
19
[ "PUB00035996", "PUB00035997", "PUB00053138" ]
[ "17266443", "16936281", "19665976" ]
[ "Unique features of different members of the human guanylate-binding protein family.", "Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis.", "A class of dynamin-like GTPases involved in the generation of th...
[ 2007, 2006, 2009 ]
3
[]
[ "IPR037684" ]
0
1
0
[ "Eukaryota" ]
[ 10438 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 14, 3, 43, 32, 34, 12, 28, 55 ]
8
true
Domain
Guanylate-binding protein/Atlastin, C-terminal
Guanylate-binding protein/Atlastin, C-terminal
Guanylate-bd/ATL_C
2
IPR003192
3,192
Porin, LamB-type
Porin_LamB
Family
6,552
false
false
Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel β-barrel [ ]. Loop 3 folds into the core to constrict pore size. Long irregular loops are found on the extracelllul...
[ "GO:0015288", "GO:0034219", "GO:0016020" ]
[ "porin activity", "carbohydrate transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "CDD" ]
[ "PF02264", "cd01346" ]
[ "LamB", "Maltoporin-like" ]
[ 6552, 3943 ]
2
[]
[]
[]
0
[ "1a0s", "1a0t", "1af6", "1mal", "1mpm", "1mpn", "1mpo", "1mpq", "1mpr", "1oh2", "2mpr", "8b7v", "8xcj" ]
13
[ "PUB00006315", "PUB00023232", "PUB00027409", "PUB00061720" ]
[ "7824948", "9437428", "9102468", "1649946" ]
[ "Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution.", "Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose.", "Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.", "A sugar-speci...
[ 1995, 1998, 1997, 1991 ]
4
[]
[ "IPR023738" ]
0
1
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 6537, 8, 7 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Porin, LamB-type
Porin, LamB-type
Porin_LamB
5
IPR003193
3,193
ADP-ribosyl cyclase (CD38/157)
ADP-ribosyl_cyclase
Family
2,302
false
false
CD38, the HUGO gene name, is also called T10 or ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase ( ). CD38 is a novel enzyme capable of catalysing multiple reactions, including NAD glycohydrolase, ADP-ribosyl cyclase, cyclic ADP ribose hydrolase and base-exchange activities. Two of the enzymatic products, cyclic ADP-rib...
[ "GO:0061809" ]
[ "NAD+ nucleosidase activity, cyclic ADP-ribose generating" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02267", "PTHR10912", "cd04759" ]
[ "Rib_hydrolayse", "", "Rib_hydrolase" ]
[ 2302, 2253, 1354 ]
3
[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.4.99.20", "3.2.2.-", "3.2.2.6", "PWY-2681", "PWY-5316", "PWY-5381", "PWY-7342", "PWY-7564", "PWY-8106", "R-HSA-163125", "R-HSA-196807", "R-HSA-6798695", "R-MMU-163125", "R-MMU-196807", "R-MMU-6798695", "R-RNO-163125", "R-RNO-196807", "R-RNO-6798695" ]
[ "EC:2.4.99.20", "EC:3.2.2.-", "EC:3.2.2.6", "METACYC:PWY-2681", "METACYC:PWY-5316", "METACYC:PWY-5381", "METACYC:PWY-7342", "METACYC:PWY-7564", "METACYC:PWY-8106", "REACTOME:R-HSA-163125", "REACTOME:R-HSA-196807", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-163125", "REACTOME:R-MMU-196807", ...
18
[ "1isf", "1isg", "1ish", "1isi", "1isj", "1ism", "1lbe", "1r0s", "1r12", "1r15", "1r16", "1yh3", "1zvm", "2ef1", "2eg9", "2hct", "2i65", "2i66", "2i67", "2o3q", "2o3r", "2o3s", "2o3t", "2o3u", "2pgj", "2pgl", "3dzf", "3dzg", "3dzh", "3dzi", "3dzj", "3dzk"...
85
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 8, 2294 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 12, 6, 7 ]
4
true
Family
ADP-ribosyl cyclase (CD38/157)
ADP-ribosyl cyclase (CD38/157)
ADP-ribosyl_cyclase
6
IPR003194
3,194
Transcription initiation factor IIA, gamma subunit
TFIIA_gsu
Family
4,725
false
false
Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-in...
[ "GO:0006367", "GO:0005672" ]
[ "transcription initiation at RNA polymerase II promoter", "transcription factor TFIIA complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PIRSF", "PANTHER" ]
[ "PIRSF009415", "PTHR10966" ]
[ "Hum_TFIIA_gamma", "" ]
[ 3944, 4725 ]
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-CEL-674695", "R-CEL-6807505", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953", "R-CEL-76042", "R-DDI-674695", "R-DDI-6807505", "R-DDI-73776", "R-DDI-73779", "R-DDI-75953", "R-DDI-76042", "R-DDI-9018519", "R-DME-674695", "R-DME-6807505", "R-DME-73776", "R-DME-73779", "R-DME-75953", ...
[ "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6807505", "REACTOME:R-CEL-73776", "REACTOME:R-CEL-73779", "REACTOME:R-CEL-75953", "REACTOME:R-CEL-76042", "REACTOME:R-DDI-674695", "REACTOME:R-DDI-6807505", "REACTOME:R-DDI-73776", "REACTOME:R-DDI-73779", "REACTOME:R-DDI-75953", "REACTOME:R-DDI-76042", ...
58
[ "1nh2", "1nvp", "1rm1", "1ytf", "5fmf", "5fur", "5fyw", "5fz5", "5iy6", "5iy7", "5iy8", "5iy9", "5iya", "5iyb", "5iyc", "5iyd", "5oqj", "5oqm", "5sva", "6gyk", "6gyl", "6gym", "6mzm", "6o9l", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7egd"...
84
[ "PUB00013248", "PUB00013320" ]
[ "12818428", "8610010" ]
[ "TFIIA abrogates the effects of inhibition by HMGB1 but not E1A during the early stages of assembly of the transcriptional preinitiation complex.", "Crystal structure of a yeast TFIIA/TBP/DNA complex." ]
[ 2003, 1996 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4725 ]
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...
[ 4, 2, 1, 4, 5, 9, 2, 4, 11, 1, 1, 7 ]
12
true
Family
Transcription initiation factor IIA, gamma subunit
Transcription initiation factor IIA, gamma subunit
TFIIA_gsu
4
IPR003195
3,195
Transcription initiation factor IID, subunit 13
TFIID_TAF13
Family
8,159
false
false
This family includes the Spt3 yeast transcription factors and the 18kDa subunit from human transcription initiation factor IID, known as TAF13 or TAFII18. Determination of the crystal structure reveals an atypical histone fold [ ]. TBP-associated factor 13 (TAF13) is one of several TAFs that bind TBP and is involved in...
[ "GO:0006366" ]
[ "transcription by RNA polymerase II" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02269", "PTHR11380" ]
[ "TFIID-18kDa", "" ]
[ 7851, 7929 ]
2
[ "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2053", "GenProp2054", "GenProp2057", "R-DDI-674695", "R-DDI-6807505", "R-DDI-73776", "R-DDI-73779", "R-DDI-75953", "R-DDI-76042", "R-HSA-167161", "R-HSA-167162", "R-HSA-167172", "R-HSA-3214847", "R-HSA-674695", "R-HSA-6804756", "R-HSA-6807505", "R-HSA-73776", "R-HSA-73779",...
[ "GP:GenProp2053", "GP:GenProp2054", "GP:GenProp2057", "REACTOME:R-DDI-674695", "REACTOME:R-DDI-6807505", "REACTOME:R-DDI-73776", "REACTOME:R-DDI-73779", "REACTOME:R-DDI-75953", "REACTOME:R-DDI-76042", "REACTOME:R-HSA-167161", "REACTOME:R-HSA-167162", "REACTOME:R-HSA-167172", "REACTOME:R-HSA-...
39
[ "1bh8", "1bh9", "6hqa", "6mzd", "6mzl", "6t9i", "6t9k", "6tb4", "6tbm", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7egd", "7ege", "7egf", "7egi", "7egj", "7ena", "7enc", "7ktr", "7kts", "8gxq", "8gxs", "8h7g", "8wak", "8wal", "8wan", "8wao"...
36
[ "PUB00006419" ]
[ "9695952" ]
[ "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Ectocarpus siliculosus virus 1 (isolate New Zealand/Kaikoura/1988)", "Eukaryota" ]
[ 2, 8157 ]
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, 2, 4, 3, 8, 6, 2, 3, 17, 2, 2, 6 ]
12
true
Family
Transcription initiation factor IID, subunit 13
Transcription initiation factor IID, subunit 13
TFIID_TAF13
7
IPR003196
3,196
Transcription initiation factor IIF, beta subunit
TFIIF_beta
Family
5,424
false
false
Accurate transcription in vivo requires at least six general transcription initiation factors, in addition to RNA polymerase II. Transcription initiation factor IIF (TFIIF) is a tetramer consisting of two large subunits (TFIIF alpha or RAP74) and two small subunits (TFIIF beta or RAP30) [ ]. The beta subunit of TFIIF i...
[ "GO:0006366", "GO:0006367", "GO:0005674" ]
[ "transcription by RNA polymerase II", "transcription initiation at RNA polymerase II promoter", "transcription factor TFIIF complex" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PIRSF", "PANTHER" ]
[ "PIRSF015849", "PTHR10445" ]
[ "TFIIF-beta", "" ]
[ 1486, 5424 ]
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-112382", "R-BTA-113418", "R-BTA-674695", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-73776", "R-BTA-73779", "R-BTA-75953", "R-BTA-75955", "R-BTA-76042", "R-BTA-77075", "R-BTA-9018519", "R-DDI-113418", ...
[ "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-6803529", "REACTOME:R-BTA-6807505", "REACTOME:R-BTA-72086", "REACTOME:R-BTA-72163", "REACTOME:R-BTA-72165", "REACTOME:R-BTA-72203", "REACTOME:R-BTA-73776", "REACTOME:R-BTA-73779...
137
[ "1bby", "1f3u", "2bby", "4v1n", "4v1o", "5fmf", "5fyw", "5fz5", "5iy6", "5iy7", "5iy8", "5iy9", "5iya", "5iyb", "5iyc", "5iyd", "5oqj", "5oqm", "5sva", "6gyk", "6gyl", "6gym", "6o9l", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7ena", "7enc"...
92
[ "PUB00020428" ]
[ "7596813" ]
[ "Molecular cloning of cDNA encoding the small subunit of Drosophila transcription initiation factor TFIIF." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5424 ]
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...
[ 9, 1, 3, 1, 2, 3, 1, 7, 8, 1, 1, 13 ]
12
true
Family
Transcription initiation factor IIF, beta subunit
Transcription initiation factor IIF, beta subunit
TFIIF_beta
6
IPR003197
3,197
Cytochrome b-c1 complex subunit 7
QCR7
Family
5,453
false
false
Cytochrome b-c1 complex subunit 7 (QCR7, also known as UQCRB) is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. QCR7 is involved in redox-linked proton pumping [ , , ].
