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
IPR008111
8,111
RNA-binding motif protein 8
RNA-bd_8
Family
4,496
false
false
RNA-binding motif protein 8 (RBM8), also termed binder of OVCA1-1 (BOV-1) or RNA-binding protein Y14, is one of the components of the exon-exon junction complex (EJC) [ ]. It has two isoforms, RBM8A and RBM8B, both of which are identical except that RBM8B is 16 amino acids shorter at its N terminus [ ]. Three-dimension...
[ "GO:0003723", "GO:0006396", "GO:0005634", "GO:0005737" ]
[ "RNA binding", "RNA processing", "nucleus", "cytoplasm" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PRINTS", "PANTHER" ]
[ "PR01738", "PTHR45894" ]
[ "RNABINDINGM8", "" ]
[ 3955, 4439 ]
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-159236", "R-CEL-72163", "R-CEL-72187", "R-CEL-73856", "R-CEL-975957", "R-DME-159236", "R-DME-72163", "R-DME-72187", "R-DME-73856", "R-DME-975957", "R-DRE-72163", "R-DRE-975957", "R-HSA-159236", "R-HSA-72163", "R-HSA-72187", "R-HSA-73856", "R-HSA-9010553", "R-HSA-975957", "...
[ "REACTOME:R-CEL-159236", "REACTOME:R-CEL-72163", "REACTOME:R-CEL-72187", "REACTOME:R-CEL-73856", "REACTOME:R-CEL-975957", "REACTOME:R-DME-159236", "REACTOME:R-DME-72163", "REACTOME:R-DME-72187", "REACTOME:R-DME-73856", "REACTOME:R-DME-975957", "REACTOME:R-DRE-72163", "REACTOME:R-DRE-975957", ...
33
[ "1hl6", "1oo0", "1p27", "1rk8", "2hyi", "2j0q", "2j0s", "2x1g", "2xb2", "3ex7", "5xjc", "5yzg", "6icz", "6qdv", "7a5p", "7w59", "7w5a", "7w5b", "7znj", "8c6j", "8i0w", "9fmd" ]
22
[ "PUB00007285", "PUB00010263", "PUB00010370", "PUB00010398", "PUB00094479" ]
[ "10662555", "1991323", "11013075", "11691839", "29301961" ]
[ "MAGOH interacts with a novel RNA-binding protein.", "Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence.", "Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif protei...
[ 2000, 1991, 2000, 2001, 2018 ]
5
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4496 ]
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...
[ 2, 1, 1, 2, 3, 4, 1, 5, 2, 1, 17 ]
11
true
Family
RNA-binding motif protein 8
RNA-binding motif protein 8
RNA-bd_8
1
IPR008113
8,113
Septin 2
Septin2
Family
2,340
false
false
Septin 2, also termed NEDD5, was originally cloned in mice. Orthologues from several other species have also been identified. Micro-injection of cells with an anti-septin 2 antibody blocks cytokinesis, giving rise to binucleated cells. Septins were first discovered in budding yeast as a major component of bud neck fila...
[ "GO:0005525", "GO:0051301" ]
[ "GTP binding", "cell division" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR01740" ]
[ "SEPTIN2" ]
[ 2340 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5620912", "R-HSA-5620912", "R-MMU-5620912", "R-RNO-5620912" ]
[ "REACTOME:R-BTA-5620912", "REACTOME:R-HSA-5620912", "REACTOME:R-MMU-5620912", "REACTOME:R-RNO-5620912" ]
4
[ "2qa5", "2qag", "2qnr", "3ftq", "6upa", "6upq", "6upr", "9bht" ]
8
[ "PUB00010278", "PUB00073422", "PUB00073423", "PUB00073424", "PUB00073425" ]
[ "4950437", "773946", "22314400", "21990096", "24469395" ]
[ "Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis.", "A highly ordered ring of membrane-associated filaments in budding yeast.", "Septins: the fourth component of the cytoskeleton.", "Mammalian septins: dynamic heteromers with roles in cellular morphogen...
[ 1971, 1976, 2012, 2012, 2014 ]
5
[ "IPR016491" ]
[]
1
0
1
[ "Eumetazoa" ]
[ 2340 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 5, 4, 5 ]
4
true
Family
Septin 2
Septin 2
Septin2
2
IPR008115
8,115
Septin 7
Septin7
Family
3,167
false
false
Septin 7 (SEPT7) belongs to the septin family. It forms complexes with SEPT4/SEPT8 or SEPT5/SEPT11, and appears to be a common element in most such septin complexes and it has both unusual genomic and structural features [ ]. There are two paralogous septin 7 genes in zebrafish, sept7a and sept7b, among which Sept7b is...
[ "GO:0005525", "GO:0031105" ]
[ "GTP binding", "septin complex" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01742" ]
[ "SEPTIN7" ]
[ 3167 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-5687128", "R-MMU-5687128", "R-RNO-5687128" ]
[ "REACTOME:R-HSA-5687128", "REACTOME:R-MMU-5687128", "REACTOME:R-RNO-5687128" ]
3
[ "2qag", "9bht", "9bhw" ]
3
[ "PUB00010278", "PUB00073422", "PUB00073423", "PUB00073424", "PUB00073425", "PUB00073430", "PUB00073431", "PUB00073432", "PUB00073433" ]
[ "4950437", "773946", "22314400", "21990096", "24469395", "18460473", "24496452", "24346071", "24345743" ]
[ "Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis.", "A highly ordered ring of membrane-associated filaments in budding yeast.", "Septins: the fourth component of the cytoskeleton.", "Mammalian septins: dynamic heteromers with roles in cellular morphogen...
[ 1971, 1976, 2012, 2012, 2014, 2008, 2014, 2013, 2013 ]
9
[ "IPR016491" ]
[]
1
0
1
[ "Bilateria" ]
[ 3167 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 19, 14, 6, 12 ]
4
true
Family
Septin 7
Septin 7
Septin7
2
IPR008116
8,116
Sequence-specific single-strand DNA-binding protein
SSDP_DNA-bd
Family
5,609
false
false
The sequence-specific single-strand DNA-binding protein (SSDP) family is thought to be involved in transciption regulation. SSDP specifically binds single-stranded pyrimidine-rich mirror repeat elements commonly found in promoter regions, and is believed to regulate alpha-2(I) collagen [ ]. It has been identified as a ...
[ "GO:0003697" ]
[ "single-stranded DNA binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01743" ]
[ "SSDNABINDING" ]
[ 5609 ]
1
[]
[]
[]
0
[ "6iwv", "6s9r", "6tyd", "8hib" ]
4
[ "PUB00010325" ]
[ "9531483" ]
[ "Cloning and characterization of a novel sequence-specific single-stranded-DNA-binding protein." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5609 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 15, 4, 12, 13, 22 ]
5
true
Family
Sequence-specific single-strand DNA-binding protein
Sequence-specific single-strand DNA-binding protein
SSDP_DNA-bd
6
IPR008117
8,117
Micronemal protein 1
Microneme_MIC1
Family
58
false
false
Toxoplasma gondii is an obligate intracellular apicomplexan protozoan parasite, with a complex lifestyle involving varied hosts [ ]. It has two phases of growth: an intestinal phase in feline hosts, and an extra-intestinal phase in other mammals. Oocysts from infected cats develop into tachyzoites, and eventually, brad...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01744" ]
[ "MIC1MICRNEME" ]
[ 58 ]
1
[]
[]
[]
0
[ "2bvb", "2jh1", "2jh7", "2jhd", "2k2s", "3f53", "3f5a", "3f5e" ]
8
[ "PUB00010384", "PUB00010595" ]
[ "11269320", "10631570" ]
[ "Armed and dangerous: Toxoplasma gondii uses an arsenal of secretory proteins to infect host cells.", "Experimental approaches to understanding virulence in toxoplasmosis." ]
[ 1999, 1999 ]
2
[]
[]
0
0
null
[ "Sarcocystidae" ]
[ 58 ]
1
[]
[]
0
true
Family
Micronemal protein 1
Micronemal protein 1
Microneme_MIC1
2
IPR008118
8,118
Dense granule Gra2 protein
Gra2_protein
Family
35
false
false
Toxoplasma gondii is an obligate intracellular apicomplexan protozoan parasite, with a complex lifestyle involving varied hosts [ ]. It has two phases of growth: an intestinal phase in feline hosts, and an extra-intestinal phase in other mammals. Oocysts from infected cats develop into tachyzoites, and eventually, brad...
[]
[]
[]
0
[ "PIRSF", "PRINTS" ]
[ "PIRSF007972", "PR01745" ]
[ "Gra2_protein", "DENSEGRNULE2" ]
[ 8, 35 ]
2
[]
[]
[]
0
[]
0
[ "PUB00010297", "PUB00010333", "PUB00010384" ]
[ "8384696", "9664038", "11269320" ]
[ "Molecular characterization of a dense granule antigen (Gra 2) associated with the network of the parasitophorous vacuole in Toxoplasma gondii.", "The amphipathic alpha helices of the toxoplasma protein GRA2 mediate post-secretory membrane association.", "Armed and dangerous: Toxoplasma gondii uses an arsenal o...
[ 1993, 1998, 1999 ]
3
[]
[]
0
0
null
[ "Gammaproteobacteria", "Sarcocystidae" ]
[ 15, 20 ]
2
[]
[]
0
true
Family
Dense granule Gra2 protein
Dense granule Gra2 protein
Gra2_protein
2
IPR008120
8,120
Dense granule Gra7 protein
Dense_granule_Gra7_protein
Family
166
false
false
Toxoplasma gondii is an obligate intracellular apicomplexan protozoan parasite, with a complex lifestyle involving varied hosts [ ]. It has two phases of growth: an intestinal phase in feline hosts, and an extra-intestinal phase in other mammals. Oocysts from infected cats develop into tachyzoites, and eventually, brad...
[ "GO:0005576" ]
[ "extracellular region" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR01747" ]
[ "DENSEGRNULE7" ]
[ 166 ]
1
[]
[]
[]
0
[]
0
[ "PUB00010326", "PUB00010384" ]
[ "9566517", "11269320" ]
[ "Identification and heterologous expression of a new dense granule protein (GRA7) from Toxoplasma gondii.", "Armed and dangerous: Toxoplasma gondii uses an arsenal of secretory proteins to infect host cells." ]
[ 1998, 1999 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "hydrothermal vent metagenome" ]
[ 84, 75, 6, 1 ]
4
[]
[]
0
true
Family
Dense granule Gra7 protein
Dense granule Gra7 protein
Dense_granule_Gra7_protein
7
IPR008121
8,121
Transcription factor AP-2 alpha, N-terminal
TF_AP2_alpha_N
Domain
1,360
false
false
Activator protein-2 (AP-2) transcription factors constitute a family of closely related and evolutionarily conserved proteins that bind to the DNA consensus sequence 5'-GCCNNNGGC-3' and stimulate target gene transcription [ , ]. Five different isoforms of AP-2 have been identified in mammals, termed AP-2 alpha, beta, g...
[ "GO:0003700", "GO:0006355", "GO:0005634" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01749" ]
[ "AP2ATNSCPFCT" ]
[ 1360 ]
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-8864260", "R-BTA-8866904", "R-BTA-8866907", "R-BTA-8869496", "R-BTA-9834899", "R-HSA-3232118", "R-HSA-8864260", "R-HSA-8866904", "R-HSA-8866906", "R-HSA-8866907", "R-HSA-8866910", "R-HSA-8866911", "R-HSA-8869496", "R-HSA-9764790", "R-HSA-9824585", "R-HSA-9834899", "R-HSA-99382...
[ "REACTOME:R-BTA-8864260", "REACTOME:R-BTA-8866904", "REACTOME:R-BTA-8866907", "REACTOME:R-BTA-8869496", "REACTOME:R-BTA-9834899", "REACTOME:R-HSA-3232118", "REACTOME:R-HSA-8864260", "REACTOME:R-HSA-8866904", "REACTOME:R-HSA-8866906", "REACTOME:R-HSA-8866907", "REACTOME:R-HSA-8866910", "REACTOM...
27
[]
0
[ "PUB00010264", "PUB00010265", "PUB00010273", "PUB00010302", "PUB00010332", "PUB00010369", "PUB00010381", "PUB00099637", "PUB00099638" ]
[ "1998122", "2010091", "3040262", "8622766", "9632718", "10864206", "11137286", "27176626", "11694877" ]
[ "Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins.", "Analysis of the DNA-binding and activation properties of the human transcription factor AP-2.", "Positive and negative regulation of transcription in vitro: enhancer-binding protein AP-2 is inhibited by S...
[ 1991, 1991, 1987, 1996, 1998, 2000, 2000, 2016, 2001 ]
9
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1360 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 4, 7, 10 ]
4
true
Domain
Transcription factor AP-2 alpha, N-terminal
Transcription factor AP-2 alpha, N-terminal
TF_AP2_alpha_N
3
IPR008122
8,122
Transcription factor AP-2 beta
TF_AP2_beta
Family
1,202
false
false
Activator protein-2 (AP-2) transcription factors constitute a family of closely related and evolutionarily conserved proteins that bind to the DNA consensus sequence 5'-GCCNNNGGC-3' and stimulate target gene transcription [ , ]. Five different isoforms of AP-2 have been identified in mammals, termed AP-2 alpha, beta, g...
[ "GO:0003700", "GO:0006355", "GO:0005634" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01750" ]
[ "AP2BTNSCPFCT" ]
[ 1202 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-8866904", "R-CFA-8866907", "R-CFA-9834899", "R-HSA-3232118", "R-HSA-8866904", "R-HSA-8866907", "R-HSA-8866910", "R-HSA-9834899", "R-MMU-8866904", "R-MMU-8866907", "R-MMU-9834899" ]
[ "REACTOME:R-CFA-8866904", "REACTOME:R-CFA-8866907", "REACTOME:R-CFA-9834899", "REACTOME:R-HSA-3232118", "REACTOME:R-HSA-8866904", "REACTOME:R-HSA-8866907", "REACTOME:R-HSA-8866910", "REACTOME:R-HSA-9834899", "REACTOME:R-MMU-8866904", "REACTOME:R-MMU-8866907", "REACTOME:R-MMU-9834899" ]
11
[]
0
[ "PUB00010264", "PUB00010265", "PUB00010283", "PUB00010332", "PUB00010369", "PUB00010381", "PUB00099637", "PUB00099638" ]
[ "1998122", "2010091", "7555706", "9632718", "10864206", "11137286", "27176626", "11694877" ]
[ "Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins.", "Analysis of the DNA-binding and activation properties of the human transcription factor AP-2.", "Cloning and characterization of a second AP-2 transcription factor: AP-2 beta.", "Loss of AP-2 results in...
[ 1991, 1991, 1995, 1998, 2000, 2000, 2016, 2001 ]
8
[ "IPR004979" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1202 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 4, 5, 5 ]
4
true
Family
Transcription factor AP-2 beta
Transcription factor AP-2 beta
TF_AP2_beta
1
IPR008123
8,123
Transcription factor AP-2 gamma
TF_AP2_gamma
Family
259
false
false
Activator protein-2 (AP-2) transcription factors constitute a family of closely related and evolutionarily conserved proteins that bind to the DNA consensus sequence 5'-GCCNNNGGC-3' and stimulate target gene transcription [ , ]. Five different isoforms of AP-2 have been identified in mammals, termed AP-2 alpha, beta, g...
[ "GO:0003700", "GO:0006355", "GO:0005634" ]
[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription", "nucleus" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01751" ]
[ "AP2CTNSCPFCT" ]
[ 259 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-3232118", "R-HSA-8866904", "R-HSA-8866906", "R-HSA-8866907", "R-HSA-8866910", "R-HSA-8866911", "R-HSA-9827857", "R-HSA-9834899", "R-HSA-9938206", "R-MMU-3232118", "R-MMU-8866904", "R-MMU-8866907", "R-MMU-8866911", "R-MMU-9834899" ]
[ "REACTOME:R-HSA-3232118", "REACTOME:R-HSA-8866904", "REACTOME:R-HSA-8866906", "REACTOME:R-HSA-8866907", "REACTOME:R-HSA-8866910", "REACTOME:R-HSA-8866911", "REACTOME:R-HSA-9827857", "REACTOME:R-HSA-9834899", "REACTOME:R-HSA-9938206", "REACTOME:R-MMU-3232118", "REACTOME:R-MMU-8866904", "REACTOM...
14
[]
0
[ "PUB00010264", "PUB00010265", "PUB00010304", "PUB00010332", "PUB00010369", "PUB00010381", "PUB00099637", "PUB00099638", "PUB00099639" ]
[ "1998122", "2010091", "8808408", "9632718", "10864206", "11137286", "27176626", "11694877", "24413532" ]
[ "Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins.", "Analysis of the DNA-binding and activation properties of the human transcription factor AP-2.", "AP-2.2, a novel gene related to AP-2, is expressed in the forebrain, limbs and face during mouse embryogene...
[ 1991, 1991, 1996, 1998, 2000, 2000, 2016, 2001, 2014 ]
9
[ "IPR004979" ]
[]
1
0
1
[ "Eutheria" ]
[ 259 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 5, 5 ]
3
true
Family
Transcription factor AP-2 gamma
Transcription factor AP-2 gamma
TF_AP2_gamma
2
IPR008124
8,124
Streptokinase
SK
Family
194
false
false
Streptokinase (SK) can be found in several species of Streptococci. It can bind not only plasminogen, but also host fibrinogen [ ]. This close interaction with the human fibrinolytic system allows the microbe to acquire unregulatable cell-surface enzymatic activity, promoting further spread from the site of infection. ...
[ "GO:0031639", "GO:0005576" ]
[ "plasminogen activation", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01753" ]
[ "STREPKINASE" ]
[ 194 ]
1
[]
[]
[]
0
[ "1bml", "1c4p", "1l4z", "1qqr" ]
4
[ "PUB00010284", "PUB00070735" ]
[ "7565010", "17948083" ]
[ "Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen.", "A history of streptokinase use in acute myocardial infarction." ]
[ 1995, 2007 ]
2
[]
[]
0
0
null
[ "Streptococcus" ]
[ 194 ]
1
[]
[]
0
true
Family
Streptokinase
Streptokinase
SK
6
IPR008125
8,125
Streptothricin acetyltransferase
Streptothricin_AcTrfase
Family
1,756
false
false
A small number of bacterial pathogens are implicated in urinary tract infections (UTIs), amongst the most frequent infections in the developed world. The commonest bacterium isolated from UTI is Escherichia coli, with streptococcal and staphylococcal species coming a close second [ ]. Virulent microbes that colonise th...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01754" ]
[ "SACTRNSFRASE" ]
[ 1756 ]
1
[]
[]
[]
0
[ "3pp9" ]
1
[ "PUB00010405" ]
[ "11753131" ]
[ "Virulence factors of uropathogens." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 1707, 47, 2 ]
3
[]
[]
0
true
Family
Streptothricin acetyltransferase
Streptothricin acetyltransferase
Streptothricin_AcTrfase
8
IPR008126
8,126
Outer membrane adhesion, Yersinia
OM_adhesion_Yersinia
Family
59
false
false
The genus Yersinia contains just three species: Yersinia enterocolitica, Yersinia pestis, and Yersinia pseudotuberculosis [ ]. Although the three use different routes to infect their host, each targets the lymphoid tissue for invasion, and all have developed specific systems to evade host immune cells [ ]. PYV, a major...
[ "GO:0005518", "GO:0007155", "GO:0019867" ]
[ "collagen binding", "cell adhesion", "outer membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01756" ]
[ "OMADHESIN" ]
[ 59 ]
1
[]
[]
[]
0
[]
0
[ "PUB00010288", "PUB00010303", "PUB00010380", "PUB00010396" ]
[ "7689542", "8767710", "11080146", "11554561" ]
[ "The Yersinia pseudotuberculosis adhesin YadA mediates intimate bacterial attachment to and entry into HEp-2 cells.", "Molecular determinants of Yersinia pathogenesis.", "Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins.", "YadA, the multifaceted Yersinia a...
[ 1993, 1996, 2000, 2001 ]
4
[]
[]
0
0
null
[ "Pseudomonadota" ]
[ 59 ]
1
[]
[]
0
true
Family
Outer membrane adhesion, Yersinia
Outer membrane adhesion, Yersinia
OM_adhesion_Yersinia
5
IPR008128
8,128
Glycine receptor alpha1
Glycine_rcpt_A1
Family
696
false
false
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [ , ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily: Nicot...
[ "GO:0016934", "GO:0006821", "GO:0016020", "GO:0045211" ]
[ "extracellularly glycine-gated chloride channel activity", "chloride transport", "membrane", "postsynaptic membrane" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01674" ]
[ "GLYRALPHA1" ]
[ 696 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-112314", "R-DRE-112314", "R-HSA-112314", "R-MMU-112314", "R-RNO-112314" ]
[ "REACTOME:R-BTA-112314", "REACTOME:R-DRE-112314", "REACTOME:R-HSA-112314", "REACTOME:R-MMU-112314", "REACTOME:R-RNO-112314" ]
5
[ "6plo", "6plp", "6plq", "6plr", "6pls", "6plt", "6plu", "6plv", "6plw", "6plx", "6ply", "6plz", "6pm0", "6pm1", "6pm2", "6pm3", "6pm4", "6pm5", "6pm6", "6pxd", "6ubs", "6ubt", "6ud3", "6vm0", "6vm2", "6vm3", "7m6m", "7m6n", "7m6o", "7m6p", "7m6q", "7m6r"...
42
[ "PUB00000213", "PUB00002675", "PUB00003455", "PUB00010340", "PUB00010348", "PUB00010386", "PUB00010388", "PUB00010391", "PUB00010598", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]
[ "1323284", "1721053", "1846404", "10026168", "10414351", "11358478", "11396606", "11437237", "12036901", "18446614", "15383648", "18760291", "15165736" ]
[ "Proposed tertiary structure of the sodium channel.", "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.", "Structural features of the ligand-binding ...
[ 1992, 1991, 1991, 1999, 1999, 2001, 2001, 2001, 2002, 2008, 2004, 2008, 2004 ]
13
[ "IPR008127" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 696 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 1, 2, 5 ]
4
true
Family
Glycine receptor alpha1
Glycine receptor alpha1
Glycine_rcpt_A1
3
IPR008129
8,129
Glycine receptor alpha2
Glycine_rcpt_A2
Family
642
false
false
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [ , ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily: Nicot...
