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
IPR005035
5,035
Herpesvirus UL3
Herpes_UL3
Family
381
false
false
Herpes simplex viruses are large DNA viruses, the genome of which encode approximately 80 genes. The UL3 gene of Human herpesvirus 2 (HHV-2) is predicted to encode a 233 amino acid protein with a molecular mass of 26kDa. Homologues of the UL3 protein are encoded only among alphaherpesviruses. The function of the UL3 pr...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03369" ]
[ "Herpes_UL3" ]
[ 381 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007245" ]
[ "10466815" ]
[ "Nucleolar localization of the UL3 protein of herpes simplex virus type 2." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Alphaherpesvirinae", "Corallococcus aberystwythensis" ]
[ 380, 1 ]
2
[]
[]
0
true
Family
Herpesvirus UL3
Herpesvirus UL3
Herpes_UL3
6
IPR005036
5,036
CBM21 (carbohydrate binding type-21) domain
CBM21_dom
Domain
11,119
false
false
The carbohydrate binding type-21 or CBM21 domain is a 90-130 amino acid carbohydrate binding domain. The domain is named after proteins classified in carbohydrate-binding module (CBM) family 21 and is sometimes called starch-binding domain (SBD) [ ]. The CBM21 domain occurs in several eukaryotic proteins implicated in ...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF03370", "PS51159" ]
[ "CBM_21", "CBM21" ]
[ 11069, 10859 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC51159", "R-BTA-3322077", "R-DRE-3322077", "R-HSA-3322077", "R-HSA-3785653", "R-MMU-3322077", "R-RNO-3322077", "R-SCE-3322077" ]
[ "PROSITEDOC:PDOC51159", "REACTOME:R-BTA-3322077", "REACTOME:R-DRE-3322077", "REACTOME:R-HSA-3322077", "REACTOME:R-HSA-3785653", "REACTOME:R-MMU-3322077", "REACTOME:R-RNO-3322077", "REACTOME:R-SCE-3322077" ]
8
[ "2djm", "2eef", "2m83", "2v8l", "2v8m", "2vq4", "4bfn", "4bfo", "4eib", "7qf7", "7qfa", "7qm2" ]
12
[ "PUB00019263", "PUB00019264", "PUB00033748", "PUB00033749" ]
[ "9045612", "9046081", "15939348", "16262690" ]
[ "PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism.", "Yeast PIG genes: PIG1 encodes a putative type 1 phosphatase subunit that interacts with the yeast glycogen synthase Gsy2p.", "Microbial starch-binding domain.", "A new clan of CBM families based on bioinformatics of starch-bi...
[ 1997, 1997, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 235, 10884 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 5, 19, 6, 12, 9, 2, 13, 4 ]
8
true
Domain
CBM21 (carbohydrate binding type-21) domain
CBM21 (carbohydrate binding type-21) domain
CBM21_dom
2
IPR005037
5,037
Pre-mRNA-splicing factor 38
PRP38
Family
8,865
false
false
Members of this family are related to the pre mRNA splicing factor PRP38 from yeast [ ], therefore all the members of this family could be involved in splicing. This conserved region could be involved in RNA binding. The putative domain is about 180 amino acids in length. PRP38 is a unique component of the U4/U6.U5 tri...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03371", "PTHR23142" ]
[ "PRP38", "" ]
[ 8644, 8588 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-72163", "R-HSA-72163", "R-MMU-72163" ]
[ "REACTOME:R-BTA-72163", "REACTOME:R-HSA-72163", "REACTOME:R-MMU-72163" ]
3
[ "4rz9", "4rza", "5f5s", "5f5t", "5f5u", "5f5v", "5nrl", "5o9z", "5zwo", "6ahd", "7aav", "7abf", "7abg", "7abi", "8h6k", "8q7n", "8qo9", "8qpe", "8qzs" ]
19
[ "PUB00007246", "PUB00007247" ]
[ "1508195", "9582287" ]
[ "PRP38 encodes a yeast protein required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels.", "Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation." ]
[ 1992, 1998 ]
2
[]
[]
0
0
null
[ "Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630)", "Eukaryota", "Rice tungro bacilliform virus" ]
[ 1, 8862, 2 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 15, 2, 10, 6, 5, 6, 1, 10, 6, 1, 1, 23 ]
12
true
Family
Pre-mRNA-splicing factor 38
Pre-mRNA-splicing factor 38
PRP38
4
IPR005038
5,038
Octapeptide repeat
Octapeptide
Repeat
658
false
false
This octapeptide repeat is found in several bacterial proteins, including immunoglobulin G-binding protein A from Staphylococcus. The function of this repeat is unknown.
[ "GO:0019865" ]
[ "immunoglobulin binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03373" ]
[ "Octapeptide" ]
[ 658 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria" ]
[ 658 ]
1
[]
[]
0
true
Repeat
Octapeptide repeat
Octapeptide repeat
Octapeptide
7
IPR005039
5,039
Antirepressor protein, C-terminal
Ant_C
Domain
7,037
false
false
This entry represents the C-terminal domain of the antirepressor protein (Ant) from Enterobacteria phage P1. Prophages P1 and P7 exist as unit copy DNA plasmids in the bacterial cell. Maintenance of the prophage state requires the continuous expression of two repressors: (i) C1 is a protein which negatively regulates t...
[ "GO:0003677" ]
[ "DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03374" ]
[ "ANT" ]
[ 7037 ]
1
[]
[]
[]
0
[]
0
[ "PUB00010111" ]
[ "11897024" ]
[ "Extensive domain shuffling in transcription regulators of DNA viruses and implications for the origin of fungal APSES transcription factors." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Halobaculum halobium", "Opisthokonta", "Viruses", "metagenomes" ]
[ 6111, 1, 9, 873, 43 ]
5
[]
[]
0
true
Domain
Antirepressor protein, C-terminal
Antirepressor protein, C-terminal
Ant_C
9
IPR005041
5,041
Adenovirus E3B protein
Adeno_E3B
Family
167
false
false
Adenoviruses are medium-sized, non-enveloped viruses containing double-stranded DNA. They can cause a variety of diseases including pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised [ ]. These viruses have many mechanisms to evade the host immune response...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF03376" ]
[ "Adeno_E3B" ]
[ 167 ]
1
[]
[]
[]
0
[]
0
[ "PUB00005244", "PUB00010442", "PUB00034706", "PUB00034707" ]
[ "7704534", "9707602", "7555057", "2522818" ]
[ "Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution.", "The adenovirus E3/10.4K-14.5K proteins down-modulate the apoptosis receptor Fas/Apo-1 by inducing its internalization.", "E3 transcription unit of adenovirus.", "Epidermal growth factor receptor is dow...
[ 1994, 1998, 1995, 1989 ]
4
[]
[]
0
0
null
[ "Mastadenovirus" ]
[ 167 ]
1
[]
[]
0
true
Family
Adenovirus E3B protein
Adenovirus E3B protein
Adeno_E3B
5
IPR005042
5,042
TAL effector repeat
TAL_effector_rpt
Repeat
395
false
false
The proteins in this group bind to DNA. Each repeat binds to a base pair in a predictable way. The structure shows that each repeat is composed of two α helices [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03377" ]
[ "TAL_effector" ]
[ 395 ]
1
[]
[]
[]
0
[ "2kq5", "2ypf", "3ugm", "3v6p", "3v6t", "4gg4", "4gjp", "4gjr", "4hpz", "4osh", "4osi", "4osj", "4osk", "4osl", "4osm", "4osq", "4osr", "4oss", "4ost", "4osv", "4osw", "4osz", "4ot0", "4ot3", "4oto", "6jtq", "6jvz", "6jw0", "6jw1", "6jw2", "6jw3", "6jw4"...
36
[ "PUB00081212" ]
[ "22223736" ]
[ "The crystal structure of TAL effector PthXo1 bound to its DNA target." ]
[ 2012 ]
1
[]
[]
0
0
null
[ "Effrenium voratum", "Pseudomonadota" ]
[ 1, 394 ]
2
[]
[]
0
true
Repeat
TAL effector repeat
TAL effector repeat
TAL_effector_rpt
2
IPR005043
5,043
Exportin-2, C-terminal
XPO2_C
Domain
5,158
false
false
Exportin-2, also known as CAS, is an export receptor for importin-alpha [ ]. It binds strongly to importin alpha only in the presence of RanGTP, forming an importin alpha/CAS/RanGTP complex. Exportin-2 mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into th...
[ "GO:0005515", "GO:0031267" ]
[ "protein binding", "small GTPase binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF03378" ]
[ "CAS_CSE1" ]
[ 5158 ]
1
[]
[]
[]
0
[ "1wa5", "1z3h" ]
2
[ "PUB00007252", "PUB00032221", "PUB00090423" ]
[ "9323134", "15602554", "10394916" ]
[ "Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor.", "Structural basis for the assembly of a nuclear export complex.", "Genetic evidence for interactions between yeast importin alpha (Srp1p) and its nuclear export receptor, Cse1p." ]
[ 1997, 2004, 1999 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5158 ]
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...
[ 3, 2, 1, 1, 7, 5, 1, 4, 4, 1, 1, 6 ]
12
true
Domain
Exportin-2, C-terminal
Exportin-2, C-terminal
XPO2_C
3
IPR005044
5,044
Protein of unknown function DUF282, Caenorhabditis species
DUF282_CAE_spp
Family
145
false
false
This family consists of proteins of unknown function found in Caenorhabditis species.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03380" ]
[ "DUF282" ]
[ 145 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Caenorhabditis" ]
[ 145 ]
1
[ "Caenorhabditis elegans" ]
[ 19 ]
1
true
Family
Protein of unknown function DUF282, Caenorhabditis species
Protein of unknown function DUF282, Caenorhabditis species
DUF282_CAE_spp
7
IPR005045
5,045
CDC50/LEM3 family
CDC50/LEM3_fam
Family
10,019
false
false
CDC50/LEM3 is a family of membrane proteins whose members include cell cycle control protein 50, alkylphosphocholine resistance protein LEM3, which is is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae [ ], and several ALA-interacting subunits, which are plant proteins inv...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF03381", "PIRSF015840", "PTHR10926" ]
[ "CDC50", "DUF284_TM_euk", "" ]
[ 9898, 8164, 9817 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6798695", "R-CEL-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695", "R-SCE-6798695", "R-SPO-6798695" ]
[ "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695", "REACTOME:R-SCE-6798695", "REACTOME:R-SPO-6798695" ]
7
[ "6k7g", "6k7h", "6k7i", "6k7j", "6k7k", "6k7l", "6k7m", "6k7n", "6lcp", "6lcr", "6lkn", "6psx", "6psy", "6roh", "6roi", "6roj", "7bsp", "7bsq", "7bss", "7bsu", "7bsv", "7bsw", "7drx", "7dsh", "7dsi", "7f7f", "7ky5", "7ky6", "7ky7", "7ky8", "7ky9", "7kya"...
59
[ "PUB00070975", "PUB00070976", "PUB00097883", "PUB00097884" ]
[ "12133835", "18344284", "20053675", "32493773" ]
[ "A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae.", "The Arabidopsis P4-ATPase ALA3 localizes to the golgi and requires a beta-subunit to function in lipid translocation and secretory vesicle formation.", "Intracellular targeting...
[ 2002, 2008, 2010, 2020 ]
4
[]
[]
0
0
null
[ "Eukaryota", "viral metagenome" ]
[ 10018, 1 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 20, 3, 8, 3, 9, 6, 1, 16, 9, 3, 2, 51 ]
12
true
Family
CDC50/LEM3 family
CDC50/LEM3 family
CDC50/LEM3_fam
7
IPR005046
5,046
Protein of unknown function DUF285
DUF285
Family
8,489
false
false
This is a family proteins of unknown function which includes predicted surface proteins (often lipoproteins) from Listeria monocytogenes, Listeria innocua, Enterococcus faecalis (Streptococcus faecalis), Lactobacillus plantarum, Mycoplasma spp., Helicobacter hepaticus, and other species. Eukaryotic sequences are also i...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03382" ]
[ "DUF285" ]
[ 8489 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 30, 5456, 2578, 150, 275 ]
5
[]
[]
0
true
Family
Protein of unknown function DUF285
Protein of unknown function DUF285
DUF285
2
IPR005048
5,048
Domain of unknown function DUF287
DUF287
Domain
680
false
false
This is a domain is found predominantly in Arabidopsis proteins. Its function is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03384" ]
[ "DUF287" ]
[ 680 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "rosids" ]
[ 680 ]
1
[ "Arabidopsis thaliana" ]
[ 68 ]
1
true
Domain
Domain of unknown function DUF287
Domain of unknown function DUF287
DUF287
6
IPR005049
5,049
STELLO-like
STL-like
Family
2,361
false
false
Members of this family have been characterised in plants and named STELLO. STELLO1 and 2 from Arabidopsis are Golgi-localized proteins that can interact with cellulose synthase CesA and control cellulose quantity. Cellulose is produced at the plasma membrane by cellulose synthase (CesA) complexes (CSCs), which are asse...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03385", "PTHR31362" ]
[ "STELLO", "" ]
[ 1783, 2345 ]
2
[]
[]
[]
0
[ "7xpr", "7xps", "7xpt", "7yua", "7yv0", "8hl8" ]
6
[ "PUB00081895" ]
[ "27277162" ]
[ "Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis." ]
[ 2016 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)", "Synechococcus phage S-T4", "metagenomes" ]
[ 146, 2199, 1, 1, 14 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 11, 7, 6, 9 ]
4
true
Family
STELLO-like
STELLO-like
STL-like
9
IPR005050
5,050
Early nodulin 93 ENOD93 protein
Enod93
Family
1,844
false
false
The expression of early nodulin (ENOD) genes has been well characterised in several legume species. Based on their biochemical attributes and expression patterns, they are postulated to have roles in cell structure, in the control of nodule ontogeny by the degradation of Nod factor, and in carbon metabolism [ ].
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03386", "PTHR33605" ]
[ "ENOD93", "" ]
[ 1843, 1713 ]
2
[]
[]
[]
0
[]
0
[ "PUB00007254" ]
[ "10759502" ]
[ "Dg93, a nodule-abundant mRNA of Datisca glomerata with homology to a soybean early nodulin gene." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1844 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 3, 24, 26 ]
3
true
Family
Early nodulin 93 ENOD93 protein
Early nodulin 93 ENOD93 protein
Enod93
3
IPR005051
5,051
Herpesvirus UL46
Herpes_UL46
Family
313
false
false
The UL46 protein (VP11/12) is produced in the late phase of Herpes virus infection in a manner highly dependent on viral DNA synthesis, and is mainly distributed at the edge of the nucleus in the cytoplasm. It is a tegument phosphoprotein reported to modulate the activity of UL48 (anti-TNF) protein.
[ "GO:0006355" ]
[ "regulation of DNA-templated transcription" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF03387" ]
[ "Herpes_UL46" ]
[ 313 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Alphaherpesvirinae" ]
[ 313 ]
1
[]
[]
0
true
Family
Herpesvirus UL46
Herpesvirus UL46
Herpes_UL46
2
IPR005053
5,053
MobA/MobL protein
MobA_MobL
Domain
8,641
false
false
This entry represents a domain found at the N terminus of MobA in Escherichia coli, and MobL in Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans), as well as in conjugal transfer protein TraA. MobA and MobL are mobilisation proteins, which are essential for specific plasmid transfer.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03389" ]
[ "MobA_MobL" ]
[ 8641 ]
1
[]
[]
[]
0
[ "2ns6", "4ht4" ]
2
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Plasmid pIP501", "Synechococcus phage Yong-M3-253", "unclassified sequences" ]
[ 8461, 57, 1, 1, 121 ]
5
[]
[]
0
true
Domain
MobA/MobL protein
MobA/MobL protein
MobA_MobL
3
IPR005054
5,054
Nepovirus coat protein
Nepo_coat
Domain
963
false
false
Nepoviruses are plant viruses that, together with comoviruses and picornaviruses, are classified in the picornavirus superfamily of plus strand single-stranded RNA viruses. Its genome consist of two single-stranded RNAs, both required for infection [ ]. This family aligns several nepovirus coat protein sequences. In se...