[ "GO:0006122" ]
[ "mitochondrial electron transport, ubiquinol to cytochrome c" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF02271", "PIRSF000022", "PTHR12022" ]
[ "UCR_14kD", "Bc1_14K", "" ]
[ 5444, 3973, 5284 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-611105", "R-BTA-9865881", "R-DDI-611105", "R-HSA-611105", "R-HSA-9865881", "R-MMU-611105", "R-MMU-9865881", "R-SCE-611105", "R-SCE-9865878", "R-SPO-611105" ]
[ "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9865881", "REACTOME:R-DDI-611105", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-9865881", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-9865881", "REACTOME:R-SCE-611105", "REACTOME:R-SCE-9865878", "REACTOME:R-SPO-611105" ]
10
[ "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"...
178
[ "PUB00063085", "PUB00063086", "PUB00063087" ]
[ "2170131", "6319130", "11556808" ]
[ "Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane.", "The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear ...
[ 1990, 1984, 2001 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5453 ]
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...
[ 9, 1, 1, 3, 4, 2, 1, 9, 3, 1, 1, 12 ]
12
true
Family
Cytochrome b-c1 complex subunit 7
Cytochrome b-c1 complex subunit 7
QCR7
6
IPR003200
3,200
Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase
Nict_dMeBzImd_PRibTrfase
Family
17,735
false
false
This entry represents bacterial- and archaeal-type nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase enzymes involved in dimethylbenzimidazole synthesis, as well as a group of proteins of unknown function. This function is essential to de novo cobalamin (vitamin B12) production in bacteria. Nicotina...
[ "GO:0008939" ]
[ "nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02277", "PTHR43463", "cd02439" ]
[ "DBI_PRT", "", "DMB-PRT_CobT" ]
[ 17130, 16220, 16870 ]
3
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.4.2.21", "PWY-5509", "PWY-6269", "PWY-7964", "PWY-7965", "PWY-7966", "PWY-7967", "PWY-7968", "PWY-7969", "PWY-7970" ]
[ "EC:2.4.2.21", "METACYC:PWY-5509", "METACYC:PWY-6269", "METACYC:PWY-7964", "METACYC:PWY-7965", "METACYC:PWY-7966", "METACYC:PWY-7967", "METACYC:PWY-7968", "METACYC:PWY-7969", "METACYC:PWY-7970" ]
10
[ "1d0s", "1d0v", "1j33", "1jh8", "1jha", "1jhm", "1jho", "1jhp", "1jhq", "1jhr", "1jhu", "1jhv", "1jhx", "1jhy", "1l4b", "1l4e", "1l4f", "1l4g", "1l4h", "1l4k", "1l4l", "1l4m", "1l4n", "1l5f", "1l5k", "1l5l", "1l5m", "1l5n", "1l5o", "1wx1", "3l0z", "3u4g"...
47
[ "PUB00009745", "PUB00014667", "PUB00014670", "PUB00014672", "PUB00015874", "PUB00015996" ]
[ "7592411", "12196148", "8550510", "11153269", "12101181", "8206834" ]
[ "The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli.", "Biosynthesis of cobalamin (vitamin B(12)).", "Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli.", "Multiple biosynthetic pathways for vitamin B12: variations on ...
[ 1995, 2002, 1996, 2001, 2002, 1994 ]
6
[]
[ "IPR002805", "IPR017846" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 739, 16600, 143, 253 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase
Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase
Nict_dMeBzImd_PRibTrfase
1
IPR003201
3,201
Transposase Tn5, dimerisation
Transposase_Tn5
Domain
1,120
false
false
Transposons are mobile DNA sequences capable of replication and insertion into the chromosome. Typically transposons code for the transposase enzyme, which catalyses insertion, found between terminal inverted repeats [ ]. Tn5 has a unique method of self- regulation in which a truncated version of the transposase enzyme...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02281" ]
[ "Dimer_Tnp_Tn5" ]
[ 1120 ]
1
[]
[]
[]
0
[]
0
[ "PUB00006439", "PUB00020477" ]
[ "10207011", "6306482" ]
[ "The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution.", "DNA sequences at the ends of transposon Tn5 required for transposition." ]
[ 1999, 1983 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halalkaliarchaeum desulfuricum", "ecological metagenomes" ]
[ 1094, 2, 1, 23 ]
4
[]
[]
0
true
Domain
Transposase Tn5, dimerisation
Transposase Tn5, dimerisation
Transposase_Tn5
9
IPR003202
3,202
DNA polymerase processivity factor (UL42)
Herpes_UL42
Family
299
false
false
The DNA polymerase processivity factor (UL42) of Human herpesvirus 1 (HHV-1) forms a heterodimer with UL30 to create the viral DNA polymerase complex. UL42 functions to increase the processivity of polymerisation and makes little contribution to the catalytic activity of the polymerase.
[ "GO:0003677", "GO:0006260" ]
[ "DNA binding", "DNA replication" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02282" ]
[ "Herpes_UL42" ]
[ 299 ]
1
[]
[]
[]
0
[ "1dml", "8exx", "8oj6", "8oj7", "8oja", "8v1q", "8v1r", "8v1s", "8v1t", "9enp", "9ja3" ]
11
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Alphaherpesvirinae" ]
[ 299 ]
1
[]
[]
0
true
Family
DNA polymerase processivity factor (UL42)
DNA polymerase processivity factor (UL42)
Herpes_UL42
4
IPR003203
3,203
Bifunctional adenosylcobalamin biosynthesis protein CobU/CobP
CobU/CobP
Family
15,730
false
false
This family includes Bifunctional adenosylcobalamin biosynthesis protein CobU, Bifunctional adenosylcobalamin biosynthesis protein CobP and similar proteins mainly found in bacteria. This group of bifunctional cobalamin biosynthesis enzymes display cobinamide kinase and cobinamide phosphate guanyltransferase activity. ...
[ "GO:0000166", "GO:0043752", "GO:0009236" ]
[ "nucleotide binding", "adenosylcobinamide kinase activity", "cobalamin biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PIRSF", "PANTHER", "CDD" ]
[ "PF02283", "PIRSF006135", "PTHR34848", "cd00544" ]
[ "CobU", "CobU", "", "CobU" ]
[ 15705, 12132, 14506, 13420 ]
4
[ "EC", "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.156", "2.7.7.62", "GenProp0269", "GenProp1349", "PWY-6269", "PWY-7962", "PWY-7971", "PWY-7972", "PWY-8282" ]
[ "EC:2.7.1.156", "EC:2.7.7.62", "GP:GenProp0269", "GP:GenProp1349", "METACYC:PWY-6269", "METACYC:PWY-7962", "METACYC:PWY-7971", "METACYC:PWY-7972", "METACYC:PWY-8282" ]
9
[ "1c9k", "1cbu", "7tm8", "8yep", "8yes", "8yk8", "8ykc", "9vio", "9vip", "9vis", "9vit" ]
11
[ "PUB00006412" ]
[ "9601028" ]
[ "Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution,." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 13, 15467, 35, 215 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Bifunctional adenosylcobalamin biosynthesis protein CobU/CobP
Bifunctional adenosylcobalamin biosynthesis protein CobU/CobP
CobU/CobP
2
IPR003204
3,204
Cytochrome c oxidase, subunit Va/VI
Cyt_c_oxidase_su5A/6
Family
4,028
false
false
Cytochrome c oxidase ( ) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma m...
[ "GO:0006123", "GO:0005743" ]
[ "mitochondrial electron transport, cytochrome c to oxygen", "mitochondrial inner membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02284", "PTHR14200", "cd00923" ]
[ "COX5A", "", "Cyt_c_Oxidase_Va" ]
[ 4027, 3975, 3804 ]
3
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "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-9837999", "R-BTA-9864848", "R-CEL-9837999", "R-CEL-9864848", "R-DME-5628897", "R-DME-611105", "R-DME-9707564", "R-DME-9837999", "R-DME-9864848", "R-HSA-5628897", "R-HSA-611105", "R-HSA-9707564", "R-HSA-9837999", ...
[ "GP:GenProp1426", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9864848", "REACTOME:R-CEL-9837999", "REACTOME:R-CEL-9864848", "REACTOME:R-DME-5628897", "REACTOME:R-DME-611105", "REACTOME:R-DME-9707564", "REACTOME:R-DME-98...
30
[ "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
[ "PUB00000581", "PUB00005218", "PUB00079535", "PUB00079536", "PUB00079537", "PUB00079538", "PUB00079539", "PUB00079540", "PUB00079541", "PUB00079542", "PUB00079543" ]
[ "6307356", "8638158", "16144979", "15923083", "12909344", "11035249", "9752724", "16760263", "16631971", "16199211", "15598510" ]
[ "Structure of cytochrome c oxidase.", "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.", "Modulation of cytochrome C oxidase-va is possibly involved in metallothionein protection from doxorubicin cardiotoxicity.", "Mitochondrial type I nitric oxide synthase physically interacts w...
[ 1983, 1996, 2005, 2005, 2003, 2000, 1998, 2006, 2006, 2005, 2005 ]
11
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2, 4026 ]
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, 2, 2, 6, 1, 1, 6, 1, 1 ]
9
true
Family
Cytochrome c oxidase, subunit Va/VI
Cytochrome c oxidase, subunit Va/VI
Cyt_c_oxidase_su5A/6
5
IPR003205
3,205
Cytochrome c oxidase, subunit 8
Cyt_c_oxidase_su8
Family
1,388
false
false
Cytochrome c oxidase ( ) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ , ]. In fungi (as in other eukaryotes) this enzyme complex is located in the mitochondrial inner membrane. In eukaryotes, in additi...
[ "GO:0006123" ]
[ "mitochondrial electron transport, cytochrome c to oxygen" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02285", "PTHR16717" ]
[ "COX8", "" ]
[ 1363, 1212 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5628897", "R-HSA-611105", "R-HSA-9707564", "R-HSA-9864848", "R-MMU-5628897", "R-MMU-611105", "R-MMU-9707564", "R-MMU-9864848", "R-RNO-5628897", "R-RNO-611105", "R-RNO-9707564", "R-RNO-9864848" ]
[ "REACTOME:R-HSA-5628897", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-9707564", "REACTOME:R-HSA-9864848", "REACTOME:R-MMU-5628897", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-9707564", "REACTOME:R-MMU-9864848", "REACTOME:R-RNO-5628897", "REACTOME:R-RNO-611105", "REACTOME:R-RNO-9707564", "REACTOME:R...
12
[ "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"...
109
[ "PUB00000581", "PUB00097156", "PUB00101096" ]
[ "6307356", "28870773", "30598554" ]
[ "Structure of cytochrome c oxidase.", "Mitochondrial cytochrome c oxidase biogenesis: Recent developments.", "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc<sub>1</sub>." ]
[ 1983, 2018, 2019 ]
3
[]
[]
0
0
null
[ "Bacteria", "Bilateria" ]
[ 2, 1386 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 1, 3, 4, 7 ]
5
true
Family
Cytochrome c oxidase, subunit 8
Cytochrome c oxidase, subunit 8
Cyt_c_oxidase_su8
6
IPR003206
3,206
Diol/glycerol dehydratase, large subunit
Diol/glycerol_deHydtase_lsu
Domain
1,758
false
false
This entry represents the large subunit of adenosylcobalamin-dependent diol dehydratases ( ) and glycerol dehydratases ( ). These enzymes are produced by some enterobacteria in response to growth substances. The enzyme have an TIM β/α barrel fold [ ]. Inactivated holoenzymes are reactivated by their own reactivating fa...