[ "GO:0016934", "GO:0006821", "GO:0016020", "GO:0045211" ]
[ "extracellularly glycine-gated chloride channel activity", "chloride transport", "membrane", "postsynaptic membrane" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01675" ]
[ "GLYRALPHA2" ]
[ 642 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-112314", "R-MMU-112314", "R-RNO-112314" ]
[ "REACTOME:R-HSA-112314", "REACTOME:R-MMU-112314", "REACTOME:R-RNO-112314" ]
3
[]
0
[ "PUB00000213", "PUB00002675", "PUB00003455", "PUB00010340", "PUB00010348", "PUB00010386", "PUB00010388", "PUB00010391", "PUB00010599", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]
[ "1323284", "1721053", "1846404", "10026168", "10414351", "11358478", "11396606", "11437237", "9674912", "18446614", "15383648", "18760291", "15165736" ]
[ "Proposed tertiary structure of the sodium channel.", "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.", "Structural features of the ligand-binding ...
[ 1992, 1991, 1991, 1999, 1999, 2001, 2001, 2001, 1998, 2008, 2004, 2008, 2004 ]
13
[ "IPR008127" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 642 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 2, 5 ]
4
true
Family
Glycine receptor alpha2
Glycine receptor alpha2
Glycine_rcpt_A2
5
IPR008131
8,131
Early E3 14.5kDa protein
Adeno_E3_14_5
Family
244
false
false
The E3B 14.5kDa was first identified in human adenovirus type 5. It is an integral membrane protein oriented with its C terminus in the cytoplasm. It functions to down-regulate the epidermal growth factor receptor and prevent tumour necrosis factor cytolysis. It achieves this through the interaction with E3 10.4kDa pro...
[ "GO:0009966", "GO:0016020" ]
[ "regulation of signal transduction", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF04834" ]
[ "Adeno_E3_14_5" ]
[ 244 ]
1
[]
[]
[]
0
[]
0
[ "PUB00008658", "PUB00008659" ]
[ "1531370", "9488477" ]
[ "The adenovirus E3 14.5-kilodalton protein, which is required for down-regulation of the epidermal growth factor receptor and prevention of tumor necrosis factor cytolysis, is an integral membrane protein oriented with its C terminus in the cytoplasm.", "Interaction of an adenovirus E3 14.7-kilodalton protein wit...
[ 1992, 1998 ]
2
[]
[]
0
0
null
[ "Mastadenovirus" ]
[ 244 ]
1
[]
[]
0
true
Family
Early E3 14.5kDa protein
Early E3 14.5kDa protein
Adeno_E3_14_5
3
IPR008133
8,133
5-hydroxytryptamine 3 receptor, A subunit
5HT3_rcpt_A
Family
1,213
false
false
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [ , ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily: Nicot...
[ "GO:0015276", "GO:0006811", "GO:0016020", "GO:0045211" ]
[ "ligand-gated monoatomic ion channel activity", "monoatomic ion transport", "membrane", "postsynaptic membrane" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01709" ]
[ "5HT3ARECEPTR" ]
[ 1213 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-112314", "R-MMU-112314", "R-RNO-112314" ]
[ "REACTOME:R-HSA-112314", "REACTOME:R-MMU-112314", "REACTOME:R-RNO-112314" ]
3
[ "4pir", "6be1", "6dg7", "6dg8", "6hin", "6hio", "6hiq", "6his", "6np0", "6w1j", "6w1m", "6w1y", "6y1z", "6y59", "6y5a", "6y5b", "8aw2", "8axd", "8bl8", "8bla", "8blb", "8c1w", "8c1z", "8c20", "8c21", "8cc6", "8cc7", "8frw", "8frx", "8frz", "8fsb", "8fsp"...
33
[ "PUB00002675", "PUB00003455", "PUB00010261", "PUB00010338", "PUB00010340", "PUB00010347", "PUB00010368", "PUB00010386", "PUB00010418", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]
[ "1721053", "1846404", "1718042", "9950429", "10026168", "10405996", "10825381", "11358478", "11871776", "18446614", "15383648", "18760291", "15165736" ]
[ "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.", "Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel.",...
[ 1991, 1991, 1991, 1999, 1999, 1999, 2000, 2001, 2002, 2008, 2004, 2008, 2004 ]
13
[ "IPR008132" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1213 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 5, 4, 12 ]
4
true
Family
5-hydroxytryptamine 3 receptor, A subunit
5-hydroxytryptamine 3 receptor, A subunit
5HT3_rcpt_A
4
IPR008134
8,134
5-hydroxytryptamine 3 receptor, B subunit
5HT3_rcpt_B
Family
171
false
false
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [ , ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily: Nicot...
[ "GO:0015276", "GO:0006811", "GO:0016020" ]
[ "ligand-gated monoatomic ion channel activity", "monoatomic ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01710" ]
[ "5HT3BRECEPTR" ]
[ 171 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-112314", "R-MMU-112314", "R-RNO-112314" ]
[ "REACTOME:R-HSA-112314", "REACTOME:R-MMU-112314", "REACTOME:R-RNO-112314" ]
3
[]
0
[ "PUB00002675", "PUB00003455", "PUB00010338", "PUB00010340", "PUB00010347", "PUB00010356", "PUB00010368", "PUB00010386", "PUB00010418", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]
[ "1721053", "1846404", "9950429", "10026168", "10405996", "10521471", "10825381", "11358478", "11871776", "18446614", "15383648", "18760291", "15165736" ]
[ "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-subunit in mice by alternative splicing.", "The 5-HT3B subunit is a major determinant of serotonin-receptor function.", "Structural features...
[ 1991, 1991, 1999, 1999, 1999, 1999, 2000, 2001, 2002, 2008, 2004, 2008, 2004 ]
13
[ "IPR008132" ]
[]
1
0
1
[ "Theria" ]
[ 171 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 4 ]
3
true
Family
5-hydroxytryptamine 3 receptor, B subunit
5-hydroxytryptamine 3 receptor, B subunit
5HT3_rcpt_B
3
IPR008135
8,135
Competence-induced protein CinA
Competence-induced_CinA
Family
11,098
false
false
CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation [ ]. This family consists of putative competence-damaged proteins from the cin operon, and nicotinamide-nucleotide (NMN) amidohydrolase proteins. In the case of T. t...
[]
[]
[]
0
[ "HAMAP", "PIRSF", "NCBIFAM" ]
[ "MF_00226_B", "PIRSF006728", "TIGR00200" ]
[ "CinA_B", "CinA", "cinA_nterm" ]
[ 10912, 10796, 10542 ]
3
[]
[]
[]
0
[ "4ct8", "4ct9", "4cta", "4uoc", "4uuw", "4uux", "6mr3" ]
7
[ "PUB00009509", "PUB00052316", "PUB00073253" ]
[ "7538190", "8901420", "25313401" ]
[ "The recA gene of Streptococcus pneumoniae is part of a competence-induced operon and controls lysogenic induction.", "Who's competent and when: regulation of natural genetic competence in bacteria.", "Structure and Mechanism of the Bifunctional CinA Enzyme from Thermus thermophilus." ]
[ 1995, 1996, 2014 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 10928, 13, 157 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Competence-induced protein CinA
Competence-induced protein CinA
Competence-induced_CinA
6
IPR008139
8,139
Saposin B type domain
SaposinB_dom
Domain
17,985
false
false
The saposin B-type domain is a ~80 amino acid domain present in saposins and related proteins that interact with lipids. The domain is named after the small lysosomal proteins, saposins, which serve as sphingolipid hydrolase activator proteins in vertebrates. The mammalian saposins are synthesized as a single precursor...
[]
[]
[]
0
[ "PROFILE", "SMART" ]
[ "PS50015", "SM00741" ]
[ "SAP_B", "SapB" ]
[ 17884, 12446 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC50015", "R-BTA-5683826", "R-BTA-9840310", "R-CEL-9840310", "R-DDI-6798695", "R-DDI-8964038", "R-DDI-9840310", "R-HSA-114608", "R-HSA-375276", "R-HSA-418594", "R-HSA-5683826", "R-HSA-5688031", "R-HSA-5688849", "R-HSA-5688890", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-9840310", ...
[ "PROSITEDOC:PDOC50015", "REACTOME:R-BTA-5683826", "REACTOME:R-BTA-9840310", "REACTOME:R-CEL-9840310", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-8964038", "REACTOME:R-DDI-9840310", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-5683826", "REACTOME:R-H...
29
[ "1l9l", "1m12", "1n69", "1nkl", "1of9", "1qdm", "1sn6", "2dob", "2gtg", "2js9", "2jsa", "2qyp", "2r0r", "2r1q", "2rb3", "2z9a", "3bqp", "3bqq", "3rfi", "3s63", "3s64", "4ddj", "4uex", "4uq8", "4v2o", "5fi9", "5fib", "5fic", "5i81", "5i85", "5i8r", "5j4z"...
58
[ "PUB00005721", "PUB00005742", "PUB00005747", "PUB00005765", "PUB00010538", "PUB00014083", "PUB00018079", "PUB00018080" ]
[ "8003971", "7610480", "7595087", "8868085", "12518053", "10406799", "11513801", "12826659" ]
[ "Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.", "Swaposins: circular permutations within genes encoding saposin homologues.", "Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure.", "Cytotoxic T cells: more weapons for n...
[ 1994, 1995, 1995, 1996, 2003, 1999, 2001, 2003 ]
8
[]
[ "IPR048593" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Orpheovirus IHUMI-LCC2", "metagenomes" ]
[ 10, 4, 17964, 1, 6 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 33, 35, 15, 14, 32, 40, 25, 28, 105 ]
9
true
Domain
Saposin B type domain
Saposin B type domain
SaposinB_dom
3
IPR008141
8,141
Alanine dehydrogenase
Ala_DH
Family
17,870
false
false
The family of known L-alanine dehydrogenases includes representatives from the Proteobacteria, Firmicutes, and Cyanobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homologue from Helicobacter pylori, an epsilon division Proteobacteria, which must be con...
[ "GO:0000286", "GO:0042853" ]
[ "alanine dehydrogenase activity", "L-alanine catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "NCBIFAM", "CDD" ]
[ "PIRSF000183", "TIGR00518", "cd05305" ]
[ "Alanine_dh", "alaDH", "L-AlaDH" ]
[ 15204, 15336, 17870 ]
3
[ "EC" ]
[ "1.4.1.1" ]
[ "EC:1.4.1.1" ]
1
[ "1pjb", "1pjc", "1say", "2eez", "2vhv", "2vhw", "2vhx", "2vhy", "2vhz", "2voe", "2voj", "4lmp", "6o7f", "8hye", "8hyh" ]
15
[ "PUB00070786" ]
[ "11888165" ]
[ "Glycine and alanine dehydrogenase activities are catalyzed by the same protein in Mycobacterium smegmatis: upregulation of both activities under microaerophilic adaptation." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Synechococcus phage S-N03", "unclassified sequences" ]
[ 17427, 72, 18, 1, 352 ]
5
[]
[]
0
true
Family
Alanine dehydrogenase
Alanine dehydrogenase
Ala_DH
5
IPR008142
8,142
Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1
AlaDH/PNT_CS1
Conserved_site
8,997
false
false
Alanine dehydrogenases (AlaDH) and NAD(P) transhydrogenase subunit alpha (PNT) have been shown to share regions of similarity [ ]. AlaDH catalyses the NAD-dependent reversible reductive amination of pyruvate into alanine. PNT catalyses the reduction of NADP + to NADPH with the concomitant oxidation of NADH to NAD + . T...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00836" ]
[ "ALADH_PNT_1" ]
[ 8997 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.4.1.1", "PDOC00654", "R-BTA-71403", "R-HSA-71403", "R-MMU-71403" ]
[ "EC:1.4.1.1", "PROSITEDOC:PDOC00654", "REACTOME:R-BTA-71403", "REACTOME:R-HSA-71403", "REACTOME:R-MMU-71403" ]
5
[ "1f8g", "1hzz", "1l7d", "1l7e", "1nm5", "1ptj", "1u28", "1u2d", "1u2g", "1x13", "1x14", "1x15", "1xlt", "2bru", "2fr8", "2frd", "2fsv", "2oo5", "2oor", "2vhv", "2vhw", "2vhx", "2vhy", "2vhz", "2voe", "2voj", "4lmp", "6o7f", "6qti", "6que", "6s59", "8hye"...
32
[ "PUB00000218" ]
[ "8439307" ]
[ "Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteria", "metagenomes" ]
[ 6560, 2403, 5, 29 ]
4
[ "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]
[ 2, 1, 9, 9, 1, 6 ]
6
true
Conserved_site
Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1
Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1
AlaDH/PNT_CS1
5
IPR008143
8,143
Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2
Ala_DH/PNT_CS2
Conserved_site
22,346
false
false
Alanine dehydrogenases ( ) and pyridine nucleotide transhydrogenase ( ) have been shown to share regions of similarity [ ]. Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine. Pyridine nucleotide transhydrogenase catalyzes the reduction of NADP + to NADPH with the ...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00837" ]
[ "ALADH_PNT_2" ]
[ 22346 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.4.1.1", "PDOC00654", "R-BTA-71403", "R-HSA-71403", "R-MMU-71403" ]
[ "EC:1.4.1.1", "PROSITEDOC:PDOC00654", "REACTOME:R-BTA-71403", "REACTOME:R-HSA-71403", "REACTOME:R-MMU-71403" ]
5
[ "1f8g", "1hzz", "1l7d", "1l7e", "1nm5", "1pjb", "1pjc", "1ptj", "1say", "1u28", "1u2d", "1u2g", "1x13", "1x14", "1x15", "1xlt", "2bru", "2eez", "2fr8", "2frd", "2fsv", "2oo5", "2oor", "2vhv", "2vhw", "2vhx", "2vhy", "2vhz", "2voe", "2voj", "4dio", "4izh"...
43
[ "PUB00000218" ]
[ "8439307" ]
[ "Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]
[ 19154, 2726, 52, 414 ]
4
[ "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]
[ 22, 1, 6, 9, 1, 6 ]
6
true
Conserved_site
Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2
Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2
Ala_DH/PNT_CS2
3
IPR008144
8,144
Guanylate kinase-like domain
Guanylate_kin-like_dom
Domain
88,582
false
false
Guanylate kinase ( ) (GK) [ ] catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has b...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS50052" ]
[ "GUANYLATE_KINASE_2" ]
[ 88582 ]
1
[ "EC", "EC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "2.7.4", "2.7.4.8", "PWY-7221", "PWY-8289", "PDOC00670", "R-BTA-499943", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013406", "R-BTA-9013408", "R-BTA-9013423", "R-BTA-9748787", "R-CEL-212676", "R-CEL-438066", "R-CEL-451308", "R-CEL-6794361", "R-CEL-8849932", "R-CFA-399719", "R-CFA-...
[ "EC:2.7.4", "EC:2.7.4.8", "METACYC:PWY-7221", "METACYC:PWY-8289", "PROSITEDOC:PDOC00670", "REACTOME:R-BTA-499943", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013408", "REACTOME:R-BTA-9013423", "REACTOME:R-BTA-9748787", "REACTOME:R-CEL-21267...
131
[ "1ex6", "1ex7", "1gky", "1jxm", "1jxo", "1kgd", "1kjw", "1lvg", "1s4q", "1s96", "1xzp", "1xzq", "1z6g", "1z8f", "1znw", "1znx", "1zny", "1znz", "2an9", "2anb", "2anc", "2f3r", "2f3t", "2j41", "2qor", "2xkx", "3kfv", "3lh5", "3lnc", "3ney", "3shw", "3tau"...
82
[ "PUB00000870", "PUB00001440", "PUB00003284", "PUB00003556", "PUB00005396" ]
[ "1310897", "8097461", "1314905", "8155583", "1329277" ]
[ "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene.", "Purification and sequence determination of guanylate kinase from pig brain.", "Refined structure of the complex between guanylate kinase and its sub...
[ 1992, 1993, 1992, 1993, 1992 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 51, 28338, 59384, 157, 652 ]
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",...
[ 28, 17, 577, 55, 1, 156, 87, 2, 5, 148, 1, 1, 15 ]
13
true
Domain
Guanylate kinase-like domain
Guanylate kinase-like domain
Guanylate_kin-like_dom
7
IPR008145
8,145
Guanylate kinase/L-type calcium channel beta subunit
GK/Ca_channel_bsu
Domain
99,284
false
false
This entry represents a domain found in guanylate kinase ( ) and in L-type calcium channel. Guanylate kinase ( ) (GK) [ ] catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and i...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF00625", "SM00072" ]
[ "Guanylate_kin", "GuKc" ]
[ 96176, 97027 ]
2
[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "R...
[ "2.7.4.8", "PWY-7221", "PWY-8289", "R-BTA-112308", "R-BTA-422356", "R-BTA-499943", "R-BTA-5576892", "R-BTA-5576893", "R-BTA-9013149", "R-BTA-9013404", "R-BTA-9013406", "R-BTA-9013408", "R-BTA-9013423", "R-BTA-9748787", "R-CEL-212676", "R-CEL-438066", "R-CEL-451308", "R-CEL-6794361"...
[ "EC:2.7.4.8", "METACYC:PWY-7221", "METACYC:PWY-8289", "REACTOME:R-BTA-112308", "REACTOME:R-BTA-422356", "REACTOME:R-BTA-499943", "REACTOME:R-BTA-5576892", "REACTOME:R-BTA-5576893", "REACTOME:R-BTA-9013149", "REACTOME:R-BTA-9013404", "REACTOME:R-BTA-9013406", "REACTOME:R-BTA-9013408", "REACTO...
148
[ "1ex6", "1ex7", "1gky", "1jxm", "1jxo", "1kgd", "1kjw", "1lvg", "1s4q", "1s96", "1t0h", "1t0j", "1t3l", "1t3s", "1vyt", "1vyu", "1vyv", "1z6g", "1z8f", "1znw", "1znx", "1zny", "1znz", "2an9", "2anb", "2anc", "2f3r", "2f3t", "2j41", "2qor", "2xkx", "3jbr"...
125
[ "PUB00000870", "PUB00001440", "PUB00003284", "PUB00005396" ]
[ "1310897", "8097461", "1314905", "1329277" ]
[ "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene.", "Purification and sequence determination of guanylate kinase from pig brain.", "Refined structure of the complex between guanylate kinase and its sub...
[ 1992, 1993, 1992, 1992 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 6, 29521, 68946, 157, 654 ]
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",...
[ 23, 16, 620, 64, 2, 203, 112, 2, 5, 179, 1, 1, 15 ]
13
true
Domain
Guanylate kinase/L-type calcium channel beta subunit
Guanylate kinase/L-type calcium channel beta subunit
GK/Ca_channel_bsu
7
IPR008146
8,146
Glutamine synthetase, catalytic domain
Gln_synth_cat_dom
Domain
86,868
false
false
This entry represents the C-terminal catalytic domain of GS enzymes. Glutamine synthetase ( ) (GS) [ ] plays an essential role in the metabolism of nitrogen by catalysing the condensation of glutamate and ammonia to form glutamine. There seem to be three different classes of GS [ , , ]: Class I enzymes (GSI) are specif...
[ "GO:0004356" ]
[ "glutamine synthetase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF00120", "PS51987", "SM01230" ]
[ "Gln-synt_C", "GS_CATALYTIC", "Gln-synt_C" ]
[ 84275, 86043, 82496 ]
3
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "6.3.1.2", "GenProp1279", "GenProp1434", "GenProp1489", "GenProp1554", "PWY-6963", "PWY-6964", "PWY-8291", "PWY-8294", "PDOC00162", "R-BTA-210455", "R-BTA-8964539", "R-CEL-210455", "R-CEL-8964539", "R-DME-210455", "R-DME-8964539", "R-HSA-210455", "R-HSA-8964539", "R-MMU-210455", ...
[ "EC:6.3.1.2", "GP:GenProp1279", "GP:GenProp1434", "GP:GenProp1489", "GP:GenProp1554", "METACYC:PWY-6963", "METACYC:PWY-6964", "METACYC:PWY-8291", "METACYC:PWY-8294", "PROSITEDOC:PDOC00162", "REACTOME:R-BTA-210455", "REACTOME:R-BTA-8964539", "REACTOME:R-CEL-210455", "REACTOME:R-CEL-8964539"...
26
[ "1f1h", "1f52", "1fpy", "1hto", "1htq", "1lgr", "2bvc", "2d3a", "2d3b", "2d3c", "2gls", "2j9i", "2lgs", "2ojw", "2qc8", "2uu7", "2wgs", "2whi", "3fky", "3ng0", "3o6x", "3zxr", "3zxv", "4acf", "4bax", "4hpp", "4is4", "4lnf", "4lni", "4lnk", "4lnn", "4lno"...
98
[ "PUB00000993", "PUB00003408", "PUB00003430", "PUB00004813" ]
[ "2900091", "2575672", "7916055", "8096645" ]
[ "Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCO.", "Glutamine synthetase II in Rhizobium: reexamination of the proposed horizontal transfer of DNA from eukaryotes to prokaryotes.", "Evolutionary relationships of bacterial and archaeal glutamine synthetase ge...
[ 1987, 1989, 1994, 1993 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1364, 65142, 18787, 39, 1536 ]
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",...
[ 36, 7, 25, 7, 3, 7, 6, 5, 9, 7, 1, 1, 94 ]
13
true
Domain
Glutamine synthetase, catalytic domain
Glutamine synthetase, catalytic domain
Gln_synth_cat_dom
9
IPR008147
8,147
Glutamine synthetase, N-terminal domain
Gln_synt_N
Domain
64,079
false
false
Glutamine synthetase ( ) (GS) [ ] plays an essential role in the metabolism of nitrogen by catalysing the condensation of glutamate and ammonia to form glutamine. This entry represents the glutamine synthetase N-terminal domain, which adopts a β-grasp fold [ ] and contributes to the substrate binding pocket of the enzy...
[ "GO:0004356", "GO:0006542" ]
[ "glutamine synthetase activity", "glutamine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PFAM", "PROFILE" ]
[ "PF03951", "PF16952", "PS51986" ]
[ "Gln-synt_N", "Gln-synt_N_2", "GS_BETA_GRASP" ]
[ 42875, 1236, 62266 ]
3
[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.1.2", "GenProp1489", "GenProp1554", "PWY-6963", "PWY-6964", "PWY-8291", "PWY-8294", "PDOC00162", "R-BTA-210455", "R-BTA-8964539", "R-CEL-210455", "R-CEL-8964539", "R-DME-210455", "R-DME-8964539", "R-HSA-210455", "R-HSA-8964539", "R-MMU-210455", "R-MMU-8964539", "R-RNO-210455...