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF03391" ]
[ "Nepo_coat" ]
[ 963 ]
1
[]
[]
[]
0
[ "1a6c", "2y26", "4v5t", "4v5w", "5foj" ]
5
[ "PUB00007724", "PUB00099814" ]
[ "9519407", "34370094" ]
[ "The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily.", "Metagenomic analysis of nepoviruses: diversity, evolution and identification of a genome region in members of subgroup A that appears to be important for host range." ]
[ 1998, 2021 ]
2
[]
[]
0
0
null
[ "Parasteatoda tepidariorum", "Viruses" ]
[ 1, 962 ]
2
[]
[]
0
true
Domain
Nepovirus coat protein
Nepovirus coat protein
Nepo_coat
8
IPR005055
5,055
Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3
A10/PebIII
Family
5,632
false
false
This entry represents the insect odorant-binding protein A10, also known as OS-D or pherokine-1, and ejaculatory bulb-specific protein 3 (PebIII), also known as pherokine-2 [ ].
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03392", "PTHR11257" ]
[ "OS-D", "" ]
[ 5625, 5392 ]
2
[]
[]
[]
0
[ "1k19", "1kx8", "1kx9", "1n8u", "1n8v", "2gvs", "2jnt", "7e8l", "8xkt", "9j00", "9j01" ]
11
[ "PUB00002853", "PUB00091683" ]
[ "8206941", "12899697" ]
[ "Putative Drosophila pheromone-binding proteins expressed in a subregion of the olfactory system.", "Pherokine-2 and -3." ]
[ 1994, 2003 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 17, 5615 ]
2
[ "Drosophila melanogaster" ]
[ 7 ]
1
true
Family
Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3
Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3
A10/PebIII
1
IPR005056
5,056
Matrix protein, N-terminal, pneumovirus
MATRX_N_pneumovirus
Domain
463
false
false
This entry represents the N-terminal domain of the pneumoviral matrix protein (MATRX). The N-terminal domain of the RSV M protein (residues 1-126) adopts a twisted β-sandwich fold comprised of two nearly perpendicular β-sheets - one with 3 β-strands and one with 4 β-strands [ ]. The overall topology is a curved horsesh...
[ "GO:0019068", "GO:0019031" ]
[ "virion assembly", "viral envelope" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF03393" ]
[ "Matrix_Pneumo_N" ]
[ 463 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-9820960", "R-HSA-9820962", "R-HSA-9828721", "R-HSA-9828806", "R-HSA-9833110" ]
[ "REACTOME:R-HSA-9820960", "REACTOME:R-HSA-9820962", "REACTOME:R-HSA-9828721", "REACTOME:R-HSA-9828806", "REACTOME:R-HSA-9833110" ]
5
[ "2vqp", "2ykd", "4d4t", "4lp7", "4v23" ]
5
[ "PUB00049858" ]
[ "19251668" ]
[ "Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction." ]
[ 2009 ]
1
[]
[]
0
0
null
[ "Pneumoviridae" ]
[ 463 ]
1
[]
[]
0
true
Domain
Matrix protein, N-terminal, pneumovirus
Matrix protein, N-terminal, pneumovirus
MATRX_N_pneumovirus
1
IPR005057
5,057
Poxvirus E8
Poxvirus_E8
Family
129
false
false
This entry represents a family of poxvirus proteins that includes Protein E8 from Vaccinia virus, which is also known as Protein OPG070. This protein may play a role in the biogenesis of the viral factories by recruiting and wrapping DNA replication sites in endoplasmic reticulum derived membranes. It binds DNA in vitr...
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF03394", "PIRSF015690" ]
[ "Pox_E8", "VAC_E8R" ]
[ 129, 126 ]
2
[]
[]
[]
0
[]
0
[ "PUB00103576" ]
[ "12208956" ]
[ "The Vaccinia virus E8R gene product: a viral membrane protein that is made early in infection and packaged into the virions' core." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Poxviridae" ]
[ 129 ]
1
[]
[]
0
true
Family
Poxvirus E8
Poxvirus E8
Poxvirus_E8
7
IPR005058
5,058
Poxvirus P4A
Poxvirus_P4A
Family
211
false
false
This entry represents Major core protein 4a precursor from Vaccinia virus (P4A), also known as Major core protein OPG136 precursor, and similar proteins from poxvirus. P4a is one of the most abundant structural proteins in the Vaccinia virion. It undergoes proteolytic processing during the immature virion (IV) to matur...
[ "GO:0005198", "GO:0044423" ]
[ "structural molecule activity", "virion component" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM" ]
[ "PF03395" ]
[ "Pox_P4A" ]
[ 211 ]
1
[]
[]
[]
0
[ "8p4k", "8r5i", "8wd7", "8wdc" ]
4
[ "PUB00103577" ]
[ "11390580" ]
[ "The major core protein P4a (A10L gene) of vaccinia virus is essential for correct assembly of viral DNA into the nucleoprotein complex to form immature viral particles." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Poxviridae" ]
[ 211 ]
1
[]
[]
0
true
Family
Poxvirus P4A
Poxvirus P4A
Poxvirus_P4A
3
IPR005059
5,059
DNA-directed RNA polymerase, 35kDa subunit, poxviral
DNA-dir_RNA_pol_35kDa_poxviral
Family
157
false
false
DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...
[ "GO:0003677", "GO:0003899", "GO:0019083" ]
[ "DNA binding", "DNA-directed RNA polymerase activity", "viral transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PIRSF" ]
[ "PF03396", "PIRSF000746" ]
[ "Pox_RNA_pol_35", "Rpo35" ]
[ 157, 139 ]
2
[ "EC" ]
[ "2.7.7.6" ]
[ "EC:2.7.7.6" ]
1
[ "6rfl", "6ric", "6rid", "6rie", "7amv", "7aof", "7aoh", "7aoz", "7ap8", "7ap9", "8c8h", "8p0j", "8p0k", "8p0n", "8rqk", "9ex9", "9fpy", "9fq6" ]
18
[ "PUB00000061", "PUB00033173" ]
[ "3052291", "10499798" ]
[ "Structure and function of bacterial sigma factors.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]
[ 1988, 1999 ]
2
[]
[]
0
0
null
[ "Poxviridae" ]
[ 157 ]
1
[]
[]
0
true
Family
DNA-directed RNA polymerase, 35kDa subunit, poxviral
DNA-directed RNA polymerase, 35kDa subunit, poxviral
DNA-dir_RNA_pol_35kDa_poxviral
6
IPR005060
5,060
Rhabdovirus matrix protein
Rhabdo_matrix
Family
101
false
false
The matrix (M) proteins of Rabies virus (RV) plays a key role in both assembly and budding of progeny virions. A PPPY motif (PY motif or late-budding domain) is conserved in the M proteins. These PY motifs are important for virus budding and for mediating interactions with specific cellular proteins containing WW domai...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03397" ]
[ "Rhabdo_matrix" ]
[ 101 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Novirhabdovirus" ]
[ 101 ]
1
[]
[]
0
true
Family
Rhabdovirus matrix protein
Rhabdovirus matrix protein
Rhabdo_matrix
9
IPR005061
5,061
Vacuolar protein sorting-associated protein Ist1
Ist1
Family
11,335
false
false
Budding yeast Ist1 is involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles [ ]. This entry also includes Ist1 homologues from animals and plants. Human Ist1 functions in the ESCRT (endosomal sorting complexes required for transport) pathway a...
[ "GO:0015031" ]
[ "protein transport" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF03398", "PTHR12161" ]
[ "Ist1", "" ]
[ 11205, 10945 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-6798695", "R-DDI-9668328", "R-HSA-6798695", "R-HSA-9668328", "R-MMU-6798695", "R-MMU-9668328", "R-RNO-6798695", "R-RNO-9668328", "R-SCE-6798695", "R-SCE-9668328", "R-SPO-6798695", "R-SPO-9668328" ]
[ "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9668328", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9668328", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-9668328", "REACTOME:R-RNO-6798695", "REACTOME:R-RNO-9668328", "REACTOME:R-SCE-6798695", "REACTOME:R-SCE-9668328", "REACTOME:R-SPO-6798695", "REACTOM...
12
[ "3frr", "3frs", "3ggy", "3ggz", "3jc1", "6e8g", "6tz4", "6tz5", "6tza", "8v2q", "8v2r", "8v2s" ]
12
[ "PUB00077601", "PUB00077602", "PUB00077607" ]
[ "18032584", "19129479", "25657007" ]
[ "Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting.", "Biochemical analyses of human IST1 and its function in cytokinesis.", "Distinct mechanisms of recognizing endosomal sorting complex required for transport III (ESCRT-III) protein IST1 by different microtubule interacting and tr...
[ 2008, 2009, 2015 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 11335 ]
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...
[ 67, 2, 4, 6, 12, 2, 1, 30, 5, 1, 1, 85 ]
12
true
Family
Vacuolar protein sorting-associated protein Ist1
Vacuolar protein sorting-associated protein Ist1
Ist1
2
IPR005062
5,062
SAC3/GANP/THP3, conserved domain
SAC3/GANP/THP3_conserved
Domain
11,942
false
false
This domain contains one highly conserved negatively charged residue and one highly conserved positively charged residue that are probably important for the function of these proteins. Proteins containing this domain include the yeast nuclear export factor Sac3 [ ], and mammalian GANP/MCM3-associated protein, which fac...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03399" ]
[ "SAC3_GANP" ]
[ 11942 ]
1
[]
[]
[]
0
[ "3t5v", "4trq", "5g5p", "5l3t", "5ubp", "7ewf", "7ewm", "8r7j", "8r7k", "8u8c", "8u8d", "8u8e", "9dlp", "9dlr", "9dlv" ]
15
[ "PUB00014954", "PUB00075376", "PUB00075377" ]
[ "12631707", "21149575", "11526238" ]
[ "Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex.", "New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a protein complex involved in transcription elongation.", "Germinal center-associated nuclear protein (GANP) has a phosphorylation-dependent DNA-prim...
[ 2003, 2011, 2001 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 11942 ]
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...
[ 23, 4, 3, 7, 10, 9, 2, 13, 14, 2, 3, 66 ]
12
true
Domain
SAC3/GANP/THP3, conserved domain
SAC3/GANP/THP3, conserved domain
SAC3/GANP/THP3_conserved
5
IPR005063
5,063
Transposase, IS1
Transposase_27
Family
6,618
false
false
Transposase proteins are necessary for efficient DNA transposition. This family represents bacterial IS1 transposases [ ].
[ "GO:0003677", "GO:0004803", "GO:0006313" ]
[ "DNA binding", "transposase activity", "DNA transposition" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF03400" ]
[ "DDE_Tnp_IS1" ]
[ 6618 ]
1
[]
[]
[]
0
[]
0
[ "PUB00034641" ]
[ "17106514" ]
[ "IS1 transposition is enhanced by translation errors and by bacterial growth at extreme glucose levels." ]
[ 2006 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Punavirus", "unclassified sequences" ]
[ 146, 6278, 7, 6, 181 ]
5
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 8, 1 ]
2
true
Family
Transposase, IS1
Transposase, IS1
Transposase_27
3
IPR005064
5,064
Bordetella uptake gene
BUG
Family
79,382
false
false
Bordetella pertussis, the causative agent of human whooping cough (pertussis), is an obligate human pathogen with diverse high-affinity transport systems for the assimilation of iron, a biometal that is essential for growth [ ]. Periplasmic binding proteins of a new family, particularly well represented in this organis...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF03401", "PIRSF017082", "PTHR42928" ]
[ "TctC", "YflP", "" ]
[ 78544, 74758, 79228 ]
3
[]
[]
[]
0
[ "2dvz", "2f5x", "2qpq", "4x9t", "5oei", "5oku", "6hke", "7ndr", "7nds", "8hk9", "8hka", "8hkb" ]
12
[ "PUB00040326", "PUB00040549", "PUB00043632", "PUB00043633" ]
[ "17057341", "16403514", "17724074", "17870093" ]
[ "Structural analysis of Bordetella pertussis BugE solute receptor in a bound conformation.", "Crystal structure of Bordetella pertussis BugD solute receptor unveils the basis of ligand binding in a new family of periplasmic binding proteins.", "Impact of alcaligin siderophore utilization on in vivo growth of Bo...
[ 2006, 2006, 2007, 2007 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 180, 78095, 117, 8, 964, 18 ]
6
[]
[]
0
true
Family
Bordetella uptake gene
Bordetella uptake gene
BUG
8
IPR005066
5,066
Moybdenum cofactor oxidoreductase, dimerisation
MoCF_OxRdtse_dimer
Domain
17,406
false
false
The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes functi...
[ "GO:0016491", "GO:0030151" ]
[ "oxidoreductase activity", "molybdenum ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF03404" ]
[ "Mo-co_dimer" ]
[ 17406 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.7.1", "GenProp1554", "R-DME-1614517", "R-HSA-1614517", "R-MMU-1614517", "R-RNO-1614517" ]
[ "EC:1.7.1", "GP:GenProp1554", "REACTOME:R-DME-1614517", "REACTOME:R-HSA-1614517", "REACTOME:R-MMU-1614517", "REACTOME:R-RNO-1614517" ]
6
[ "1ogp", "1sox", "2a99", "2a9a", "2a9b", "2a9c", "2a9d", "2bih", "2bii", "2blf", "2bpb", "2c9x", "2ca3", "2ca4", "2xts", "3hbg", "3hbp", "3hbq", "3hc2", "3r18", "3r19", "4pw3", "4pw9", "5k3x", "5wa0", "6y0k", "8s5s" ]
27
[ "PUB00007725", "PUB00015635", "PUB00015921", "PUB00034757", "PUB00034758", "PUB00034759" ]
[ "9428520", "12372836", "8528286", "12114025", "17198377", "16784786" ]
[ "Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.", "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli.", "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifuncti...
[ 1997, 2002, 1995, 2002, 2007, 2006 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]
[ 338, 6625, 10323, 2, 118 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 18, 2, 4, 1, 2, 1, 3, 14, 3, 30 ]
10
true
Domain
Moybdenum cofactor oxidoreductase, dimerisation
Moybdenum cofactor oxidoreductase, dimerisation
MoCF_OxRdtse_dimer
1
IPR005068
5,068
Bacteriophage lambda, Tail fiber protein, repeat-2
Phage_lambda_Stf-r2
Repeat
5,305
false
false
This entry represents repeat 2 of Tail fiber protein from Bacteriophage lambda (Stf or gp27) and similar proteins found in the tailed bacteriophages Caudovirales and in bacterial prophages. The repeats are about 40 residues long. The strain of the Bacteriophage lambda used in most laboratories in the early 1990's carri...
[ "GO:0019062", "GO:0046718" ]
[ "virion attachment to host cell", "symbiont entry into host cell" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM" ]
[ "PF03406" ]
[ "Phage_fiber_2" ]
[ 5305 ]
1
[ "GP" ]
[ "GenProp0208" ]
[ "GP:GenProp0208" ]
1
[ "5yvq", "8ju3", "9ki1" ]
3
[ "PUB00007726", "PUB00099967", "PUB00099968", "PUB00099970" ]
[ "7676622", "1439823", "30463036", "6250048" ]
[ "DNA sequence of tail fiber genes of coliphage 186 and evidence for a common ancestor shared by dsDNA phage fiber genes.", "Bacteriophage lambda PaPa: not the mother of all lambda phages.", "The role of side tail fibers during the infection cycle of phage lambda.", "Invertible DNA determines host specificity ...