[ "GO:0016836", "GO:0031419" ]
[ "hydro-lyase activity", "cobalamin binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "NCBIFAM", "PFAM", "PIRSF", "CDD" ]
[ "NF011979", "PF02286", "PIRSF018507", "cd03687" ]
[ "PRK15444.1", "Dehydratase_LU", "Prpndl_dhdrts_lg", "Dehydratase_LU" ]
[ 1577, 1758, 1030, 923 ]
4
[ "GP" ]
[ "GenProp1089" ]
[ "GP:GenProp1089" ]
1
[ "1dio", "1eex", "1egm", "1egv", "1iwb", "1iwp", "1mmf", "1uc4", "1uc5", "3auj", "5yrt", "5yrv", "5ysh", "7xrk", "7xrl" ]
15
[ "PUB00024521", "PUB00042624" ]
[ "10903944", "17916188" ]
[ "How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex.", "Molecular basis for specificities of reactivating factors for adenosylcobalamin-dependent diol and glycerol dehydratases." ]
[ 2000, 2007 ]
2
[]
[]
0
0
null
[ "Bacteria", "Cyprideis torosa", "Halobacteriales", "metagenomes" ]
[ 1729, 1, 12, 16 ]
4
[]
[]
0
true
Domain
Diol/glycerol dehydratase, large subunit
Diol/glycerol dehydratase, large subunit
Diol/glycerol_deHydtase_lsu
8
IPR003207
3,207
Propanediol/glycerol dehydratase, small subunit
Ppandiol/glycerol_DeHydtase_su
Family
1,611
false
false
Diol dehydratase ( ) and glycerol dehydratase ( ) are two iso-functional enzymes that can each catalyse the conversion of 1,2-propanediol, 1,2-ethanediol and glycerol to the corresponding deoxy aldehydes (propionaldehyde, acetaldehyde and 3-hydroxypropionaldehyde, respectively). This reaction proceeds by a radical mech...
[]
[]
[]
0
[ "NCBIFAM", "PFAM", "PIRSF" ]
[ "NF011972", "PF02287", "PIRSF018505" ]
[ "PRK15443.1-3", "Dehydratase_SU", "Prpndl_dhdrts_sm" ]
[ 1290, 1611, 1291 ]
3
[ "GP" ]
[ "GenProp1089" ]
[ "GP:GenProp1089" ]
1
[ "1dio", "1eex", "1egm", "1egv", "1iwb", "1iwp", "1mmf", "1uc4", "1uc5", "3auj", "5yrt", "5yrv", "5ysh", "7xrk", "7xrl" ]
15
[ "PUB00011184", "PUB00013627", "PUB00013628", "PUB00013629", "PUB00013630" ]
[ "10498708", "1267798", "210157", "12230560", "10949584" ]
[ "The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation.", "Substrate specificity of coenzyme B12-dependent diol dehydrase: glycerol as both a good sub...
[ 1999, 1976, 1978, 2002, 2000 ]
5
[]
[]
0
0
null
[ "Bacteria", "Cyprideis torosa", "Halobacteriales", "ecological metagenomes" ]
[ 1589, 1, 11, 10 ]
4
[]
[]
0
true
Family
Propanediol/glycerol dehydratase, small subunit
Propanediol/glycerol dehydratase, small subunit
Ppandiol/glycerol_DeHydtase_su
1
IPR003208
3,208
Diol/glycerol dehydratase/dehydratase reactivating factor
Dehydtase/Dehydtase_re
Family
3,070
false
false
This family contains the medium subunit of the trimeric diol dehydratases and glycerol dehydratases, and the small subunit of the diol/glycerol dehydratase reactivating factor [ ]. Diol dehydratases are produced by some enterobacteria in response to growth substances [ ]. Both diol dehydratase and glycerol dehydratase ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02288" ]
[ "Dehydratase_MU" ]
[ 3070 ]
1
[ "GP" ]
[ "GenProp1089" ]
[ "GP:GenProp1089" ]
1
[ "1dio", "1eex", "1egm", "1egv", "1iwb", "1iwp", "1mmf", "1nbw", "1uc4", "1uc5", "2d0o", "2d0p", "3auj", "5yrt", "5yrv", "5ysh", "7xrk", "7xrl" ]
18
[ "PUB00013589", "PUB00015077", "PUB00069745", "PUB00100250" ]
[ "9362119", "9805380", "21040475", "28475631" ]
[ "A protein factor is essential for in situ reactivation of glycerol-inactivated adenosylcobalamin-dependent diol dehydratase.", "Molecular cloning, sequencing and characterization of the genes for adenosylcobalamin-dependent diol dehydratase of Klebsiella pneumoniae.", "Diol dehydratase-reactivating factor is a...
[ 1997, 1998, 2010, 2017 ]
4
[]
[ "IPR009192", "IPR025541" ]
0
2
0
[ "Bacteria", "Cyprideis torosa", "Halobacteriales", "metagenomes" ]
[ 3032, 1, 22, 15 ]
4
[]
[]
0
true
Family
Diol/glycerol dehydratase/dehydratase reactivating factor
Diol/glycerol dehydratase/dehydratase reactivating factor
Dehydtase/Dehydtase_re
3
IPR003209
3,209
Methenyltetrahydromethanopterin cyclohydrolase
METHMP_CycHdrlase
Family
1,450
false
false
Methenyltetrahydromethanopterin cyclohydrolase ( ) catalyses the interconversion of methenyltetrahydromethanopterin and N(5)formyltetrahydromethanopterin, and is found in both archaea and bacteria [ , ]. In methanogenic archaea, this enzyme is involved in the production of methane from carbon dioxide. In the sulphate-r...
[ "GO:0018759", "GO:0006730" ]
[ "methenyltetrahydromethanopterin cyclohydrolase activity", "one-carbon metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "NCBIFAM", "CDD" ]
[ "MF_00486", "PF02289", "TIGR03120", "cd00545" ]
[ "McH", "MCH", "one_C_mch", "MCH" ]
[ 1379, 1450, 1389, 858 ]
4
[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "3.5.4.27", "GenProp0671", "PWY-1723", "PWY-5209", "PWY-7784", "PWY-8305" ]
[ "EC:3.5.4.27", "GP:GenProp0671", "METACYC:PWY-1723", "METACYC:PWY-5209", "METACYC:PWY-7784", "METACYC:PWY-8305" ]
6
[ "1qlm", "4fio", "4gvq", "4gvr", "4gvs" ]
5
[ "PUB00016914", "PUB00016915", "PUB00016916", "PUB00161764", "PUB00161765" ]
[ "8617278", "8481088", "10482517", "23013430", "23873651" ]
[ "Primary structure of cyclohydrolase (Mch) from Methanobacterium thermoautotrophicum (strain Marburg) and functional expression of the mch gene in Escherichia coli.", "N5,N10-methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its p...
[ 1996, 1993, 1999, 2012, 2013 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 637, 766, 2, 45 ]
4
[]
[]
0
true
Family
Methenyltetrahydromethanopterin cyclohydrolase
Methenyltetrahydromethanopterin cyclohydrolase
METHMP_CycHdrlase
3
IPR003210
3,210
Signal recognition particle, SRP14 subunit
Signal_recog_particle_SRP14
Family
4,265
false
false
The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ , , ]. SRP recognises the signal sequence of the nascent po...
[ "GO:0008312", "GO:0030942", "GO:0006614", "GO:0005786" ]
[ "7S RNA binding", "endoplasmic reticulum signal peptide binding", "SRP-dependent cotranslational protein targeting to membrane", "signal recognition particle, endoplasmic reticulum targeting" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PANTHER" ]
[ "PF02290", "PTHR12013" ]
[ "SRP14", "" ]
[ 4231, 4057 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1799339", "R-BTA-6798695", "R-CEL-1799339", "R-CEL-6798695", "R-DDI-1799339", "R-DDI-6798695", "R-HSA-1799339", "R-HSA-6798695", "R-MMU-1799339", "R-MMU-6798695", "R-SCE-1799339", "R-SCE-6798695", "R-SPO-1799339", "R-SPO-6798695" ]
[ "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-6798695", "REACTOME:R-DDI-1799339", "REACTOME:R-DDI-6798695", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-1799339", "REACTOME:R-MMU-6798695", "REACTOME:R-SCE-1799339", "REACTOM...
14
[ "1914", "1e8o", "1e8s", "1ry1", "2w9j", "3jaj", "3jan", "4ue5", "4uyj", "4uyk", "5aox", "6frk", "6r6g", "7nfx", "7obr" ]
15
[ "PUB00011467", "PUB00028143", "PUB00035998", "PUB00035999", "PUB00053948", "PUB00063486", "PUB00100261" ]
[ "7730321", "16469117", "17622352", "17507650", "12364595", "12605305", "34020957" ]
[ "Human signal recognition particle (SRP) Alu-associated protein also binds Alu interspersed repeat sequence RNAs. Characterization of human SRP9.", "Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.", "X-ray structures of the signal recognition...
[ 1995, 2006, 2007, 2007, 2002, 2003, 2021 ]
7
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4265 ]
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...
[ 4, 1, 1, 3, 2, 2, 1, 1, 5, 1, 1, 7 ]
12
true
Family
Signal recognition particle, SRP14 subunit
Signal recognition particle, SRP14 subunit
Signal_recog_particle_SRP14
4
IPR003211
3,211
AmiS/UreI transporter
AmiSUreI_transpt
Family
1,805
false
false
Helicobacter pylori is a Gram-negative, ureolytic bacteria that can colonise the human stomach. It does not survive in a medium with a pH less than 4.0 unless urea is present, preferring a neutral pH. Gastric juice urea is able to rapidly access intrabacterial urease when the periplasmic pH falls below approximately 6....
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF02293" ]
[ "AmiS_UreI" ]
[ 1805 ]
1
[]
[]
[]
0
[ "3ux4", "6nsj", "6nsk" ]
3
[ "PUB00006468", "PUB00043489", "PUB00043490" ]
[ "10642549", "12471160", "7642533" ]
[ "A H+-gated urea channel: the link between Helicobacter pylori urease and gastric colonization.", "The gastric biology of Helicobacter pylori.", "Identification of two new genes in the Pseudomonas aeruginosa amidase operon, encoding an ATPase (AmiB) and a putative integral membrane protein (AmiS)." ]
[ 2000, 2003, 1995 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "ecological metagenomes" ]
[ 36, 1763, 6 ]
3
[]
[]
0
true
Family
AmiS/UreI transporter
AmiS/UreI transporter
AmiSUreI_transpt
4
IPR003212
3,212
DNA-binding protein 7a-e
DNA-bd_7a-e_arc
Family
87
false
false
This family includes DNA-binding protein 7a-e (DN7A-E) from hyperthermophilic archaebacterium. There are five 7kDa DNA-binding proteins, 7a-7e, found as monomers in the cell. These proteins may be involved in maintaining the integrity of the genome at high temperature [ ]. DNA-binding protein 7a (also known as Ssoa1) h...