[ "EC:6.3.1.2", "GP:GenProp1489", "GP:GenProp1554", "METACYC:PWY-6963", "METACYC:PWY-6964", "METACYC:PWY-8291", "METACYC:PWY-8294", "PROSITEDOC:PDOC00162", "REACTOME:R-BTA-210455", "REACTOME:R-BTA-8964539", "REACTOME:R-CEL-210455", "REACTOME:R-CEL-8964539", "REACTOME:R-DME-210455", "REACTOME...
24
[ "1f1h", "1f52", "1fpy", "1hto", "1htq", "1lgr", "2bvc", "2d3a", "2d3b", "2d3c", "2gls", "2lgs", "2ojw", "2qc8", "2uu7", "2wgs", "2whi", "3fky", "3ng0", "3o6x", "3zxr", "3zxv", "4acf", "4bax", "4hpp", "4is4", "4lnf", "4lni", "4lnk", "4lnn", "4lno", "4s0r"...
96
[ "PUB00000993", "PUB00075486", "PUB00075487", "PUB00097383" ]
[ "2900091", "17605815", "2876389", "24699643" ]
[ "Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCO.", "Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold.", "Novel subunit-subunit interactions in the structure of glutamine synthetase.", "The structures of cyto...
[ 1987, 2007, 1986, 2014 ]
4
[]
[ "IPR022147" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1193, 51235, 10620, 38, 993 ]
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",...
[ 23, 6, 25, 7, 3, 9, 6, 3, 5, 10, 1, 1, 50 ]
13
true
Domain
Glutamine synthetase, N-terminal domain
Glutamine synthetase, N-terminal domain
Gln_synt_N
7
IPR008148
8,148
DNA photolyase class 2
DNA_photolyase_2
Family
1,866
false
false
The cryptochrome and photolyase families consist of structurally related flavin adenine dinucleotide (FAD) proteins that use the absorption of blue light to accomplish different tasks. The photolyasess use the blue light for light-driven electron transfer to repair UV-damaged DNA, while the cryptochromes are blue-light...
[ "GO:0003904", "GO:0006281" ]
[ "deoxyribodipyrimidine photo-lyase activity", "DNA repair" ]
[ "molecular_function", "biological_process" ]
2
[ "NCBIFAM" ]
[ "TIGR00591" ]
[ "phr2" ]
[ 1866 ]
1
[ "EC", "PROSITEDOC" ]
[ "4.1.99.3", "PDOC00832" ]
[ "EC:4.1.99.3", "PROSITEDOC:PDOC00832" ]
2
[ "2xry", "2xrz", "3umv", "4cdm", "4cdn", "5o86", "5o8d", "5o8e", "5zcw", "7f8t", "7viw", "7vix", "7viy", "7viz", "7vj0", "7vj1", "7vj2", "7vj3", "7vj4", "7vj5", "7vj6", "7vj7", "7vj8", "7vj9", "7vja", "7vjb", "7vjc", "7vje", "7vjg", "7vjh", "7vji", "7vjj"...
62
[ "PUB00001269", "PUB00059547", "PUB00063939", "PUB00076729", "PUB00076730", "PUB00163231" ]
[ "7813451", "22170053", "21892138", "25910181", "26352435", "22066008" ]
[ "A new class of DNA photolyases present in various organisms including aplacental mammals.", "Eukaryotic class II cyclobutane pyrimidine dimer photolyase structure reveals basis for improved ultraviolet tolerance in plants.", "Crystal structures of an archaeal class II DNA photolyase and its complex with UV-dam...
[ 1994, 2012, 2011, 2015, 2015, 2011 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses" ]
[ 117, 1670, 47, 32 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 7, 4, 2, 1 ]
5
true
Family
DNA photolyase class 2
DNA photolyase class 2
DNA_photolyase_2
4
IPR008150
8,150
Phytoene dehydrogenase, bacterial-type, conserved site
Phytoene_DH_bac_CS
Conserved_site
3,958
false
false
Phytoene dehydrogenase (phytoene desaturase) is an enzyme of carotenoid biosynthesis that converts phytoene into zeta-carotene via the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene. The sequence of phytoene dehydrogenase from bacteria (gene crtI or carC) and fungi (gene AL-1) ...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00982" ]
[ "PHYTOENE_DH" ]
[ 3958 ]
1
[ "EC", "PROSITEDOC" ]
[ "1.3.99", "PDOC00755" ]
[ "EC:1.3.99", "PROSITEDOC:PDOC00755" ]
2
[ "4dgk" ]
1
[ "PUB00002578" ]
[ "2144293" ]
[ "Carotenoid desaturases from Rhodobacter capsulatus and Neurospora crassa are structurally and functionally conserved and contain domains homologous to flavoprotein disulfide oxidoreductases." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "ecological metagenomes" ]
[ 3267, 684, 4, 3 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Conserved_site
Phytoene dehydrogenase, bacterial-type, conserved site
Phytoene dehydrogenase, bacterial-type, conserved site
Phytoene_DH_bac_CS
3
IPR008152
8,152
Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain
Clathrin_a/b/g-adaptin_app_Ig
Domain
24,585
false
false
This entry represents a β-sandwich structural motif found in the appendage (ear) domain of alpha-, beta-and gamma-adaptin from AP clathrin adaptor complexes, and the GAE (gamma-adaptin ear) domain of GGA adaptor proteins. These domains have an immunoglobulin-like β-sandwich fold containing 7 or 8 strands in 2 β-sheets ...
[ "GO:0006886", "GO:0016192" ]
[ "intracellular protein transport", "vesicle-mediated transport" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "SMART" ]
[ "PF02883", "SM00809" ]
[ "Alpha_adaptinC2", "Alpha_adaptinC2" ]
[ 24403, 24079 ]
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-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-432720", "R-DDI-437239", "R-DDI-6798695", "R-DDI-8856825", "R-DDI-8856828", "R-DDI-8866427", ...
[ "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...
92
[ "1b9k", "1e42", "1gyu", "1gyv", "1gyw", "1iu1", "1ky6", "1ky7", "1kyd", "1kyf", "1kyu", "1na8", "1om9", "1p4u", "1qtp", "1qts", "1w80", "2a7b", "2dwx", "2dwy", "2e9g", "2g30", "2iv8", "2iv9", "2vj0", "2ymt", "3h1z", "3hs8", "3hs9", "3mnm", "3zhf", "3zy7"...
53
[ "PUB00010644", "PUB00011810", "PUB00026558", "PUB00027621", "PUB00029720", "PUB00035753", "PUB00035754", "PUB00035755", "PUB00035756", "PUB00035757", "PUB00035758", "PUB00035759", "PUB00035760", "PUB00035761", "PUB00035765", "PUB00035769" ]
[ "11080148", "12042876", "11859376", "12808037", "12858162", "17449236", "15107467", "12952931", "16542748", "17254016", "14973137", "14745135", "16413283", "15966896", "11598180", "15261670" ]
[ "Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.", "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.", "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1.", "Binding partners for the CO...
[ 2000, 2002, 2002, 2003, 2003, 2007, 2004, 2003, 2006, 2007, 2004, 2003, 2005, 2005, 2001, 2004 ]
16
[]
[ "IPR008153" ]
0
1
0
[ "Eukaryota" ]
[ 24585 ]
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...
[ 29, 3, 38, 10, 42, 31, 3, 13, 52, 4, 5, 99 ]
12
true
Domain
Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain
Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain
Clathrin_a/b/g-adaptin_app_Ig
3
IPR008153
8,153
Gamma-adaptin ear (GAE) domain
GAE_dom
Domain
13,434
false
false
The adaptor proteins AP-1 and GGA (Golgi-localized, gamma ear-containing, ADP- ribosylation factor (ARF)-binding proteins) regulate membrane traffic between the trans-Golgi network (TGN) and endosome/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and ac...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS50180" ]
[ "GAE" ]
[ 13434 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50180", "R-DDI-432720", "R-HSA-164940", "R-HSA-2132295", "R-HSA-432720", "R-HSA-432722", "R-HSA-8854214", "R-HSA-8875656", "R-HSA-977225", "R-MMU-2132295", "R-MMU-432720", "R-MMU-432722", "R-MMU-8875656", "R-RNO-8875656", "R-SPO-432720" ]
[ "PROSITEDOC:PDOC50180", "REACTOME:R-DDI-432720", "REACTOME:R-HSA-164940", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-432720", "REACTOME:R-HSA-432722", "REACTOME:R-HSA-8854214", "REACTOME:R-HSA-8875656", "REACTOME:R-HSA-977225", "REACTOME:R-MMU-2132295", "REACTOME:R-MMU-432720", "REACTOME:R-MMU-...
15
[ "1gyu", "1gyv", "1gyw", "1iu1", "1na8", "1om9", "1p4u", "2a7b", "2dwx", "2dwy", "2e9g", "2ymt", "3mnm", "3zhf", "3zy7", "4bcx", "5cn1", "5cn2" ]
18
[ "PUB00011792", "PUB00011808", "PUB00011809", "PUB00011810" ]
[ "12176391", "10747088", "10702286", "12042876" ]
[ "Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin.", "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome.", "Vear, a novel Golgi-associated protein with VHS and gamma-adaptin \"ear\" ...
[ 2002, 2000, 2000, 2002 ]
4
[ "IPR008152" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "termite gut metagenome" ]
[ 3, 11, 13419, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 12, 1, 14, 6, 21, 14, 2, 7, 25, 2, 4, 30 ]
12
true
Domain
Gamma-adaptin ear (GAE) domain
Gamma-adaptin ear (GAE) domain
GAE_dom
7
IPR008154
8,154
Amyloidogenic glycoprotein, extracellular
Amyloid_glyco_extra
Domain
6,918
false
false
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D...
[]
[]
[]
0
[ "PROFILE", "SMART" ]
[ "PS51869", "SM00006" ]
[ "APP_E1", "A4_EXTRA" ]
[ 6897, 6801 ]
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-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-416476", "R-CEL-8957275", "R-CEL-9609523", "R-DME-114608", "R-DME-3000178", "R-DME-381426", "R-DME-416476", "R-DME-8957275", "R-DME-9609523", "R-DME-9837999", "R-HSA-114608", "R-HSA-3000178", "R-HSA-381426", "R-HSA-416476", "R...
[ "REACTOME:R-CEL-114608", "REACTOME:R-CEL-3000178", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-416476", "REACTOME:R-CEL-8957275", "REACTOME:R-CEL-9609523", "REACTOME:R-DME-114608", "REACTOME:R-DME-3000178", "REACTOME:R-DME-381426", "REACTOME:R-DME-416476", "REACTOME:R-DME-8957275", "REACTOME:R-DM...
67
[ "1mwp", "1owt", "2fjz", "2fk1", "2fk2", "2fk3", "2fkl", "2fma", "2m05", "3ktm", "4jfn", "4pqd", "4pwq", "7mqy", "7mrk", "7mrm", "7mrn", "7mrs", "8kew", "8kf1", "8kf3", "8kf4", "8kf5", "8kf6", "8otf" ]
25
[ "PUB00029624", "PUB00033916", "PUB00033917", "PUB00033918", "PUB00099232", "PUB00099233" ]
[ "12611883", "16301322", "16406235", "16364896", "28713158", "33302541" ]
[ "Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.", "Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.", "The amyloid precursor protein and postnatal neurogenesis/...
[ 2003, 2006, 2006, 2005, 2017, 2020 ]
6
[]
[]
0
0
null
[ "Eukaryota", "marine sediment metagenome" ]
[ 6917, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 16, 6, 25, 22, 16 ]
6
true
Domain
Amyloidogenic glycoprotein, extracellular
Amyloidogenic glycoprotein, extracellular
Amyloid_glyco_extra
3
IPR008155
8,155
Amyloidogenic glycoprotein
Amyloid_glyco
Family
7,276
false
false
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [ , , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with D...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PRINTS", "PANTHER" ]
[ "PR00203", "PTHR23103" ]
[ "AMYLOIDA4", "" ]
[ 6522, 7274 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00204", "R-CEL-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-416476", "R-CEL-8957275", "R-CEL-9609523", "R-DME-114608", "R-DME-3000178", "R-DME-381426", "R-DME-416476", "R-DME-8957275", "R-DME-9609523", "R-DME-9837999", "R-HSA-114608", "R-HSA-3000178", "R-HSA-381426", "R-HS...
[ "PROSITEDOC:PDOC00204", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-3000178", "REACTOME:R-CEL-381426", "REACTOME:R-CEL-416476", "REACTOME:R-CEL-8957275", "REACTOME:R-CEL-9609523", "REACTOME:R-DME-114608", "REACTOME:R-DME-3000178", "REACTOME:R-DME-381426", "REACTOME:R-DME-416476", "REACTOME:R-DME-...
68
[ "1mwp", "1owt", "1tkn", "2fjz", "2fk1", "2fk2", "2fk3", "2fkl", "2fma", "2lp1", "2m05", "2roz", "3dxc", "3dxd", "3dxe", "3k66", "3k6b", "3ktm", "3nyj", "3nyl", "3pmr", "3q7g", "3q7l", "3qmk", "3umh", "3umi", "3umk", "4jfn", "4pqd", "4pwq", "4rd9", "4rda"...
52
[ "PUB00029624", "PUB00033916", "PUB00033917", "PUB00033918", "PUB00099232", "PUB00099233" ]
[ "12611883", "16301322", "16406235", "16364896", "28713158", "33302541" ]
[ "Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis.", "Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.", "The amyloid precursor protein and postnatal neurogenesis/...
[ 2003, 2006, 2006, 2005, 2017, 2020 ]
6
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 7276 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 16, 6, 31, 27, 17 ]
6
true
Family
Amyloidogenic glycoprotein
Amyloidogenic glycoprotein
Amyloid_glyco
3
IPR008156
8,156
Annexin A10
ANX10
Family
500
false
false
The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...
[ "GO:0005509", "GO:0005544" ]
[ "calcium ion binding", "calcium-dependent phospholipid binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR01809" ]
[ "ANNEXINX" ]
[ 500 ]
1
[]
[]
[]
0
[]
0
[ "PUB00001395", "PUB00013921", "PUB00013938", "PUB00015121" ]
[ "1646719", "9797403", "10458909", "15059252" ]
[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "Novel human and mouse annexin A10 are linked to the genome duplications during early chordate evolution."...
[ 1991, 1998, 1999, 2004 ]
4
[ "IPR001464" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 500 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 6 ]
3
true
Family
Annexin A10
Annexin A10
ANX10
4
IPR008158
8,158
Protein translocase SEC61 complex, gamma subunit
Translocase_Sec61-g
Family
5,001
false
false
This family is the protein translocase SEC61 complex gamma subunit of the archaeal and eukaryotic type. It does not hit bacterial SecE proteins. Sec61 is required for protein translocation in the endoplasmic reticulum. The Sec61 complex (eukaryotes) or SecY complex (prokaryotes) forms a conserved heterotrimeric integra...
[ "GO:0008320", "GO:0015031", "GO:0016020" ]
[ "protein transmembrane transporter activity", "protein transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "NCBIFAM" ]
[ "TIGR00327" ]
[ "secE_euk_arch" ]
[ 5001 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9609523", "R-CEL-9609523", "R-CFA-9609523", "R-DDI-9609523", "R-DME-9609523", "R-HSA-1236974", "R-HSA-1799339", "R-HSA-9609523", "R-MMU-9609523", "R-SCE-9609523", "R-SPO-9609523" ]
[ "REACTOME:R-BTA-9609523", "REACTOME:R-CEL-9609523", "REACTOME:R-CFA-9609523", "REACTOME:R-DDI-9609523", "REACTOME:R-DME-9609523", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-9609523", "REACTOME:R-MMU-9609523", "REACTOME:R-SCE-9609523", "REACTOME:R-SPO-9609523" ]
11
[ "1rh5", "1rhz", "2ww9", "2wwa", "2wwb", "2yxq", "2yxr", "3bo0", "3bo1", "3dkn", "3j7q", "3j7r", "3jc2", "3mp7", "4cg5", "4cg6", "4cg7", "4v4n", "4v7i", "5a6u", "6ftg", "6fti", "6ftj", "6n3q", "6nd1", "6r7q", "6w6l", "6z3t", "7aft", "7kah", "7kai", "7kaj"...
69
[ "PUB00022601", "PUB00028068" ]
[ "14661030", "11597451" ]
[ "X-ray structure of a protein-conducting channel.", "The Sec protein-translocation pathway." ]
[ 2004, 2001 ]
2
[ "IPR001901" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 775, 3, 4196, 27 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 8, 1, 1, 6, 1, 3, 1, 3, 10, 1, 1, 7 ]
12
true
Family
Protein translocase SEC61 complex, gamma subunit
Protein translocase SEC61 complex, gamma subunit
Translocase_Sec61-g
8
IPR008160
8,160
Collagen triple helix repeat
Collagen
Repeat
120,413
false
false
Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The sequence is predominantly repeats of the G-X-Y and the polypeptide chains form a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are freque...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01391" ]
[ "Collagen" ]
[ 120413 ]
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-114604", "R-BTA-1442490", "R-BTA-1566977", "R-BTA-1650814", "R-BTA-166016", "R-BTA-166662", "R-BTA-166663", "R-BTA-173623", "R-BTA-186797", "R-BTA-198933", "R-BTA-2022090", "R-BTA-202733", "R-BTA-216083", "R-BTA-2243919", "R-BTA-2855086", "R-BTA-3000157", "R-BTA-3000171", "R...
[ "REACTOME:R-BTA-114604", "REACTOME:R-BTA-1442490", "REACTOME:R-BTA-1566977", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-166016", "REACTOME:R-BTA-166662", "REACTOME:R-BTA-166663", "REACTOME:R-BTA-173623", "REACTOME:R-BTA-186797", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-2022090", "REACTOME:R-BTA...
194
[ "1wck", "2mqs", "2n8r", "2y5t", "3dmw", "3hqv", "3hr2", "4auo", "4bkl", "4dmu", "5ctd", "5cti", "5cva", "5cvb", "5mv4", "6hg7", "6los", "6q3p", "6q41", "6q43", "7pkq", "8zxl", "9c9u", "9han", "9ius" ]
25
[ "PUB00001059", "PUB00076482", "PUB00100841", "PUB00100842" ]
[ "8240831", "21726633", "11158359", "1720597" ]
[ "New members of the collagen superfamily.", "Characterisation of a large family of polymorphic collagen-like proteins in the endospore-forming bacterium Pasteuria ramosa.", "Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure.", "Ascorbate req...
[ 1993, 2011, 2001, 1991 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 105, 12614, 105233, 1686, 775 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 172, 432, 51, 321, 231, 342 ]
7
true
Repeat
Collagen triple helix repeat
Collagen triple helix repeat
Collagen
4
IPR008162
8,162
Inorganic pyrophosphatase
Pyrophosphatase
Family
32,337
false
false
Inorganic pyrophosphatase ( ) (PPase) [ , ] is the enzyme responsible for the hydrolysis of pyrophosphate (PPi) which is formed principally as the product of the many biosynthetic reactions that utilise ATP. All known PPases require the presence of divalent metal cations, with magnesium conferring the highest activity....
[ "GO:0000287", "GO:0004427", "GO:0006796", "GO:0005737" ]
[ "magnesium ion binding", "inorganic diphosphate phosphatase activity", "phosphate-containing compound metabolic process", "cytoplasm" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "HAMAP", "PFAM", "PANTHER", "CDD" ]
[ "MF_00209", "PF00719", "PTHR10286", "cd00412" ]
[ "Inorganic_PPase", "Pyrophosphatase", "", "pyrophosphatase" ]
[ 19943, 32232, 31101, 28591 ]
4
[ "EC", "GP", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "3.6.1.1", "GenProp1630", "PWY-7805", "PWY-7807", "PDOC00325", "R-BTA-379716", "R-BTA-71737", "R-CEL-379716", "R-CEL-379726", "R-CEL-71737", "R-DDI-379716", "R-DDI-379726", "R-DDI-71737", "R-DME-379716", "R-DME-379726", "R-DME-71737", "R-HSA-379716", "R-HSA-379726", "R-HSA-71737"...
[ "EC:3.6.1.1", "GP:GenProp1630", "METACYC:PWY-7805", "METACYC:PWY-7807", "PROSITEDOC:PDOC00325", "REACTOME:R-BTA-379716", "REACTOME:R-BTA-71737", "REACTOME:R-CEL-379716", "REACTOME:R-CEL-379726", "REACTOME:R-CEL-71737", "REACTOME:R-DDI-379716", "REACTOME:R-DDI-379726", "REACTOME:R-DDI-71737",...
31
[ "117e", "1e6a", "1e9g", "1faj", "1huj", "1huk", "1i40", "1i6t", "1igp", "1ino", "1ipw", "1jfd", "1m38", "1mjw", "1mjx", "1mjy", "1mjz", "1obw", "1pyp", "1qez", "1sxv", "1twl", "1ude", "1wcf", "1wgi", "1wgj", "1ygz", "1ypp", "2au6", "2au7", "2au8", "2au9"...
107
[ "PUB00000598", "PUB00005389" ]
[ "2160278", "1323891" ]
[ "Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases.", "Evolutionary conservation of the active site of soluble inorganic pyrophosphatase." ]
[ 1990, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 684, 19059, 12273, 3, 318 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 16, 1, 11, 5, 1, 13, 7, 2, 28, 8, 2, 2, 43 ]
13
true
Family
Inorganic pyrophosphatase
Inorganic pyrophosphatase
Pyrophosphatase
3
IPR008164
8,164
Repeat of unknown function XGLTT
XGLTT_rpt
Repeat
810
false
false
This short repeat of unknown function is found in one or multiple copies in a group of uncharacterised eukaryotic and bacterial proteins. The repeat is five residues long and consists of XGLTT where X can be any amino acid.