[ 1995, 1992, 2019, 1980 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "feces metagenome" ]
[ 5121, 13, 169, 2 ]
4
[]
[]
0
true
Repeat
Bacteriophage lambda, Tail fiber protein, repeat-2
Bacteriophage lambda, Tail fiber protein, repeat-2
Phage_lambda_Stf-r2
9
IPR005069
5,069
Nucleotide-diphospho-sugar transferase
Nucl-diP-sugar_transferase
Domain
12,979
false
false
This entry represents a domain found in a group of glycosyltransferases, including Arabidopsis arabinosyltransferase RRA1/2/3/XEG113 [ ], beta-arabinofuranosyltransferase RAY1 [ ] and UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferases [ ]. The biosynthesis of disaccharides, oligosaccharides and polysaccharides invol...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03407" ]
[ "Nucleotid_trans" ]
[ 12979 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.4.2.-", "PWY-5381", "PWY-5800", "PWY-6148", "PWY-6720", "PWY-7018", "PWY-7025", "PWY-7450", "PWY-7817", "PWY-7981" ]
[ "EC:2.4.2.-", "METACYC:PWY-5381", "METACYC:PWY-5800", "METACYC:PWY-6148", "METACYC:PWY-6720", "METACYC:PWY-7018", "METACYC:PWY-7025", "METACYC:PWY-7450", "METACYC:PWY-7817", "METACYC:PWY-7981" ]
10
[]
0
[ "PUB00009409", "PUB00076686", "PUB00076687", "PUB00076688" ]
[ "9334165", "17056709", "23396039", "24619997" ]
[ "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities.", "Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II.", "Arabinosylation of a Yariv-precipitable c...
[ 1997, 2006, 2013, 2014 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 4, 388, 12504, 10, 73 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 100, 14, 1, 56, 89 ]
5
true
Domain
Nucleotide-diphospho-sugar transferase
Nucleotide-diphospho-sugar transferase
Nucl-diP-sugar_transferase
2
IPR005070
5,070
Foamy virus envelope protein
Foamy_env
Family
354
false
false
Expression of the envelope (Env) glycoprotein is essential for viral particle egress. This feature is unique to the Spumavirinae, a subclass of the Retroviridae.
[ "GO:0019031" ]
[ "viral envelope" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF03408" ]
[ "Foamy_virus_ENV" ]
[ 354 ]
1
[]
[]
[]
0
[ "8aez", "8aic", "8ozh", "8ozj", "8ozp", "8ozq", "8rm0", "8rm1" ]
8
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Pleurodeles waltl", "Retroviridae" ]
[ 18, 336 ]
2
[]
[]
0
true
Family
Foamy virus envelope protein
Foamy virus envelope protein
Foamy_env
6
IPR005071
5,071
Transmembrane glycoprotein
Glycoprotein
Family
280
false
false
This family of proteins has some GO annotations for positive regulation of growth rate and nematode larval development. This is probably a family of membrane glycoproteins [ ].
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF03409", "PTHR21733" ]
[ "Glycoprotein", "" ]
[ 279, 270 ]
2
[]
[]
[]
0
[]
0
[ "PUB00061891" ]
[ "17761667" ]
[ "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." ]
[ 2007 ]
1
[]
[]
0
0
null
[ "Rhabditomorpha" ]
[ 280 ]
1
[ "Caenorhabditis elegans" ]
[ 25 ]
1
true
Family
Transmembrane glycoprotein
Transmembrane glycoprotein
Glycoprotein
6
IPR005072
5,072
Peptidase M44, metalloendopeptidase G1
Peptidase_M44
Family
181
false
false
This entry includes metallopeptidases from poxvirus that belong to MEROPS peptidase family M44 (clan ME). The active site residues for members of this family occur in the motif HXXEH. This protein family inlcudes Metalloendopeptidase G1 from Vaccinia virus, also known as Metalloendopeptidase OPG085, which appears to pl...
[ "GO:0004222", "GO:0008270", "GO:0019058" ]
[ "metalloendopeptidase activity", "zinc ion binding", "viral life cycle" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PIRSF" ]
[ "PF03410", "PIRSF015679" ]
[ "Peptidase_M44", "Peptidase_M44" ]
[ 179, 152 ]
2
[ "EC", "METACYC" ]
[ "3.4.24.-", "PWY-8119" ]
[ "EC:3.4.24.-", "METACYC:PWY-8119" ]
2
[]
0
[ "PUB00103578", "PUB00103579" ]
[ "15194761", "15331728" ]
[ "Vaccinia virus G1 protein, a predicted metalloprotease, is essential for morphogenesis of infectious virions but not for cleavage of major core proteins.", "The vaccinia virus G1L putative metalloproteinase is essential for viral replication in vivo." ]
[ 2004, 2004 ]
2
[]
[]
0
0
null
[ "Poxviridae" ]
[ 181 ]
1
[]
[]
0
true
Family
Peptidase M44, metalloendopeptidase G1
Peptidase M44, metalloendopeptidase G1
Peptidase_M44
3
IPR005073
5,073
Peptidase M74, penicillin-insensitive murein endopeptidase
Peptidase_M74
Family
4,529
false
false
This group of peptidases belong to MEROPS peptidase family M74 (murein endopeptidase family, clan MD). The type example is murein endopeptidase from Escherichia coli (MepA). The entry represents a family of penicillin-insensitive murein endopeptidases involved in the removal of murein from the sacculus by cleaving the ...
[ "GO:0004252", "GO:0006508", "GO:0030288" ]
[ "serine-type endopeptidase activity", "proteolysis", "outer membrane-bounded periplasmic space" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "NCBIFAM", "PFAM", "PIRSF" ]
[ "MF_01623", "NF006947", "PF03411", "PIRSF018455" ]
[ "MepA", "PRK09429.1", "Peptidase_M74", "MepA" ]
[ 997, 3802, 4529, 3637 ]
4
[ "EC", "METACYC" ]
[ "3.4.24.-", "PWY-8119" ]
[ "EC:3.4.24.-", "METACYC:PWY-8119" ]
2
[ "1tzp", "1u10" ]
2
[ "PUB00016068", "PUB00033901" ]
[ "2187143", "15292190" ]
[ "Cloning and characterization of mepA, the structural gene of the penicillin-insensitive murein endopeptidase from Escherichia coli.", "Peptidoglycan amidase MepA is a LAS metallopeptidase." ]
[ 1990, 2004 ]
2
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 4502, 4, 23 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Peptidase M74, penicillin-insensitive murein endopeptidase
Peptidase M74, penicillin-insensitive murein endopeptidase
Peptidase_M74
8
IPR005074
5,074
Peptidase C39, bacteriocin processing
Peptidase_C39
Domain
25,818
false
false
This group of sequences defined by this cysteine peptidase domain belong to the MEROPS peptidase family C39 (clan CA). It is found in a wide range of ABC transporters, which are maturation proteases for peptide bacteriocins, the proteolytic domain residing in the N-terminal region of the protein [ ]. A number of the pr...
[ "GO:0005524", "GO:0008233", "GO:0006508", "GO:0016020" ]
[ "ATP binding", "peptidase activity", "proteolysis", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PROFILE" ]
[ "PF03412", "PS50990" ]
[ "Peptidase_C39", "PEPTIDASE_C39" ]
[ 20222, 24471 ]
2
[ "GP", "PROSITEDOC", "REACTOME" ]
[ "GenProp1090", "PDOC50990", "R-HSA-9760173" ]
[ "GP:GenProp1090", "PROSITEDOC:PDOC50990", "REACTOME:R-HSA-9760173" ]
3
[ "3b79", "3k8u", "3zua", "4ry2", "4s0f", "5xe8", "5xe9", "6mpz", "6v9z", "7n87", "7s5j", "7sgr", "7t54", "7t55", "7t56", "7t57", "8dck", "8hf4", "8hf5", "8hf6", "8hf7", "8k4b", "8k7a", "8ssk", "8ssm", "8vp3", "8vp5", "8vp6", "8vp8", "8vp9", "8vpa", "8vpb"...
37
[ "PUB00003579", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953" ]
[ "7674922", "11517925", "9891971", "14725770", "7044372" ]
[ "Evolutionary families of metallopeptidases.", "Evolutionary lines of cysteine peptidases.", "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.", "The structure of sortase B, a cysteine transpeptidase that tethers surface p...
[ 1995, 2001, 1998, 2004, 1982 ]
5
[]
[ "IPR033838", "IPR033839", "IPR039395" ]
0
3
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "Plasmid pAD1", "unclassified sequences" ]
[ 88, 25554, 2, 26, 1, 147 ]
6
[]
[]
0
true
Domain
Peptidase C39, bacteriocin processing
Peptidase C39, bacteriocin processing
Peptidase_C39
8
IPR005076
5,076
Glycosyl transferase, family 6
Glyco_trans_6
Family
5,051
false
false
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas...
[ "GO:0016758", "GO:0005975", "GO:0016020" ]
[ "hexosyltransferase activity", "carbohydrate metabolic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF03414", "PTHR10462" ]
[ "Glyco_transf_6", "" ]
[ 5051, 4990 ]
2
[ "CAZY", "EC", "GP", "REACTOME", "REACTOME", "REACTOME" ]
[ "GT6", "2.4.1", "GenProp1304", "R-HSA-9033807", "R-MMU-9033807", "R-RNO-9033807" ]
[ "CAZY:GT6", "EC:2.4.1", "GP:GenProp1304", "REACTOME:R-HSA-9033807", "REACTOME:R-MMU-9033807", "REACTOME:R-RNO-9033807" ]
6
[ "1fg5", "1g8o", "1g93", "1gwv", "1gww", "1gx0", "1gx4", "1k4v", "1lz0", "1lz7", "1lzi", "1lzj", "1o7o", "1o7q", "1r7t", "1r7u", "1r7v", "1r7x", "1r7y", "1r80", "1r81", "1r82", "1vzt", "1vzu", "1vzx", "1wsz", "1wt0", "1wt1", "1wt2", "1wt3", "1xz6", "1zhj"...
184
[ "PUB00009409" ]
[ "9334165" ]
[ "A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities." ]
[ 1997 ]
1
[]
[ "IPR048174" ]
0
1
0
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 160, 4865, 16, 10 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 26, 370, 14, 40 ]
4
true
Family
Glycosyl transferase, family 6
Glycosyl transferase, family 6
Glyco_trans_6
4
IPR005078
5,078
Peptidase C54
Peptidase_C54
Family
10,724
false
false
This is a group of cysteine peptidases which constitute MEROPS peptidase family C54 (Aut2 peptidase family, clan CA). Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. ...
[ "GO:0008234" ]
[ "cysteine-type peptidase activity" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR22624" ]
[ "" ]
[ 10724 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.22.-", "R-BTA-1632852", "R-CEL-1632852", "R-CFA-1632852", "R-DDI-1632852", "R-DRE-1632852", "R-GGA-1632852", "R-HSA-1632852", "R-MMU-1632852", "R-RNO-1632852", "R-SSC-1632852" ]
[ "EC:3.4.22.-", "REACTOME:R-BTA-1632852", "REACTOME:R-CEL-1632852", "REACTOME:R-CFA-1632852", "REACTOME:R-DDI-1632852", "REACTOME:R-DRE-1632852", "REACTOME:R-GGA-1632852", "REACTOME:R-HSA-1632852", "REACTOME:R-MMU-1632852", "REACTOME:R-RNO-1632852", "REACTOME:R-SSC-1632852" ]
11
[ "2cy7", "2d1i", "2p82", "2z0d", "2z0e", "2zzp" ]
6
[ "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953" ]
[ "11517925", "9891971", "14725770", "7044372" ]
[ "Evolutionary lines of cysteine peptidases.", "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.", "The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.", ...
[ 2001, 1998, 2004, 1982 ]
4
[]
[]
0
0
null
[ "Bodo saltans virus", "Eukaryota", "bird metagenome" ]
[ 1, 10722, 1 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 14, 2, 20, 4, 35, 16, 1, 3, 22, 1, 1, 26 ]
12
true
Family
Peptidase C54
Peptidase C54
Peptidase_C54
3
IPR005079
5,079
Peptidase C45, hydrolase domain
Peptidase_C45_hydrolase
Domain
9,847
false
false
The peptidase C45 family includes the characterised protein acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferases from fungi and TAN from Drosophila. The active site residue for members of this family and family T1 is C-terminal to the autolytic cleavage site. In Penicillium chrysogenum, A:6-aminopenicillanic-acid-...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03417" ]
[ "AAT" ]
[ 9847 ]
1
[ "EC", "METACYC" ]
[ "2.3.1.164", "PWY-5630" ]
[ "EC:2.3.1.164", "METACYC:PWY-5630" ]
2
[ "2x1c", "2x1d", "2x1e", "3gvz" ]
4
[ "PUB00011704", "PUB00020025", "PUB00030423", "PUB00054422", "PUB00070795", "PUB00076953" ]
[ "11517925", "9891971", "14725770", "20223213", "2110531", "7044372" ]
[ "Evolutionary lines of cysteine peptidases.", "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.", "The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.", ...
[ 2001, 1998, 2004, 2010, 1990, 1982 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Klosneuvirinae", "unclassified sequences" ]
[ 110, 6878, 2744, 2, 113 ]
5
[ "Drosophila melanogaster", "Homo sapiens", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 2, 1, 3, 3 ]
4
true
Domain
Peptidase C45, hydrolase domain
Peptidase C45, hydrolase domain
Peptidase_C45_hydrolase
5
IPR005080
5,080
Peptidase A25, germination protease
Peptidase_A25
Family
2,763
false
false
This group of peptidases belong to MEROPS peptidase family A25 (GPR peptidase family, clan AE). During the germination of bacterial spores, the GPR peptidase initiates the degradation of the small acid-soluble proteins that make up 10-20% of the spore content [ ]. The peptidase prefers an acidic residue in P1' and P4' ...
[ "GO:0008233", "GO:0006508", "GO:0009847" ]
[ "peptidase activity", "proteolysis", "spore germination" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "HAMAP", "PFAM", "PIRSF", "NCBIFAM" ]
[ "MF_00626", "PF03418", "PIRSF019549", "TIGR01441" ]
[ "Germination_prot", "Peptidase_A25", "Peptidase_A25", "GPR" ]
[ 2653, 2763, 2425, 2748 ]
4
[ "EC", "GP" ]
[ "3.4.24.78", "GenProp0610" ]
[ "EC:3.4.24.78", "GP:GenProp0610" ]
2
[ "1c8b", "7c4x" ]
2
[ "PUB00000093", "PUB00000113", "PUB00000349", "PUB00000522", "PUB00001330", "PUB00011023", "PUB00011707", "PUB00021296", "PUB00042504", "PUB00065205", "PUB00066803", "PUB00076784", "PUB00076785", "PUB00076786", "PUB00076868", "PUB00076869", "PUB00076870" ]
[ "2194475", "3059997", "1851433", "8439290", "6795036", "10331925", "11566868", "10864493", "2682266", "23254940", "21765428", "4912600", "10497172", "21751400", "16199582", "6801023", "11847292" ]
[ "The structure and function of the aspartic proteinases.", "Small, acid-soluble spore proteins of Bacillus species: structure, synthesis, genetics, function, and degradation.", "Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.", "Evolutionary families of peptid...