[ "GO:0003677", "GO:0004521" ]
[ "DNA binding", "RNA endonuclease activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "NCBIFAM", "PFAM", "PIRSF" ]
[ "NF045555", "PF02294", "PIRSF036912" ]
[ "Sul7d", "7kD_DNA_binding", "Sac7" ]
[ 85, 87, 47 ]
3
[]
[]
[]
0
[ "1azp", "1azq", "1b4o", "1bbx", "1bf4", "1bnz", "1c8c", "1ca5", "1ca6", "1jic", "1sap", "1sso", "1wd0", "1wd1", "1wto", "1wtp", "1wtq", "1wtr", "1wtv", "1wtw", "1wtx", "1wvl", "1xx8", "1xyi", "2cvr", "2xiw", "4cj0", "4cj1", "4cj2", "5b02", "5b03", "5b0i"...
60
[ "PUB00019072", "PUB00023884", "PUB00153708", "PUB00153709", "PUB00154615", "PUB00154616" ]
[ "3130377", "11031116", "7887965", "8425540", "27853299", "32518188" ]
[ "Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius.", "Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.", "In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in ...
[ 1988, 2000, 1995, 1993, 2016, 2020 ]
6
[]
[]
0
0
null
[ "Sulfolobaceae" ]
[ 87 ]
1
[]
[]
0
true
Family
DNA-binding protein 7a-e
DNA-binding protein 7a-e
DNA-bd_7a-e_arc
6
IPR003213
3,213
Cytochrome c oxidase, subunit VIb
Cyt_c_oxidase_su6B
Family
5,409
false
false
Cytochrome c oxidase ( ) is an oligomeric enzymatic complex that is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ ]. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasm...
[ "GO:0005739", "GO:0045277" ]
[ "mitochondrion", "respiratory chain complex IV" ]
[ "cellular_component", "cellular_component" ]
2
[ "PIRSF", "PANTHER", "PANTHER" ]
[ "PIRSF000278", "PTHR11387", "PTHR46281" ]
[ "Cyt_c_oxidase_6B", "", "" ]
[ 2606, 2600, 2809 ]
3
[ "GP", "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-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-9864848", "REACTOME:R-MMU-5628897", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-970...
16
[ "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"...
128
[ "PUB00000581", "PUB00014035", "PUB00081733", "PUB00081734" ]
[ "6307356", "11136449", "16364442", "12874793" ]
[ "Structure of cytochrome c oxidase.", "Cytochrome oxidase subunit VI of Trypanosoma brucei is imported without a cleaved presequence and is developmentally regulated at both RNA and protein levels.", "Copper deficiency increases fibulin-5 (DANCE/EVEC) but decreases cytochrome C oxidase VIb subunit expression in...
[ 1983, 2001, 2006, 2003 ]
4
[ "IPR048280" ]
[ "IPR042289" ]
1
1
0
[ "Eukaryota" ]
[ 5409 ]
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...
[ 10, 1, 2, 3, 4, 9, 1, 12, 8, 1, 1, 16 ]
12
true
Family
Cytochrome c oxidase, subunit VIb
Cytochrome c oxidase, subunit VIb
Cyt_c_oxidase_su6B
2
IPR003220
3,220
InsA N-terminal zinc ribbon domain
InsA_N_dom_Znf
Domain
3,251
false
false
Insertion elements are mobile elements in DNA, usually encoding proteins required for transposition, for example transposases. Protein InsA is absolutely required for transposition of insertion element 1. This entry represents a short zinc binding domain found in IS1 InsA family protein. It is found at the N terminus o...
[ "GO:0006313" ]
[ "DNA transposition" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF03811" ]
[ "Zn_ribbon_InsA" ]
[ 3251 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Viruses", "metagenomes" ]
[ 7, 3167, 5, 72 ]
4
[ "Escherichia coli (strain K12)" ]
[ 9 ]
1
true
Domain
InsA N-terminal zinc ribbon domain
InsA N-terminal zinc ribbon domain
InsA_N_dom_Znf
6
IPR003222
3,222
Antitermination protein
Antitermntn
Family
2,117
false
false
This entry consists of antitermination proteins found in bacteriophages, such as protein Q from phage lambda, and some bacterial homologues. Protein Q positively regulates expression of the phage late gene operon by binding to the bacterial host RNA polymerase (RNAP) and modifying it. This protein binds a specific DNA ...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM" ]
[ "MF_04158", "PF03589" ]
[ "Antitermination_lambda", "Antiterm" ]
[ 1788, 2117 ]
2
[]
[]
[]
0
[ "4mo1", "7ubj", "7ubk", "7ubl", "7ubm", "7ubn" ]
6
[ "PUB00034461", "PUB00097868", "PUB00097869" ]
[ "15150248", "25092034", "31455742" ]
[ "DNA binding regions of Q proteins of phages lambda and phi80.", "Commitment to lysogeny is preceded by a prolonged period of sensitivity to the late lytic regulator Q in bacteriophage λ.", "Structural basis of Q-dependent antitermination." ]
[ 2004, 2014, 2019 ]
3
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "Viruses", "bioreactor metagenome" ]
[ 2071, 4, 41, 1 ]
4
[ "Escherichia coli (strain K12)", "Mus musculus" ]
[ 1, 1 ]
2
true
Family
Antitermination protein
Antitermination protein
Antitermntn
2
IPR003223
3,223
Flagellin phase1 repressor
Flag1_repressor
Family
510
false
false
Flagellin is the subunit which polymerises to form the filaments of bacterial flagella. The proteins in this family are transcriptional repressors of phase-1 flagellin genes.
[ "GO:0003700", "GO:0006355" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03614" ]
[ "Flag1_repress" ]
[ 510 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Enterobacterales" ]
[ 510 ]
1
[]
[]
0
true
Family
Flagellin phase1 repressor
Flagellin phase1 repressor
Flag1_repressor
7
IPR003224
3,224
RING finger protein Z, zinc finger
Z_RING_Znf
Domain
627
false
false
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...
[ "GO:0003723", "GO:0008270" ]
[ "RNA binding", "zinc ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF03854" ]
[ "zf-P11" ]
[ 627 ]
1
[]
[]
[]
0
[ "2m1s", "5i72", "7ckl", "7ckm", "7eju", "7el9", "7ela", "7elb", "7elc", "7vgq", "7vh1", "7x6v" ]
12
[ "PUB00001094", "PUB00005712", "PUB00006216", "PUB00014077", "PUB00033859", "PUB00033860", "PUB00033861", "PUB00033862", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812" ]
[ "8804826", "8317827", "8744354", "12665246", "9420283", "10708446", "12970458", "14990716", "17210253", "15963892", "15718139", "10529348", "11179890" ]
[ "The RING finger domain: a recent example of a sequence-structure family.", "The RING finger. A novel protein sequence motif related to the zinc finger.", "Does this have a familiar RING?", "Zinc fingers--folds for many occasions.", "An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocy...
[ 1996, 1993, 1996, 2002, 1998, 2000, 2003, 2004, 2007, 2005, 2005, 1999, 2001 ]
13
[]
[]
0
0
null
[ "Arenaviridae", "Bacteria" ]
[ 625, 2 ]
2
[]
[]
0
true
Domain
RING finger protein Z, zinc finger
RING finger protein Z, zinc finger
Z_RING_Znf
4
IPR003225
3,225
Viral protein of unknown function DUF325
DUF325
Family
70
false
false
This is a family of uncharacterised proteins from Alphabaculovirus.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03804" ]
[ "DUF325" ]
[ 70 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Baculoviridae" ]
[ 70 ]
1
[]
[]
0
true
Family
Viral protein of unknown function DUF325
Viral protein of unknown function DUF325
DUF325
8
IPR003226
3,226
MYG1 exonuclease
MYG1_exonuclease
Family
6,808
false
false
This family includes MYG1 exonuclease from human and its orthologues, a 3'-5' RNA exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. It is involved in regulating spatially segregated organellar RNA processing, acting as a coordinator of nucleo-mitochondrial crosstalk [ ]. In nu...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03690", "PTHR11215" ]
[ "MYG1_exonuc", "" ]
[ 6808, 6608 ]
2
[]
[]
[]
0
[]
0
[ "PUB00155300", "PUB00155301", "PUB00155302" ]
[ "31081026", "23706493", "36888656" ]
[ "Myg1 exonuclease couples the nuclear and mitochondrial translational programs through RNA processing.", "Correlation of increased MYG1 expression and its promoter polymorphism with disease progression and higher susceptibility in vitiligo patients.", "Diverse yeast antiviral systems prevent lethal pathogenesis...
[ 2019, 2013, 2023 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 2, 1524, 5249, 5, 28 ]
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...
[ 13, 1, 1, 4, 10, 4, 1, 2, 3, 1, 1, 9 ]
12
true
Family
MYG1 exonuclease
MYG1 exonuclease
MYG1_exonuclease
5
IPR003228
3,228
Transcription initiation factor TFIID subunit 12 domain
TFIID_TAF12_dom
Domain
5,364
false
false
TBP-associated factor 12 (TAF12) is one of several TAFs that bind TBP and are involved in forming the TFIID complex. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes [ ]. This entry represents a domain found in TAF12. TFIID is one ...
[ "GO:0006352", "GO:0005669" ]
[ "DNA-templated transcription initiation", "transcription factor TFIID complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "CDD" ]
[ "PF03847", "cd07981" ]
[ "TFIID_20kDa", "HFD_TAF12" ]
[ 5361, 5127 ]
2
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2054", "R-BTA-674695", "R-BTA-6804756", "R-BTA-73776", "R-BTA-73779", "R-BTA-75953", "R-BTA-76042", "R-CEL-674695", "R-CEL-73776", "R-CEL-73779", "R-CEL-75953", "R-CEL-76042", "R-DDI-674695", "R-DDI-73776", "R-DDI-73779", "R-DDI-75953", "R-DDI-76042", "R-DME-674695", "R-D...
[ "GP:GenProp2054", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6804756", "REACTOME:R-BTA-73776", "REACTOME:R-BTA-73779", "REACTOME:R-BTA-75953", "REACTOME:R-BTA-76042", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-73776", "REACTOME:R-CEL-73779", "REACTOME:R-CEL-75953", "REACTOME:R-CEL-76042", "REACT...
49
[ "1h3o", "6hqa", "6mzc", "6mzd", "6mzl", "6mzm", "6t9i", "6t9j", "6t9k", "6tb4", "6tbm", "7edx", "7eg7", "7eg8", "7eg9", "7ega", "7egb", "7egc", "7egd", "7ege", "7egf", "7egg", "7egi", "7egj", "7ena", "7enc", "7ktr", "7kts", "8gxq", "8gxs", "8h7g", "8wak"...
39
[ "PUB00006329", "PUB00079481", "PUB00079563" ]
[ "7667268", "10664584", "19635797" ]
[ "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors.", "TBP-associated factors (TAFIIs): multiple, selective transcriptional mediators in common complexes.", "TAF4/4b x TAF12 displa...