[]
[]
[]
0
[ "PFAM" ]
[ "PF01744" ]
[ "GLTT" ]
[ 810 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halorientalis pallida", "metagenomes" ]
[ 577, 229, 1, 3 ]
4
[]
[]
0
true
Repeat
Repeat of unknown function XGLTT
Repeat of unknown function XGLTT
XGLTT_rpt
6
IPR008166
8,166
Glycosyltransferase family 92
Glyco_transf_92
Family
14,408
false
false
This entry represents the glycosyltransferase family 92 [ , , ]. The aligned region contains several conserved cysteine residues and several charged residues that may be catalytic residues. This is supported by the inclusion of this family in the GT-A glycosyl transferase superfamily.
[]
[]
[]
0
[ "PFAM" ]
[ "PF01697" ]
[ "Glyco_transf_92" ]
[ 14408 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "2.4.1.-", "PWY-1901", "PWY-1961", "PWY-1981", "PWY-2021", "PWY-2881", "PWY-2901", "PWY-2902", "PWY-4421", "PWY-4801", "PWY-5094", "PWY-5105", "PWY-5129", "PWY-5139", "PWY-5160", "PWY-5161", "PWY-5268", "PWY-5284", "PWY-5286", "PWY-5310", "PWY-5312", "PWY-5313", "PWY-5317...
[ "EC:2.4.1.-", "METACYC:PWY-1901", "METACYC:PWY-1961", "METACYC:PWY-1981", "METACYC:PWY-2021", "METACYC:PWY-2881", "METACYC:PWY-2901", "METACYC:PWY-2902", "METACYC:PWY-4421", "METACYC:PWY-4801", "METACYC:PWY-5094", "METACYC:PWY-5105", "METACYC:PWY-5129", "METACYC:PWY-5139", "METACYC:PWY-5...
200
[ "8d3t", "8d3z" ]
2
[ "PUB00075505", "PUB00075506", "PUB00075507" ]
[ "19858195", "19959475", "22629278" ]
[ "Molecular basis for galactosylation of core fucose residues in invertebrates: identification of caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family.", "Molecular cloning of pigeon UDP-galactose:beta-D-galactoside alpha1,4-g...
[ 2009, 2010, 2012 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "metagenomes" ]
[ 2302, 11989, 2, 16, 99 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 41, 75, 6, 9, 14, 27 ]
6
true
Family
Glycosyltransferase family 92
Glycosyltransferase family 92
Glyco_transf_92
5
IPR008168
8,168
Cytochrome c, class IC
Cyt_C_IC
Family
17,147
false
false
Cytochrome c (CytC) proteins can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide r...
[ "GO:0005506", "GO:0009055" ]
[ "iron ion binding", "electron transfer activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PRINTS" ]
[ "PR00605" ]
[ "CYTCHROMECIC" ]
[ 17147 ]
1
[]
[]
[]
0
[ "1a2s", "1c53", "1c6o", "1c6r", "1c6s", "1ced", "1ctj", "1cyi", "1cyj", "1f1f", "1gdv", "1kib", "1ls9", "2v08", "2zbo", "2zzs", "3dmi", "3dr0", "3ph2", "4eic", "4eid", "4eie", "4eif", "4gyd", "4h0j", "4h0k", "6r6n", "6tr1", "6tsy", "7o38", "7vzg", "7vzr"...
40
[ "PUB00000610", "PUB00002343", "PUB00003350" ]
[ "1646017", "1964450", "7623381" ]
[ "Sequence variability in bacterial cytochromes c.", "S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method.", "The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for...
[ 1991, 1990, 1995 ]
3
[]
[ "IPR004678", "IPR023655" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 16371, 563, 213 ]
3
[]
[]
0
true
Family
Cytochrome c, class IC
Cytochrome c, class IC
Cyt_C_IC
6
IPR008173
8,173
Adenylyl cyclase CyaB
Adenylyl_cyclase_CyaB
Family
4,675
false
false
These sequences are functionally identified as members of the adenylate cyclase family , which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. The protein CyaB from Aeromonas hydrophila is a second adenylyl cyclase from that species, as demonstrated by complementation in Escherichia coli and by a...
[]
[]
[]
0
[ "PANTHER", "NCBIFAM", "CDD" ]
[ "PTHR21028", "TIGR00318", "cd07890" ]
[ "", "cyaB", "CYTH-like_AC_IV-like" ]
[ 4454, 1867, 4310 ]
3
[]
[]
[]
0
[ "1yem", "2aca", "2dc4", "2een", "2fjt", "3n0y", "3n0z", "3n10", "7ns8", "7ns9", "7nsa", "7nsd", "7nsf", "7oa2" ]
14
[ "PUB00005824" ]
[ "9642185" ]
[ "Aeromonas hydrophila adenylyl cyclase 2: a new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic archaebacteria." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Pithoviruses", "ecological metagenomes" ]
[ 804, 2918, 886, 2, 65 ]
5
[ "Caenorhabditis elegans", "Drosophila melanogaster" ]
[ 1, 3 ]
2
true
Family
Adenylyl cyclase CyaB
Adenylyl cyclase CyaB
Adenylyl_cyclase_CyaB
5
IPR008174
8,174
Galanin
Galanin
Domain
1,172
false
false
Galanin is a peptide hormone that controls various biological activities [ ]. Galanin-like immuno-reactivity has been found in the central and peripheral nervous systems of mammals, with high concentrations demonstrated in discrete regions of the central nervous system, including the median eminence, hypothalamus, arcu...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PROSITE" ]
[ "PF01296", "PR00273", "PS00861" ]
[ "Galanin", "GALANIN", "GALANIN" ]
[ 1172, 677, 1047 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00673", "R-BTA-375276", "R-BTA-418594", "R-DRE-375276", "R-DRE-418594", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "PROSITEDOC:PDOC00673", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418594", "REACTOME:R-DRE-375276", "REACTOME:R-DRE-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
11
[ "1smz", "7s3o", "7s3q", "7s3r", "7wq3", "7wq4", "7xbd", "7xjj", "7xjk", "8dhz", "8dj4" ]
11
[ "PUB00001611", "PUB00004652" ]
[ "1710578", "2448788" ]
[ "Human galanin: primary structure and identification of two molecular forms.", "Tissue-specific expression of the rat galanin gene." ]
[ 1991, 1988 ]
2
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 1172 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 5, 4 ]
4
true
Domain
Galanin
Galanin
Galanin
3
IPR008175
8,175
Galanin precursor
Galanin_pre
Family
1,071
false
false
Galanin is a peptide hormone that controls various biological activities [ ]. Galanin-like immuno-reactivity has been found in the central and peripheral nervous systems of mammals, with high concentrations demonstrated in discrete regions of the central nervous system, including the median eminence, hypothalamus, arcu...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PANTHER", "SMART" ]
[ "PTHR16839", "SM00071" ]
[ "", "Galanin" ]
[ 1065, 1005 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-375276", "R-BTA-418594", "R-DRE-375276", "R-DRE-418594", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]
[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418594", "REACTOME:R-DRE-375276", "REACTOME:R-DRE-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]
10
[ "7wq3", "7wq4", "7xbd", "7xjj", "7xjk", "8dj4" ]
6
[ "PUB00001611", "PUB00004652" ]
[ "1710578", "2448788" ]
[ "Human galanin: primary structure and identification of two molecular forms.", "Tissue-specific expression of the rat galanin gene." ]
[ 1991, 1988 ]
2
[]
[]
0
0
null
[ "Chordata" ]
[ 1071 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 3, 2 ]
4
true
Family
Galanin precursor
Galanin precursor
Galanin_pre
7
IPR008179
8,179
Phosphoribosyl-ATP pyrophosphohydrolase
HisE
Family
24,693
false
false
Phosphoribosyl-ATP pyrophosphatase, catalyses the second step in the histidine biosynthetic pathway [ ]: 5-phosphoribosyl-ATP + H2O = 5-phosphoribosyl-AMP + PPi In E. coli, HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl [ ]. HisIE is a bifunctional enzyme responsible for the second and t...
[ "GO:0004636", "GO:0000105" ]
[ "phosphoribosyl-ATP diphosphatase activity", "L-histidine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM", "CDD" ]
[ "MF_01020", "TIGR03188", "cd11534" ]
[ "HisE", "histidine_hisI", "NTP-PPase_HisIE_like" ]
[ 21113, 24491, 18459 ]
3
[ "EC", "GP" ]
[ "3.6.1.31", "GenProp0109" ]
[ "EC:3.6.1.31", "GP:GenProp0109" ]
2
[ "1y6x", "1yvw", "1yxb", "2a7w", "3c90", "6j22", "6j2l", "7bgm", "7bgn" ]
9
[ "PUB00001753", "PUB00003234", "PUB00046911", "PUB00053975", "PUB00070280", "PUB00074101", "PUB00079689", "PUB00079704", "PUB00079795", "PUB00080202", "PUB00080203", "PUB00080204", "PUB00080205", "PUB00080206", "PUB00080207" ]
[ "3005109", "3062174", "18560150", "3018428", "14342333", "9733547", "16359314", "15740738", "2664449", "2163392", "11006846", "1400209", "9209067", "9778800", "7049842" ]
[ "Cloning and characterization of the multifunctional his-3 gene of Neurospora crassa.", "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons.", "The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis.", "Nucleotid...
[ 1985, 1988, 2008, 1986, 1965, 1998, 2006, 2005, 1989, 1990, 2000, 1992, 1997, 1998, 1982 ]
15
[ "IPR021130" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 677, 20931, 2714, 7, 364 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 7, 1, 1, 2, 1, 1, 4 ]
7
true
Family
Phosphoribosyl-ATP pyrophosphohydrolase
Phosphoribosyl-ATP pyrophosphohydrolase
HisE
6
IPR008181
8,181
Deoxyuridine triphosphate nucleotidohydrolase
dUTPase
Family
29,792
false
false
The essential enzyme dUTP pyrophosphatase ( , dUTPase) is specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. dUTPase decreases the intracellular concentrati...
[ "GO:0000287", "GO:0004170", "GO:0006226", "GO:0046081" ]
[ "magnesium ion binding", "dUTP diphosphatase activity", "dUMP biosynthetic process", "dUTP catabolic process" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00116", "PTHR11241", "TIGR00576" ]
[ "dUTPase_bact", "", "dut" ]
[ 17205, 29613, 24645 ]
3
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.6.1.23", "GenProp1617", "R-DDI-499943", "R-HSA-499943", "R-MMU-499943", "R-RNO-499943", "R-SCE-499943", "R-SPO-499943" ]
[ "EC:3.6.1.23", "GP:GenProp1617", "REACTOME:R-DDI-499943", "REACTOME:R-HSA-499943", "REACTOME:R-MMU-499943", "REACTOME:R-RNO-499943", "REACTOME:R-SCE-499943", "REACTOME:R-SPO-499943" ]
8
[ "1duc", "1dud", "1dun", "1dup", "1dut", "1eu5", "1euw", "1f7d", "1f7k", "1f7n", "1f7o", "1f7p", "1f7q", "1f7r", "1mq7", "1q5h", "1q5u", "1rn8", "1rnj", "1seh", "1six", "1sjn", "1slh", "1sm8", "1smc", "1snf", "1syl", "1vyq", "2baz", "2hqu", "2hr6", "2hrm"...
122
[ "PUB00005269" ]
[ "8805593" ]
[ "Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 43, 21544, 5925, 1574, 706 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 5, 1, 3, 2, 1, 10, 1, 1, 4, 4, 1, 1, 3 ]
13
true
Family
Deoxyuridine triphosphate nucleotidohydrolase
Deoxyuridine triphosphate nucleotidohydrolase
dUTPase
2
IPR008183
8,183
Aldose 1-/Glucose-6-phosphate 1-epimerase
Aldose_1/G6P_1-epimerase
Family
58,769
false
false
Aldose 1-epimerase ( ) (mutarotase) is the enzyme responsible for the anomeric interconversion of D-glucose and other aldoses between their alpha- and beta-forms. Glucose-6-phosphate 1-epimerase ( ) has been shown to catalyse the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate ...
[ "GO:0016853", "GO:0005975" ]
[ "isomerase activity", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01263" ]
[ "Aldose_epim" ]
[ 58769 ]
1
[ "EC", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.1.3", "GenProp1310", "GenProp1661", "PDOC00471", "R-BTA-70370", "R-HSA-70370", "R-HSA-9931929", "R-MMU-70370", "R-RNO-70370", "R-SCE-70370", "R-SPO-70370", "R-SSC-70370" ]
[ "EC:5.1.3", "GP:GenProp1310", "GP:GenProp1661", "PROSITEDOC:PDOC00471", "REACTOME:R-BTA-70370", "REACTOME:R-HSA-70370", "REACTOME:R-HSA-9931929", "REACTOME:R-MMU-70370", "REACTOME:R-RNO-70370", "REACTOME:R-SCE-70370", "REACTOME:R-SPO-70370", "REACTOME:R-SSC-70370" ]
12
[ "1jov", "1l7j", "1l7k", "1lur", "1mmu", "1mmx", "1mmy", "1mmz", "1mn0", "1ns0", "1ns2", "1ns4", "1ns7", "1ns8", "1nsm", "1nsr", "1nss", "1nsu", "1nsv", "1nsx", "1nsz", "1snz", "1so0", "1yga", "1z45", "2ciq", "2cir", "2cis", "2hta", "2htb", "3dcd", "3imh"...
42
[ "PUB00047186" ]
[ "16857670" ]
[ "Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase." ]
[ 2006 ]
1
[]
[ "IPR025532", "IPR037480", "IPR037481", "IPR047215" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctmP19", "unclassified sequences" ]
[ 80, 41780, 16500, 1, 408 ]
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",...
[ 53, 1, 2, 22, 4, 6, 4, 4, 42, 5, 4, 1, 76 ]
13
true
Family
Aldose 1-/Glucose-6-phosphate 1-epimerase
Aldose 1-/Glucose-6-phosphate 1-epimerase
Aldose_1/G6P_1-epimerase
4
IPR008187
8,187
Vpu protein
Vpu
Family
16,709
false
false
The human immunodeficiency virus type 1 Vpu transmembrane protein is required for the induction of degradation human CD4 receptor degradation in the endoplasmic reticulum, and for the enhancement of virus particle release from the plasma membrane of infected cells. The cytoplasmic domain of Vpu directly interacts with ...
[ "GO:0005261", "GO:0019076", "GO:0032801", "GO:0033644" ]
[ "monoatomic cation channel activity", "viral release from host cell", "receptor catabolic process", "host cell membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "HAMAP", "PFAM" ]
[ "MF_04082", "PF00558" ]
[ "HIV_VPU", "Vpu" ]
[ 15728, 16709 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-162585", "R-HSA-162588", "R-HSA-162592", "R-HSA-162594", "R-HSA-164516", "R-HSA-164525", "R-HSA-164843", "R-HSA-171286", "R-HSA-173107", "R-HSA-175474", "R-HSA-175567", "R-HSA-177539", "R-HSA-180534", "R-HSA-180689", "R-HSA-180910" ]
[ "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-162594", "REACTOME:R-HSA-164516", "REACTOME:R-HSA-164525", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-171286", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-175474", "REACTOME:R-HSA-175567", "REACTOME:R-HSA-177...
15
[ "1pi7", "1pi8", "1pje", "1vpu", "2gof", "2goh", "2jpx", "2k7y", "2n28", "2n29", "4p6z" ]
11
[ "PUB00001473", "PUB00003513", "PUB00029868" ]
[ "9182993", "7853484", "14529626" ]
[ "Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.", "The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation.", "Three-dimensional structure of ...
[ 1997, 1995, 2003 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Lentivirus", "bioreactor metagenome" ]
[ 9, 5, 16694, 1 ]
4
[]
[]
0
true
Family
Vpu protein
Vpu protein
Vpu
1
IPR008189
8,189
rRNA small subunit methyltransferase I
rRNA_ssu_MeTfrase_I
Family
31,211
false
false
Ribosomal RNA small subunit methyltransferase I (RsmI) is an S-adenosyl-L-methionine-dependent methyltransferase that catalyses the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA [ ]. It may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity [ ]. In...
[ "GO:0008168" ]
[ "methyltransferase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_01877", "PIRSF005917", "PTHR46111", "TIGR00096", "cd11648" ]
[ "16SrRNA_methyltr_I", "MTase_YraL", "", "", "RsmI" ]
[ 25626, 29310, 31203, 26270, 26404 ]
5
[ "EC", "GP", "PROSITEDOC" ]
[ "2.1.1.198", "GenProp1082", "PDOC00998" ]
[ "EC:2.1.1.198", "GP:GenProp1082", "PROSITEDOC:PDOC00998" ]
3
[ "1wyz", "3ffy", "3fq6", "3hh1", "3kwp", "5hw4", "9pzg" ]
7
[ "PUB00054204", "PUB00095802", "PUB00095803" ]
[ "19965768", "27711192", "25195904" ]
[ "Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA.", "Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI.", "Purification, crystallization and preliminary crystallographic analysis of the 16S rRNA methyltransfera...
[ 2010, 2016, 2014 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 29527, 954, 727, 3 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 3, 1, 3, 8 ]
4
true
Family
rRNA small subunit methyltransferase I
rRNA small subunit methyltransferase I
rRNA_ssu_MeTfrase_I
6
IPR008195
8,195
Large ribosomal subunit protein eL34
Ribosomal_eL34
Family
6,411
false
false
This entry represents a number of eukaryotic and archaebacterial ribosomal proteins that belong to the eL34 family. These were previously known as vertebrate L34, mosquito L31 [ ], plant L34 [ ], yeast putative ribosomal protein YIL052c and archaebacterial L34e. Ribosomes are the particles that catalyse mRNA-directed p...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PANTHER", "PANTHER" ]
[ "PF01199", "PR01250", "PTHR10759", "PTHR46595" ]
[ "Ribosomal_L34e", "RIBOSOMALL34", "", "" ]
[ 6356, 6031, 3886, 2239 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00882", "R-DRE-156827", "R-DRE-1799339", "R-DRE-72689", "R-DRE-975956", "R-DRE-975957", "R-HSA-156827", "R-HSA-156902", "R-HSA-1799339", "R-HSA-192823", "R-HSA-2408557", "R-HSA-6791226", "R-HSA-72689", "R-HSA-72706", "R-HSA-72764", "R-HSA-9010553", "R-HSA-9633012", "R-HSA-9759...
[ "PROSITEDOC:PDOC00882", "REACTOME:R-DRE-156827", "REACTOME:R-DRE-1799339", "REACTOME:R-DRE-72689", "REACTOME:R-DRE-975956", "REACTOME:R-DRE-975957", "REACTOME:R-HSA-156827", "REACTOME:R-HSA-156902", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-192823", "REACTOME:R-HSA-2408557", "REACTOME:R-HSA-67...
33
[ "3j6x", "3j6y", "3j77", "3j78", "3j79", "3j7o", "3j7p", "3j7q", "3j7r", "3j92", "3jag", "3jah", "3jai", "3jaj", "3jan", "3jbn", "3jbo", "3jbp", "3jcs", "3jct", "4adx", "4d5y", "4d67", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q", "4u4r", "4u4u", "4u4y"...
571
[ "PUB00000669", "PUB00004568", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "8049275", "8075394", "11297922", "11290319", "11114498" ]
[ "Mosquito ribosomal protein rpL31 resembles rat rpL34: cDNA and deduced amino acid sequence.", "Developmental and environmental regulation of two ribosomal protein genes in tobacco.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies ...
[ 1994, 1994, 2001, 2001, 2000 ]
5
[]
[ "IPR047868" ]
0
1
0
[ "Archaea", "Eukaryota", "Pseudomonadati", "ecological metagenomes" ]
[ 282, 6120, 4, 5 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 9, 1, 3, 3, 2, 3, 1, 7, 6, 2, 2, 31 ]
12
true
Family
Large ribosomal subunit protein eL34
Large ribosomal subunit protein eL34
Ribosomal_eL34
3
IPR008197
8,197
WAP-type 'four-disulfide core' domain
WAP_dom
Domain
17,737
false
false
The four-disulfide core (4-DSC) or WAP domain comprises eight cysteine residues involved in disulfide bonds in a conserved arrangement [ ]. The four disulphide core containing Whey Acidic Proteins (WAP) are the major whey proteins in the milk of many mammals and are considered to be the prototypic members of the family...
[ "GO:0030414", "GO:0005576" ]
[ "peptidase inhibitor activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF00095", "PR00003", "PS51390", "SM00217" ]
[ "WAP", "4DISULPHCORE", "WAP", "WAP" ]
[ 16483, 6310, 16382, 14032 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00026", "R-HSA-190373", "R-HSA-5654726", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-6809371", "R-HSA-9830364", "R-MMU-6798695", "R-MMU-6803157", "R-RNO-6803157", "R-SSC-6803157", "R-SSC-6809371" ]
[ "PROSITEDOC:PDOC00026", "REACTOME:R-HSA-190373", "REACTOME:R-HSA-5654726", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-6809371", "REACTOME:R-HSA-9830364", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-6803157", "REACTOME:R-RNO-6803157", "REACTOME:R-SSC-6803157", "REACTOME:R...
12
[ "1fle", "1udk", "1zlg", "2rel", "2z7f", "3ngg", "4doq", "6atu" ]
8
[ "PUB00000779", "PUB00000860", "PUB00002575", "PUB00002618", "PUB00004330", "PUB00063800", "PUB00085073", "PUB00151166", "PUB00151167" ]
[ "3136918", "1913827", "2394696", "2324101", "6896234", "11965550", "11076767", "21936823", "18676177" ]
[ "Differential expression of a novel gene, WDNM1, in nonmetastatic rat mammary adenocarcinoma cells.", "The candidate gene for the X-linked Kallmann syndrome encodes a protein related to adhesion molecules.", "Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amin...
[ 1988, 1991, 1990, 1990, 1982, 2002, 2000, 2011, 2008 ]
9
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati", "bird metagenome" ]
[ 17732, 4, 1 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 18, 13, 31, 44, 66 ]
6
true
Domain
WAP-type 'four-disulfide core' domain
WAP-type 'four-disulfide core' domain
WAP_dom
5
IPR008201
8,201
Ribonuclease HepT-like
HepT-like
Domain
12,462
false
false
This entry includes the toxic component HepT of a type II toxin-antitoxin (TA) system, which has RNase activity. These proteins contain a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain and are neutralised through tri-AMPylation by the cognate antitoxin MntA, containing a MNT (minimal nucleotidyltran...