[ 1990, 1988, 1991, 1993, 1981, 1999, 2001, 2000, 1989, 2013, 2011, 1970, 1999, 2011, 2005, 1982, 2002 ]
17
[]
[]
0
0
null
[ "Bacteria", "Methanosarcina mazei", "Phytophthora kernoviae 00238/432", "metagenomes" ]
[ 2739, 1, 1, 22 ]
4
[]
[]
0
true
Family
Peptidase A25, germination protease
Peptidase A25, germination protease
Peptidase_A25
1
IPR005081
5,081
Sigma-E processing peptidase SpoIIGA
SpoIIGA
Family
2,784
false
false
Sporulation in bacteria such as Bacillus subtilis involves the formation of a polar septum, which divides the sporangium into a mother cell and a forespore. The sigma E factor, which is encoded within the spoIIG operon, is a cell-specific regulatory protein that directs gene transcription in the mother cell. Sigma E is...
[ "GO:0004190", "GO:0006508", "GO:0030436" ]
[ "aspartic-type endopeptidase activity", "proteolysis", "asexual sporulation" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PIRSF", "NCBIFAM" ]
[ "PF03419", "PIRSF018571", "TIGR02854" ]
[ "Peptidase_U4", "SpoIIGA", "spore_II_GA" ]
[ 2784, 2031, 1550 ]
3
[ "EC", "GP" ]
[ "3.4.23.-", "GenProp0610" ]
[ "EC:3.4.23.-", "GP:GenProp0610" ]
2
[]
0
[ "PUB00011862", "PUB00076890", "PUB00076893" ]
[ "11849534", "18378688", "3125985" ]
[ "An investigation into the compartmentalization of the sporulation transcription factor sigmaE in Bacillus subtilis.", "Evidence that the Bacillus subtilis SpoIIGA protein is a novel type of signal-transducing aspartic protease.", "Processing of a sporulation sigma factor in Bacillus subtilis: how morphological...
[ 2002, 2008, 1988 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 2764, 2, 18 ]
3
[]
[]
0
true
Family
Sigma-E processing peptidase SpoIIGA
Sigma-E processing peptidase SpoIIGA
SpoIIGA
6
IPR005082
5,082
Prohead core protein protease
Prohead_core_protease
Family
806
false
false
This group of peptidases belongs to MEROPS peptidase family U9 (phage prohead processing peptidase family, clan U-), which play a role in the head assembly of Bacteriophage T4, this includes Prohead core protein protease from Enterobacteria phage T4. This entry also includes eukaryotic and bacterial proteins. The pepti...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03420" ]
[ "Peptidase_S77" ]
[ 806 ]
1
[ "GP" ]
[ "GenProp0208" ]
[ "GP:GenProp0208" ]
1
[ "5jbl" ]
1
[ "PUB00043277" ]
[ "3552886" ]
[ "The nucleotide sequence of gene 21 of bacteriophage T4 coding for the prohead protease." ]
[ 1986 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 3, 28, 42, 673, 60 ]
5
[]
[]
0
true
Family
Prohead core protein protease
Prohead core protein protease
Prohead_core_protease
3
IPR005083
5,083
Serine/Threonine acetyltransferase YopJ-like
YopJ-like
Family
1,112
false
false
The infection of mammalian host cells by Yersinia sp. causes a rapid induction of the mitogen-activated protein kinase (MAPK; including the ERK, JNK and p38 pathways) and nuclear factor kappaB (NF-kappaB) signalling pathways that would typically result in cytokine production and initiation of the innate immune response...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03421" ]
[ "Acetyltransf_14" ]
[ 1112 ]
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"...
[ "2.3.1.-", "PWY-3602", "PWY-361", "PWY-4801", "PWY-4922", "PWY-5048", "PWY-5139", "PWY-5268", "PWY-5284", "PWY-5292", "PWY-5307", "PWY-5313", "PWY-5317", "PWY-5318", "PWY-5353", "PWY-5400", "PWY-5473", "PWY-5475", "PWY-5477", "PWY-5660", "PWY-5679", "PWY-5710", "PWY-5794"...
[ "EC:2.3.1.-", "METACYC:PWY-3602", "METACYC:PWY-361", "METACYC:PWY-4801", "METACYC:PWY-4922", "METACYC:PWY-5048", "METACYC:PWY-5139", "METACYC:PWY-5268", "METACYC:PWY-5284", "METACYC:PWY-5292", "METACYC:PWY-5307", "METACYC:PWY-5313", "METACYC:PWY-5317", "METACYC:PWY-5318", "METACYC:PWY-53...
219
[ "5klp", "5klq", "5w3t", "5w3x", "5w3y", "5w40", "6be0", "7f3n" ]
8
[ "PUB00011704", "PUB00020025", "PUB00030423", "PUB00035762", "PUB00035763", "PUB00055964", "PUB00076953", "PUB00095605" ]
[ "11517925", "9891971", "14725770", "17412595", "17116858", "20430892", "7044372", "26810037" ]
[ "Evolutionary lines of cysteine peptidases.", "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.", "The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.", ...
[ 2001, 1998, 2004, 2007, 2006, 2010, 1982, 2016 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "viral metagenome" ]
[ 1097, 9, 6 ]
3
[]
[]
0
true
Family
Serine/Threonine acetyltransferase YopJ-like
Serine/Threonine acetyltransferase YopJ-like
YopJ-like
7
IPR005084
5,084
Carbohydrate binding module family 6
CBM6
Domain
25,300
false
false
This entry represents which was previously known as cellulose-binding domain family VI (CBD VI). CBM6 bind to amorphous cellulose, xylan, mixed beta-(1,3)(1,4)glucan and beta-1,3-glucan [ , , ]. CBM6 adopts a classic lectin-like β-jelly roll fold, predominantly consisting of five antiparallel β-strands on one face and ...
[ "GO:0030246" ]
[ "carbohydrate binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PROFILE" ]
[ "PF03422", "PF16990", "PS51175" ]
[ "CBM_6", "CBM_35", "CBM6" ]
[ 17097, 3940, 23309 ]
3
[ "EC", "PROSITEDOC" ]
[ "3.2.1", "PDOC51175" ]
[ "EC:3.2.1", "PROSITEDOC:PDOC51175" ]
2
[ "1gmm", "1nae", "1o8p", "1o8s", "1od3", "1ux7", "1uxx", "1uxz", "1uy0", "1uy1", "1uy2", "1uy3", "1uy4", "1uyx", "1uyy", "1uyz", "1uz0", "1w0n", "1w9s", "1w9t", "1w9w", "2bgo", "2bgp", "2cdo", "2cdp", "2dcj", "2dck", "2v4v", "2vzo", "2vzp", "2vzq", "2vzr"...
99
[ "PUB00031940", "PUB00032219", "PUB00033743", "PUB00033744", "PUB00054922", "PUB00054923", "PUB00054924" ]
[ "15010454", "15501830", "15004011", "11673472", "3338453", "3134347", "15214846" ]
[ "The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities.", "Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by ...
[ 2004, 2005, 2004, 2001, 1988, 1988, 2004 ]
7
[]
[ "IPR006584", "IPR041342" ]
0
2
0
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "unclassified sequences" ]
[ 23680, 1273, 267, 80 ]
4
[ "Arabidopsis thaliana" ]
[ 1 ]
1
true
Domain
Carbohydrate binding module family 6
Carbohydrate binding module family 6
CBM6
8
IPR005085
5,085
Carbohydrate binding module family 25
CBM25
Domain
2,682
false
false
This entry represents , which has been shown to bind starch [ ]. A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare insta...
[ "GO:2001070" ]
[ "starch binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "SMART" ]
[ "PF03423", "PF16760", "SM01066" ]
[ "CBM_25", "CBM53", "CBM_25" ]
[ 1022, 1391, 2650 ]
3
[]
[]
[]
0
[ "2c3v", "2c3w", "2c3x", "2laa", "2lab" ]
5
[ "PUB00039874", "PUB00054922", "PUB00054923", "PUB00054924" ]
[ "16230347", "3338453", "3134347", "15214846" ]
[ "A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.", "Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.", ...
[ 2006, 1988, 1988, 2004 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Thermococcus", "ecological metagenomes" ]
[ 1369, 1299, 5, 9 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 6, 9, 32 ]
3
true
Domain
Carbohydrate binding module family 25
Carbohydrate binding module family 25
CBM25
9
IPR005086
5,086
Carbohydrate binding module family 17/28
CBM17/28
Domain
99
false
false
A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existi...
[ "GO:0008810", "GO:0030245" ]
[ "cellulase activity", "cellulose catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03424" ]
[ "CBM_17_28" ]
[ 99 ]
1
[ "EC", "METACYC" ]
[ "3.2.1.4", "PWY-6788" ]
[ "EC:3.2.1.4", "METACYC:PWY-6788" ]
2
[ "1j83", "1j84", "1uww", "3acf", "3acg", "3ach", "3aci", "5ecu" ]
8
[ "PUB00026290", "PUB00037901", "PUB00054922", "PUB00054923", "PUB00054924" ]
[ "11733998", "15136030", "3338453", "3134347", "15214846" ]
[ "Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study.", "X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28.", "Studies of the cellulolytic system of Trichoderma reesei QM 9...
[ 2001, 2004, 1988, 1988, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria" ]
[ 99 ]
1
[]
[]
0
true
Domain
Carbohydrate binding module family 17/28
Carbohydrate binding module family 17/28
CBM17/28
8
IPR005087
5,087
Carbohydrate binding module family 11
CBM11
Domain
903
false
false
This entry represents , which binds both beta-1,4-glucan and beta-1,3-1,4-mixed linked glucans. A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaf...
[ "GO:0008810", "GO:0030245" ]
[ "cellulase activity", "cellulose catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03425" ]
[ "CBM_11" ]
[ 903 ]
1
[]
[]
[]
0
[ "1v0a", "2lro", "2lrp", "6r31", "6r3m" ]
5
[ "PUB00054922", "PUB00054923", "PUB00054924" ]
[ "3338453", "3134347", "15214846" ]
[ "Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.", "Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis.", "Carbohydrate-bindin...
[ 1988, 1988, 2004 ]
3
[]
[]
0
0
null
[ "Bacteria", "Methanosarcinales", "metagenomes" ]
[ 890, 2, 11 ]
3
[]
[]
0
true
Domain
Carbohydrate binding module family 11
Carbohydrate binding module family 11
CBM11
6
IPR005088
5,088
Carbohydrate binding module family 15
CBM15
Domain
16
false
false
This entry represents which binds to xylan and xylooligosaccharides [ ]. A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and ra...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF03426", "PS51759" ]
[ "CBM_15", "CBM15" ]
[ 16, 12 ]
2
[]
[]
[]
0
[ "1gny", "1us2", "1us3" ]
3
[ "PUB00021702", "PUB00054922", "PUB00054923", "PUB00054924" ]
[ "11598143", "3338453", "3134347", "15214846" ]
[ "Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation.", "Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.", "Preci...
[ 2001, 1988, 1988, 2004 ]
4
[]
[]
0
0
null
[ "Pseudomonadota" ]
[ 16 ]
1
[]
[]
0
true
Domain
Carbohydrate binding module family 15
Carbohydrate binding module family 15
CBM15
6
IPR005090
5,090
Plasmid replication protein C, N-terminal
RepC_N
Domain
3,621
false
false
Proteins in this group have homology with the RepC protein of Agrobacterium Ri and Ti plasmids [ ]. repABC plasmids are widely distributed among alphaproteobacteria; all repABC operons contain at least three protein-encoding genes: repA, repB and repC. The first two genes encode proteins involved in plasmid segregation...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03428" ]
[ "RP-C" ]
[ 3621 ]
1
[ "GP" ]
[ "GenProp0487" ]
[ "GP:GenProp0487" ]
1
[]
0
[ "PUB00007727", "PUB00043441", "PUB00106104" ]
[ "7991675", "18433868", "3462754" ]
[ "The large nonsymbiotic plasmid pRmeGR4a of Rhizobium meliloti GR4 encodes a protein involved in replication that has homology with the RepC protein of Agrobacterium plasmids.", "The repABC plasmid family.", "RepC is rate limiting for pT181 plasmid replication." ]
[ 1994, 2008, 1986 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Plasmid pTiB6S3", "metagenomes", "unclassified Caudoviricetes" ]
[ 3584, 8, 1, 26, 2 ]
5
[]
[]
0
true
Domain
Plasmid replication protein C, N-terminal
Plasmid replication protein C, N-terminal
RepC_N
5
IPR005091
5,091
Major surface protein 1B
MSP1b
Family
60
false
false
The major surface protein (MSP1) of the cattle pathogen Anaplasma is a heterodimer comprised of MSP1a and MSP1b. This family is the MSP1b chain. The MSP1 proteins are putative adhesins for bovine erythrocytes [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03429" ]
[ "MSP1b" ]
[ 60 ]
1
[]
[]
[]
0
[]
0
[ "PUB00019886" ]
[ "11239934" ]
[ "Differential adhesion of major surface proteins 1a and 1b of the ehrlichial cattle pathogen Anaplasma marginale to bovine erythrocytes and tick cells." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Bacteria", "Hevea brasiliensis" ]
[ 56, 4 ]
2
[]
[]
0
true
Family
Major surface protein 1B
Major surface protein 1B
MSP1b
7
IPR005092
5,092
Trans-activating transcriptional regulator
TATR
Family
148
false
false
This family of trans-activating transcriptional regulators (TATR), also known as intermediate early protein 1, are common to the Nucleopolyhedroviruses [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03430" ]
[ "TATR" ]
[ 148 ]
1
[]
[]
[]
0
[]
0
[ "PUB00020408" ]
[ "7815565" ]
[ "The roles of eighteen baculovirus late expression factor genes in transcription and DNA replication." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Baculoviridae" ]
[ 148 ]
1
[]
[]
0
true
Family
Trans-activating transcriptional regulator
Trans-activating transcriptional regulator
TATR
3
IPR005093
5,093
RNA-directed RNA polymerase beta-chain
RNArep_beta
Family
2,415
false
false
RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw...
[ "GO:0003968", "GO:0039694" ]
[ "RNA-directed RNA polymerase activity", "viral RNA genome replication" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03431" ]
[ "RNA_replicase_B" ]
[ 2415 ]
1
[ "EC" ]
[ "2.7.7.48" ]
[ "EC:2.7.7.48" ]
1
[ "3agp", "3agq", "3avt", "3avu", "3avv", "3avw", "3avx", "3avy", "3mmp", "3vnu", "3vnv", "4fwt", "4q7j", "4r71" ]
14
[ "PUB00009392", "PUB00030617", "PUB00033622", "PUB00033623", "PUB00033624", "PUB00033625" ]
[ "9878607", "9309225", "2759231", "8709232", "11531403", "10827187" ]
[ "Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.", "Structure of the RNA-dependent RNA polymerase of poliovirus.", "Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat...
[ 1998, 1997, 1989, 1996, 2001, 2000 ]
6
[]
[]
0
0
null
[ "Viridiplantae", "Viruses" ]
[ 2, 2413 ]
2
[]
[]
0
true
Family
RNA-directed RNA polymerase beta-chain
RNA-directed RNA polymerase beta-chain
RNArep_beta
9
IPR005094
5,094
MobA/VirD2-like, nuclease domain
Endonuclease_MobA/VirD2
Domain
21,565
false
false
Relaxases/mobilisation proteins are required for the horizontal transfer of genetic information contained on plasmids that occurs during bacterial conjugation. The relaxase, in conjunction with several auxiliary proteins, forms the relaxation complex or relaxosome. Relaxases nick duplex DNA in a specific manner by cata...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03432" ]
[ "Relaxase" ]
[ 21565 ]
1
[]
[]
[]
0
[]
0
[ "PUB00007728", "PUB00082596" ]
[ "9350859", "8265585" ]
[ "Nicking by transesterification: the reaction catalysed by a relaxase.", "Site-specific cleavage and joining of single-stranded DNA by VirD2 protein of Agrobacterium tumefaciens Ti plasmids: analogy to bacterial conjugation." ]
[ 1997, 1993 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "plasmids", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 21181, 29, 36, 12, 306, 1 ]
6
[]
[]
0
true
Domain
MobA/VirD2-like, nuclease domain
MobA/VirD2-like, nuclease domain
Endonuclease_MobA/VirD2
1
IPR005095
5,095
EspA-like secreted protein
EspA
Family
894
false
false
EspA, together with EspB, EspD and Tir are exported by a type III secretion system. These proteins are essential for attaching and effacing lesion formation. EspA is a structural protein and a major component of a large, transiently expressed, filamentous surface organelle which forms a direct link between the bacteriu...