[ 1995, 2000, 2009 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5364 ]
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...
[ 9, 1, 1, 5, 10, 3, 1, 6, 3, 1, 1, 16 ]
12
true
Domain
Transcription initiation factor TFIID subunit 12 domain
Transcription initiation factor TFIID subunit 12 domain
TFIID_TAF12_dom
2
IPR003230
3,230
D-alanyl carrier protein
DltC
Family
1,675
false
false
This entry represents D-alanyl carrier protein DltC, which is part of the operon for incorporation of D-Ala residues into lipoteichoic acids (LTAs), which requires the activity of four gene products (DltA to DltD). DltA is a cytoplasmic D-alanine-D-alanyl carrier protein ligase that catalyses the D-alanylation of the D...
[ "GO:0036370", "GO:0019350" ]
[ "D-alanyl carrier activity", "teichoic acid biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM" ]
[ "MF_00565", "TIGR01688" ]
[ "DltC", "dltC" ]
[ 1665, 1661 ]
2
[ "GP" ]
[ "GenProp0958" ]
[ "GP:GenProp0958" ]
1
[ "1dv5", "1hqb", "4bpf", "4bpg", "4bph", "6bug", "6buh", "7r49", "8i31", "8i32", "8jf2" ]
11
[ "PUB00043379", "PUB00043380", "PUB00043381", "PUB00043382", "PUB00086696", "PUB00086797" ]
[ "14665680", "16885447", "16166534", "17194792", "11849532", "8682792" ]
[ "A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria.", "A functional dlt operon, encoding proteins required for incorporation of d-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus p...
[ 2003, 2006, 2005, 2007, 2002, 1996 ]
6
[]
[]
0
0
null
[ "Bacteria", "bioreactor metagenome" ]
[ 1671, 4 ]
2
[]
[]
0
true
Family
D-alanyl carrier protein
D-alanyl carrier protein
DltC
3
IPR003231
3,231
Acyl carrier protein
ACP
Family
39,178
false
false
There are two types of fatty acid synthase systems. The type I system is found in metazoans and is carried out by a multifunctional polypeptide with multiple active sites. In contrast, the type II system found in bacteria and plants consists of a set of discrete monofunctional proteins, each encoded by a separate gene....
[ "GO:0006633" ]
[ "fatty acid biosynthetic process" ]
[ "biological_process" ]
1
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_01217", "PTHR20863", "TIGR00517" ]
[ "Acyl_carrier", "", "acyl_carrier" ]
[ 35761, 34574, 26793 ]
3
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1104", "R-DDI-77289", "R-DDI-9857492", "R-DME-611105", "R-DME-6799198", "R-DME-77289", "R-DME-9857492", "R-HSA-611105", "R-HSA-6799198", "R-HSA-77289", "R-HSA-9857492", "R-HSA-9937383", "R-MMU-611105", "R-MMU-6799198", "R-MMU-77289", "R-MMU-9857492", "R-MMU-9937383", "R-SCE...
[ "GP:GenProp1104", "REACTOME:R-DDI-77289", "REACTOME:R-DDI-9857492", "REACTOME:R-DME-611105", "REACTOME:R-DME-6799198", "REACTOME:R-DME-77289", "REACTOME:R-DME-9857492", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-HSA-77289", "REACTOME:R-HSA-9857492", "REACTOME:R-HSA-9937383"...
21
[ "1acp", "1f80", "1hy8", "1klp", "1l0h", "1l0i", "1t8k", "1vku", "1x3o", "2ava", "2cgq", "2cnr", "2dnw", "2ehs", "2eht", "2fac", "2fad", "2fae", "2fhs", "2fq0", "2fq2", "2fva", "2fve", "2fvf", "2k92", "2k93", "2k94", "2koo", "2kop", "2koq", "2kor", "2kos"...
494
[ "PUB00028023", "PUB00028024" ]
[ "10997907", "12859187" ]
[ "Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.", "Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus." ]
[ 2000, 2003 ]
2
[]
[ "IPR044813" ]
0
1
0
[ "Bacteria", "Eukaryota", "Halobacteriales", "Viruses", "unclassified sequences" ]
[ 29540, 8960, 17, 27, 634 ]
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, 2, 2, 4, 1, 4, 5, 1, 22, 4, 1, 1, 34 ]
13
true
Family
Acyl carrier protein
Acyl carrier protein
ACP
9
IPR003235
3,235
Nematode insulin-like peptide, beta type
Nem_insulin-like_b-type
Family
389
false
false
Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological effects, such as increasing the permeability of cells to monosaccharides, amino acids and fatty acids, and accelerating glycolysis and glycogen synthesis in the liver [ ]. Insulin ...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF03488" ]
[ "Ins_beta" ]
[ 389 ]
1
[]
[]
[]
0
[ "2kji", "8tk9", "8tkt", "8tku" ]
4
[ "PUB00001397", "PUB00003970", "PUB00003972", "PUB00003973", "PUB00023078", "PUB00037375", "PUB00053639", "PUB00053640", "PUB00053641", "PUB00053642", "PUB00096613" ]
[ "1868853", "503234", "6243748", "6107857", "2036417", "9141131", "10601981", "8735594", "8683595", "1319992", "24671950" ]
[ "Characterization of a cDNA clone encoding molluscan insulin-related peptide II of Lymnaea stagnalis.", "Nucleotide sequence of a cDNA clone encoding human preproinsulin.", "Sequence of the human insulin gene.", "Hormone families: pancreatic hormones and homologous growth factors.", "Solution structure of h...
[ 1991, 1979, 1980, 1980, 1991, 1997, 1999, 1996, 1996, 1992, 2014 ]
11
[]
[]
0
0
null
[ "Bilateria", "Winogradskyella damuponensis" ]
[ 388, 1 ]
2
[ "Caenorhabditis elegans" ]
[ 26 ]
1
true
Family
Nematode insulin-like peptide, beta type
Nematode insulin-like peptide, beta type
Nem_insulin-like_b-type
6
IPR003245
3,245
Phytocyanin domain
Phytocyanin_dom
Domain
26,874
false
false
Among the blue copper proteins with a single type I (or "blue") mononuclear copper site, the plant-specific phytocyanins constitute a distinct subfamily that can be further subdivided into the families of uclacyanins, stellacyanins, plantacyanins, and early nodulins. Stellacyanins have a blue copper coordinated by two ...
[ "GO:0009055" ]
[ "electron transfer activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02298", "PS51485" ]
[ "Cu_bind_like", "PHYTOCYANIN" ]
[ 26018, 26152 ]
2
[]
[]
[]
0
[ "1f56", "1jer", "1ws7", "1ws8", "1x9r", "1x9u", "2cbp" ]
7
[ "PUB00024795", "PUB00032358", "PUB00038139", "PUB00071545", "PUB00071546", "PUB00078682", "PUB00078683" ]
[ "11085657", "15631465", "15858169", "9761472", "19897921", "5089608", "11945593" ]
[ "Crystal structure of plantacyanin, a basic blue cupredoxin from spinach.", "Crystal structures of oxidized and reduced stellacyanin from horseradish roots.", "Structural reorganization of the copper binding site involving Thr15 of mavicyanin from Cucurbita pepo medullosa (zucchini) upon reduction.", "Uclacya...
[ 2000, 2005, 2005, 1998, 2009, 1971, 1971 ]
7
[]
[ "IPR041846" ]
0
1
0
[ "Bacillales", "Eukaryota" ]
[ 2, 26872 ]
2
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 161, 1, 161, 174 ]
4
true
Domain
Phytocyanin domain
Phytocyanin domain
Phytocyanin_dom
3
IPR003251
3,251
Rubrerythrin, diiron-binding domain
Rr_diiron-bd_dom
Domain
19,247
false
false
This entry represents the N-terminal diiron-binding domain of Rr, which has a has a ferritin-like fold [ ]. Rubrerythrin (Rr) is a fusion protein containing an N-terminal diiron-binding domain and a C-terminal domain homologous to rubredoxin [ ]. This protein has been related to the response to oxidative stress [ , , ]...
[ "GO:0016491", "GO:0046872" ]
[ "oxidoreductase activity", "metal ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "CDD" ]
[ "PF02915", "cd01041" ]
[ "Rubrerythrin", "Rubrerythrin" ]
[ 19246, 7053 ]
2
[ "EC", "GP" ]
[ "1.14.13.81", "GenProp0842" ]
[ "EC:1.14.13.81", "GP:GenProp0842" ]
2
[ "1b71", "1dvb", "1j30", "1jyb", "1lkm", "1lko", "1lkp", "1mft", "1nnq", "1qyb", "1ryt", "1s2z", "1s30", "1u7m", "1vjx", "1yux", "1yuz", "1yv1", "2e0z", "2fzf", "2hr5", "2hz8", "2oh3", "3mps", "3pwf", "3pza", "3qhb", "3qhc", "3qvd", "3sid", "4di0", "5c39"...
56
[ "PUB00000489", "PUB00002663", "PUB00003266", "PUB00008022", "PUB00008055", "PUB00008767", "PUB00098338", "PUB00100839", "PUB00100840" ]
[ "2244884", "1657933", "1992166", "7726577", "7830612", "8646540", "19118342", "35150262", "11972784" ]
[ "Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data.", "The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin.", "Structure of ...
[ 1990, 1991, 1991, 1995, 1994, 1996, 2009, 2022, 2002 ]
9
[]
[ "IPR045236" ]
0
1
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 1525, 15120, 14, 1948, 640 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 3, 3, 6 ]
3
true
Domain
Rubrerythrin, diiron-binding domain
Rubrerythrin, diiron-binding domain
Rr_diiron-bd_dom
6
IPR003256
3,256
Large ribosomal subunit protein uL24
Ribosomal_uL24
Family
28,816
false
false
Ribosomal protein uL24 is one of the proteins from the large ribosomal subunit. In their mature form, these proteins have 103 to 150 amino-acid residues. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. ...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_01326_B", "PTHR12903", "TIGR01079" ]
[ "Ribosomal_uL24_B", "", "rplX_bact" ]
[ 26735, 28731, 27147 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5389840", "R-BTA-5419276", "R-BTA-9937383", "R-CEL-5389840", "R-CEL-5419276", "R-CEL-9937383", "R-DME-5389840", "R-DME-5419276", "R-DME-9937383", "R-DRE-5389840", "R-DRE-5419276", "R-HSA-5368286", "R-HSA-5389840", "R-HSA-5419276", "R-HSA-9937383", "R-MMU-5389840", "R-MMU-54192...
[ "REACTOME:R-BTA-5389840", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-9937383", "REACTOME:R-CEL-5389840", "REACTOME:R-CEL-5419276", "REACTOME:R-CEL-9937383", "REACTOME:R-DME-5389840", "REACTOME:R-DME-5419276", "REACTOME:R-DME-9937383", "REACTOME:R-DRE-5389840", "REACTOME:R-DRE-5419276", "REACTOM...