[ "GO:0004540", "GO:0110001" ]
[ "RNA nuclease activity", "toxin-antitoxin complex" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF01934" ]
[ "HepT-like" ]
[ 12462 ]
1
[]
[]
[]
0
[ "1ylm", "5yep", "6m6u", "6m6v", "6m6w", "7ae2", "7ae6", "7ae8", "7ae9", "7aer", "7bxo" ]
11
[ "PUB00097219", "PUB00097220", "PUB00097221" ]
[ "29555683", "33045733", "26112399" ]
[ "Structure-function analyses reveal the molecular architecture and neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin system.", "Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system.", "Identification and characterization of a HEPN-MNT family type II to...
[ 2018, 2020, 2015 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences" ]
[ 1137, 10983, 8, 1, 333 ]
5
[]
[]
0
true
Domain
Ribonuclease HepT-like
Ribonuclease HepT-like
HepT-like
9
IPR008203
8,203
AF2212-like
AF2212-like
Family
701
false
false
This family includes short bacterial and archaebacterial proteins, thought to be antitoxin components of the a type II toxin-antitoxin (TA) system. This entry includes AF2212 from Archaeoglobus fulgidus, which has sequence similarity with the AbrB superfamily of DNA-binding proteins, identified as antitoxins [ , ]. The...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01954" ]
[ "AF2212-like" ]
[ 701 ]
1
[]
[]
[]
0
[ "2nwt" ]
1
[ "PUB00056164", "PUB00056596" ]
[ "19493340", "15718296" ]
[ "Comprehensive comparative-genomic analysis of type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes.", "Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes." ]
[ 2009, 2005 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Geodia barretti", "ecological metagenomes" ]
[ 377, 311, 1, 12 ]
4
[]
[]
0
true
Family
AF2212-like
AF2212-like
AF2212-like
7
IPR008205
8,205
Geranylgeranylglyceryl phosphate synthase/Heptaprenylglyceryl phosphate synthase
GGGP_HepGP_synthase
Family
4,322
false
false
This entry represents geranylgeranylglyceryl phosphate (GGGP) synthase and Heptaprenylglyceryl phosphate (HepGP) synthase. GGGP synthase is a prenyltransferase that catalyses the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction...
[ "GO:0016765" ]
[ "transferase activity, transferring alkyl or aryl (other than methyl) groups" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM", "NCBIFAM", "CDD" ]
[ "MF_00112", "PF01884", "TIGR01768", "cd02812" ]
[ "GGGP_HepGP_synthase", "PcrB", "GGGP-family", "PcrB_like" ]
[ 3778, 4321, 4040, 2981 ]
4
[]
[]
[]
0
[ "1viz", "2f6u", "2f6x", "3vk5", "3vka", "3vkb", "3vkc", "3vkd", "3vzx", "3vzy", "3vzz", "3w00", "3w01", "3w02", "4jej", "4mm1", "4nae", "4naf", "5ndy", "5nez", "5nf1", "6jo3", "6nke", "8ruw" ]
24
[ "PUB00052581", "PUB00060473" ]
[ "18558723", "21761520" ]
[ "Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.", "Functional Assignment of an Enzyme that Catalyzes the Synthesis of an Archaea-Type Ether Lipid in Bacteria." ]
[ 2008, 2011 ]
2
[]
[ "IPR010946", "IPR039074" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 1180, 3058, 5, 79 ]
4
[]
[]
0
true
Family
Geranylgeranylglyceryl phosphate synthase/Heptaprenylglyceryl phosphate synthase
Geranylgeranylglyceryl phosphate synthase/Heptaprenylglyceryl phosphate synthase
GGGP_HepGP_synthase
9
IPR008207
8,207
Signal transduction histidine kinase, phosphotransfer (Hpt) domain
Sig_transdc_His_kin_Hpt_dom
Domain
82,499
false
false
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt...
[ "GO:0000160" ]
[ "phosphorelay signal transduction system" ]
[ "biological_process" ]
1
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF01627", "PS50894", "SM00073", "cd00088" ]
[ "Hpt", "HPT", "HPT", "HPT" ]
[ 77512, 77357, 42249, 49997 ]
4
[ "PROSITEDOC" ]
[ "PDOC50894" ]
[ "PROSITEDOC:PDOC50894" ]
1
[ "1a0b", "1bdj", "1c02", "1c03", "1fr0", "1i5n", "1oxb", "1oxk", "1qsp", "1sr2", "1tqg", "1ufb", "1wn0", "1y6d", "1yvi", "2a0b", "2lch", "2ld6", "2lp4", "2ooc", "2q4f", "2r25", "3iqt", "3kyi", "3kyj", "3myf", "3u3b", "3us6", "4euk", "4g78", "4pac", "5kbx"...
45
[ "PUB00000966", "PUB00007866", "PUB00010651", "PUB00011096", "PUB00013246", "PUB00013247", "PUB00013562", "PUB00013563", "PUB00020801", "PUB00042804", "PUB00042805", "PUB00042806", "PUB00042807" ]
[ "9989504", "11406410", "12372152", "10966457", "8868347", "10426948", "8029829", "1482126", "11145881", "16176121", "18076326", "11934609", "11489844" ]
[ "Structure of CheA, a signal-transducing histidine kinase.", "Histidine kinases and response regulator proteins in two-component signaling systems.", "Histidine protein kinases: key signal transducers outside the animal kingdom.", "Two-component signal transduction.", "Protein aspartate phosphatases control...
[ 1999, 2001, 2002, 2000, 1996, 1999, 1994, 1992, 2000, 2005, 2007, 2002, 2001 ]
13
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 639, 74477, 6629, 5, 749 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 28, 6, 2, 12, 1, 1, 23 ]
7
true
Domain
Signal transduction histidine kinase, phosphotransfer (Hpt) domain
Signal transduction histidine kinase, phosphotransfer (Hpt) domain
Sig_transdc_His_kin_Hpt_dom
7
IPR008209
8,209
Phosphoenolpyruvate carboxykinase, GTP-utilising
PEP_carboxykinase_GTP
Family
14,974
false
false
Phosphoenolpyruvate carboxykinase (PEPCK) catalyses the first committed (rate-limiting) step in hepatic gluconeogenesis, namely the reversible decarboxylation of oxaloacetate to phosphoenolpyruvate (PEP) and carbon dioxide, using either ATP or GTP as a source of phosphate. The ATP-utilising ( ) and GTP-utilising ( ) en...
[ "GO:0004611", "GO:0005525", "GO:0006094" ]
[ "phosphoenolpyruvate carboxykinase activity", "GTP binding", "gluconeogenesis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM", "PIRSF", "PANTHER", "CDD" ]
[ "MF_00452", "NF003253", "PIRSF001348", "PTHR11561", "cd00819" ]
[ "PEPCK_GTP", "PRK04210.1", "PEP_carboxykinase_GTP", "", "PEPCK_GTP" ]
[ 10707, 10787, 10046, 14973, 10220 ]
5
[ "EC", "GP", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.1.1.32", "GenProp1612", "PWY-7383", "PDOC00421", "R-DDI-70263", "R-DME-70263", "R-GGA-352875", "R-HSA-2161541", "R-HSA-381340", "R-HSA-70263", "R-HSA-9615017", "R-HSA-9632974", "R-MMU-70263", "R-RNO-70263", "R-SSC-70263" ]
[ "EC:4.1.1.32", "GP:GenProp1612", "METACYC:PWY-7383", "PROSITEDOC:PDOC00421", "REACTOME:R-DDI-70263", "REACTOME:R-DME-70263", "REACTOME:R-GGA-352875", "REACTOME:R-HSA-2161541", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-70263", "REACTOME:R-HSA-9615017", "REACTOME:R-HSA-9632974", "REACTOME:R-MMU...
15
[ "1khb", "1khe", "1khf", "1khg", "1m51", "1nhx", "2faf", "2fah", "2gmv", "2qew", "2qey", "2qf1", "2qf2", "2qzy", "2rk7", "2rk8", "2rka", "2rkd", "2rke", "2zci", "3dt2", "3dt4", "3dt7", "3dtb", "3moe", "3mof", "3moh", "4gmm", "4gmu", "4gmw", "4gmz", "4gnl"...
86
[ "PUB00003355", "PUB00035740", "PUB00035741", "PUB00035742", "PUB00035743", "PUB00035744" ]
[ "8609605", "16330239", "15023367", "15890557", "17403375", "16126724" ]
[ "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold.", "Nucleotide specificity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase Kinetics, fluorescence spectroscopy, and molecular simulation studies.",...
[ 1996, 2006, 2004, 2005, 2007, 2005 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Yasminevirus sp. GU-2018", "metagenomes" ]
[ 146, 7333, 7193, 2, 300 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 2, 4, 14, 15, 12 ]
6
true
Family
Phosphoenolpyruvate carboxykinase, GTP-utilising
Phosphoenolpyruvate carboxykinase, GTP-utilising
PEP_carboxykinase_GTP
7
IPR008210
8,210
Phosphoenolpyruvate carboxykinase, N-terminal
PEP_carboxykinase_N
Homologous_superfamily
29,873
false
false
Phosphoenolpyruvate carboxykinase (PEPCK) catalyses the first committed (rate-limiting) step in hepatic gluconeogenesis, namely the reversible decarboxylation of oxaloacetate to phosphoenolpyruvate (PEP) and carbon dioxide, using either ATP or GTP as a source of phosphate. The ATP-utilising ( ) and GTP-utilising ( ) en...
[ "GO:0004611", "GO:0017076", "GO:0006094" ]
[ "phosphoenolpyruvate carboxykinase activity", "purine nucleotide binding", "gluconeogenesis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.40.449.10", "SSF68923" ]
[ "", "" ]
[ 29465, 29736 ]
2
[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.1.1.49", "PWY-561", "PWY-7117", "R-DDI-70263", "R-DME-70263", "R-GGA-352875", "R-HSA-2161541", "R-HSA-381340", "R-HSA-70263", "R-HSA-9615017", "R-HSA-9632974", "R-MMU-70263", "R-RNO-70263", "R-SSC-70263" ]
[ "EC:4.1.1.49", "METACYC:PWY-561", "METACYC:PWY-7117", "REACTOME:R-DDI-70263", "REACTOME:R-DME-70263", "REACTOME:R-GGA-352875", "REACTOME:R-HSA-2161541", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-70263", "REACTOME:R-HSA-9615017", "REACTOME:R-HSA-9632974", "REACTOME:R-MMU-70263", "REACTOME:R-RN...
14
[ "1aq2", "1ayl", "1ii2", "1j3b", "1k3c", "1k3d", "1khb", "1khe", "1khf", "1khg", "1m51", "1nhx", "1oen", "1os1", "1xkv", "1ygg", "1ylh", "1ytm", "1yvy", "2faf", "2fah", "2gmv", "2olq", "2olr", "2pc9", "2pxz", "2py7", "2qew", "2qey", "2qf1", "2qf2", "2qzy"...
119
[ "PUB00003355", "PUB00035740", "PUB00035741", "PUB00035742", "PUB00035743", "PUB00035744" ]
[ "8609605", "16330239", "15023367", "15890557", "17403375", "16126724" ]
[ "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold.", "Nucleotide specificity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase Kinetics, fluorescence spectroscopy, and molecular simulation studies.",...
[ 1996, 2006, 2004, 2005, 2007, 2005 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 367, 20396, 8635, 7, 468 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 16, 6, 2, 3, 1, 12, 13, 1, 14, 8, 1, 25 ]
12
true
Homologous_superfamily
Phosphoenolpyruvate carboxykinase, N-terminal
Phosphoenolpyruvate carboxykinase, N-terminal
PEP_carboxykinase_N
2
IPR008213
8,213
CpcD-like domain
CpcD-like_dom
Domain
2,194
false
false
Ferredoxin-NADP(+) oxydoreductase (FNR) ( ) transfers electrons from ferredoxin (or flavodoxin) to NADP(+) to generate NADPH. In eukaryotes, the nuclear-encoded, chloroplast-targeted enzyme contains two domains: an FAD-binding domain (see ) and an NADP(+)-binding domain. With the exception of Gloeobacter violaceus PCC ...
[ "GO:0030089" ]
[ "phycobilisome" ]
[ "cellular_component" ]
1
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01383", "PS51441", "SM01094" ]
[ "CpcD", "CPCD_LIKE", "CpcD" ]
[ 2136, 2190, 2167 ]
3
[]
[]
[]
0
[ "1b33", "2b5o", "5y6p", "6kgx", "7ext", "7eyd", "7ezx", "7sc7", "7sc8", "7sc9", "7sca", "7scb", "7scc", "7vea", "7veb", "7y4l", "7y5e", "7y7a", "8hfq", "8imi", "8imj", "8imk", "8iml", "8imm", "8imn", "8imo", "8to2", "8to5", "8tpj", "8tro", "8uhe", "8wql"...
38
[ "PUB00014263", "PUB00052594", "PUB00052595", "PUB00052596" ]
[ "9990029", "1554697", "2040095", "4636046" ]
[ "Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.", "Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus s...
[ 1999, 1992, 1991, 1972 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2144, 50 ]
2
[]
[]
0
true
Domain
CpcD-like domain
CpcD-like domain
CpcD-like_dom
2
IPR008215
8,215
Tachykinin domain
Tachykinin_dom
Domain
781
false
false
Tachykinins [ , , ] are a group of biologically active peptides which excite neurons, evoke behavioral responses, are potent vasodilatators and contract (directly or indirectly) many smooth muscles. This family includes many other peptides. Tachykinins, like most other active peptides, are synthesized as larger protein...
[ "GO:0007217" ]
[ "tachykinin receptor signaling pathway" ]
[ "biological_process" ]
1
[ "PFAM", "SMART" ]
[ "PF02202", "SM00203" ]
[ "Tachykinin", "TK" ]
[ 670, 642 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-380095", "R-BTA-416476", "R-HSA-380095", "R-HSA-416476", "R-MMU-380095", "R-MMU-416476", "R-RNO-380095", "R-RNO-416476" ]
[ "REACTOME:R-BTA-380095", "REACTOME:R-BTA-416476", "REACTOME:R-HSA-380095", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-380095", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-380095", "REACTOME:R-RNO-416476" ]
8
[ "2gfr", "2ks9", "2ksa", "2ksb", "4hom", "7p00", "7p02", "7rmg", "7rmh", "7vdm", "8jbh", "8u26" ]
12
[ "PUB00000127", "PUB00001502", "PUB00003623" ]
[ "3284438", "1969374", "1324401" ]
[ "Tachykinins.", "Diversity in mammalian tachykinin peptidergic neurons: multiple peptides, receptors, and regulatory mechanisms.", "[Tachykinins and conformational aspects of their interactions with receptors]" ]
[ 1988, 1990, 1992 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 7, 774 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 3, 3 ]
4
true
Domain
Tachykinin domain
Tachykinin domain
Tachykinin_dom
2
IPR008216
8,216
Tachykinin family
Tachykinin_fam
Family
1,194
false
false
Tachykinins [ , , ] are a group of biologically active peptides which excite neurons, evoke behavioral responses, are potent vasodilatators, and contract (directly or indirectly) many smooth muscles. This family includes the precursors that are enzymatically converted to their mature forms. Tachykinins are from ten to ...
[ "GO:0007217" ]
[ "tachykinin receptor signaling pathway" ]
[ "biological_process" ]
1
[ "PRINTS" ]
[ "PR01829" ]
[ "PROTACHYKNIN" ]
[ 1194 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-380095", "R-BTA-416476", "R-HSA-380095", "R-HSA-416476", "R-MMU-380095", "R-MMU-416476", "R-RNO-380095", "R-RNO-416476" ]
[ "REACTOME:R-BTA-380095", "REACTOME:R-BTA-416476", "REACTOME:R-HSA-380095", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-380095", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-380095", "REACTOME:R-RNO-416476" ]
8
[]
0
[ "PUB00000127", "PUB00001502", "PUB00003623" ]
[ "3284438", "1969374", "1324401" ]
[ "Tachykinins.", "Diversity in mammalian tachykinin peptidergic neurons: multiple peptides, receptors, and regulatory mechanisms.", "[Tachykinins and conformational aspects of their interactions with receptors]" ]
[ 1988, 1990, 1992 ]
3
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1194 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 4, 6 ]
4
true
Family
Tachykinin family
Tachykinin family
Tachykinin_fam
1
IPR008217
8,217
Ccc1 family
Ccc1_fam
Family
23,348
false
false
This entry represents the Ccc1 family, which consists of a group of putative vacuolar ion transporters. Proteins in this family include yeast Ccc1, which has a role in calcium and manganese homeostasis [ ], and Arabidopsis VIT1, which serves as a vacuolar Fe2+ uptake transporter [ ].
[ "GO:0005384", "GO:0030026" ]
[ "manganese ion transmembrane transporter activity", "intracellular manganese ion homeostasis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER" ]
[ "PF01988", "PTHR31851" ]
[ "VIT1", "" ]
[ 23319, 20509 ]
2
[]
[]
[]
0
[ "6iu3", "6iu4", "6iu5", "6iu6", "6iu8", "6iu9" ]
6
[ "PUB00071818", "PUB00071819" ]
[ "8866476", "17082420" ]
[ "The role of the Saccharomyces cerevisiae CCC1 gene in the homeostasis of manganese ions.", "Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1." ]
[ 1996, 2006 ]
2
[]
[ "IPR006682", "IPR017040" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae sp. ChoanoV1", "unclassified sequences" ]
[ 670, 14885, 7405, 1, 387 ]
5
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 22, 1, 15, 1, 1, 27 ]
6
true
Family
Ccc1 family
Ccc1 family
Ccc1_fam
8
IPR008218
8,218
ATPase, V1 complex, subunit F
ATPase_V1-cplx_f_g_su
Family
7,724
false
false
This entry represents subunit F in the V1 complex of V-ATPases and Na(+)-translocating ATPase in Enterococcus hirae. Subunit F is a 16kDa protein that is required for the assembly and activity of V-ATPase, and has a potential role in the differential targeting and regulation of the enzyme for specific organelles. This ...
[ "GO:0046961", "GO:0034220" ]
[ "proton-transporting ATPase activity, rotational mechanism", "monoatomic ion transmembrane transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01990" ]
[ "ATP-synt_F" ]
[ 7724 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp0629", "R-BTA-1222556", "R-BTA-77387", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-77387", "R-CEL-917977", "R-CEL-9639288", "R-CEL-983712", "R-DDI-1222556", "R-DDI-77387", "R-DDI-917977", "R-DDI-9639288", "R-DME-1222556", "R-DME-77387", "R-DME-9...
[ "GP:GenProp0629", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-77387", "REACTOME:R-CEL-917977", "REACTOME:R-CEL-9639288", "REACTOME:R-CEL-983712", "REACTOME:R-DDI-1222556"...
43
[ "2d00", "2i4r", "2ov6", "2qai", "3a5c", "3a5d", "3aon", "3j0j", "3j9t", "3j9u", "3j9v", "3vr4", "3vr5", "3vr6", "3w3a", "4ix9", "4rnd", "5d80", "5gar", "5gas", "5knb", "5knc", "5knd", "5tsj", "5vox", "5voy", "5voz", "5y5x", "5y5y", "5y5z", "5y60", "6ly8"...
131
[ "PUB00007886", "PUB00020603", "PUB00020604", "PUB00020608", "PUB00020609", "PUB00020639", "PUB00063567", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160299" ]
[ "11533110", "15473999", "15078220", "15907459", "15629643", "14963028", "11248190", "20450191", "18937357", "1385979", "9741106", "9874757" ]
[ "Structure-function relationships of A-, F- and V-ATPases.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "A new view of an old pore.", "A structural model of the vac...
[ 2001, 2004, 2004, 2005, 2005, 2004, 2001, 2010, 2008, 1992, 1998, 1992 ]
12
[]
[ "IPR005772", "IPR022944" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 913, 2312, 4394, 105 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 2, 1, 1, 7, 2, 3, 1, 3, 5, 1, 1, 11 ]
12
true
Family
ATPase, V1 complex, subunit F
ATPase, V1 complex, subunit F
ATPase_V1-cplx_f_g_su
8
IPR008219
8,219
Proline dehydrogenase, bacteria and archaea
PRODH_bac_arc
Family
6,204
false
false
This entry represents a group of proline dehydrogenases from bacteria and archaea.
[ "GO:0004657", "GO:0010133" ]
[ "proline dehydrogenase activity", "L-proline catabolic process to L-glutamate" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF" ]
[ "PIRSF000196" ]
[ "Pro_dehydrog" ]
[ 6204 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "1.5.5.2", "PWY-5737", "PWY-6922" ]
[ "EC:1.5.5.2", "METACYC:PWY-5737", "METACYC:PWY-6922" ]
3
[ "2ekg", "2g37", "4h6q", "4h6r", "5m42" ]
5
[]
[]
[]
[]
0
[ "IPR015659" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Rhynchospora breviuscula", "unclassified sequences" ]
[ 450, 5702, 1, 51 ]
4
[]
[]
0
true
Family
Proline dehydrogenase, bacteria and archaea
Proline dehydrogenase, bacteria and archaea
PRODH_bac_arc
4
IPR008220
8,220
Homoserine/serine acetyltransferase MetX-like
HAT_MetX-like
Family
22,954
false
false
Homoserine acetyltransferase (homoserine transacetylase) catalyses the first step unique to methionine biosynthesis, converting L-homoserine to O-acetyl-L-homoserine using acetyl-CoA as an acetyl group donor [ ]. This enzyme regulates homoserine in a number of biosynthetic pathways, making it vital to cell growth and v...
[ "GO:0016747", "GO:0009058" ]
[ "acyltransferase activity, transferring groups other than amino-acyl groups", "biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM", "PIRSF", "PANTHER" ]
[ "MF_00296", "NF001209", "PIRSF000443", "PTHR32268" ]
[ "MetX_acyltransf", "PRK00175.1", "Homoser_Ac_trans", "" ]
[ 16339, 12964, 19849, 22921 ]
4
[ "EC", "GP" ]
[ "2.3.1", "GenProp1507" ]
[ "EC:2.3.1", "GP:GenProp1507" ]
2
[ "2b61", "2pl5", "2vat", "2vav", "2vax", "3i1i", "3vvl", "3vvm", "4qlo", "5d6o", "5d7b", "5e4y", "5efz", "5jkf", "5jkj", "5w8o", "5w8p", "6iog", "6ioh", "6ioi", "6pux", "7ryt", "8f2l" ]
23
[ "PUB00010721", "PUB00043341", "PUB00083454", "PUB00083455", "PUB00085652", "PUB00100237" ]
[ "10913262", "17353245", "1569032", "11021945", "9209059", "30051576" ]
[ "Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase.", "Role of homoserine transacetylase as a new target for antifungal agents.", "The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and encodes a deacet...