[]
[]
[]
0
[ "NCBIFAM", "PFAM" ]
[ "NF011891", "PF03433" ]
[ "PRK15364.1", "EspA" ]
[ 514, 894 ]
2
[]
[]
[]
0
[ "1xou", "7k7k", "7khw" ]
3
[ "PUB00007729", "PUB00007730" ]
[ "9545230", "10760148" ]
[ "A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells.", "The type III protein translocation system of enteropathogenic Escherichia coli involves EspA-EspB protein interactions." ]
[ 1998, 2000 ]
2
[]
[]
0
0
null
[ "Bracon brevicornis", "Pseudomonadati" ]
[ 1, 893 ]
2
[]
[]
0
true
Family
EspA-like secreted protein
EspA-like secreted protein
EspA
6
IPR005096
5,096
Protein of unknown function DUF276
DUF276
Family
183
false
false
This family is specific to Borrelia burgdorferi (Lyme disease spirochete). The protein is encoded on extrachromosomal DNA and is of unknown function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03434" ]
[ "DUF276" ]
[ 183 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria" ]
[ 183 ]
1
[]
[]
0
true
Family
Protein of unknown function DUF276
Protein of unknown function DUF276
DUF276
6
IPR005097
5,097
Saccharopine dehydrogenase, NADP binding domain
Sacchrp_dh_NADP-bd
Domain
37,166
false
false
This entry represents the NADP binding domain of saccharopine dehydrogenase. In some organisms, this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase [ , ]. Saccharopine dehydrogenase ( ) catalyses the condens...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03435" ]
[ "Sacchrp_dh_NADP" ]
[ 37166 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1487", "R-BTA-71064", "R-CEL-114608", "R-HSA-114608", "R-HSA-71064", "R-MMU-114608", "R-MMU-71064", "R-RNO-114608", "R-RNO-71064", "R-SCE-71064", "R-SPO-71064" ]
[ "GP:GenProp1487", "REACTOME:R-BTA-71064", "REACTOME:R-CEL-114608", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-71064", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-71064", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-71064", "REACTOME:R-SCE-71064", "REACTOME:R-SPO-71064" ]
11
[ "1e5l", "1e5q", "1ff9", "2axq", "2ph5", "3abi", "3ic5", "4ina", "4plp", "4rl6", "4tvb", "4xq9", "4xqc", "4xqe", "4xqg", "4xr4", "4xrg", "5l76", "5l78", "5o1n", "5o1o", "5o1p", "6s3x", "6s49", "6s4d", "6s65", "6s6g", "6s72", "6sep", "6y87", "8deb", "8h4z"...
34
[ "PUB00012373", "PUB00019119", "PUB00020296", "PUB00053404", "PUB00057880", "PUB00057887" ]
[ "8841401", "11354603", "11080625", "19449898", "19196710", "20194510" ]
[ "Purification, molecular cloning and expression in Escherichia coli of homospermidine synthase from Rhodopseudomonas viridis.", "Lysine metabolism in higher plants.", "Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.", "Ch...
[ 1996, 2001, 2000, 2009, 2009, 2010 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 542, 23498, 12632, 13, 481 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 13, 4, 19, 4, 14, 7, 2, 11, 13, 1, 1, 32 ]
12
true
Domain
Saccharopine dehydrogenase, NADP binding domain
Saccharopine dehydrogenase, NADP binding domain
Sacchrp_dh_NADP-bd
6
IPR005098
5,098
Domain of unknown function DUF281
DUF281
Domain
173
false
false
This domain is found in a number of worm proteins and has no known function. The boundaries of the presumed domain are rather uncertain.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03436" ]
[ "DUF281" ]
[ 173 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Caenorhabditis" ]
[ 173 ]
1
[ "Caenorhabditis elegans" ]
[ 15 ]
1
true
Domain
Domain of unknown function DUF281
Domain of unknown function DUF281
DUF281
4
IPR005100
5,100
NGN domain
NGN-domain
Domain
7,193
false
false
Spt5p and prokaryotic NusG are shown to contain a novel 'NGN' domain. The combined NGN and KOW motif regions of Spt5 form the binding domain with Spt4 [ ]. Spt5 complexes with Spt4 as a 1:1 heterodimer snf this Spt5-Spt4 complex regulates early transcription elongation by RNA polymerase II and has an imputed role in pr...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03439" ]
[ "Spt5-NGN" ]
[ 7193 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-112382", "R-CEL-113418", "R-CEL-674695", "R-CEL-6796648", "R-CEL-72086", "R-CEL-75955", "R-CEL-77075", "R-DME-112382", "R-DME-113418", "R-DME-674695", "R-DME-6796648", "R-DME-6807505", "R-DME-72086", "R-DME-75955", "R-DME-77075", "R-DRE-674695", "R-DRE-6796648", "R-DRE-72086...
[ "REACTOME:R-CEL-112382", "REACTOME:R-CEL-113418", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-6796648", "REACTOME:R-CEL-72086", "REACTOME:R-CEL-75955", "REACTOME:R-CEL-77075", "REACTOME:R-DME-112382", "REACTOME:R-DME-113418", "REACTOME:R-DME-674695", "REACTOME:R-DME-6796648", "REACTOME:R-DME-6807...
55
[ "2exu", "3ewg", "3h7h", "3lpe", "3p8b", "3qqc", "4zn1", "4zn3", "5oik", "5xon", "6gmh", "6gml", "6ir9", "6j4w", "6j4x", "6j4y", "6j4z", "6j50", "6j51", "6ted", "7nkx", "7nky", "7okx", "7oky", "7ol0", "7pks", "7unc", "7und", "7wbv", "7wbw", "7wbx", "7xn7"...
84
[ "PUB00009700", "PUB00053692" ]
[ "12202748", "19460865" ]
[ "Novel domains and orthologues of eukaryotic transcription elongation factors.", "Characterization of the Schizosaccharomyces pombe Spt5-Spt4 complex." ]
[ 2002, 2009 ]
2
[]
[ "IPR039385" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 931, 4, 6224, 34 ]
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...
[ 14, 1, 5, 1, 4, 2, 1, 7, 5, 1, 1, 49 ]
12
true
Domain
NGN domain
NGN domain
NGN-domain
6
IPR005101
5,101
Cryptochrome/DNA photolyase, FAD-binding domain
Cryptochr/Photolyase_FAD-bd
Domain
37,063
false
false
This entry represents a multi-helical domain found in the C terminus of the cryptochrome proteins and DNA photolyases. It acts as a FAD-binding domain [ ]. The cryptochrome and photolyase families consist of structurally related flavin adenine dinucleotide (FAD) proteins that use the absorption of blue light to accompl...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03441" ]
[ "FAD_binding_7" ]
[ 37063 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-432395", "R-DME-432553", "R-DME-538864", "R-HSA-9931510", "R-HSA-9931521", "R-HSA-9931530", "R-HSA-9932298" ]
[ "REACTOME:R-DME-432395", "REACTOME:R-DME-432553", "REACTOME:R-DME-538864", "REACTOME:R-HSA-9931510", "REACTOME:R-HSA-9931521", "REACTOME:R-HSA-9931530", "REACTOME:R-HSA-9932298" ]
7
[ "1dnp", "1iqr", "1iqu", "1np7", "1owl", "1owm", "1own", "1owo", "1owp", "1qnf", "1tez", "1u3c", "1u3d", "2e0i", "2ijg", "2j07", "2j08", "2j09", "2j4d", "2vtb", "2wb2", "2wq6", "2wq7", "3cvu", "3cvv", "3cvw", "3cvx", "3cvy", "3fy4", "4ct0", "4gu5", "4i6e"...
112
[ "PUB00024259", "PUB00029173", "PUB00029622", "PUB00076729", "PUB00076730", "PUB00163260" ]
[ "7604260", "12535521", "15213381", "25910181", "26352435", "36441642" ]
[ "Crystal structure of DNA photolyase from Escherichia coli.", "Identification of a new cryptochrome class. Structure, function, and evolution.", "DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction.", "Binding of Substrate Locks the Electrochemistry...
[ 1995, 2003, 2004, 2015, 2015, 2023 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Nucleocytoviricota", "unclassified sequences" ]
[ 741, 20734, 15113, 37, 438 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...
[ 32, 22, 4, 1, 8, 3, 2, 19, 6, 1, 37 ]
11
true
Domain
Cryptochrome/DNA photolyase, FAD-binding domain
Cryptochrome/DNA photolyase, FAD-binding domain
Cryptochr/Photolyase_FAD-bd
1
IPR005102
5,102
Carbohydrate binding X2 domain
Carbo-bd_X2
Domain
2,287
false
false
This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its sub...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03442" ]
[ "CBM_X2" ]
[ 2287 ]
1
[]
[]
[]
0
[ "1ehx", "4v2x", "4yzp", "4yzt", "5e09", "5e0c", "5xrc", "9l3d", "9l3j", "9l3o", "9l3p", "9qa6" ]
12
[ "PUB00007734", "PUB00057467" ]
[ "11080456", "15375114" ]
[ "Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum.", "Hydrophilic domains of scaffolding protein CbpA promote glycosyl hydrolase activity and localization of cellulosomes to the cell surface of Clostridium cellulovorans." ]
[ 2000, 2004 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanosalsum", "metagenomes" ]
[ 1773, 504, 2, 8 ]
4
[]
[]
0
true
Domain
Carbohydrate binding X2 domain
Carbohydrate binding X2 domain
Carbo-bd_X2
3
IPR005103
5,103
Auxiliary Activity family 9, catalytic domain
AA9_LPMO
Domain
17,515
false
false
This entry represents the lytic polysaccharide monooxygenase (LPMO) domain of AA9 [ ]. Although weak endoglucanase activity has been demonstrated in several members of this family [ , , ], they lack the clustered conserved catalytic acidic amino acids present in most glycoside hydrolases. Many members of this family la...
[]
[]
[]
0
[ "PFAM", "CDD" ]
[ "PF03443", "cd21175" ]
[ "AA9", "LPMO_AA9" ]
[ 17515, 15798 ]
2
[ "CAZY", "EC" ]
[ "GH61", "1.14.99.56" ]
[ "CAZY:GH61", "EC:1.14.99.56" ]
2
[ "2vtc", "2yet", "3eii", "3eja", "3zud", "4b5q", "4d7u", "4d7v", "4eir", "4eis", "4qi8", "5acf", "5acg", "5ach", "5aci", "5acj", "5foh", "5n04", "5n05", "5nkw", "5nln", "5nlo", "5nlp", "5nlq", "5nlr", "5nls", "5nlt", "5nns", "5o2w", "5o2x", "5tkf", "5tkg"...
110
[ "PUB00057681", "PUB00078763", "PUB00079200", "PUB00098631", "PUB00098632", "PUB00148242" ]
[ "20230050", "24912171", "16844780", "22057939", "11737205", "28900033" ]
[ "Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family.", "Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.", "Development and applica...
[ 2010, 2014, 2006, 2012, 2001, 2017 ]
6
[]
[]
0
0
null
[ "Archangium minus", "Eukaryota", "viral metagenome" ]
[ 1, 17513, 1 ]
3
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Zea mays" ]
[ 14, 1 ]
2
true
Domain
Auxiliary Activity family 9, catalytic domain
Auxiliary Activity family 9, catalytic domain
AA9_LPMO
8
IPR005104
5,104
Winged helix-turn-helix transcription repressor, HrcA DNA-binding domain
WHTH_HrcA_DNA-bd
Domain
5,725
false
false
Prokaryotic cells have a defence mechanism against a sudden heat-shock stress. Commonly, they induce a set of proteins that protect cellular proteins from being denatured by heat. Among such proteins are the GroE and DnaK chaperones whose transcription is regulated by a heat-shock repressor protein HrcA. HrcA is a wing...
[ "GO:0003677", "GO:0006355" ]
[ "DNA binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF03444" ]
[ "WHD_HrcA" ]
[ 5725 ]
1
[]
[]
[]
0
[]
0
[ "PUB00037641", "PUB00053432", "PUB00053433" ]
[ "15979091", "19277496", "12486078" ]
[ "Crystal structure of a heat-inducible transcriptional repressor HrcA from Thermotoga maritima: structural insight into DNA binding and dimerization.", "Reduction-sensitive and cysteine residue-mediated Streptococcus pneumoniae HrcA oligomerization in vitro.", "Identification of a helix-turn-helix motif of Baci...
[ 2005, 2009, 2003 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 848, 4728, 10, 139 ]
4
[]
[]
0
true
Domain
Winged helix-turn-helix transcription repressor, HrcA DNA-binding domain
Winged helix-turn-helix transcription repressor, HrcA DNA-binding domain
WHTH_HrcA_DNA-bd
9
IPR005105
5,105
Protein-PII uridylyltransferase, N-terminal
GlnD_Uridyltrans_N
Domain
10,290
false
false
This domain is found associated with an N-terminal cyclic nucleotide-binding domain ( ) and two CBS domains ( ). This domain, normally represents the C-terminal region, is uncharacterised; however, it seems to be similar to the nucleotidyltransferase domain ( ), conserving the DXD motif, which strongly suggests that pr...
[ "GO:0008773" ]
[ "[protein-PII] uridylyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03445" ]
[ "DUF294" ]
[ 10290 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.7.59", "3.1.4.-", "PWY-5978", "PWY-6129", "PWY-6689", "PWY-7119", "PWY-7366" ]
[ "EC:2.7.7.59", "EC:3.1.4.-", "METACYC:PWY-5978", "METACYC:PWY-6129", "METACYC:PWY-6689", "METACYC:PWY-7119", "METACYC:PWY-7366" ]
7
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 27, 9646, 556, 61 ]
4
[ "Arabidopsis thaliana" ]
[ 1 ]
1
true
Domain
Protein-PII uridylyltransferase, N-terminal
Protein-PII uridylyltransferase, N-terminal
GlnD_Uridyltrans_N
7
IPR005106
5,106
Aspartate/homoserine dehydrogenase, NAD-binding
Asp/hSer_DH_NAD-bd
Domain
39,457
false
false
This entry represents the NAD(P)-binding domain of aspartate and homoserine dehydrogenase. Asparate dehydrogenase ( ) is strictly specific for L-aspartate as substrate and catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [ ]. Note that the C terminus of t...
[ "GO:0016491", "GO:0050661" ]
[ "oxidoreductase activity", "NADP binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF03447" ]
[ "NAD_binding_3" ]
[ 39457 ]
1
[ "GP", "GP", "GP", "GP", "GP" ]
[ "GenProp1358", "GenProp1419", "GenProp1475", "GenProp1553", "GenProp1581" ]
[ "GP:GenProp1358", "GP:GenProp1419", "GP:GenProp1475", "GP:GenProp1553", "GP:GenProp1581" ]
5
[ "1ebf", "1ebu", "1h2h", "1j5p", "1q7g", "1tve", "2dc1", "2ejw", "3c8m", "3do5", "3ing", "3jsa", "3mtj", "3upl", "3upy", "4pg4", "4pg5", "4pg6", "4pg7", "4pg8", "4xb1", "4xb2", "4ydr", "5avo", "5x9d", "5xdf", "6a0r", "6a0s", "6a0t", "6a0u", "6dzs", "7f4b"...