21
[ "1nkw", "1nwx", "1nwy", "1sm1", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xbp", "2d3o", "2ftc", "2j28", "2rdo", "2vrh", "2zjp", "2zjq", "2zjr", "3bbx", "3cf5", "3dll", "3iy9", "3j3v", "3j3w", "3j45", "3j46", "3j5l", "3j6b", "3j7y", "3j7z", "3j8g", "3j9m"...
1,272
[ "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "11297922", "11290319", "11114498" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]
[ 2001, 2001, 2000 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 23609, 4790, 417 ]
3
[ "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",...
[ 8, 1, 1, 1, 1, 3, 1, 1, 7, 4, 1, 1, 8 ]
13
true
Family
Large ribosomal subunit protein uL24
Large ribosomal subunit protein uL24
Ribosomal_uL24
9
IPR003263
3,263
CD40 ligand
CD40L
Family
677
false
false
CD40 ligand (CD40L) is a transmembrane protein belonging to the Tumour Necrosis Factor (TNF) superfamily. It can be found on the surface of B lymphocytes, dendritic cells, follicular dendritic cells, hematopoietic progenitor cells, epithelial cells, and carcinomas [ ]. CD40L is importance for effective interaction with...
[ "GO:0005164", "GO:0006955", "GO:0016020" ]
[ "tumor necrosis factor receptor binding", "immune response", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PIRSF", "PRINTS" ]
[ "PIRSF016527", "PR01702" ]
[ "TNF_5", "CD40LIGAND" ]
[ 621, 662 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-198933", "R-CFA-5668541", "R-CFA-5676594", "R-GGA-198933", "R-GGA-5668541", "R-GGA-5676594", "R-HSA-198933", "R-HSA-5668541", "R-HSA-5676594", "R-MMU-198933", "R-MMU-5668541", "R-MMU-5676594", "R-RNO-198933", "R-RNO-5668541", "R-RNO-5676594" ]
[ "REACTOME:R-CFA-198933", "REACTOME:R-CFA-5668541", "REACTOME:R-CFA-5676594", "REACTOME:R-GGA-198933", "REACTOME:R-GGA-5668541", "REACTOME:R-GGA-5676594", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-5668541", "REACTOME:R-HSA-5676594", "REACTOME:R-MMU-198933", "REACTOME:R-MMU-5668541", "REACTOME:R-...
15
[ "1aly", "1i9r", "3lkj", "3qd6", "6brb", "6w9g", "7sgm" ]
7
[ "PUB00002042", "PUB00004130", "PUB00006091", "PUB00006095", "PUB00006098", "PUB00006101", "PUB00015257", "PUB00073752", "PUB00073753", "PUB00073754" ]
[ "8095800", "1377364", "2989794", "3349526", "2777790", "2268312", "15335677", "25479079", "7516669", "15193700" ]
[ "A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors.", "Emerging cytokine family.", "Molecular cloning of mouse tumour necrosis factor cDNA and its eukaryotic expression.", "A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein:...
[ 1993, 1992, 1985, 1988, 1989, 1990, 1993, 2014, 1994, 2004 ]
10
[]
[]
0
0
null
[ "Dipnotetrapodomorpha" ]
[ 677 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 2, 3 ]
3
true
Family
CD40 ligand
CD40 ligand
CD40L
1
IPR003265
3,265
HhH-GPD domain
HhH-GPD_domain
Domain
101,162
false
false
The HhH-GPD superfamily gets its name from its hallmark helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate [ , ]. This domain is found in a diverse range of structurally related DNA repair proteins that include: endonuclease III, and DNA glycosylase MutY, an A/G-specific adenine glycosylase. Bo...
[ "GO:0006284" ]
[ "base-excision repair" ]
[ "biological_process" ]
1
[ "PFAM", "SMART", "CDD" ]
[ "PF00730", "SM00478", "cd00056" ]
[ "HhH-GPD", "ENDO3c", "ENDO3c" ]
[ 92266, 95716, 95171 ]
3
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "3.2.2", "4.2.99.18", "R-BTA-110329", "R-BTA-110357", "R-CEL-110329", "R-CEL-110357", "R-DME-110329", "R-DME-110330", "R-DME-110331", "R-DME-110357", "R-GGA-110329", "R-HSA-110328", "R-HSA-110329", "R-HSA-110330", "R-HSA-110331", "R-HSA-110357", "R-HSA-5649702", "R-HSA-9608287", ...
[ "EC:3.2.2", "EC:4.2.99.18", "REACTOME:R-BTA-110329", "REACTOME:R-BTA-110357", "REACTOME:R-CEL-110329", "REACTOME:R-CEL-110357", "REACTOME:R-DME-110329", "REACTOME:R-DME-110330", "REACTOME:R-DME-110331", "REACTOME:R-DME-110357", "REACTOME:R-GGA-110329", "REACTOME:R-HSA-110328", "REACTOME:R-HS...
39
[ "1diz", "1ebm", "1fn7", "1hu0", "1kea", "1kg2", "1kg3", "1kg4", "1kg5", "1kg6", "1kg7", "1ko9", "1kqj", "1lwv", "1lww", "1lwy", "1m3h", "1m3q", "1mpg", "1mud", "1mun", "1muy", "1n39", "1n3a", "1n3c", "1ngn", "1orn", "1orp", "1p59", "1pu6", "1pu7", "1pu8"...
178
[ "PUB00013719", "PUB00019698", "PUB00074987" ]
[ "10706276", "10499592", "8805338" ]
[ "Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA.", "The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites.", "Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily."...
[ 2000, 1999, 1996 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3364, 74845, 21441, 14, 1498 ]
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",...
[ 63, 1, 6, 5, 3, 38, 10, 7, 26, 13, 4, 4, 115 ]
13
true
Domain
HhH-GPD domain
HhH-GPD domain
HhH-GPD_domain
4
IPR003268
3,268
FPotassium channel, inwardly rectifying, Kir1.1
K_chnl_inward-rec_Kir1.1
Family
1,679
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005242", "GO:0034765", "GO:1990573" ]
[ "inward rectifier potassium channel activity", "regulation of monoatomic ion transmembrane transport", "potassium ion import across plasma membrane" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PRINTS" ]
[ "PR01321" ]
[ "KIR11CHANNEL" ]
[ 1679 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296067", "R-MMU-1296067", "R-RNO-1296067" ]
[ "REACTOME:R-HSA-1296067", "REACTOME:R-MMU-1296067", "REACTOME:R-RNO-1296067" ]
3
[]
0
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00009378", "PUB00009410", "PUB00009411", "PUB00101807", "PUB00101808", "PUB00101809", "PUB00101810" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "11178249", "10102275", "10449331", "28630040", "25344677", "16357011", "23782368" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 2000, 1999, 1999, 2017, 2015, 2006, 2013 ]
14
[ "IPR016449" ]
[]
1
0
1
[ "Bilateria" ]
[ 1679 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 15, 2, 2, 7 ]
4
true
Family
FPotassium channel, inwardly rectifying, Kir1.1
FPotassium channel, inwardly rectifying, Kir1.1
K_chnl_inward-rec_Kir1.1
1
IPR003269
3,269
Potassium channel, inwardly rectifying, Kir1.2
K_chnl_inward-rec_Kir1.2
Family
621
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005242", "GO:0006813", "GO:0016020" ]
[ "inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01322" ]
[ "KIR12CHANNEL" ]
[ 621 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296041", "R-HSA-1296067", "R-HSA-997272", "R-MMU-1296041", "R-MMU-1296067", "R-MMU-997272", "R-RNO-1296041", "R-RNO-1296067", "R-RNO-997272" ]
[ "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-1296067", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-1296067", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-1296067", "REACTOME:R-RNO-997272" ]
9
[ "8i5m", "8i5n" ]
2
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008057", "PUB00008058", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "9729515", "9647694", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 1998, 1998, 2000, 1999, 1999 ]
12
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 621 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 5, 5 ]
3
true
Family
Potassium channel, inwardly rectifying, Kir1.2
Potassium channel, inwardly rectifying, Kir1.2
K_chnl_inward-rec_Kir1.2
6
IPR003270
3,270
Potassium channel, inwardly rectifying, Kir1.3
K_chnl_inward-rec_Kir1.3
Family
701
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005242", "GO:0006813", "GO:0016020" ]
[ "inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01323" ]
[ "KIR13CHANNEL" ]
[ 701 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296041", "R-HSA-997272", "R-MMU-1296041", "R-MMU-997272", "R-RNO-1296041", "R-RNO-997272" ]
[ "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-997272" ]
6
[]
0
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008059", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "8995301", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 1997, 2000, 1999, 1999 ]
11
[ "IPR016449" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 701 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 9, 3 ]
3
true
Family
Potassium channel, inwardly rectifying, Kir1.3
Potassium channel, inwardly rectifying, Kir1.3
K_chnl_inward-rec_Kir1.3
1
IPR003272
3,272
Potassium channel, inwardly rectifying, Kir2.2
K_chnl_inward-rec_Kir2.2
Family
1,008
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005242", "GO:0006813", "GO:0016020" ]
[ "inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01325" ]
[ "KIR22CHANNEL" ]
[ 1008 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1296041", "R-BTA-1296053", "R-BTA-5576886", "R-BTA-997272", "R-GGA-1296041", "R-GGA-1296053", "R-GGA-5576886", "R-GGA-997272", "R-HSA-1296041", "R-HSA-1296053", "R-HSA-5576886", "R-HSA-997272", "R-MMU-1296041", "R-MMU-1296053", "R-MMU-5576886", "R-MMU-997272", "R-RNO-1296041",...
[ "REACTOME:R-BTA-1296041", "REACTOME:R-BTA-1296053", "REACTOME:R-BTA-5576886", "REACTOME:R-BTA-997272", "REACTOME:R-GGA-1296041", "REACTOME:R-GGA-1296053", "REACTOME:R-GGA-5576886", "REACTOME:R-GGA-997272", "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-1296053", "REACTOME:R-HSA-5576886", "REACTOME:...
20
[ "3jyc", "3spc", "3spg", "3sph", "3spi", "3spj", "5kuk", "5kum", "6m84", "6m85", "6m86" ]
11
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008060", "PUB00009378", "PUB00009410", "PUB00009411", "PUB00092680" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "8647284", "11178249", "10102275", "10449331", "20074522" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 1996, 2000, 1999, 1999, 2010 ]
12
[ "IPR016449" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1008 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 3, 4 ]
4
true
Family
Potassium channel, inwardly rectifying, Kir2.2
Potassium channel, inwardly rectifying, Kir2.2
K_chnl_inward-rec_Kir2.2
8
IPR003273
3,273
Potassium channel, inwardly rectifying, Kir2.3
K_chnl_inward-rec_Kir2.3
Family
611
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005242", "GO:0006813", "GO:0016020" ]
[ "inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01326" ]
[ "KIR23CHANNEL" ]
[ 611 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296041", "R-HSA-1296053", "R-HSA-5576886", "R-HSA-997272", "R-MMU-1296041", "R-MMU-1296053", "R-MMU-5576886", "R-MMU-997272", "R-RNO-1296041", "R-RNO-1296053", "R-RNO-5576886", "R-RNO-997272" ]
[ "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-1296053", "REACTOME:R-HSA-5576886", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-1296053", "REACTOME:R-MMU-5576886", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-1296053", "REACTOME:R-RNO-5576886", "REACTOME:...