[ 2000, 2007, 1992, 2000, 1997, 2018 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 535, 15714, 6268, 437 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 2, 1, 2 ]
3
true
Family
Homoserine/serine acetyltransferase MetX-like
Homoserine/serine acetyltransferase MetX-like
HAT_MetX-like
1
IPR008221
8,221
Urease
Urease
Family
2,022
false
false
Urease (urea amidohydrolase, ) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [ ], but each holoenzyme consists of four structural domains [ ]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [ ]. U...
[ "GO:0009039", "GO:0016151" ]
[ "urease activity", "nickel cation binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PIRSF" ]
[ "PIRSF001222" ]
[ "Urease" ]
[ 2022 ]
1
[ "EC", "METACYC" ]
[ "3.5.1.5", "PWY-5704" ]
[ "EC:3.5.1.5", "METACYC:PWY-5704" ]
2
[ "3la4", "4g7e", "4goa", "4gy7", "4h9m", "7kns" ]
6
[ "PUB00004994", "PUB00005206", "PUB00010725" ]
[ "9144792", "7754395", "7565414" ]
[ "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.", "The crystal structure of urease from Klebsiella aerogenes.", "Molecular biology of microbial ureases." ]
[ 1997, 1995, 1995 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2022 ]
1
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 5, 2, 1, 1, 5 ]
5
true
Family
Urease
Urease
Urease
3
IPR008223
8,223
Urease, gamma-beta subunit
Urease_gamma-beta_su
Family
1,469
false
false
This entry represents the fused gamma-beta organisation typified by the H. pylori alpha subunit. Urease (urea amidohydrolase, ) is a nickel-dependent metalloenzyme that catalyses the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their p...
[ "GO:0043419" ]
[ "urea catabolic process" ]
[ "biological_process" ]
1
[ "HAMAP", "PIRSF" ]
[ "MF_01955", "PIRSF001225" ]
[ "Urease_beta_gamma", "Urease_gammabeta" ]
[ 649, 1455 ]
2
[ "EC", "METACYC" ]
[ "3.5.1.5", "PWY-5704" ]
[ "EC:3.5.1.5", "METACYC:PWY-5704" ]
2
[ "1e9y", "1e9z", "3qga", "3qgk", "6qsu", "6zja", "8hc1" ]
7
[ "PUB00004994", "PUB00005206", "PUB00010725" ]
[ "9144792", "7754395", "7565414" ]
[ "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.", "The crystal structure of urease from Klebsiella aerogenes.", "Molecular biology of microbial ureases." ]
[ 1997, 1995, 1995 ]
3
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "Sulfolobaceae", "ecological metagenomes" ]
[ 1430, 5, 24, 10 ]
4
[]
[]
0
true
Family
Urease, gamma-beta subunit
Urease, gamma-beta subunit
Urease_gamma-beta_su
9
IPR008225
8,225
Coenzyme F420:L-glutamate ligase
F420-0_g-glutamyl_ligase
Family
4,780
false
false
FbiB catalyses the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives [ , , , ]. It is also involved in the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0 [ ].
[ "GO:0043773", "GO:0046872" ]
[ "coenzyme F420-0 gamma-glutamyl ligase activity", "metal ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "NCBIFAM" ]
[ "TIGR01916" ]
[ "F420_cofE" ]
[ 4780 ]
1
[ "EC", "EC", "GP", "GP", "METACYC" ]
[ "6.3.2.31", "6.3.2.34", "GenProp0791", "GenProp1682", "PWY-5199" ]
[ "EC:6.3.2.31", "EC:6.3.2.34", "GP:GenProp0791", "GP:GenProp1682", "METACYC:PWY-5199" ]
5
[ "2g9i", "2phn", "7uld", "7ule", "7ulf", "8g8p" ]
6
[ "PUB00002622", "PUB00003870", "PUB00044776", "PUB00044777", "PUB00093753" ]
[ "2110564", "8577249", "12867481", "15215601", "30952857" ]
[ "DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans.", "Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11.", "Methanococcus jannaschii coenzyme F420 analogs contain a terminal alpha-linked glutamate.", "Identification and cloning of th...
[ 1990, 1995, 2003, 2004, 2019 ]
5
[]
[ "IPR023659", "IPR023661" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 827, 3801, 12, 140 ]
4
[]
[]
0
true
Family
Coenzyme F420:L-glutamate ligase
Coenzyme F420:L-glutamate ligase
F420-0_g-glutamyl_ligase
8
IPR008228
8,228
Uncharacterised conserved protein UCP006173
UCP006173
Family
7,117
false
false
There are currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. They contain multiple conserved cysteine residues, which may indicate metal binding.
[]
[]
[]
0
[ "HAMAP", "PIRSF", "PANTHER" ]
[ "MF_00676", "PIRSF006173", "PTHR37421" ]
[ "UPF0260", "UCP006173", "" ]
[ 6031, 6814, 7116 ]
3
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[ "IPR005358" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Methanococcus", "unclassified sequences" ]
[ 7027, 9, 4, 77 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Uncharacterised conserved protein UCP006173
Uncharacterised conserved protein UCP006173
UCP006173
6
IPR008229
8,229
tRNA nucleotidyltransferase, archaea
CCA-adding_arc
Family
1,016
false
false
All mature tRNAs contain a terminal CCA sequence essential for function [ ]. CCA-adding enzyme ensures that each tRNA contains a terminal CCA, either by de novo addition or by repair of a damaged end [ ]. CCA-adding enzyme of this group is a class I nucleotidyltransferase unrelated, except at the active site, to class ...
[ "GO:0003723", "GO:0004810", "GO:0001680" ]
[ "RNA binding", "CCA tRNA nucleotidyltransferase activity", "tRNA 3'-terminal CCA addition" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "MF_01264", "PIRSF005335", "PTHR39643", "TIGR03671" ]
[ "CCA_arch", "CCA_arch", "", "cca_archaeal" ]
[ 986, 946, 1016, 963 ]
4
[ "EC" ]
[ "2.7.7.72" ]
[ "EC:2.7.7.72" ]
1
[ "1r89", "1r8a", "1r8b", "1r8c", "1sz1", "1tfw", "1tfy", "1uet", "1ueu", "1uev", "2dr5", "2dr7", "2dr8", "2dr9", "2dra", "2drb", "2dvi", "2zh1", "2zh2", "2zh3", "2zh4", "2zh5", "2zh6", "2zh7", "2zh8", "2zh9", "2zha", "2zhb", "3ouy", "3ov7", "3ova", "3ovb"...
42
[ "PUB00010739", "PUB00010740", "PUB00010741", "PUB00010742" ]
[ "11592395", "8809016", "9792681", "11090289" ]
[ "This is the end: processing, editing and repair at the tRNA 3'-terminus.", "CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae.", "The CCA-adding enzyme has a...
[ 2001, 1996, 1998, 2000 ]
4
[]
[]
0
0
null
[ "Archaea", "Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_54_20", "Cylicocyclus nassatus", "ecological metagenomes" ]
[ 968, 1, 1, 46 ]
4
[]
[]
0
true
Family
tRNA nucleotidyltransferase, archaea
tRNA nucleotidyltransferase, archaea
CCA-adding_arc
1
IPR008231
8,231
Probable chaperone CsaA
CsaA
Family
6,439
false
false
This entry describes CsaA, an export-related chaperone that interacts with the Sec system, and related proteins from a number of other bacteria and archaea [ ]. The crystal structure is known for the homodimer from Thermus thermophilus [ ].
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR02222" ]
[ "chap_CsaA" ]
[ 6439 ]
1
[]
[]
[]
0
[ "1gd7", "2nzh", "2nzo", "2q2h", "2q2i", "3g48", "5zdi" ]
7
[ "PUB00017744", "PUB00017745" ]
[ "11157762", "13129613" ]
[ "The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.", "Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY." ]
[ 2001, 2003 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 16, 6332, 19, 72 ]
4
[]
[]
0
true
Family
Probable chaperone CsaA
Probable chaperone CsaA
CsaA
9
IPR008240
8,240
Chorismate mutase, periplasmic
Chorismate_mutase_periplasmic
Family
3,163
false
false
Chorismate mutase (CM; ) catalyses the reaction at the branch point of the biosynthetic pathway leading to the three aromatic amino acids, phenylalanine, tryptophan and tyrosine (chorismic acid is the last common intermediate, and CM leads to the L-phenylalanine/L-tyrosine branch). It is part of the shikimate pathway, ...
[]
[]
[]
0
[ "PIRSF", "NCBIFAM" ]
[ "PIRSF026640", "TIGR01806" ]
[ "Peripl_chor_mut", "CM_mono2" ]
[ 2147, 3162 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "5.4.99.5", "PWY-3461", "PWY-3462", "PWY-6120", "PWY-6627", "PWY-7626" ]
[ "EC:5.4.99.5", "METACYC:PWY-3461", "METACYC:PWY-3462", "METACYC:PWY-6120", "METACYC:PWY-6627", "METACYC:PWY-7626" ]
6
[ "2ao2", "2f6l", "2fp1", "2fp2", "2gbb", "5ts9", "6cnz", "8cq4", "8cq6", "8pnh", "9bt3", "9bt6", "9bt7", "9rvg" ]
14
[ "PUB00003037", "PUB00011045", "PUB00011060", "PUB00011066", "PUB00011067", "PUB00011070" ]
[ "9497350", "9843375", "11528003", "11450855", "9383421", "11532214" ]
[ "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins.", "Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.", "...
[ 1998, 1998, 2001, 2001, 1995, 2001 ]
6
[]
[]
0
0
null
[ "Bacteria", "Ecdysozoa", "freshwater metagenome" ]
[ 3083, 79, 1 ]
3
[]
[]
0
true
Family
Chorismate mutase, periplasmic
Chorismate mutase, periplasmic
Chorismate_mutase_periplasmic
7
IPR008241
8,241
Salicylate biosynthesis protein PchB
Isochorismate_pyruvate-lyase
Family
1,341
false
false
Isochorismate pyruvate-lyase (IPL; PchB) catalyses the second reaction in the pyochelin biosynthetic pathway of Pseudomonas aeruginosa, conversion of isochorismate to salicylate plus pyruvate (following the initial PchA-dependent conversion of chorismate to isochorismate) [ ]. This enzyme can also carry out the chorism...
[ "GO:0004106", "GO:0016835", "GO:0009697" ]
[ "chorismate mutase activity", "carbon-oxygen lyase activity", "salicylic acid biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PIRSF", "NCBIFAM" ]
[ "PIRSF029775", "TIGR01803" ]
[ "Isochor_pyr_lyas", "CM-like" ]
[ 1043, 667 ]
2
[ "GP" ]
[ "GenProp1243" ]
[ "GP:GenProp1243" ]
1
[ "2h9c", "2h9d", "3hgw", "3hgx", "3rem", "3ret" ]
6
[ "PUB00011060", "PUB00011065", "PUB00011066", "PUB00011067", "PUB00011071", "PUB00011072" ]
[ "11528003", "11481470", "11450855", "9383421", "7500944", "11937513" ]
[ "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.", "Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism.", "A metabolic node in action: chorismate-utilizing enzymes in microo...
[ 2001, 2001, 2001, 1995, 1995, 2002 ]
6
[]
[]
0
0
null
[ "Bacteria", "Diploscapter pachys", "Methanobacterium veterum", "ecological metagenomes" ]
[ 1329, 1, 2, 9 ]
4
[]
[]
0
true
Family
Salicylate biosynthesis protein PchB
Salicylate biosynthesis protein PchB
Isochorismate_pyruvate-lyase
9
IPR008242
8,242
Bifunctional P-protein, chorismate mutase/prephenate dehydratase
Chor_mutase/pphenate_deHydtase
Family
21,013
false
false
The bifunctional P-protein, which plays a central role in phenylalanine biosynthesis, contains two catalytic domains (chorismate mutase and prephenate dehydratase) and a regulatory domain (ACT). It is part of the shikimate pathway, which is present only in bacteria, fungi, and plants. Chorismate mutase (CM; ) catalyses...
[ "GO:0004664", "GO:0009094" ]
[ "prephenate dehydratase activity", "L-phenylalanine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF" ]
[ "PIRSF001500" ]
[ "Chor_mut_pdt_Ppr" ]
[ 21013 ]
1
[ "EC", "METACYC" ]
[ "4.2.1.51", "PWY-7432" ]
[ "EC:4.2.1.51", "METACYC:PWY-7432" ]
2
[ "2qmx", "3luy", "3mwb", "6vh5", "7alz", "7am0" ]
6
[ "PUB00005850", "PUB00011035", "PUB00011060" ]
[ "10222208", "10493788", "11528003" ]
[ "Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches.", "Regulation of phenylalanine biosynthesis. Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein.", "Allosteric regulation of catalytic...
[ 1999, 1999, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 139, 18978, 1602, 294 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 1, 1, 2, 1, 1, 4 ]
6
true
Family
Bifunctional P-protein, chorismate mutase/prephenate dehydratase
Bifunctional P-protein, chorismate mutase/prephenate dehydratase
Chor_mutase/pphenate_deHydtase
4
IPR008243
8,243
Chorismate mutase, AroH class
Chorismate_mutase_AroH
Family
4,031
false
false
Chorismate mutase (CM) ( ) catalyses the conversion of chorismate to prephenate in the shikimate pathway of tyrosine and phenylalanine biosynthesis in bacteria, fungi and plants [ , ]. The three types of CM are AroH class, AroQ class, prokaryotic type and AroQ class, eukaryotic type. Structurally CMs can be divided int...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PROFILE", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF07736", "PIRSF005965", "PS51167", "PTHR21164", "TIGR01796", "cd02185" ]
[ "CM_1", "Chor_mut_AroH", "CHORISMATE_MUT_1", "", "CM_mono_aroH", "AroH" ]
[ 4026, 3736, 4027, 4004, 3944, 3823 ]
6
[ "PROSITEDOC" ]
[ "PDOC51167" ]
[ "PROSITEDOC:PDOC51167" ]
1
[ "1com", "1dbf", "1fnj", "1fnk", "1ode", "1ufy", "1ui9", "1xho", "2chs", "2cht", "3zo8", "3zop", "3zp4", "3zp7", "4nwo", "4zk7", "7l85", "7r4b", "8cuu", "8cuv", "8cuw", "8cux" ]
22
[ "PUB00011060", "PUB00011077", "PUB00094276" ]
[ "11528003", "8378335", "17965159" ]
[ "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.", "Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.", "The two chorismate mutases from both Mycobacterium tu...
[ 2001, 1993, 2008 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 3814, 16, 201 ]
3
[]
[]
0
true
Family
Chorismate mutase, AroH class
Chorismate mutase, AroH class
Chorismate_mutase_AroH
4
IPR008244
8,244
Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
Chor_mut/prephenate_DH_T
Family
2,624
false
false
The bifunctional T-protein (TyrA), which plays a central role in tyrosine biosynthesis, contains two catalytic domains (chorismate mutase and prephenate dehydrogenase). It is part of the shikimate pathway, which is present only in bacteria, fungi and plants. It is feedback inhibited by tyrosine. Chorismate mutase (CM; ...
[ "GO:0004106", "GO:0008977", "GO:0006571", "GO:0005737" ]
[ "chorismate mutase activity", "prephenate dehydrogenase (NAD+) activity", "L-tyrosine biosynthetic process", "cytoplasm" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "NCBIFAM", "PIRSF" ]
[ "NF008400", "PIRSF001499" ]
[ "PRK11199.1", "Chor_mut_pdh_Tpr" ]
[ 2606, 2411 ]
2
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "1.3.1.12", "5.4.99.5", "PWY-3461", "PWY-3462", "PWY-6120", "PWY-6627", "PWY-7303", "PWY-7626" ]
[ "EC:1.3.1.12", "EC:5.4.99.5", "METACYC:PWY-3461", "METACYC:PWY-3462", "METACYC:PWY-6120", "METACYC:PWY-6627", "METACYC:PWY-7303", "METACYC:PWY-7626" ]
8
[ "2pv7" ]
1
[ "PUB00011045", "PUB00011057", "PUB00011058", "PUB00011066", "PUB00011067", "PUB00011079", "PUB00011080", "PUB00066096" ]
[ "9843375", "8094464", "7533594", "11450855", "9383421", "11958996", "10518299", "20944228" ]
[ "Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.", "The pheA/tyrA/aroF region from Erwinia herbicola: an emerging comparative basis for analysis of gene organization and regulation in enteric bacteria."...
[ 1998, 1993, 1994, 2001, 1995, 2002, 1999, 2010 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Sulfolobaceae", "ecological metagenomes" ]
[ 2600, 2, 18, 4 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
Chor_mut/prephenate_DH_T
9
IPR008248
8,248
Protein-glutamate methylesterase/protein-glutamine glutaminase, CheB type
CheB-like
Family
17,870
false
false
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt...
[ "GO:0000156", "GO:0008984", "GO:0000160", "GO:0006935", "GO:0005737" ]
[ "phosphorelay response regulator activity", "protein-glutamate methylesterase activity", "phosphorelay signal transduction system", "chemotaxis", "cytoplasm" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]
5
[ "HAMAP", "PIRSF" ]
[ "MF_00099", "PIRSF000876" ]
[ "CheB_chemtxs", "RR_chemtxs_CheB" ]
[ 16751, 17407 ]
2
[ "EC", "EC" ]
[ "3.1.1.61", "3.5.1.44" ]
[ "EC:3.1.1.61", "EC:3.5.1.44" ]
2
[ "1a2o", "6ymz", "7esg" ]
3
[ "PUB00007866", "PUB00010651", "PUB00011096", "PUB00011097", "PUB00011100", "PUB00011107", "PUB00011108", "PUB00011109", "PUB00011110", "PUB00011111", "PUB00011112", "PUB00042804", "PUB00042805", "PUB00042806", "PUB00042807" ]
[ "11406410", "12372152", "10966457", "11851334", "8218244", "10049806", "2677005", "9442881", "9760239", "12196531", "9687374", "16176121", "18076326", "11934609", "11489844" ]
[ "Histidine kinases and response regulator proteins in two-component signaling systems.", "Histidine protein kinases: key signal transducers outside the animal kingdom.", "Two-component signal transduction.", "Dimer formation and transcription activation in the sporulation response regulator Spo0A.", "Struct...
[ 2001, 2002, 2000, 2002, 1993, 1998, 1989, 1997, 1998, 2002, 1998, 2005, 2007, 2002, 2001 ]
15
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 515, 17167, 8, 180 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Protein-glutamate methylesterase/protein-glutamine glutaminase, CheB type
Protein-glutamate methylesterase/protein-glutamine glutaminase, CheB type
CheB-like
7
IPR008249
8,249
Uncharacterised protein family UPF0231
UPF0231
Family
2,209
false
false
This family of uncharacterised proteins contains UPF0231 protein YacL from Escherichia coli and other proteins mainly found in Gammaproteobacteria.
[]
[]
[]
0
[ "HAMAP", "PFAM", "PIRSF" ]
[ "MF_01053", "PF06062", "PIRSF006287" ]
[ "UPF0231", "UPF0231", "UCP006287" ]
[ 1460, 2209, 1867 ]
3
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "metagenomes" ]
[ 2204, 5 ]
2
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Uncharacterised protein family UPF0231
Uncharacterised protein family UPF0231
UPF0231
7
IPR008250
8,250
P-type ATPase, A domain superfamily
ATPase_P-typ_transduc_dom_A_sf
Homologous_superfamily
289,280
false
false
This superfamily represents the actuator (A) domain, and some transmembrane helices found in P-type ATPases (also known as E1-E2 ATPases) [ ]. It contains the TGES-loop which is essential for the metal ion binding which results in tight association between the A and P (phosphorylation) domains [ ]. It does not contain ...
[]
[]
[]
0
[ "SSF" ]
[ "SSF81653" ]
[ "" ]
[ 289280 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "7.2.2", "R-BTA-418359", "R-BTA-5578775", "R-BTA-936837", "R-CEL-418359", "R-CEL-5578775", "R-CEL-6798695", "R-CEL-936837", "R-CFA-418359", "R-CFA-5578775", "R-CFA-936837", "R-DDI-418359", "R-DDI-5578775", "R-DDI-936837", "R-DME-418359", "R-DME-5578775", "R-DME-936837", "R-DRE-9368...
[ "EC:7.2.2", "REACTOME:R-BTA-418359", "REACTOME:R-BTA-5578775", "REACTOME:R-BTA-936837", "REACTOME:R-CEL-418359", "REACTOME:R-CEL-5578775", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-936837", "REACTOME:R-CFA-418359", "REACTOME:R-CFA-5578775", "REACTOME:R-CFA-936837", "REACTOME:R-DDI-418359", "...
54
[ "1iwo", "1kju", "1mhs", "1su4", "1t5s", "1t5t", "1vfp", "1wpg", "1xp5", "2agv", "2by4", "2c88", "2c8k", "2c8l", "2c9m", "2dqs", "2ear", "2eat", "2eau", "2hc8", "2kij", "2o9j", "2oa0", "2voy", "2xzb", "2yfy", "2yn9", "2zbd", "2zbe", "2zbf", "2zbg", "2zxe"...
404
[ "PUB00002805", "PUB00009616", "PUB00020603", "PUB00020604", "PUB00038122", "PUB00039927", "PUB00050553", "PUB00052687", "PUB00055017", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00160065", "PUB00160066" ]
[ "8226755", "9419228", "15473999", "15078220", "15448704", "16710301", "18075584", "19645496", "18930923", "20450191", "18937357", "1385979", "9741106", "37264943", "37838176" ]
[ "Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium.", "Evolution of substrate specificities in the P-type ATPase superfamily.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "...
[ 1993, 1998, 2004, 2004, 2004, 2006, 2007, 2009, 2008, 2010, 2008, 1992, 1998, 2023, 2023 ]
15
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 4089, 131518, 152149, 22, 1502 ]
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",...