34
[ "PUB00000699", "PUB00001656", "PUB00014412", "PUB00021481", "PUB00034672" ]
[ "8395899", "8500624", "12496312", "10700284", "11352712" ]
[ "Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.", "Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.", "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643.", "Crys...
[ 1993, 1993, 2003, 2000, 2001 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 905, 33684, 4268, 600 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "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)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...
[ 11, 1, 2, 2, 2, 3, 1, 11, 4, 1, 1, 28 ]
12
true
Domain
Aspartate/homoserine dehydrogenase, NAD-binding
Aspartate/homoserine dehydrogenase, NAD-binding
Asp/hSer_DH_NAD-bd
5
IPR005107
5,107
CO dehydrogenase flavoprotein, C-terminal
CO_DH_flav_C
Domain
44,550
false
false
Proteins containing this domain form structural complexes with other known families, such as and . The carbon monoxide (CO) dehydrogenase of Oligotropha carboxidovorans is a heterotrimeric complex composed of a apoflavoprotein, a molybdoprotein, and an iron-sulphur protein. It can be dissociated with sodium dodecylsulp...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03450", "SM01092" ]
[ "CO_deh_flav_C", "CO_deh_flav_C" ]
[ 39860, 43732 ]
2
[ "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1236", "GenProp1255", "GenProp1469", "GenProp1753", "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", "R-MMU-964975...
[ "GP:GenProp1236", "GP:GenProp1255", "GP:GenProp1469", "GP:GenProp1753", "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-74259", "REACTOME:R-HSA-88516...
23
[ "1ffu", "1ffv", "1fiq", "1fo4", "1jro", "1jrp", "1n5w", "1n5x", "1n60", "1n61", "1n62", "1n63", "1rm6", "1sb3", "1t3q", "1v97", "1vdv", "1wyg", "1zxi", "2ckj", "2e1q", "2e3t", "2w3r", "2w3s", "2w54", "2w55", "3am9", "3amz", "3an1", "3ax7", "3ax9", "3b9j"...
73
[ "PUB00015703", "PUB00019122", "PUB00043387" ]
[ "11076018", "10430865", "10636886" ]
[ "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.", "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.", "Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase fro...
[ 2000, 1999, 2000 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 480, 30964, 12485, 621 ]
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",...
[ 38, 1, 4, 7, 3, 6, 15, 1, 20, 23, 78 ]
11
true
Domain
CO dehydrogenase flavoprotein, C-terminal
CO dehydrogenase flavoprotein, C-terminal
CO_DH_flav_C
6
IPR005108
5,108
HELP motif
HELP
Conserved_site
11,673
false
false
This entry represents the HELP (Hydrophobic ELP) motif found in animal EMAP and EMAP-like proteins (ELPs). These proteins are involved in the formation of the mitotic spindle and interphase microtubule network and for normal proliferation of neuronal progenitor cells in the developing brain and normal brain development...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03451" ]
[ "HELP" ]
[ 11673 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-9648025", "R-HSA-9648025", "R-HSA-9700645", "R-HSA-9725370", "R-MMU-9648025", "R-XTR-9648025" ]
[ "REACTOME:R-CEL-9648025", "REACTOME:R-HSA-9648025", "REACTOME:R-HSA-9700645", "REACTOME:R-HSA-9725370", "REACTOME:R-MMU-9648025", "REACTOME:R-XTR-9648025" ]
6
[ "4ci8" ]
1
[ "PUB00007735", "PUB00007736", "PUB00103956", "PUB00103957" ]
[ "11694528", "7989351", "24706829", "24859200" ]
[ "The human EMAP-like protein-70 (ELP70) is a microtubule destabilizer that localizes to the mitotic apparatus.", "Molecular characterization of the 77-kDa echinoderm microtubule-associated protein. Homology to the beta-transducin family.", "Crystal structure of EML1 reveals the basis for Hsp90 dependence of onc...
[ 2002, 1994, 2014, 2014 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 11673 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 49, 3, 34, 21, 38 ]
6
true
Conserved_site
HELP motif
HELP motif
HELP
4
IPR005109
5,109
Mannan polymerase complex subunit ANP1/MNN9/VAN1
ANP1/MNN9/VAN1
Family
4,652
false
false
The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for proper Golgi function. These proteins colocalize within the cis Golgi, where they are physically associated in two distinct complexes [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF03452" ]
[ "Anp1" ]
[ 4652 ]
1
[]
[]
[]
0
[ "3zf8" ]
1
[ "PUB00007737" ]
[ "9430634" ]
[ "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halapricum salinum", "metagenomes", "uncultured Caudovirales phage" ]
[ 161, 4473, 1, 12, 5 ]
5
[ "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)" ]
[ 3, 3, 2 ]
3
true
Family
Mannan polymerase complex subunit ANP1/MNN9/VAN1
Mannan polymerase complex subunit ANP1/MNN9/VAN1
ANP1/MNN9/VAN1
7
IPR005111
5,111
MoeA, C-terminal, domain IV
MoeA_C_domain_IV
Domain
36,025
false
false
The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes functi...
[ "GO:0032324" ]
[ "molybdopterin cofactor biosynthetic process" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF03454" ]
[ "MoeA_C" ]
[ 36025 ]
1
[ "EC", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.10.1.1", "GenProp1711", "PWY-8171", "R-DDI-947581", "R-DME-947581", "R-HSA-947581", "R-MMU-947581", "R-RNO-947581" ]
[ "EC:2.10.1.1", "GP:GenProp1711", "METACYC:PWY-8171", "REACTOME:R-DDI-947581", "REACTOME:R-DME-947581", "REACTOME:R-HSA-947581", "REACTOME:R-MMU-947581", "REACTOME:R-RNO-947581" ]
8
[ "1fc5", "1g8l", "1g8r", "1t3e", "1uz5", "1wu2", "1xi8", "2fts", "2fu3", "2nqk", "2nqm", "2nqn", "2nqq", "2nqr", "2nqs", "2nqu", "2nqv", "2nro", "2nrp", "2nrs", "4pd0", "4pd1", "4tk1", "4tk2", "4tk3", "4tk4", "4u90", "4u91", "5erq", "5err", "5ers", "5ert"...
54
[ "PUB00007738", "PUB00015635", "PUB00015921", "PUB00034757", "PUB00034758", "PUB00034759" ]
[ "11525167", "12372836", "8528286", "12114025", "17198377", "16784786" ]
[ "The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin.", "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli.", "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cn...
[ 2001, 2002, 1995, 2002, 2007, 2006 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1653, 27788, 5979, 605 ]
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",...
[ 5, 1, 58, 2, 1, 6, 3, 2, 2, 8, 10 ]
11
true
Domain
MoeA, C-terminal, domain IV
MoeA, C-terminal, domain IV
MoeA_C_domain_IV
7
IPR005112
5,112
dDENN domain
dDENN_dom
Domain
33,789
false
false
This entry represents the dDENN domain. The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pat...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03455", "SM00801" ]
[ "dDENN", "dDENN" ]
[ 21904, 33248 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50211", "R-CEL-1483248", "R-CEL-8876198", "R-DME-8876198", "R-HSA-1483248", "R-HSA-1660499", "R-HSA-5357905", "R-HSA-8876198", "R-MMU-1483248", "R-MMU-5357905", "R-MMU-8876198", "R-RNO-5357905", "R-RNO-8876198", "R-SPO-8876198" ]
[ "PROSITEDOC:PDOC50211", "REACTOME:R-CEL-1483248", "REACTOME:R-CEL-8876198", "REACTOME:R-DME-8876198", "REACTOME:R-HSA-1483248", "REACTOME:R-HSA-1660499", "REACTOME:R-HSA-5357905", "REACTOME:R-HSA-8876198", "REACTOME:R-MMU-1483248", "REACTOME:R-MMU-5357905", "REACTOME:R-MMU-8876198", "REACTOME:...
14
[ "3tw8", "6ekk" ]
2
[ "PUB00007739", "PUB00018213", "PUB00065679", "PUB00160349", "PUB00160351", "PUB00160352", "PUB00160390", "PUB00160391" ]
[ "11563850", "12906859", "22065758", "35196081", "37454296", "38296963", "20472560", "28970336" ]
[ "uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways.", "Molecular cloning, structural analysis, and expression of a human IRLB, MYC promoter-binding protein: new DENN domain-containing protein family emerges small star, filled.", "Insights regarding guanine nucleotide exchan...
[ 2001, 2003, 2011, 2022, 2023, 2024, 2010, 2017 ]
8
[ "IPR037516" ]
[]
1
0
1
[ "Eukaryota" ]
[ 33789 ]
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...
[ 11, 13, 121, 25, 78, 43, 2, 6, 85, 1, 9 ]
11
true
Domain
dDENN domain
dDENN domain
dDENN_dom
8
IPR005113
5,113
uDENN domain
uDENN_dom
Domain
35,475
false
false
The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03456", "SM00800" ]
[ "uDENN", "uDENN" ]
[ 35184, 32480 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50211", "R-CEL-1483248", "R-CEL-8876198", "R-DME-8876198", "R-HSA-1483248", "R-HSA-1660499", "R-HSA-5357905", "R-HSA-8876198", "R-MMU-1483248", "R-MMU-5357905", "R-MMU-8876198", "R-RNO-5357905", "R-RNO-8876198", "R-SPO-8876198" ]
[ "PROSITEDOC:PDOC50211", "REACTOME:R-CEL-1483248", "REACTOME:R-CEL-8876198", "REACTOME:R-DME-8876198", "REACTOME:R-HSA-1483248", "REACTOME:R-HSA-1660499", "REACTOME:R-HSA-5357905", "REACTOME:R-HSA-8876198", "REACTOME:R-MMU-1483248", "REACTOME:R-MMU-5357905", "REACTOME:R-MMU-8876198", "REACTOME:...
14
[ "3tw8", "6ekk" ]
2
[ "PUB00007739", "PUB00018213", "PUB00065679", "PUB00160349", "PUB00160351", "PUB00160352", "PUB00160390", "PUB00160391" ]
[ "11563850", "12906859", "22065758", "35196081", "37454296", "38296963", "20472560", "28970336" ]
[ "uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways.", "Molecular cloning, structural analysis, and expression of a human IRLB, MYC promoter-binding protein: new DENN domain-containing protein family emerges small star, filled.", "Insights regarding guanine nucleotide exchan...
[ 2001, 2003, 2011, 2022, 2023, 2024, 2010, 2017 ]
8
[ "IPR037516" ]
[]
1
0
1
[ "Eukaryota" ]
[ 35475 ]
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...
[ 17, 13, 122, 23, 100, 52, 4, 10, 78, 1, 30 ]
11
true
Domain
uDENN domain
uDENN domain
uDENN_dom
2
IPR005114
5,114
Helicase-associated
Helicase_assoc
Domain
6,453
false
false
This short domain can be found in multiple copies in helicase proteins. The domain is predicted to contain 3 α helices. The function of this domain may be to bind nucleic acid.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03457" ]
[ "HA" ]
[ 6453 ]
1
[]
[]
[]
0
[ "2kta" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 2459, 3954, 14, 26 ]
4
[]
[]
0
true
Domain
Helicase-associated
Helicase-associated
Helicase_assoc
5
IPR005115
5,115
Glycine transporter
Gly_transporter
Domain
20,165
false
false
This domain contains three transmembrane helices. Proteins containing this domain are important for glycine utilisation, being identified as glycine transporters. Some proteins containing this domain are also important for alanine utilisation. In these proteins this domain is found in pairs [ ]. An archaeal protein whi...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03458" ]
[ "Gly_transporter" ]
[ 20165 ]
1
[]
[]
[]
0
[ "5h35", "5h36", "5wtr", "5wuc", "5wud", "5wue", "5wuf" ]
7
[ "PUB00093610", "PUB00098630" ]
[ "29769716", "28524849" ]
[ "Mutant phenotypes for thousands of bacterial genes of unknown function.", "Structural basis for conductance through TRIC cation channels." ]
[ 2018, 2017 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Phage sp. ctWVj20", "unclassified sequences" ]
[ 435, 19276, 240, 1, 213 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
Glycine transporter
Glycine transporter
Gly_transporter
9
IPR005116
5,116
Transport-associated OB, type 1
Transp-assoc_OB_typ1
Domain
29,366
false
false
The TOBE domain [ ] (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. It is probably involved in the recognition of small ligands such as molybdenum ( , ) and sulphate ( ), and is found in ABC transporters immediately after the ATPase domain.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03459" ]
[ "TOBE" ]
[ 29366 ]
1
[ "EC", "EC", "METACYC" ]
[ "7.3.2", "7.3.2.5", "PWY-8171" ]
[ "EC:7.3.2", "EC:7.3.2.5", "METACYC:PWY-8171" ]
3
[ "1b9m", "1b9n", "1fr3", "1gug", "1gun", "1guo", "1gus", "1gut", "1h9j", "1h9k", "1h9m", "1h9r", "1h9s", "1o7l", "2d62", "3d31", "4tqu", "4tqv", "4xig", "4xtc", "6yir", "7x0q", "9beb", "9bed", "9bel", "9bem", "9beo", "9bjf", "9d2c" ]
29
[ "PUB00007673" ]
[ "10829230" ]
[ "Protein fold recognition using sequence profiles and its application in structural genomics." ]
[ 2000 ]
1
[]
[ "IPR004606" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences" ]
[ 967, 28056, 27, 1, 315 ]
5
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
Transport-associated OB, type 1
Transport-associated OB, type 1
Transp-assoc_OB_typ1
7
IPR005117
5,117
Nitrite/Sulfite reductase ferredoxin-like domain
NiRdtase/SiRdtase_haem-b_fer
Domain
52,193
false
false
Sulphite reductases (SiRs) and related nitrite reductases (NiRs) catalyse the six-electron reduction reactions of sulphite to sulphide, and nitrite to ammonia, respectively. The Escherichia coli SiR enzyme is a complex composed of two proteins, a flavoprotein alpha-component (SiR-FP) and a hemoprotein beta-component (S...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF03460" ]
[ "NIR_SIR_ferr" ]
[ 52193 ]
1
[ "EC", "GP", "GP", "METACYC", "REACTOME" ]
[ "1.8.1.2", "GenProp1554", "GenProp1746", "PWY-6683", "R-MTU-936721" ]
[ "EC:1.8.1.2", "GP:GenProp1554", "GP:GenProp1746", "METACYC:PWY-6683", "REACTOME:R-MTU-936721" ]
5
[ "1aop", "1zj8", "1zj9", "2akj", "2aop", "2gep", "2v4j", "2xsj", "3aop", "3b0g", "3b0h", "3b0j", "3b0l", "3b0m", "3b0n", "3geo", "3mm5", "3mm6", "3mm7", "3mm8", "3mm9", "3mma", "3mmb", "3mmc", "3or1", "3or2", "3vkp", "3vkq", "3vkr", "3vks", "3vkt", "3vlx"...
56
[ "PUB00014351", "PUB00014496" ]
[ "10984484", "7569952" ]
[ "A simplifed functional version of the Escherichia coli sulfite reductase.", "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions." ]
[ 2000, 1995 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctWdm1", "unclassified sequences" ]
[ 1244, 44829, 5202, 1, 917 ]
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" ]
[ 11, 2, 2, 12, 1, 1, 17 ]
7
true
Domain
Nitrite/Sulfite reductase ferredoxin-like domain
Nitrite/Sulfite reductase ferredoxin-like domain
NiRdtase/SiRdtase_haem-b_fer
9
IPR005118
5,118
Transcription-repair-coupling factor, C-terminal domain
TRCF_C
Domain
27,030
false
false
The transcription-repair coupling factor (TRCF, product of the mfd gene) couples transcription and DNA repair in bacteria. TRCF removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair (NER) machinery to the site. This protein, comprised of eight domains, including r...