12
[]
0
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 2000, 1999, 1999 ]
10
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 611 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 4, 3 ]
3
true
Family
Potassium channel, inwardly rectifying, Kir2.3
Potassium channel, inwardly rectifying, Kir2.3
K_chnl_inward-rec_Kir2.3
6
IPR003274
3,274
Potassium channel, inwardly rectifying, Kir3.1
K_chnl_inward-rec_Kir3.1
Family
2,078
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0015467", "GO:0006813", "GO:0016020" ]
[ "G-protein activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01327" ]
[ "KIR31CHANNEL" ]
[ 2078 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1296041", "R-BTA-997272", "R-HSA-1296041", "R-HSA-997272", "R-MMU-1296041", "R-MMU-997272", "R-RNO-1296041", "R-RNO-997272" ]
[ "REACTOME:R-BTA-1296041", "REACTOME:R-BTA-997272", "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-997272" ]
8
[ "1n9p", "1u4e", "2qks", "3k6n", "5um4" ]
5
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 2000, 1999, 1999 ]
10
[ "IPR016449" ]
[]
1
0
1
[ "Bilateria" ]
[ 2078 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 6, 5, 6 ]
4
true
Family
Potassium channel, inwardly rectifying, Kir3.1
Potassium channel, inwardly rectifying, Kir3.1
K_chnl_inward-rec_Kir3.1
4
IPR003275
3,275
Potassium channel, inwardly rectifying, Kir3.2
K_chnl_inward-rec_Kir3.2
Family
927
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0015467", "GO:0006813", "GO:0016020" ]
[ "G-protein activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01328" ]
[ "KIR32CHANNEL" ]
[ 927 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296041", "R-HSA-997272", "R-MMU-1296041", "R-MMU-997272", "R-RNO-1296041", "R-RNO-997272" ]
[ "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-997272" ]
6
[]
0
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008061", "PUB00008062", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "9920664", "10544173", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 1999, 1999, 2000, 1999, 1999 ]
12
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 927 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 7, 12 ]
4
true
Family
Potassium channel, inwardly rectifying, Kir3.2
Potassium channel, inwardly rectifying, Kir3.2
K_chnl_inward-rec_Kir3.2
2
IPR003276
3,276
Potassium channel, inwardly rectifying, Kir3.3
K_chnl_inward-rec_Kir3.3
Family
442
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0015467", "GO:0006813", "GO:0016020" ]
[ "G-protein activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01329" ]
[ "KIR33CHANNEL" ]
[ 442 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296041", "R-HSA-997272", "R-MMU-1296041", "R-MMU-997272", "R-RNO-1296041", "R-RNO-997272" ]
[ "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-997272" ]
6
[]
0
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 2000, 1999, 1999 ]
10
[ "IPR016449" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 442 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 3 ]
3
true
Family
Potassium channel, inwardly rectifying, Kir3.3
Potassium channel, inwardly rectifying, Kir3.3
K_chnl_inward-rec_Kir3.3
8
IPR003277
3,277
Potassium channel, inwardly rectifying, Kir3.4
K_chnl_inward-rec_Kir3.4
Family
646
false
false
Inwardly-rectifying potassium channels (Kir) are the principal class of two-TM domain potassium channels. They are characterised by the property of inward-rectification, which is described as the ability to allow large inward currents and smaller outward currents. Inwardly rectifying potassium channels (Kir) are respon...
[ "GO:0015467", "GO:0006813", "GO:0016020" ]
[ "G-protein activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01330" ]
[ "KIR34CHANNEL" ]
[ 646 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1296041", "R-BTA-997272", "R-HSA-1296041", "R-HSA-997272", "R-MMU-1296041", "R-MMU-997272", "R-RNO-1296041", "R-RNO-997272", "R-SSC-1296041", "R-SSC-997272" ]
[ "REACTOME:R-BTA-1296041", "REACTOME:R-BTA-997272", "REACTOME:R-HSA-1296041", "REACTOME:R-HSA-997272", "REACTOME:R-MMU-1296041", "REACTOME:R-MMU-997272", "REACTOME:R-RNO-1296041", "REACTOME:R-RNO-997272", "REACTOME:R-SSC-1296041", "REACTOME:R-SSC-997272" ]
10
[]
0
[ "PUB00001069", "PUB00008063", "PUB00008064", "PUB00009410", "PUB00009411", "PUB00094735", "PUB00094736" ]
[ "7580148", "9284339", "9430664", "10102275", "10449331", "21311022", "20560207" ]
[ "The inward rectifier potassium channel family.", "An immunocytochemical study on the distribution of two G-protein-gated inward rectifier potassium channels (GIRK2 and GIRK4) in the adult rat brain.", "Mechanosensitivity of the cardiac muscarinic potassium channel. A novel property conferred by Kir3.4 subunit....
[ 1995, 1997, 1998, 1999, 1999, 2011, 2010 ]
7
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 646 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 4, 4 ]
3
true
Family
Potassium channel, inwardly rectifying, Kir3.4
Potassium channel, inwardly rectifying, Kir3.4
K_chnl_inward-rec_Kir3.4
6
IPR003278
3,278
Potassium channel, inwardly rectifying, Kir6.1
K_chnl_inward-rec_Kir6.1
Family
783
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0015272", "GO:0006813", "GO:0016020" ]
[ "ATP-activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01331" ]
[ "KIR61CHANNEL" ]
[ 783 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-1296025", "R-MMU-1296025", "R-RNO-1296025" ]
[ "REACTOME:R-HSA-1296025", "REACTOME:R-MMU-1296025", "REACTOME:R-RNO-1296025" ]
3
[ "7mit", "7mjo", "7mjp", "7mjq" ]
4
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008065", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "2555158", "10531400", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1989, 1999, 2000, 1999, 1999 ]
11
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 783 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 3, 3 ]
4
true
Family
Potassium channel, inwardly rectifying, Kir6.1
Potassium channel, inwardly rectifying, Kir6.1
K_chnl_inward-rec_Kir6.1
1
IPR003279
3,279
Potassium channel, inwardly rectifying, Kir6.2
K_chnl_inward-rec_Kir6.2
Family
703
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0015272", "GO:0006813", "GO:0016020" ]
[ "ATP-activated inward rectifier potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01332" ]
[ "KIR62CHANNEL" ]
[ 703 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp2099", "R-HSA-1296025", "R-HSA-382556", "R-HSA-422356", "R-HSA-5578775", "R-HSA-5678420", "R-HSA-5683177", "R-MMU-1296025", "R-MMU-382556", "R-MMU-422356", "R-MMU-5578775", "R-RNO-1296025", "R-RNO-382556", "R-RNO-422356", "R-RNO-5578775" ]
[ "GP:GenProp2099", "REACTOME:R-HSA-1296025", "REACTOME:R-HSA-382556", "REACTOME:R-HSA-422356", "REACTOME:R-HSA-5578775", "REACTOME:R-HSA-5678420", "REACTOME:R-HSA-5683177", "REACTOME:R-MMU-1296025", "REACTOME:R-MMU-382556", "REACTOME:R-MMU-422356", "REACTOME:R-MMU-5578775", "REACTOME:R-RNO-1296...
15
[ "5twv", "5yke", "5ykf", "5ykg", "5yw8", "5yw9", "5ywa", "5ywb", "5ywc", "6baa", "6c3o", "6c3p", "6jb1", "6pz9", "6pza", "7s5t", "7s5x", "7s5y", "7s5z", "7s60", "7s61", "7tys", "7tyt", "7u1e", "7u1q", "7u1s", "7u24", "7u2x", "7u6y", "7u7m", "7uaa", "7uqr"...
38
[ "PUB00001055", "PUB00001069", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00005551", "PUB00006577", "PUB00009378", "PUB00009410", "PUB00009411" ]
[ "1772658", "7580148", "1879548", "1373731", "2448635", "2451788", "9683320", "2555158", "11178249", "10102275", "10449331" ]
[ "The molecular biology of K+ channels.", "The inward rectifier potassium channel family.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced ...
[ 1991, 1995, 1991, 1992, 1988, 1988, 1998, 1989, 2000, 1999, 1999 ]
11
[ "IPR016449" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 703 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 8, 4, 2 ]
4
true
Family
Potassium channel, inwardly rectifying, Kir6.2
Potassium channel, inwardly rectifying, Kir6.2
K_chnl_inward-rec_Kir6.2
6
IPR003280
3,280
Two pore domain potassium channel
2pore_dom_K_chnl
Family
35,427
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0005267", "GO:0071805", "GO:0016020" ]
[ "potassium channel activity", "potassium ion transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PANTHER" ]
[ "PR01333", "PTHR11003" ]
[ "2POREKCHANEL", "" ]
[ 27845, 34331 ]
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-1299308", "R-BTA-5576886", "R-CEL-1299316", "R-CEL-1299503", "R-CEL-5576886", "R-HSA-1299287", "R-HSA-1299308", "R-HSA-1299316", "R-HSA-1299344", "R-HSA-1299361", "R-HSA-1299503", "R-HSA-5576886", "R-MMU-1299287", "R-MMU-1299308", "R-MMU-1299316", "R-MMU-1299344", "R-MMU-12993...
[ "REACTOME:R-BTA-1299308", "REACTOME:R-BTA-5576886", "REACTOME:R-CEL-1299316", "REACTOME:R-CEL-1299503", "REACTOME:R-CEL-5576886", "REACTOME:R-HSA-1299287", "REACTOME:R-HSA-1299308", "REACTOME:R-HSA-1299316", "REACTOME:R-HSA-1299344", "REACTOME:R-HSA-1299361", "REACTOME:R-HSA-1299503", "REACTOM...
32
[ "2ahy", "2ahz", "2q67", "2q68", "2q69", "2q6a", "3e83", "3e86", "3e89", "3e8b", "3e8f", "3e8g", "3e8h", "3k03", "3k04", "3k06", "3k08", "3k0d", "3k0g", "3ouf", "3t1c", "3t2m", "3t4d", "3t4z", "3tcu", "3tet", "3ukm", "3um7", "3vou", "4bw5", "4i9w", "4pdl"...
141
[ "PUB00001055", "PUB00001278", "PUB00001298", "PUB00001308", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00004219", "PUB00004878", "PUB00006577", "PUB00009378" ]
[ "1772658", "8605869", "9003761", "9312005", "1879548", "1373731", "2448635", "2451788", "7651518", "8917578", "2555158", "11178249" ]
[ "The molecular biology of K+ channels.", "TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a novel structure.", "Cloning, functional expression and brain localization of a novel unconventional outward rectifier K+ channel.", "TASK, a human background K+ channel to sense external pH variatio...
[ 1991, 1996, 1996, 1997, 1991, 1992, 1988, 1988, 1995, 1996, 1989, 2000 ]
12
[]
[ "IPR003092", "IPR003976", "IPR005410", "IPR008074" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 234, 1044, 34125, 6, 18 ]
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...