[ 226, 46, 195, 82, 4, 147, 131, 18, 135, 195, 16, 14, 438 ]
13
true
Homologous_superfamily
P-type ATPase, A domain superfamily
P-type ATPase, A domain superfamily
ATPase_P-typ_transduc_dom_A_sf
5
IPR008251
8,251
Chromo shadow domain
Chromo_shadow_dom
Domain
8,474
false
false
Chromo shadow domain is distantly related to chromo domain. It is always found in association with a chromo domain.
[ "GO:0005634" ]
[ "nucleus" ]
[ "cellular_component" ]
1
[ "PFAM", "SMART" ]
[ "PF01393", "SM00300" ]
[ "Chromo_shadow", "ChSh" ]
[ 7859, 7211 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-73772", "R-CEL-983231", "R-HSA-427389", "R-HSA-4551638", "R-HSA-73772", "R-HSA-8953750", "R-HSA-9609690", "R-HSA-983231", "R-HSA-9843940", "R-MMU-8953750", "R-MMU-983231", "R-SPO-73772", "R-SPO-983231" ]
[ "REACTOME:R-CEL-73772", "REACTOME:R-CEL-983231", "REACTOME:R-HSA-427389", "REACTOME:R-HSA-4551638", "REACTOME:R-HSA-73772", "REACTOME:R-HSA-8953750", "REACTOME:R-HSA-9609690", "REACTOME:R-HSA-983231", "REACTOME:R-HSA-9843940", "REACTOME:R-MMU-8953750", "REACTOME:R-MMU-983231", "REACTOME:R-SPO-...
13
[ "1dz1", "1e0b", "1s4z", "2fmm", "3i3c", "3kup", "3p7j", "3q6s", "5t1g", "5t1i", "5xyv", "5xyw", "6fto", "6hw2", "8jzw", "8uxq", "9baq", "9baz", "9cdw", "9cea", "9cmt" ]
21
[ "PUB00004399", "PUB00004460", "PUB00004461", "PUB00005519" ]
[ "1708124", "7667093", "7501439", "1982376" ]
[ "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants.", "The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.", "The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcriptio...
[ 1991, 1995, 1995, 1990 ]
4
[ "IPR000953" ]
[]
1
0
1
[ "Eukaryota", "Paenibacillus sp. SYP-B3998" ]
[ 8473, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (stra...
[ 7, 2, 12, 27, 11, 8, 1, 1, 11, 2, 3 ]
11
true
Domain
Chromo shadow domain
Chromo shadow domain
Chromo_shadow_dom
5
IPR008252
8,252
Peptidase S15, X-Pro dipeptidyl-peptidase
Pept_S15_Xpro
Family
3,338
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[ "GO:0004177", "GO:0006508" ]
[ "aminopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PRINTS" ]
[ "MF_00698", "PR00923" ]
[ "Aminopeptidase_S15", "LACTOPTASE" ]
[ 1042, 3336 ]
2
[ "EC" ]
[ "3.4.14.11" ]
[ "EC:3.4.14.11" ]
1
[ "1lns", "6nff" ]
2
[ "PUB00000522", "PUB00003576", "PUB00027070" ]
[ "8439290", "7845208", "12377124" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis." ]
[ 1993, 1994, 2002 ]
3
[]
[]
0
0
null
[ "Bacteria", "Halobacteriales", "marine metagenome" ]
[ 3320, 15, 3 ]
3
[]
[]
0
true
Family
Peptidase S15, X-Pro dipeptidyl-peptidase
Peptidase S15, X-Pro dipeptidyl-peptidase
Pept_S15_Xpro
6
IPR008253
8,253
Marvel domain
Marvel
Domain
38,122
false
false
This entry represents the ~130-residue MARVEL (MAL and related proteins for vesicle trafficking and membrane link) domain. The MARVEL domain is a module with a four transmembrane-helix architecture that has been identified in proteins of the myelin and lymphocyte (MAL), physins, gyrins and occludin families. All descri...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PROFILE" ]
[ "PF01284", "PS51225" ]
[ "MARVEL", "MARVEL" ]
[ 33811, 30270 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC51225", "R-CEL-6798695", "R-DME-6798695", "R-HSA-351906", "R-HSA-6798695", "R-HSA-8935964", "R-HSA-9662360", "R-MMU-351906", "R-MMU-6798695", "R-RNO-351906", "R-RNO-6798695" ]
[ "PROSITEDOC:PDOC51225", "REACTOME:R-CEL-6798695", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-351906", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-8935964", "REACTOME:R-HSA-9662360", "REACTOME:R-MMU-351906", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-351906", "REACTOME:R-RNO-6798695" ]
11
[ "8a6m", "9b8o", "9bra", "9brb", "9brc", "9brd", "9brq", "9brt", "9brz" ]
9
[ "PUB00011120" ]
[ "12468223" ]
[ "MARVEL: a conserved domain involved in membrane apposition events." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacillales", "Eukaryota", "organismal metagenomes" ]
[ 3, 38117, 2 ]
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", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 13, 65, 5, 83, 65, 7, 105, 3, 1 ]
9
true
Domain
Marvel domain
Marvel domain
Marvel
1
IPR008254
8,254
Flavodoxin/nitric oxide synthase
Flavodoxin/NO_synth
Domain
106,593
false
false
This domain is found in a number of proteins including flavodoxin and nitric-oxide synthase. Flavodoxins are electron-transfer proteins that function in various electron transport systems. They bind one FMN molecule, which serves as a redox-active prosthetic group [ ] and are functionally interchangeable with ferredoxi...
[ "GO:0010181" ]
[ "FMN binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PFAM", "PROFILE" ]
[ "PF00258", "PF12641", "PF12682", "PS50902" ]
[ "Flavodoxin_1", "Flavodoxin_3", "Flavodoxin_4", "FLAVODOXIN_LIKE" ]
[ 68028, 1401, 6320, 101395 ]
4
[ "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "GenProp1320", "GenProp1481", "PDOC50902", "R-CEL-156581", "R-CEL-1614635", "R-CEL-9759218", "R-DDI-1222556", "R-DDI-1474151", "R-DDI-203615", "R-DDI-203754", "R-DDI-392154", "R-DDI-5218920", "R-DDI-5578775", "R-DDI-9009391", "R-DDI-9033241", "R-DDI-9856530", "R-DME-1222556", "R-DM...
[ "GP:GenProp1320", "GP:GenProp1481", "PROSITEDOC:PDOC50902", "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-1222556", "REACTOME:R-DDI-1474151", "REACTOME:R-DDI-203615", "REACTOME:R-DDI-203754", "REACTOME:R-DDI-392154", "REACTOME:R-DDI-5218920", "R...
96
[ "1ag9", "1ahn", "1akq", "1akr", "1akt", "1aku", "1akv", "1akw", "1amo", "1azl", "1b1c", "1bu5", "1bvy", "1c7e", "1c7f", "1czh", "1czk", "1czl", "1czn", "1czo", "1czr", "1czu", "1d03", "1d04", "1dx9", "1e5d", "1f4p", "1fla", "1fld", "1fln", "1flv", "1ftg"...
247
[ "PUB00000480", "PUB00004914", "PUB00018372", "PUB00018374", "PUB00018375", "PUB00018376" ]
[ "2597140", "9237990", "8160268", "7756978", "10048323", "10610791" ]
[ "The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus.", "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.", "Two highly homologous putative DNA-binding proteins in yeast and E. coli.", "Six new candidate members of...
[ 1989, 1997, 1994, 1994, 1999, 1999 ]
6
[]
[ "IPR026816" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1687, 68329, 35792, 64, 721 ]
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",...
[ 36, 5, 36, 9, 9, 48, 28, 6, 22, 38, 7, 5, 56 ]
13
true
Domain
Flavodoxin/nitric oxide synthase
Flavodoxin/nitric oxide synthase
Flavodoxin/NO_synth
5
IPR008255
8,255
Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
Pyr_nucl-diS_OxRdtase_2_AS
Active_site
37,839
false
false
null
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00573" ]
[ "PYRIDINE_REDOX_2" ]
[ 37839 ]
1
[ "EC", "PROSITEDOC", "REACTOME" ]
[ "1.8.1.9", "PDOC00496", "R-HSA-1222541" ]
[ "EC:1.8.1.9", "PROSITEDOC:PDOC00496", "REACTOME:R-HSA-1222541" ]
3
[ "1cl0", "1fl2", "1hyu", "1tde", "1vdc", "2a87", "2q0k", "2q0l", "2q7v", "2whd", "3d8x", "3f8p", "3f8r", "3ish", "3itj", "3r9u", "4a5l", "4a65", "4cbq", "4ccq", "4ccr", "4gcm", "4jnq", "4o5q", "4o5u", "4xvg", "4ykf", "4ykg", "4zn0", "5m5j", "5mh4", "5mip"...
56
[ "PUB00000510", "PUB00001601", "PUB00002259", "PUB00002349", "PUB00002489", "PUB00002553", "PUB00003319", "PUB00004100" ]
[ "1637309", "1995341", "8106340", "1917890", "3288628", "2191951", "8114095", "2067578" ]
[ "Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum.", "Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes.", "The thioredoxin system of Penicillium chrysogenum and its possible ro...
[ 1992, 1991, 1994, 1991, 1988, 1990, 1994, 1991 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 763, 32649, 3816, 27, 584 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 13, 2, 1, 5, 2, 1, 19 ]
7
true
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
Pyr_nucl-diS_OxRdtase_2_AS
9
IPR008256
8,256
Peptidase S1B
Peptidase_S1B
Family
6,559
false
false
This group of serine peptidases belong to the MEROPS peptidase family S1, subfamily S1B (clan PA(S)). A type example is glutamyl endopeptidase I from Staphylococcus aureus. Other members include S. aureus V8 protease, which preferentially cleaves peptide bonds C-terminal to Asp and Glu residues; Bacillus licheniformis ...
[ "GO:0008236", "GO:0006508" ]
[ "serine-type peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00839" ]
[ "V8PROTEASE" ]
[ 6559 ]
1
[ "EC", "METACYC" ]
[ "3.4.21.-", "PWY-7884" ]
[ "EC:3.4.21.-", "METACYC:PWY-7884" ]
2
[ "1agj", "1dt2", "1dua", "1due", "1exf", "1p3c", "1p3e", "1qtf", "1qy6", "1wcz", "2as9", "2o8l", "2vid", "2w7s", "2w7u", "3ufa", "4ink", "4inl", "4jcn", "4k1s", "4k1t", "4mvn", "5c2z", "5mm8", "6e0u", "6pym", "6q12", "6q24", "6sf7", "6tya", "6u1b", "6yv5"...
40
[ "PUB00000488", "PUB00001410", "PUB00001590", "PUB00002096" ]
[ "2117445", "1346764", "2384148", "2105291" ]
[ "The reactive serine residue of epidermolytic toxin A.", "Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis.", "The epidermolytic toxins are serine proteases.", "Gene encoding a novel extracellular metalloprotease in Bacillus subtilis." ]
[ 1990, 1992, 1990, 1990 ]
4
[]
[ "IPR008353", "IPR017344" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 25, 5243, 1216, 12, 63 ]
5
[ "Danio rerio", "Escherichia coli (strain K12)", "Zea mays" ]
[ 5, 1, 4 ]
3
true
Family
Peptidase S1B
Peptidase S1B
Peptidase_S1B
1
IPR008257
8,257
Peptidase M19
Pept_M19
Family
26,596
false
false
This group of peptidases belong to the MEROPS peptidase family M19 (membrane dipeptidase family, clan MJ). The protein fold of the peptidase domain for members of this family resembles that of Klebsiella urease, the type example for clan MJ [ ]. Renal dipeptidase ( ), also known as microsomal dipeptidase or membrane-bo...
[ "GO:0070573", "GO:0006508" ]
[ "metallodipeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "PANTHER", "CDD" ]
[ "PF01244", "PS51365", "PTHR10443", "cd01301" ]
[ "Peptidase_M19", "RENAL_DIPEPTIDASE_2", "", "rDP_like" ]
[ 26472, 26280, 26170, 16008 ]
4
[ "EC", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.13.19", "GenProp1653", "PWY-7533", "PWY-8355", "PWY-8397", "R-BTA-2142691", "R-BTA-5423646", "R-HSA-2142691", "R-HSA-5423646", "R-HSA-9664535", "R-MMU-2142691", "R-MMU-5423646", "R-RNO-2142691", "R-RNO-5423646", "R-SPO-2142691", "R-SPO-5423646", "R-SSC-2142691", "R-SSC-5423646...
[ "EC:3.4.13.19", "GP:GenProp1653", "METACYC:PWY-7533", "METACYC:PWY-8355", "METACYC:PWY-8397", "REACTOME:R-BTA-2142691", "REACTOME:R-BTA-5423646", "REACTOME:R-HSA-2142691", "REACTOME:R-HSA-5423646", "REACTOME:R-HSA-9664535", "REACTOME:R-MMU-2142691", "REACTOME:R-MMU-5423646", "REACTOME:R-RNO-...
18
[ "1itq", "1itu", "2i5g", "2rag", "3b40", "3fdg", "3id7", "3isi", "3itc", "3k5x", "3lu2", "3ly0", "3neh", "3s2j", "3s2l", "3s2m", "3s2n", "5lwz", "5lx0", "5lx1", "5lx4", "5lx7", "5nrt", "5nru", "5nrx", "5nry", "5nrz", "5ns1", "5ns2", "5ns5", "6vgo", "6vgr"...
33
[ "PUB00000644", "PUB00003579", "PUB00021853" ]
[ "8097406", "7674922", "12144777" ]
[ "Importance of Glu-125 in the catalytic activity of human renal dipeptidase.", "Evolutionary families of metallopeptidases.", "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis." ]
[ 1993, 1995, 2002 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 226, 19100, 6863, 407 ]
4
[ "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", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 3, 8, 13, 7, 1, 8, 2 ]
7
true
Family
Peptidase M19
Peptidase M19
Pept_M19
2
IPR008258
8,258
Transglycosylase SLT domain 1
Transglycosylase_SLT_dom_1
Domain
92,397
false
false
This domain is found mainly in proteins from phages and type II, type III and type IV secretion systems [ , , , ]. Bacterial lytic transglycosylases degrade murein via cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine, with the concomitant formation of a 1,6-anhydrobond in th...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01464" ]
[ "SLT" ]
[ 92397 ]
1
[]
[]
[]
0
[ "153l", "154l", "1gbs", "1lsp", "1qsa", "1qte", "1sly", "2y8p", "3bkh", "3bkv", "3gxk", "3gxr", "3mgw", "3t36", "3w6b", "3w6c", "3w6e", "3w6f", "3wyh", "4c5f", "4cfo", "4cfp", "4chx", "4g9s", "4hjv", "4hjy", "4hjz", "4owd", "4oxv", "4oyv", "4oz9", "4p0g"...
92
[ "PUB00004897", "PUB00005413", "PUB00011783", "PUB00020347" ]
[ "8692991", "8203016", "10452894", "14625683" ]
[ "A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals.", "A conserved domain in putative bacterial and bacteriophage transglycosylases.", "High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment.", ...
[ 1996, 1994, 1999, 2003 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 11, 87384, 2176, 1664, 6, 1156 ]
6
[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 1, 7, 2, 13 ]
5
true
Domain
Transglycosylase SLT domain 1
Transglycosylase SLT domain 1
Transglycosylase_SLT_dom_1
6
IPR008259
8,259
FMN-dependent alpha-hydroxy acid dehydrogenase, active site
FMN_hydac_DH_AS
Active_site
31,514
false
false
A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown [ , , ] to be structurally related. The first step in the reaction mechanism of these enzymes is the abstraction of the proton from the α-carbon of the substrate producing a carbanion which can subsequ...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00557" ]
[ "FMN_HYDROXY_ACID_DH_1" ]
[ 31514 ]
1
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00482", "R-BTA-390918", "R-BTA-9033241", "R-DDI-389661", "R-DDI-390918", "R-DDI-9033241", "R-HSA-389661", "R-HSA-390918", "R-HSA-9033241", "R-MMU-389661", "R-MMU-390918", "R-MMU-9033241", "R-RNO-389661", "R-RNO-390918", "R-RNO-9033241" ]
[ "PROSITEDOC:PDOC00482", "REACTOME:R-BTA-390918", "REACTOME:R-BTA-9033241", "REACTOME:R-DDI-389661", "REACTOME:R-DDI-390918", "REACTOME:R-DDI-9033241", "REACTOME:R-HSA-389661", "REACTOME:R-HSA-390918", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-389661", "REACTOME:R-MMU-390918", "REACTOME:R-MMU-9...
15
[ "1al7", "1al8", "1fcb", "1gox", "1gyl", "1huv", "1kbi", "1kbj", "1lco", "1ldc", "1ltd", "1p4c", "1p5b", "1qcw", "1sze", "1szf", "1szg", "1tb3", "2a7n", "2a7p", "2a85", "2cdh", "2du2", "2e77", "2j6x", "2nli", "2nzl", "2rdt", "2rdu", "2rdw", "2w0u", "2zfa"...
109
[ "PUB00000334", "PUB00002533", "PUB00002617", "PUB00002664" ]
[ "2271624", "2644287", "2324094", "1939137" ]
[ "Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.", "The active site of spinach glycolate oxidase.", "L-lactate 2-monooxygenase from Myco...
[ 1990, 1989, 1990, 1991 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 92, 17554, 13561, 307 ]
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",...
[ 31, 2, 6, 4, 1, 3, 6, 1, 5, 4, 1, 1, 29 ]
13
true
Active_site
FMN-dependent alpha-hydroxy acid dehydrogenase, active site
FMN-dependent alpha-hydroxy acid dehydrogenase, active site
FMN_hydac_DH_AS
9
IPR008261
8,261
Iodothyronine deiodinase, active site
Iodothyronine_deiodinase_AS
Active_site
510
false
false
Iodothyronine deiodinase ( ) (DI) [ ] is the vertebrate enzyme responsible for the deiodination of the prohormone thyroxine (T4 or 3,5,3',5'-tetraiodothyronine) into the biologically active hormone T3 (3,5,3'-triiodothyronine) and of T3 into the inactive metabolite T2 (3,3'-diiodothyronine). All known DI are proteins o...
[ "GO:0004800" ]
[ "thyroxine 5'-deiodinase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01205" ]
[ "T4_DEIODINASE" ]
[ 510 ]
1
[ "EC", "EC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.21.99.3", "1.21.99.4", "PWY-6260", "PWY-6261", "PDOC00925", "R-BTA-350864", "R-CFA-350864", "R-HSA-350864", "R-HSA-9844594", "R-MMU-350864", "R-RNO-350864", "R-SSC-350864" ]
[ "EC:1.21.99.3", "EC:1.21.99.4", "METACYC:PWY-6260", "METACYC:PWY-6261", "PROSITEDOC:PDOC00925", "REACTOME:R-BTA-350864", "REACTOME:R-CFA-350864", "REACTOME:R-HSA-350864", "REACTOME:R-HSA-9844594", "REACTOME:R-MMU-350864", "REACTOME:R-RNO-350864", "REACTOME:R-SSC-350864" ]
12
[ "4tr3", "4tr4", "9h48" ]
3
[ "PUB00002931" ]
[ "7592917" ]
[ "Cloning of a cDNA for the type II iodothyronine deiodinase." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 510 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 4, 5, 3 ]
4
true
Active_site
Iodothyronine deiodinase, active site
Iodothyronine deiodinase, active site
Iodothyronine_deiodinase_AS
5
IPR008263
8,263
Glycoside hydrolase, family 16, active site
GH16_AS
Active_site
11,150
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS01034" ]
[ "GH16_1" ]
[ 11150 ]
1
[ "CAZY", "EC", "PROSITEDOC" ]
[ "GH16", "2.4.1.207", "PDOC00794" ]
[ "CAZY:GH16", "EC:2.4.1.207", "PROSITEDOC:PDOC00794" ]
3
[ "1ajk", "1ajo", "1axk", "1byh", "1cpm", "1cpn", "1dyp", "1gbg", "1glh", "1mac", "1mve", "1umz", "1un1", "1zm1", "2ayh", "2r49", "3axd", "3axe", "3d6e", "3h0o", "3hr9", "3i4i", "3iln", "3o5s", "3wvj" ]
25
[ "PUB00000503", "PUB00002845", "PUB00004870", "PUB00005266", "PUB00010686", "PUB00029321" ]
[ "1747104", "8182059", "7624375", "8535779", "11435116", "12970344" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.", "Conserved catalytic machinery and the prediction of a common fold for sever...
[ 1991, 1994, 1995, 1995, 2001, 2003 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 959, 10187, 4 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 69, 44, 53 ]
3
true
Active_site
Glycoside hydrolase, family 16, active site
Glycoside hydrolase, family 16, active site
GH16_AS
2
IPR008264
8,264
Beta-glucanase
Beta_glucanase
Family
6,578
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR00737" ]
[ "GLHYDRLASE16" ]
[ 6578 ]
1
[ "CAZY" ]
[ "GH16" ]
[ "CAZY:GH16" ]
1
[ "1ajk", "1ajo", "1axk", "1byh", "1cpm", "1cpn", "1gbg", "1glh", "1mac", "1mve", "1u0a", "1zm1", "2ayh", "2r49", "3axd", "3axe", "3d6e", "3h0o", "3hr9", "3i4i", "3o5s", "3wvj", "5dze", "5dzf", "5dzg", "5sv8" ]
26
[ "PUB00000503", "PUB00002845", "PUB00004870", "PUB00005266", "PUB00010686", "PUB00029321" ]
[ "1747104", "8182059", "7624375", "8535779", "11435116", "12970344" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.", "Conserved catalytic machinery and the prediction of a common fold for sever...
[ 1991, 1994, 1995, 1995, 2001, 2003 ]
6
[ "IPR044791" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "unclassified sequences" ]
[ 1416, 5134, 7, 21 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]
[ 50, 25, 1, 43 ]
4
true
Family
Beta-glucanase
Beta-glucanase
Beta_glucanase
7
IPR008265
8,265
Lipase, GDSL, active site
Lipase_GDSL_AS
Active_site
11,160
false
false
A variety of lipolytic enzymes with serine as part of the active site have been identified [ ]. Protein sequences which contain this active site signature include; Aeromonas hydrophila lipase, Vibrio mimicus arylesterase, Vibrio parahaemolyticus thermolabile haemolysin, rabbit phospholipase (AdRab-B), and Brassica napu...