[ "GO:0006281" ]
[ "DNA repair" ]
[ "biological_process" ]
1
[ "PFAM", "SMART" ]
[ "PF03461", "SM00982" ]
[ "TRCF", "TRCF" ]
[ 26950, 26905 ]
2
[ "EC", "METACYC" ]
[ "3.6.4.-", "PWY-7250" ]
[ "EC:3.6.4.-", "METACYC:PWY-7250" ]
2
[ "2eyq", "2qsr", "6ac6", "6ac8", "6aca", "6acx", "6m6a", "6m6b", "6x26", "6x2f", "6x2n", "6x43", "6x4w", "6x4y", "6x50", "6xeo", "7ssg", "9n07", "9n11" ]
19
[ "PUB00019253", "PUB00069799" ]
[ "7876261", "14602898" ]
[ "Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties.", "A DNA translocation motif in the bacterial transcription--repair coupling factor, Mfd." ]
[ 1995, 2003 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 26027, 391, 612 ]
3
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 1, 5, 5 ]
3
true
Domain
Transcription-repair-coupling factor, C-terminal domain
Transcription-repair-coupling factor, C-terminal domain
TRCF_C
6
IPR005119
5,119
LysR, substrate-binding
LysR_subst-bd
Domain
635,426
false
false
The LysR-type transcriptional regulator (LTTR) domain is a key component of one of the largest families of prokaryotic transcriptional regulators [ ]. Its structure, similar to periplasmic binding proteins, consists of an N-terminal DNA-binding domain (DBD) with a helix-turn-helix motif and a C-terminal effector-bindin...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03466" ]
[ "LysR_substrate" ]
[ 635426 ]
1
[ "GP" ]
[ "GenProp1072" ]
[ "GP:GenProp1072" ]
1
[ "1al3", "1i69", "1i6a", "1ixc", "1iz1", "1utb", "1uth", "2esn", "2f6g", "2f6p", "2f78", "2f7a", "2f7b", "2f7c", "2f8d", "2f97", "2fyi", "2h98", "2h99", "2h9b", "2hxr", "2ql3", "2qsx", "2uye", "2uyf", "2y7k", "2y7p", "2y7r", "2y7w", "2y84", "3fd3", "3fxq"...
168
[ "PUB00002150", "PUB00002180", "PUB00003277", "PUB00004664", "PUB00004739", "PUB00005283", "PUB00086898", "PUB00099685", "PUB00117984", "PUB00160345", "PUB00160346" ]
[ "1907267", "1592818", "1840615", "3413113", "2034653", "9309218", "19047729", "34424339", "12595552", "37285554", "34254827" ]
[ "rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum.", "The Escherichia coli K-12 cyn operon is positively regul...
[ 1991, 1992, 1991, 1988, 1991, 1997, 2008, 2021, 2003, 2023, 2021 ]
11
[]
[ "IPR037400", "IPR037402", "IPR037403", "IPR037404", "IPR037405", "IPR037406", "IPR037408", "IPR037409", "IPR037410", "IPR037411", "IPR037412", "IPR037414", "IPR037415", "IPR037416", "IPR037417", "IPR037418", "IPR037420", "IPR037421", "IPR037422", "IPR037423", "IPR037424", "...
0
23
0
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "plasmids", "unclassified sequences" ]
[ 57, 631247, 10, 1072, 10, 3030 ]
6
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 47 ]
2
true
Domain
LysR, substrate-binding
LysR, substrate-binding
LysR_subst-bd
8
IPR005121
5,121
Ferrodoxin-fold anticodon-binding domain
Fdx_antiC-bd
Domain
33,774
false
false
Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to their cognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among the most complex enzymes of the aaRS family. Bacterial ...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF03147", "PS51447", "SM00896" ]
[ "FDX-ACB", "FDX_ACB", "FDX-ACB" ]
[ 32493, 33512, 33491 ]
3
[ "EC", "REACTOME" ]
[ "6.1.1.20", "R-HSA-379726" ]
[ "EC:6.1.1.20", "REACTOME:R-HSA-379726" ]
2
[ "1b70", "1b7y", "1eiy", "1jjc", "1pys", "2akw", "2aly", "2amc", "2iy5", "2rhq", "2rhs", "3cmq", "3hfv", "3hfz", "3pco", "3teg", "3teh", "3tup", "4p71", "4p72", "4p73", "4p74", "4p75", "4tva", "5mgh", "5mgu", "5mgv", "5mgw", "6oz5", "6p24", "6p26", "6p8t"...
46
[ "PUB00007741", "PUB00020104", "PUB00051056", "PUB00052597", "PUB00052598" ]
[ "9016717", "7664121", "18611382", "10049785", "12962494" ]
[ "The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.", "Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.", "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase.", "Human phenylalanyl-tRNA...
[ 1997, 1995, 2008, 1999, 2003 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 56, 27104, 5965, 11, 638 ]
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",...
[ 3, 3, 2, 1, 1, 3, 4, 1, 2, 9, 1, 1, 12 ]
13
true
Domain
Ferrodoxin-fold anticodon-binding domain
Ferrodoxin-fold anticodon-binding domain
Fdx_antiC-bd
4
IPR005122
5,122
Uracil-DNA glycosylase-like
Uracil-DNA_glycosylase-like
Domain
72,880
false
false
This entry represents various uracil-DNA glycosylases and related DNA glycosylases ( ), such as uracil-DNA glycosylase [ ], thermophilic uracil-DNA glycosylase [ ], G:T/U mismatch-specific DNA glycosylase (Mug) [ ], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) [ ]. These proteins have a 3-l...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03167", "SM00986" ]
[ "UDG", "UDG" ]
[ 72765, 61126 ]
2
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.2.2", "3.2.2.27", "R-BTA-110329", "R-BTA-110357", "R-DDI-110329", "R-DDI-110357", "R-HSA-110328", "R-HSA-110329", "R-HSA-110357", "R-HSA-3108214", "R-HSA-5221030", "R-HSA-9609690", "R-HSA-9821002", "R-MMU-110329", "R-MMU-110357", "R-MMU-3108214", "R-MMU-5221030", "R-RNO-110329",...
[ "EC:3.2.2", "EC:3.2.2.27", "REACTOME:R-BTA-110329", "REACTOME:R-BTA-110357", "REACTOME:R-DDI-110329", "REACTOME:R-DDI-110357", "REACTOME:R-HSA-110328", "REACTOME:R-HSA-110329", "REACTOME:R-HSA-110357", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-5221030", "REACTOME:R-HSA-9609690", "REACTOME:R-...
23
[ "1akz", "1emh", "1emj", "1eug", "1eui", "1flz", "1l9g", "1lau", "1lqg", "1lqj", "1lqm", "1mtl", "1mug", "1mwi", "1mwj", "1oe4", "1oe5", "1oe6", "1okb", "1q3f", "1ssp", "1udg", "1udh", "1udi", "1ugh", "1ui0", "1ui1", "1uug", "1vk2", "1wyw", "1yuo", "2boo"...
183
[ "PUB00000916", "PUB00001176", "PUB00004816", "PUB00008091", "PUB00042575", "PUB00042576", "PUB00042577", "PUB00042578" ]
[ "7697717", "2555154", "8389453", "9489705", "10339434", "2820976", "16860315", "17116429" ]
[ "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis.", "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme.", "Identification of a poxvirus gene encoding a uracil DNA glycosylase.", "Crystal structure o...
[ 1995, 1989, 1993, 1998, 1999, 1987, 2006, 2007 ]
8
[]
[ "IPR005273", "IPR044147" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1954, 59390, 9400, 646, 1490 ]
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",...
[ 2, 1, 23, 5, 2, 21, 11, 2, 4, 13, 1, 2, 6 ]
13
true
Domain
Uracil-DNA glycosylase-like
Uracil-DNA glycosylase-like
Uracil-DNA_glycosylase-like
9
IPR005123
5,123
Oxoglutarate/iron-dependent dioxygenase domain
Oxoglu/Fe-dep_dioxygenase_dom
Domain
190,996
false
false
Enzymes with the Fe(2+) and 2-oxoglutarate (2OG)-dependent dioxygenase domain typically catalyse the oxidation of an organic substrate using a dioxygen molecule, mostly by using ferrous iron as the active site cofactor and 2OG as a co-substrate which is decarboxylated to succinate and CO2 [ ]. Iron 2OG dioxygenase doma...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51471" ]
[ "FE2OG_OXY" ]
[ 190996 ]
1
[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.11", "GenProp0724", "GenProp1657", "R-BTA-1650814", "R-BTA-9629569", "R-CEL-1234176", "R-CEL-1650814", "R-DME-1650814", "R-DME-9629569", "R-GGA-1650814", "R-HSA-112122", "R-HSA-112126", "R-HSA-1234176", "R-HSA-1650814", "R-HSA-6782315", "R-HSA-9629569", "R-MMU-1234176", "R-MM...
[ "EC:1.14.11", "GP:GenProp0724", "GP:GenProp1657", "REACTOME:R-BTA-1650814", "REACTOME:R-BTA-9629569", "REACTOME:R-CEL-1234176", "REACTOME:R-CEL-1650814", "REACTOME:R-DME-1650814", "REACTOME:R-DME-9629569", "REACTOME:R-GGA-1650814", "REACTOME:R-HSA-112122", "REACTOME:R-HSA-112126", "REACTOME:...
23
[ "1bk0", "1blz", "1dcs", "1e5h", "1e5i", "1gp4", "1gp5", "1gp6", "1hb1", "1hb2", "1hb3", "1hb4", "1hjf", "1hjg", "1ips", "1obn", "1oc1", "1odm", "1odn", "1qiq", "1qje", "1qjf", "1rxf", "1rxg", "1unb", "1uo9", "1uob", "1uof", "1uog", "1uzw", "1w03", "1w04"...
389
[ "PUB00007742", "PUB00016787", "PUB00040896", "PUB00054927", "PUB00057910" ]
[ "11276424", "14697267", "16782814", "19756382", "19786499" ]
[ "The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases.", "Cupins: the most functionally diverse protein superfamily?", "Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).", "Hypoxia, hypoxia-induc...
[ 2001, 2004, 2006, 2009, 2009 ]
5
[]
[ "IPR006620", "IPR039558", "IPR044861" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 20, 45384, 142972, 1891, 729 ]
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",...
[ 650, 13, 93, 60, 2, 66, 47, 16, 310, 76, 1, 5, 430 ]
13
true
Domain
Oxoglutarate/iron-dependent dioxygenase domain
Oxoglutarate/iron-dependent dioxygenase domain
Oxoglu/Fe-dep_dioxygenase_dom
4
IPR005126
5,126
NapC/NirT cytochrome c, N-terminal
NapC/NirT_cyt_c_N
Domain
7,993
false
false
Within the NapC/NirT family of cytochrome c proteins, some members, such as NapC and NirT , bind four haem groups, while others, such as TorC , bind five haems. This family aligns the common N-terminal region that contains four haem-binding C-X(2)-CH motifs.
[]
[]
[]
0
[ "PFAM" ]
[ "PF03264" ]
[ "Cytochrom_NNT" ]
[ 7993 ]
1
[]
[]
[]
0
[ "2j7a", "2vr0" ]
2
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Siphoviridae sp. ctPAi1", "metagenomes" ]
[ 7845, 10, 18, 1, 119 ]
5
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
NapC/NirT cytochrome c, N-terminal
NapC/NirT cytochrome c, N-terminal
NapC/NirT_cyt_c_N
5
IPR005127
5,127
Giardia variant-specific surface protein
Giardia_VSP
Family
1,523
false
false
During infection, the intestinal protozoan parasite Giardia lamblia virus undergoes continuous antigenic variation which is determined by diversification of the parasite's major surface antigen, named VSP (variant surface protein).
[]
[]
[]
0
[ "PFAM" ]
[ "PF03302" ]
[ "VSP" ]
[ 1523 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1523 ]
1
[]
[]
0
true
Family
Giardia variant-specific surface protein
Giardia variant-specific surface protein
Giardia_VSP
9
IPR005128
5,128
Alpha-acetolactate decarboxylase
Acetolactate_a_deCO2ase
Family
4,915
false
false
Alpha-acetolactate decarboxylase converts acetolactate into acetoin. In Streptococcus thermophilus, it regulates leucine and valine biosynthesis by diverting the flux of alpha-acetolactate towards acetoin when the branched-chain amino acids are present in high concentration [ ].
[ "GO:0047605", "GO:0045151" ]
[ "acetolactate decarboxylase activity", "acetoin biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF03306", "PIRSF001332", "PTHR35524", "TIGR01252", "cd17299" ]
[ "AAL_decarboxy", "Acetolac_decarb", "", "acetolac_decarb", "acetolactate_decarboxylase" ]
[ 4915, 4163, 4739, 3933, 4359 ]
5
[ "EC", "GP", "METACYC" ]
[ "4.1.1.5", "GenProp0272", "PWY-5939" ]
[ "EC:4.1.1.5", "GP:GenProp0272", "METACYC:PWY-5939" ]
3
[ "1xv2", "4bt2", "4bt3", "4bt4", "4bt5", "4bt6", "4bt7", "5xne", "5yho", "6inb", "6inc", "6j3d", "6j92" ]
13
[ "PUB00070780" ]
[ "12753249" ]
[ "Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase in Streptococcus thermophilus." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 130, 3900, 809, 76 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Alpha-acetolactate decarboxylase
Alpha-acetolactate decarboxylase
Acetolactate_a_deCO2ase
4
IPR005129
5,129
SIMIBI class G3E GTPase, ArgK/MeaB
GTPase_ArgK
Family
13,967
false
false
This family includes ArgK (also known as YgfD) from E. coli, Methylmalonic aciduria type A protein (MMA) from human and similar proteins [ ], which belong to the G3E family of P-loop GTPases, a family defined by the glutamate residue in the Walker B motif and an intact NKxD, members of which include: UreG, HypB, CobW, ...
[ "GO:0003924", "GO:0005525" ]
[ "GTPase activity", "GTP binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PANTHER", "NCBIFAM" ]
[ "PTHR23408", "TIGR00750" ]
[ "", "lao" ]
[ 9367, 13145 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-71032", "R-CEL-9759218", "R-HSA-3359475", "R-HSA-3359478", "R-HSA-71032", "R-HSA-9759218", "R-MMU-71032", "R-MMU-9759218" ]
[ "REACTOME:R-CEL-71032", "REACTOME:R-CEL-9759218", "REACTOME:R-HSA-3359475", "REACTOME:R-HSA-3359478", "REACTOME:R-HSA-71032", "REACTOME:R-HSA-9759218", "REACTOME:R-MMU-71032", "REACTOME:R-MMU-9759218" ]
8
[ "2p67", "2qm7", "2qm8", "2www", "3md0", "3nxs", "3p32", "3tk1", "4gt1", "4jyb", "4jyc", "4lc1", "6cum", "8dpb", "8gju" ]
15
[ "PUB00013952", "PUB00019162", "PUB00054406", "PUB00057891", "PUB00057892", "PUB00076901", "PUB00100594", "PUB00106871" ]
[ "11916378", "9733684", "20876572", "18950999", "16843692", "25832174", "28497574", "28943303" ]
[ "Classification and evolution of P-loop GTPases and related ATPases.", "Phosphorylation of the periplasmic binding protein in two transport systems for arginine incorporation in Escherichia coli K-12 is unrelated to the function of the transport system.", "Structures of the human GTPase MMAA and vitamin B12-dep...