[ 22, 93, 57, 23, 36, 40, 2, 5, 44, 1, 14 ]
11
true
Family
Two pore domain potassium channel
Two pore domain potassium channel
2pore_dom_K_chnl
1
IPR003282
3,282
Type III secretion system lipoprotein SctJ
T3SS_SctJ
Family
3,628
false
false
Secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior. There have been four secretion systems described in animal enteropathogens such as Salmonella and Yersinia, with further sequence similarities in plant pathogens like Ralstoni...
[ "GO:0009306" ]
[ "protein secretion" ]
[ "biological_process" ]
1
[ "PRINTS", "NCBIFAM" ]
[ "PR01338", "TIGR02544" ]
[ "TYPE3OMKPROT", "III_secr_YscJ" ]
[ 3612, 3482 ]
2
[ "GP" ]
[ "GenProp0052" ]
[ "GP:GenProp0052" ]
1
[ "1yj7", "2y9j", "3j6d", "4oyc", "5tcp", "5tcr", "6duz", "6pem", "6q14", "6q15", "6q16", "6rwx", "6uot", "6uov", "7ah9", "7ahi", "8axk", "8axn" ]
18
[ "PUB00007583", "PUB00007701", "PUB00007898", "PUB00106888", "PUB00106889", "PUB00159950" ]
[ "10564516", "8733226", "10334981", "31744874", "32092125", "36790757" ]
[ "Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium.", "Molecular genetic bases of Salmonella entry into host cells.", "Type III secretion machines: bacterial devices for protein delivery into host cells.", "High-re...
[ 1999, 1996, 1999, 2019, 2020, 2023 ]
6
[ "IPR043427" ]
[]
1
0
1
[ "Bacteria", "Beauveria bassiana D1-5", "metagenomes" ]
[ 3621, 1, 6 ]
3
[]
[]
0
true
Family
Type III secretion system lipoprotein SctJ
Type III secretion system lipoprotein SctJ
T3SS_SctJ
2
IPR003283
3,283
Type III secretion system outer membrane, SpaO
T3SS_OMP_SpaO
Family
987
false
false
null
[ "GO:0009306" ]
[ "protein secretion" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01339" ]
[ "TYPE3OMOPROT" ]
[ 987 ]
1
[]
[]
[]
0
[ "3uep", "4tt9", "4yx1", "4yx5", "4yx7", "4yxa" ]
6
[ "PUB00007583", "PUB00007701", "PUB00007898" ]
[ "10564516", "8733226", "10334981" ]
[ "Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium.", "Molecular genetic bases of Salmonella entry into host cells.", "Type III secretion machines: bacterial devices for protein delivery into host cells." ]
[ 1999, 1996, 1999 ]
3
[ "IPR013385" ]
[]
1
0
1
[ "Bacteria", "Candidatus Thalassarchaeum betae", "Diploscapter pachys" ]
[ 985, 1, 1 ]
3
[]
[]
0
true
Family
Type III secretion system outer membrane, SpaO
Type III secretion system outer membrane, SpaO
T3SS_OMP_SpaO
9
IPR003284
3,284
Salmonella virulence plasmid 65kDa B protein
Sal_SpvB
Family
4,239
false
false
null
[ "GO:0005737" ]
[ "cytoplasm" ]
[ "cellular_component" ]
1
[ "PFAM", "PRINTS" ]
[ "PF03534", "PR01341" ]
[ "SpvB", "SALSPVBPROT" ]
[ 4239, 1473 ]
2
[ "EC" ]
[ "2.4.2.31" ]
[ "EC:2.4.2.31" ]
1
[ "4igl", "4o9x", "5kis", "6h6e", "6h6f", "6h6g", "6l7i", "6p0x", "6sue", "6suf", "6sup", "6suq" ]
12
[ "PUB00008066", "PUB00008067", "PUB00008068", "PUB00008069" ]
[ "2164511", "1657882", "8483415", "9234805" ]
[ "Genetic and DNA sequence analysis of the Salmonella typhimurium virulence plasmid gene encoding the 28,000-molecular-weight protein.", "The Salmonella typhimurium virulence plasmid encodes a positive regulator of a plasmid-encoded virulence gene.", "Molecular analysis of spv virulence genes of the Salmonella v...
[ 1990, 1991, 1993, 1997 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 3881, 312, 22, 24 ]
4
[]
[]
0
true
Family
Salmonella virulence plasmid 65kDa B protein
Salmonella virulence plasmid 65kDa B protein
Sal_SpvB
9
IPR003285
3,285
Eukaryotic peptide chain release factor GTP-binding subunit
Sup35
Family
2,084
false
false
Sup35 (also known as eRF3) is a translation termination factor that mediates mRNA decay through the regulation of deadenylation [ ].
[ "GO:0003747", "GO:0005525", "GO:0000288", "GO:0006415" ]
[ "translation release factor activity", "GTP binding", "nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay", "translational termination" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "PRINTS" ]
[ "PR01343" ]
[ "YEASTERF" ]
[ 2084 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-SCE-72764", "R-SCE-975956", "R-SCE-975957", "R-SPO-72764", "R-SPO-975956", "R-SPO-975957" ]
[ "REACTOME:R-SCE-72764", "REACTOME:R-SCE-975956", "REACTOME:R-SCE-975957", "REACTOME:R-SPO-72764", "REACTOME:R-SPO-975956", "REACTOME:R-SPO-975957" ]
6
[ "1r5b", "1r5n", "1r5o", "4crn" ]
4
[ "PUB00078340" ]
[ "12923185" ]
[ "Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2084 ]
1
[ "Arabidopsis thaliana", "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)" ]
[ 4, 2, 1, 1 ]
4
true
Family
Eukaryotic peptide chain release factor GTP-binding subunit
Eukaryotic peptide chain release factor GTP-binding subunit
Sup35
9
IPR003287
3,287
GPCR, family 2, calcitonin receptor family
GPCR_2_calcitonin_rcpt_fam
Family
3,589
false
false
null
[ "GO:0004948", "GO:0007186", "GO:0016020" ]
[ "calcitonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01350" ]
[ "CTRFAMILY" ]
[ 3589 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DRE-419812", "R-HSA-418555", "R-HSA-419812", "R-HSA-9856530", "R-MMU-418555", "R-MMU-419812", "R-MMU-9856530", "R-RNO-419812", "R-RNO-9856530", "R-SSC-418555", "R-SSC-419812", "R-XTR-418555", "R-XTR-419812" ]
[ "REACTOME:R-DRE-419812", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-419812", "REACTOME:R-HSA-9856530", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-419812", "REACTOME:R-MMU-9856530", "REACTOME:R-RNO-419812", "REACTOME:R-RNO-9856530", "REACTOME:R-SSC-418555", "REACTOME:R-SSC-419812", "REACTOME:R-XTR-...
13
[ "3aqf", "3n7p", "3n7r", "3n7s", "5ii0", "5uz7", "6e3y", "6niy", "6umg", "6uun", "6uus", "6uva", "7knt", "7knu", "7tyf", "7tyh", "7tyi", "7tyl", "7tyn", "7tyo", "7tyw", "7tyx", "7tyy", "7tzf", "8f0j", "8f0k", "8f2a", "8f2b", "9auc", "9blb", "9blc", "9blw"...
40
[ "PUB00000991", "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00008072", "PUB00008073", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "8222502", "1646711", "1314625", "8170923", "1658940", "1658941", "8626685", "7818539", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "A new calcitonin-receptor-like sequence in rat pulmonary blood vessels.", "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", ...
[ 1993, 1991, 1992, 1994, 1991, 1991, 1996, 1995, 2003, 1994, 2005, 2009, 2006, 2013 ]
14
[ "IPR000832" ]
[ "IPR001688", "IPR003289" ]
1
2
0
[ "Bilateria" ]
[ 3589 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 6, 7, 7, 10 ]
5
true
Family
GPCR, family 2, calcitonin receptor family
GPCR, family 2, calcitonin receptor family
GPCR_2_calcitonin_rcpt_fam
1
IPR003288
3,288
GPCR, family 2, growth hormone-releasing hormone receptor
GPCR_2_GHRH_rcpt
Family
920
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01352" ]
[ "GHRHRECEPTOR" ]
[ 920 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "247", "R-HSA-418555", "R-HSA-420092", "R-MMU-418555", "R-MMU-420092", "R-RNO-420092" ]
[ "IUPHAR:247", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-420092", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-420092", "REACTOME:R-RNO-420092" ]
6
[ "2xdg", "7cz5", "7v9l", "7v9m" ]
4
[ "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00010569", "PUB00010570", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00100458" ]
[ "1646711", "1314625", "8170923", "1658940", "1658941", "8413847", "7680413", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293", "33060564" ]
[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", "Expression cloning of an adenylate cyclase-coupled calcitonin receptor.", ...
[ 1991, 1992, 1994, 1991, 1991, 1993, 1993, 2003, 1994, 2005, 2009, 2006, 2013, 2020 ]
14
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 920 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 7, 2, 9 ]
4
true
Family
GPCR, family 2, growth hormone-releasing hormone receptor
GPCR, family 2, growth hormone-releasing hormone receptor
GPCR_2_GHRH_rcpt
9
IPR003289
3,289
GPCR, family 2, calcitonin gene-related peptide, type 1 receptor
GPCR_2_CGRP1_rcpt
Family
1,381
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01351" ]
[ "CGRPRECEPTOR" ]
[ 1381 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "48", "R-DRE-419812", "R-HSA-418555", "R-HSA-419812", "R-HSA-9856530", "R-MMU-418555", "R-MMU-419812", "R-MMU-9856530", "R-RNO-419812", "R-RNO-9856530", "R-XTR-418555", "R-XTR-419812" ]
[ "IUPHAR:48", "REACTOME:R-DRE-419812", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-419812", "REACTOME:R-HSA-9856530", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-419812", "REACTOME:R-MMU-9856530", "REACTOME:R-RNO-419812", "REACTOME:R-RNO-9856530", "REACTOME:R-XTR-418555", "REACTOME:R-XTR-419812" ]
12
[ "3aqf", "3n7p", "3n7r", "3n7s", "6e3y", "6umg", "6uun", "6uus", "6uva", "7knt", "7knu", "9mni" ]
12
[ "PUB00000991", "PUB00001208", "PUB00004310", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00008072", "PUB00008073", "PUB00053635", "PUB00061270", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00100463" ]
[ "8222502", "1646711", "1314625", "8170923", "1658940", "1658941", "8626685", "7818539", "12679517", "22102369", "8081729", "15914470", "18948278", "16753280", "23020293", "30115739" ]
[ "A new calcitonin-receptor-like sequence in rat pulmonary blood vessels.", "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.", "Fingerprinting G-protein-coupled receptors.", ...
[ 1993, 1991, 1992, 1994, 1991, 1991, 1996, 1995, 2003, 2012, 1994, 2005, 2009, 2006, 2013, 2018 ]
16
[ "IPR003287" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1381 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 2, 3 ]
4
true
Family
GPCR, family 2, calcitonin gene-related peptide, type 1 receptor
GPCR, family 2, calcitonin gene-related peptide, type 1 receptor
GPCR_2_CGRP1_rcpt
4