[ "GO:0016298", "GO:0006629" ]
[ "lipase activity", "lipid metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS01098" ]
[ "LIPASE_GDSL_SER" ]
[ 11160 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.1", "PDOC00842", "R-HSA-1482788", "R-HSA-975634", "R-MMU-1482788", "R-MMU-975634", "R-RNO-1482788", "R-RNO-975634" ]
[ "EC:3.1.1", "PROSITEDOC:PDOC00842", "REACTOME:R-HSA-1482788", "REACTOME:R-HSA-975634", "REACTOME:R-MMU-1482788", "REACTOME:R-MMU-975634", "REACTOME:R-RNO-1482788", "REACTOME:R-RNO-975634" ]
8
[ "1ivn", "1j00", "1jrl", "1u8u", "1v2g", "3kvn", "5jd3", "5tic", "5tid", "5tie", "5tif", "6jkz", "6jl0", "6jl1", "6jl2", "6lfb", "6lfc", "7ddy", "8h09", "8h0a", "8h0b", "8h0c", "8h0d" ]
23
[ "PUB00005440" ]
[ "7610479" ]
[ "A new family of lipolytic enzymes?" ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "Viruses", "unclassified sequences" ]
[ 6274, 4836, 3, 3, 44 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 114, 4, 1, 1, 4, 1, 21, 5, 36 ]
9
true
Active_site
Lipase, GDSL, active site
Lipase, GDSL, active site
Lipase_GDSL_AS
3
IPR008266
8,266
Tyrosine-protein kinase, active site
Tyr_kinase_AS
Active_site
221,877
false
false
This entry represents the tyrosine protein kinase active site. It also matches a number of proteins belonging to the atypical serine/threonine protein kinase BUD32 family, which lack the conventional structural elements necessary for the substrate recognition and also lack the lysine residue that in all other serine/th...
[ "GO:0004672", "GO:0006468" ]
[ "protein kinase activity", "protein phosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00109" ]
[ "PROTEIN_KINASE_TYR" ]
[ 221877 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.10", "PDOC00100", "R-BTA-114604", "R-BTA-1227986", "R-BTA-1257604", "R-BTA-1433557", "R-BTA-1433559", "R-BTA-180292", "R-BTA-202427", "R-BTA-202733", "R-BTA-2029481", "R-BTA-210990", "R-BTA-210993", "R-BTA-2424491", "R-BTA-2565942", "R-BTA-354192", "R-BTA-373753", "R-BTA-37516...
[ "EC:2.7.10", "PROSITEDOC:PDOC00100", "REACTOME:R-BTA-114604", "REACTOME:R-BTA-1227986", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-1433557", "REACTOME:R-BTA-1433559", "REACTOME:R-BTA-180292", "REACTOME:R-BTA-202427", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-2029481", "REACTOME:R-BTA-210990", ...
1,372
[ "1ad5", "1agw", "1byg", "1fgi", "1fgk", "1fmk", "1fpu", "1fvr", "1gag", "1gjo", "1i44", "1iep", "1ir3", "1irk", "1jpa", "1jqh", "1k2p", "1k3a", "1k9a", "1ksw", "1luf", "1m14", "1m17", "1m52", "1m7n", "1mp8", "1mqb", "1oec", "1opj", "1p4o", "1pkg", "1qcf"...
2,023
[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00052410", "PUB00052411", "PUB00052412" ]
[ "3291115", "12368087", "12471243", "15078142", "15320712", "19275641", "16700535", "15845350" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery: protein kinases.", "Creating chemical dive...
[ 1988, 2002, 2002, 2004, 2004, 2009, 2006, 2005 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1053, 11334, 208643, 685, 162 ]
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...
[ 98, 102, 649, 344, 495, 330, 6, 92, 434, 1, 1, 137 ]
12
true
Active_site
Tyrosine-protein kinase, active site
Tyrosine-protein kinase, active site
Tyr_kinase_AS
5
IPR008268
8,268
Peptidase S16, active site
Peptidase_S16_AS
Active_site
30,097
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[ "GO:0004176", "GO:0004252", "GO:0006508" ]
[ "ATP-dependent peptidase activity", "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PROSITE" ]
[ "PS01046" ]
[ "LON_SER" ]
[ 30097 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21.53", "PDOC00803", "R-BTA-9033241", "R-CEL-9837999", "R-DDI-9837999", "R-DME-9837999", "R-HSA-390471", "R-HSA-9033241", "R-HSA-9837999", "R-HSA-9841251", "R-MMU-9033241", "R-MMU-9837999", "R-RNO-9033241", "R-RNO-9837999", "R-SCE-9837999", "R-SPO-9837999" ]
[ "EC:3.4.21.53", "PROSITEDOC:PDOC00803", "REACTOME:R-BTA-9033241", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-9033241", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9841251", "REACTOME:R-MMU-9033241", "REACTOME:R-MMU-98379...
16
[ "2x36", "4ypl", "4ypm", "5e7s", "6on2", "6v11", "6wqh", "6wys", "6wzv", "6x1m", "6x27", "7fd4", "7fd5", "7fid", "7fie", "7fiz", "7krz", "7ksl", "7ksm", "7nfy", "7ng4", "7ng5", "7ngc", "7ngf", "7ngl", "7ngp", "7ngq", "7oxo", "7p09", "7p0b", "7p0m", "7p6u"...
53
[ "PUB00000522", "PUB00001838", "PUB00002223", "PUB00002870", "PUB00003576", "PUB00004808" ]
[ "8439290", "8294008", "8331083", "8276800", "7845208", "8248235" ]
[ "Evolutionary families of peptidases.", "Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease.", "The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus.", "PIM1 encodes a m...
[ 1993, 1993, 1993, 1994, 1994, 1993 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 408, 21784, 7564, 7, 334 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 21, 1, 2, 2, 1, 15, 6, 1, 8, 7, 1, 1, 38 ]
13
true
Active_site
Peptidase S16, active site
Peptidase S16, active site
Peptidase_S16_AS
5
IPR008269
8,269
Peptidase S16, Lon proteolytic domain
Lon_proteolytic
Domain
57,243
false
false
Lon (also known as endopeptidase La) is a multi-domain ATP- dependent protease found throughout all kingdoms of life. It is involved in protein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecular machines, and a proteolytic domain w...
[ "GO:0004176", "GO:0004252", "GO:0006508" ]
[ "ATP-dependent peptidase activity", "serine-type endopeptidase activity", "proteolysis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PROFILE" ]
[ "PF05362", "PS51786" ]
[ "Lon_C", "LON_PROTEOLYTIC" ]
[ 57143, 50355 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21.53", "R-BTA-9033241", "R-CEL-9033241", "R-CEL-9837999", "R-DDI-9837999", "R-DME-9837999", "R-HSA-390471", "R-HSA-9033241", "R-HSA-9837999", "R-HSA-9841251", "R-MMU-9033241", "R-MMU-9837999", "R-RNO-9033241", "R-RNO-9837999", "R-SCE-9837999", "R-SPO-9837999" ]
[ "EC:3.4.21.53", "REACTOME:R-BTA-9033241", "REACTOME:R-CEL-9033241", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-9033241", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9841251", "REACTOME:R-MMU-9033241", "REACTOME:R-MMU-983...
16
[ "1rr9", "1rre", "1x37", "1xhk", "1z0b", "1z0c", "1z0e", "1z0g", "1z0t", "1z0v", "1z0w", "2x36", "3k1j", "3m6a", "3wu3", "3wu4", "3wu5", "3wu6", "4fw9", "4fwd", "4fwg", "4fwh", "4git", "4ypl", "4ypm", "5e7s", "6on2", "6u5z", "6v11", "6wqh", "6wys", "6wzv"...
98
[ "PUB00030777", "PUB00038301", "PUB00038694", "PUB00075692", "PUB00084291", "PUB00084292" ]
[ "14665623", "15456757", "16002085", "20834233", "20222013", "24520911" ]
[ "The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.", "The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.", "Atomic-resolution crystal structure of the proteolytic doma...
[ 2004, 2004, 2005, 2010, 2010, 2014 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1250, 44339, 10567, 54, 1033 ]
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",...
[ 25, 11, 2, 2, 2, 16, 6, 2, 8, 7, 1, 1, 40 ]
13
true
Domain
Peptidase S16, Lon proteolytic domain
Peptidase S16, Lon proteolytic domain
Lon_proteolytic
4
IPR008270
8,270
Glycosyl hydrolases family 25, active site
Glyco_hydro_25_AS
Active_site
2,697
false
false
It has been shown [ , ] that a number of cell-wall lytic enzymes (EC 3.2.1.17) are evolutionary related and can be classified into a single family: Lysozymes (lysin) from Streptococcus pneumoniae bacteriophages of the Cp family. Lysozyme (endolysin) from Lactococcus delbrueckii phage mv1. Autolytic lysozyme from Clostr...
[ "GO:0003796", "GO:0009253", "GO:0016998" ]
[ "lysozyme activity", "peptidoglycan catabolic process", "cell wall macromolecule catabolic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PROSITE" ]
[ "PS00953" ]
[ "GLYCOSYL_HYDROL_F25_1" ]
[ 2697 ]
1
[ "CAZY", "EC", "PROSITEDOC" ]
[ "GH25", "3.2.1.17", "PDOC00737" ]
[ "CAZY:GH25", "EC:3.2.1.17", "PROSITEDOC:PDOC00737" ]
3
[ "1h09", "1jfx", "1oba", "2ixu", "2ixv", "2j8f", "2j8g", "6zmv" ]
8
[ "PUB00000503", "PUB00001811", "PUB00019371", "PUB00026374", "PUB00093765", "PUB00093766" ]
[ "1747104", "1916274", "14527392", "11427528", "27488615", "20823508" ]
[ "A classification of glycosyl hydrolases based on amino acid sequence similarities.", "Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.", "Structural basis for selective recognition of pneumococcal cell wall by modular endolysin...
[ 1991, 1991, 2003, 2001, 2016, 2010 ]
6
[]
[]
0
0
null
[ "Aciduliprofundum boonei (strain DSM 19572 / T469)", "Bacteria", "Eukaryota", "Viruses", "bioreactor metagenome" ]
[ 1, 2357, 319, 19, 1 ]
5
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1, 1 ]
2
true
Active_site
Glycosyl hydrolases family 25, active site
Glycosyl hydrolases family 25, active site
Glyco_hydro_25_AS
4
IPR008271
8,271
Serine/threonine-protein kinase, active site
Ser/Thr_kinase_AS
Active_site
1,441,423
false
false
Eukaryotic protein kinases [ , , , ] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of th...
[ "GO:0004672", "GO:0006468" ]
[ "protein kinase activity", "protein phosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PROSITE" ]
[ "PS00108" ]
[ "PROTEIN_KINASE_ST" ]
[ 1441423 ]
1
[ "EC", "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...
[ "2.7.11", "2.7.11.1", "PDOC00100", "R-BTA-110056", "R-BTA-111933", "R-BTA-111995", "R-BTA-112382", "R-BTA-112409", "R-BTA-112411", "R-BTA-114516", "R-BTA-1169091", "R-BTA-1181150", "R-BTA-1257604", "R-BTA-1295596", "R-BTA-141444", "R-BTA-1483191", "R-BTA-1502540", "R-BTA-1538133", ...
[ "EC:2.7.11", "EC:2.7.11.1", "PROSITEDOC:PDOC00100", "REACTOME:R-BTA-110056", "REACTOME:R-BTA-111933", "REACTOME:R-BTA-111995", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-112409", "REACTOME:R-BTA-112411", "REACTOME:R-BTA-114516", "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1181150", "REACTOME:R-B...
2,615
[ "1a06", "1apm", "1aq1", "1atp", "1b38", "1b39", "1b6c", "1bi7", "1bi8", "1bkx", "1blx", "1buh", "1bx6", "1cdk", "1cki", "1ckj", "1ckp", "1cmk", "1csn", "1ctp", "1daw", "1day", "1di8", "1dm2", "1ds5", "1e1v", "1e1x", "1e9h", "1eh4", "1f0q", "1f3m", "1f5q"...
4,778
[ "PUB00001530", "PUB00003568", "PUB00003569", "PUB00005115", "PUB00005145", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]
[ "7768349", "1835513", "1956325", "3291115", "1862342", "12368087", "12471243", "15078142", "15320712" ]
[ "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.", "Protein kinase classification.", "Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.", "The ...
[ 1995, 1991, 1991, 1988, 1991, 2002, 2002, 2004, 2004 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 608, 116400, 1321159, 1681, 1575 ]
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...
[ 3802, 300, 2662, 531, 1354, 1044, 98, 3602, 1503, 111, 97, 5272 ]
12
true
Active_site
Serine/threonine-protein kinase, active site
Serine/threonine-protein kinase, active site
Ser/Thr_kinase_AS
4
IPR008274
8,274
Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
AldOxase/xan_DH_MoCoBD1
Domain
68,880
false
false
The aldehyde oxido-reductase (Mop) from the sulphate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas is a homodimer of 907 amino acid residues subunits and is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centres. It is folded in...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02738" ]
[ "MoCoBD_1" ]
[ 68880 ]
1
[ "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1236", "GenProp1255", "GenProp1469", "GenProp1753", "R-CEL-964975", "R-DDI-74259", "R-DDI-964975", "R-DDI-9748787", "R-DME-74259", "R-DME-964975", "R-DME-9748787", "R-GGA-421178", "R-HSA-74259", "R-HSA-8851680", "R-HSA-964975", "R-HSA-9748787", "R-MMU-74259", "R-MMU-8851680...
[ "GP:GenProp1236", "GP:GenProp1255", "GP:GenProp1469", "GP:GenProp1753", "REACTOME:R-CEL-964975", "REACTOME:R-DDI-74259", "REACTOME:R-DDI-964975", "REACTOME:R-DDI-9748787", "REACTOME:R-DME-74259", "REACTOME:R-DME-964975", "REACTOME:R-DME-9748787", "REACTOME:R-GGA-421178", "REACTOME:R-HSA-7425...
24
[ "1dgj", "1ffu", "1ffv", "1fiq", "1fo4", "1jro", "1jrp", "1n5w", "1n5x", "1n60", "1n61", "1n62", "1n63", "1rm6", "1sb3", "1sij", "1t3q", "1v97", "1vdv", "1vlb", "1wyg", "1zxi", "2ckj", "2e1q", "2e3t", "2w3r", "2w3s", "2w54", "2w55", "3am9", "3amz", "3an1"...
86
[ "PUB00005209", "PUB00100884" ]
[ "7502041", "27537049" ]
[ "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.", "Xanthine dehydrogenase: An old enzyme with new knowledge and prospects." ]
[ 1995, 2016 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudovirales sp. ctU7I6", "Eukaryota", "unclassified sequences" ]
[ 996, 53778, 1, 12869, 1236 ]
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",...
[ 37, 3, 4, 7, 3, 6, 16, 1, 24, 23, 76 ]
11
true
Domain
Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
AldOxase/xan_DH_MoCoBD1
9
IPR008275
8,275
Acyl-CoA dehydratase activase domain
CoA_E_activase_dom
Domain
7,042
false
false
This domain is found in a set of closely related prokaryotic [4Fe-4S]-containing ATPases, including activators of (R)-2-hydroxyglutaryl-CoA dehydratase, (R)-phenyllactate dehydratase, lactoyl-CoA dehydratase, and benzoyl-CoA reductase, as well as the uncharacterised protein YjiL of E. coli. Characterised members of thi...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00241" ]
[ "CoA_E_activ" ]
[ 7042 ]
1
[]
[]
[]
0
[ "1hux", "4eht", "4ehu", "4eia", "7yyl", "7yzm", "7yzq" ]
7
[ "PUB00061084", "PUB00077140", "PUB00106446" ]
[ "22827463", "11967068", "7607244" ]
[ "On the ATP-Dependent Activation of the Radical Enzyme (R)-2-Hydroxyisocaproyl-CoA Dehydratase.", "Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes.", "Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans." ]
[ 2012, 2002, 1995 ]
3
[ "IPR002731" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Metamonada", "Siphoviridae sp. ctjdk2", "unclassified sequences" ]
[ 360, 6427, 15, 1, 239 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Acyl-CoA dehydratase activase domain
Acyl-CoA dehydratase activase domain
CoA_E_activase_dom
5
IPR008276
8,276
Concentrative nucleoside transporter
C_nuclsd_transpt
Family
19,278
false
false
Nucleosides are hydrophilic molecules and require specialised transport proteins for permeation of cell membranes. There are two types of nucleoside transport processes: equilibrative bidirectional processes driven by chemical gradients, and inwardly directed concentrative processes driven by an electrochemical gradien...
[ "GO:0005337", "GO:1901642", "GO:0016020" ]
[ "nucleoside transmembrane transporter activity", "nucleoside transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PANTHER" ]
[ "PTHR10590" ]
[ "" ]
[ 19278 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-83936", "R-HSA-9748787", "R-HSA-9755088", "R-MMU-83936", "R-MMU-9748787", "R-MMU-9755088", "R-RNO-83936", "R-RNO-9748787", "R-RNO-9755088" ]
[ "REACTOME:R-HSA-83936", "REACTOME:R-HSA-9748787", "REACTOME:R-HSA-9755088", "REACTOME:R-MMU-83936", "REACTOME:R-MMU-9748787", "REACTOME:R-MMU-9755088", "REACTOME:R-RNO-83936", "REACTOME:R-RNO-9748787", "REACTOME:R-RNO-9755088" ]
9
[ "3tij", "4pb1", "4pb2", "4pd5", "4pd6", "4pd7", "4pd8", "4pd9", "4pda", "5l24", "5l26", "5l27", "5l2a", "5l2b", "5u9w", "6ksw", "8tz1", "8tz2", "8tz3", "8tz4", "8tz5", "8tz6", "8tz7", "8tz8", "8tz9", "8tza", "8tzd" ]
27
[ "PUB00002299", "PUB00033989", "PUB00033990", "PUB00033991", "PUB00033992", "PUB00071908", "PUB00071946", "PUB00076710" ]
[ "8550462", "10353709", "15678184", "12794928", "16265592", "23506887", "15870078", "17453413" ]
[ "Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein.", "Recent advances in the molecular biology of nucleoside transporters of mammalian cells.", "The nucleoside transport proteins, NupC and ...
[ 1996, 1998, 2005, 2003, 2005, 2013, 2005, 2007 ]
8
[]
[ "IPR018270" ]
0
1
0
[ "Bacteria", "Eukaryota", "Musca hytrovirus(isolate Musca domestica/United States/Boucias/-)", "metagenomes" ]
[ 13123, 6023, 1, 131 ]
4
[ "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)", "Rattus norvegicus" ]
[ 4, 4, 5, 3, 11, 5, 1, 19 ]
8
true
Family
Concentrative nucleoside transporter
Concentrative nucleoside transporter
C_nuclsd_transpt
6
IPR008278
8,278
4'-phosphopantetheinyl transferase domain
4-PPantetheinyl_Trfase_dom
Domain
51,745
false
false
The 4'-phosphopantetheinyl transferase superfamily of proteins transfer the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pp-binding. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [ ]...
[ "GO:0000287", "GO:0008897" ]
[ "magnesium ion binding", "holo-[acyl-carrier-protein] synthase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF01648" ]
[ "ACPS" ]
[ 51745 ]
1
[ "EC", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.8.7", "GenProp1220", "PWY-6012", "PWY-6289", "R-HSA-199220", "R-MMU-199220", "R-RNO-199220" ]
[ "EC:2.7.8.7", "GP:GenProp1220", "METACYC:PWY-6012", "METACYC:PWY-6289", "REACTOME:R-HSA-199220", "REACTOME:R-MMU-199220", "REACTOME:R-RNO-199220" ]
7
[ "1f7l", "1f7t", "1f80", "1fte", "1ftf", "1fth", "1qr0", "2bdd", "2byd", "2c43", "2cg5", "2jbz", "2jca", "2qg8", "2uv8", "2vkz", "2was", "2wat", "2wdo", "2wds", "2wdy", "3gwm", "3h7q", "3hmj", "3hqj", "3hyk", "3ne1", "3ne3", "3ne9", "3nfd", "3qmn", "4dxe"...
107
[ "PUB00002924", "PUB00011221" ]
[ "7559576", "10581256" ]
[ "Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase.", "Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily." ]
[ 1995, 1999 ]
2
[]
[ "IPR004568" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 89, 42786, 8265, 5, 600 ]
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",...
[ 26, 3, 1, 1, 3, 3, 2, 1, 8, 3, 3, 3, 10 ]
13
true
Domain
4'-phosphopantetheinyl transferase domain
4'-phosphopantetheinyl transferase domain
4-PPantetheinyl_Trfase_dom
1
IPR008279
8,279
PEP-utilising enzyme, mobile domain
PEP-util_enz_mobile_dom
Domain
70,340
false
false
A number of enzymes that catalyse the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [ , , , ]. All these enzymes share the same catalytic mechanism: they bind PEP and transfer the phosphoryl group from it to a histidine resi...
[ "GO:0016772", "GO:0016310" ]
[ "transferase activity, transferring phosphorus-containing groups", "phosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF00391" ]
[ "PEP-utilizers" ]
[ 70340 ]
1
[ "GP", "PROSITEDOC" ]
[ "GenProp1324", "PDOC00527" ]
[ "GP:GenProp1324", "PROSITEDOC:PDOC00527" ]
2
[ "1dik", "1eza", "1ezb", "1ezc", "1ezd", "1ggo", "1jde", "1kbl", "1kc7", "1vbg", "1vbh", "1zym", "2dik", "2e28", "2eza", "2ezb", "2ezc", "2fm4", "2hro", "2hwg", "2kx9", "2l5h", "2mp0", "2n5t", "2ols", "2r82", "2wqd", "2x0s", "2xdf", "3eza", "3ezb", "3eze"...
51
[ "PUB00000317", "PUB00001868", "PUB00003750", "PUB00005010", "PUB00013974" ]
[ "2176881", "8973315", "1557039", "7686067", "12083528" ]
[ "Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.", "Novel phosphotransferase-encoding genes revealed by a...
[ 1990, 1996, 1992, 1993, 2002 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1824, 64764, 2797, 10, 945 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 6, 1, 6, 6, 60 ]
5
true
Domain
PEP-utilising enzyme, mobile domain
PEP-utilising enzyme, mobile domain
PEP-util_enz_mobile_dom
9