[ 2002, 1998, 2010, 2009, 2006, 2015, 2017, 2017 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ctTrm2", "unclassified sequences" ]
[ 532, 11389, 1724, 1, 321 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 1, 8, 2, 3 ]
6
true
Family
SIMIBI class G3E GTPase, ArgK/MeaB
SIMIBI class G3E GTPase, ArgK/MeaB
GTPase_ArgK
1
IPR005130
5,130
Serine dehydratase-like, alpha subunit
Ser_deHydtase-like_asu
Domain
30,036
false
false
L-serine dehydratase is found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyses the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway. This entry also describes a number of proteins with no known function. Member...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03313" ]
[ "SDH_alpha" ]
[ 30036 ]
1
[]
[]
[]
0
[ "4rqo", "9fsl", "9fyi", "9he0", "9he2" ]
5
[ "PUB00099875" ]
[ "25380533" ]
[ "Structure of L-serine dehydratase from Legionella pneumophila: novel use of the C-terminal cysteine as an intrinsic competitive inhibitor." ]
[ 2014 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 53, 28850, 890, 243 ]
4
[ "Escherichia coli (strain K12)" ]
[ 4 ]
1
true
Domain
Serine dehydratase-like, alpha subunit
Serine dehydratase-like, alpha subunit
Ser_deHydtase-like_asu
5
IPR005131
5,131
Serine dehydratase beta chain
Ser_deHydtase_bsu
Domain
25,091
false
false
L-serine dehydratase is found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyses the deamination of serine to form pyruvate and is part of the gluconeogenesis pathway. Members of this entry adopt an α/β fold [ ].
[ "GO:0003941", "GO:0051539", "GO:0006094" ]
[ "L-serine ammonia-lyase activity", "4 iron, 4 sulfur cluster binding", "gluconeogenesis" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF03315" ]
[ "SDH_beta" ]
[ 25091 ]
1
[ "EC" ]
[ "4.3.1.17" ]
[ "EC:4.3.1.17" ]
1
[ "2iaf", "2iqq", "4rqo" ]
3
[ "PUB00099875" ]
[ "25380533" ]
[ "Structure of L-serine dehydratase from Legionella pneumophila: novel use of the C-terminal cysteine as an intrinsic competitive inhibitor." ]
[ 2014 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 11, 24066, 885, 129 ]
4
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Domain
Serine dehydratase beta chain
Serine dehydratase beta chain
Ser_deHydtase_bsu
3
IPR005133
5,133
Na+/H+ antiporter subunit G
PhaG_MnhG_YufB
Family
13,444
false
false
This is a family of small, transmembrane proteins believed to be components of Na+/H+ and K+/H+ antiporters. Members, including proteins designated MnhG from Staphylococcus aureus and PhaG from Rhizobium meliloti (Sinorhizobium meliloti), show some similarity to chain L of the NADH dehydrogenase I, which also transloca...
[ "GO:0015297", "GO:0055085" ]
[ "antiporter activity", "transmembrane transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PANTHER", "NCBIFAM" ]
[ "PF03334", "PTHR34703", "TIGR01300" ]
[ "PhaG_MnhG_YufB", "", "CPA3_mnhG_phaG" ]
[ 13444, 12641, 11380 ]
3
[]
[]
[]
0
[ "6cfw", "6u8y", "6z16", "7d3u", "7qru" ]
5
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 756, 12526, 9, 153 ]
4
[]
[]
0
true
Family
Na+/H+ antiporter subunit G
Na+/H+ antiporter subunit G
PhaG_MnhG_YufB
2
IPR005134
5,134
Uncharacterised protein family UPF0114
UPF0114
Family
8,701
false
false
This conserved hypothetical protein family with four predicted transmembrane regions is found in Escherichia coli, Haemophilus influenzae, and Helicobacter pylori 26695, among completed genomes.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF03350", "PIRSF026509" ]
[ "UPF0114", "UCP026509" ]
[ 8701, 965 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[ "IPR016804", "IPR020761" ]
0
2
0
[ "Bacteria", "Caudoviricetes", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 6666, 3, 1754, 82, 196 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 11, 1, 13, 9 ]
4
true
Family
Uncharacterised protein family UPF0114
Uncharacterised protein family UPF0114
UPF0114
5
IPR005135
5,135
Endonuclease/exonuclease/phosphatase
Endo/exonuclease/phosphatase
Domain
232,592
false
false
This domain is found in a large number of proteins including magnesium dependent endonucleases and phosphatases involved in intracellular signalling [ ]. Proteins this domain is found in include: AP endonuclease proteins ( ), DNase I proteins ( ), Synaptojanin an inositol-1,4,5-trisphosphate phosphatase ( ) and Sphingo...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PFAM", "PFAM" ]
[ "PF03372", "PF14529", "PF19580" ]
[ "Exo_endo_phos", "Exo_endo_phos_2", "Exo_endo_phos_3" ]
[ 199745, 27737, 5152 ]
3
[ "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "GenProp1229", "GenProp1363", "GenProp1395", "GenProp1509", "GenProp1605", "R-BTA-5693571", "R-BTA-8983711", "R-CEL-9840310", "R-DDI-110357", "R-DDI-110362", "R-DDI-110373", "R-DDI-5651801", "R-DDI-73930", "R-DDI-73933", "R-DDI-9840310", "R-DME-110357", "R-DME-110373", "R-DME-56518...
[ "GP:GenProp1229", "GP:GenProp1363", "GP:GenProp1395", "GP:GenProp1509", "GP:GenProp1605", "REACTOME:R-BTA-5693571", "REACTOME:R-BTA-8983711", "REACTOME:R-CEL-9840310", "REACTOME:R-DDI-110357", "REACTOME:R-DDI-110362", "REACTOME:R-DDI-110373", "REACTOME:R-DDI-5651801", "REACTOME:R-DDI-73930",...
76
[ "1ako", "1atn", "1bix", "1de8", "1de9", "1dew", "1dnk", "1e9n", "1hd7", "1sr4", "1vyb", "1wdu", "1zwx", "2a3z", "2a40", "2a41", "2a42", "2d1k", "2ddr", "2dds", "2ddt", "2dnj", "2ei9", "2f1n", "2f2f", "2isi", "2j63", "2jc4", "2jc5", "2myi", "2o3c", "2o3h"...
226
[ "PUB00007746" ]
[ "10838565" ]
[ "Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases." ]
[ 2000 ]
1
[]
[ "IPR000300", "IPR034965", "IPR034966", "IPR034967" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 791, 107848, 122246, 114, 1593 ]
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",...
[ 160, 16, 192, 37, 3, 78, 44, 9, 136, 94, 6, 4, 175 ]
13
true
Domain
Endonuclease/exonuclease/phosphatase
Endonuclease/exonuclease/phosphatase
Endo/exonuclease/phosphatase
4
IPR005137
5,137
Membrane complex biogenesis protein, BtpA family
BtpA
Family
4,038
false
false
Members of this family are found in Caenorhabditis elegans, Synechocystis sp., E. coli, and several of the Archaea. Members in Cyanobacteria have been shown to play a role in protein complex biogenesis, and designated BtpA (biogenesis of thylakoid protein) [ , ]. BtpA appears to act at the level of Photosystem I (PSI) ...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "PF03437", "PIRSF005956", "PTHR21381", "TIGR00259" ]
[ "BtpA", "BtpA", "", "thylakoid_BtpA" ]
[ 4031, 3378, 3980, 3419 ]
4
[]
[]
[]
0
[]
0
[ "PUB00014955", "PUB00015099", "PUB00083274" ]
[ "10806238", "9045660", "12651001" ]
[ "The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803 at low temperature.", "Molecular identification of a novel protein that regulates biogenesis of photosystem I, a membrane protein complex.", "Purification of recombinant BtpA and Ycf3, pro...
[ 2000, 1997, 2003 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 363, 2662, 965, 48 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)" ]
[ 1, 2, 3, 1 ]
4
true
Family
Membrane complex biogenesis protein, BtpA family
Membrane complex biogenesis protein, BtpA family
BtpA
2
IPR005138
5,138
Aerolysin/Pertussis toxin domain
APT_dom
Domain
273
false
false
This is the N-terminal domain of aerolysin and pertussis toxin which contains a type-C lectin like fold. Aerolysin causes the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process fro...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03440" ]
[ "APT" ]
[ 273 ]
1
[]
[]
[]
0
[ "1bcp", "1pre", "1prt", "1pto", "1z52", "3c0m", "3c0n", "3c0o", "3g4n", "3g4o", "5jzh", "5jzt", "5jzw", "6ro0", "9e3h", "9e3j", "9e3k", "9e3l", "9fm6", "9fml", "9fmx", "9fnp", "9fnq", "9gxj", "9mr7" ]
25
[ "PUB00004166", "PUB00007592", "PUB00020076", "PUB00037415" ]
[ "7510043", "8075982", "8637000", "7634099" ]
[ "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.", "The crystal structure of pertussis toxin.", "Crystal structure of the pertussis toxin-ATP complex: a molecular sensor.", "Structure of a pertussis toxin-sugar complex as a model for receptor binding." ]
[ 1994, 1994, 1996, 1994 ]
4
[]
[]
0
0
null
[ "Bacteria", "uncultured microorganism" ]
[ 272, 1 ]
2
[]
[]
0
true
Domain
Aerolysin/Pertussis toxin domain
Aerolysin/Pertussis toxin domain
APT_dom
8
IPR005140
5,140
eRF1/Pelota-like, N-terminal domain
eRF1_Pelota-like_N
Domain
12,758
false
false
This domain is found in the release factor eRF1 which terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [ ]. The overall shape and dimensions of eRF1 rese...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03463", "SM01194" ]
[ "eRF1_1", "eRF1_1" ]
[ 7094, 12494 ]
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-72764", "R-BTA-9629569", "R-BTA-975956", "R-BTA-975957", "R-CEL-72764", "R-CEL-9629569", "R-CEL-975956", "R-CEL-975957", "R-DDI-72764", "R-DDI-975956", "R-DDI-975957", "R-DME-72764", "R-DME-9629569", "R-DME-975956", "R-DME-975957", "R-HSA-72764", "R-HSA-9010553", "R-HSA-9629...
[ "REACTOME:R-BTA-72764", "REACTOME:R-BTA-9629569", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-72764", "REACTOME:R-CEL-9629569", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-72764", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-975957", "REACTOME:R-DME-7276...
36
[ "1dt9", "2lgt", "2llx", "2mq6", "2mq9", "2qi2", "2vgm", "2vgn", "3agk", "3e1y", "3e20", "3izq", "3j15", "3j16", "3j5y", "3jag", "3jah", "3jai", "3mca", "3obw", "3oby", "3vmf", "3wxm", "4af1", "4crn", "4d5n", "4d61", "5a8l", "5dmq", "5lzt", "5lzu", "5lzv"...
51
[ "PUB00007747" ]
[ "10676813" ]
[ "The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis." ]
[ 2000 ]
1
[]
[ "IPR058547" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 1905, 3, 10754, 15, 81 ]
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...
[ 17, 2, 5, 5, 7, 8, 2, 13, 3, 2, 2, 10 ]
12
true
Domain
eRF1/Pelota-like, N-terminal domain
eRF1/Pelota-like, N-terminal domain
eRF1_Pelota-like_N
4
IPR005141
5,141
eRF1 domain 2
eRF1_2
Domain
12,262
false
false
This domain is found in the release factor eRF1 which terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [ ]. The overall shape and dimensions of eRF1 rese...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03464" ]
[ "eRF1_2" ]
[ 12262 ]
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-72764", "R-BTA-9629569", "R-BTA-975956", "R-BTA-975957", "R-CEL-72764", "R-CEL-9629569", "R-CEL-975956", "R-CEL-975957", "R-DDI-72764", "R-DDI-975956", "R-DDI-975957", "R-DME-72764", "R-DME-9629569", "R-DME-975956", "R-DME-975957", "R-HSA-72764", "R-HSA-9010553", "R-HSA-9629...
[ "REACTOME:R-BTA-72764", "REACTOME:R-BTA-9629569", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-72764", "REACTOME:R-CEL-9629569", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-72764", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-975957", "REACTOME:R-DME-7276...
36
[ "1dt9", "2hst", "2vgm", "2vgn", "3agk", "3e1y", "3e20", "3izq", "3j15", "3j16", "3j5y", "3jag", "3jah", "3jai", "3mca", "3oby", "3vmf", "4af1", "4crm", "4crn", "4d5n", "4d61", "5a8l", "5dmq", "5lzt", "5lzu", "5lzv", "5lzw", "5lzx", "5lzy", "5lzz", "5m1j"...
46
[ "PUB00007747" ]
[ "10676813" ]
[ "The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 1497, 4, 10659, 39, 63 ]
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...
[ 17, 2, 5, 5, 5, 8, 2, 13, 3, 2, 2, 17 ]
12
true
Domain
eRF1 domain 2
eRF1 domain 2
eRF1_2
8
IPR005142
5,142
eRF1 domain 3
eRF1_3
Domain
12,843
false
false
This domain is found in the release factor eRF1 which terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [ ]. The overall shape and dimensions of eRF1 rese...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03465" ]
[ "eRF1_3" ]
[ 12843 ]
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-72764", "R-BTA-9629569", "R-BTA-975956", "R-BTA-975957", "R-CEL-72764", "R-CEL-9629569", "R-CEL-975956", "R-CEL-975957", "R-DDI-72764", "R-DDI-975956", "R-DDI-975957", "R-DME-72764", "R-DME-9629569", "R-DME-975956", "R-DME-975957", "R-HSA-72764", "R-HSA-9010553", "R-HSA-9629...
[ "REACTOME:R-BTA-72764", "REACTOME:R-BTA-9629569", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-72764", "REACTOME:R-CEL-9629569", "REACTOME:R-CEL-975956", "REACTOME:R-CEL-975957", "REACTOME:R-DDI-72764", "REACTOME:R-DDI-975956", "REACTOME:R-DDI-975957", "REACTOME:R-DME-7276...
36
[ "1dt9", "1x52", "2ktu", "2ktv", "2qi2", "2vgm", "2vgn", "3agk", "3e1y", "3e20", "3ir9", "3izq", "3j15", "3j16", "3j5y", "3jag", "3jah", "3jai", "3mca", "3obw", "3oby", "3vmf", "3wxm", "4af1", "4crm", "4crn", "4d5n", "4d61", "5a8l", "5dmq", "5dmr", "5eo3"...
55
[ "PUB00007747" ]
[ "10676813" ]
[ "The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1922, 37, 10790, 11, 83 ]
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...
[ 17, 2, 5, 5, 4, 8, 2, 13, 4, 3, 2, 16 ]
12
true
Domain
eRF1 domain 3
eRF1 domain 3
eRF1_3
1
IPR005143
5,143
Transcription factor LuxR-like, autoinducer-binding domain
TF_LuxR_autoind-bd_dom
Domain
12,786
false
false
This domain binds N-acyl homoserine lactones (AHLs), which are also known as autoinducers. These are small, diffusible molecules used as communication signals in a large variety of proteobacteria. It is almost always found in association with the DNA-binding LuxR domain ( ). The autoinducer binding domain forms the N-t...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03472" ]
[ "Autoind_bind" ]
[ 12786 ]
1
[]
[]
[]
0
[ "1h0m", "1l3l", "2avx", "2q0o", "2uv0", "3ix3", "3ix4", "3ix8", "3jpu", "3qp1", "3qp2", "3qp4", "3qp5", "3qp6", "3qp8", "3szt", "4lfu", "4lgw", "4ng2", "4y13", "4y15", "4y17", "5l07", "5l09", "5l10", "6cbq", "6cc0", "6d6a", "6d6b", "6d6c", "6d6d", "6d6l"...
52
[ "PUB00016946", "PUB00016948", "PUB00016949", "PUB00016950", "PUB00016951", "PUB00016960" ]
[ "12087407", "11544353", "12067349", "12198141", "11309123", "15237104" ]
[ "Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA.", "Quorum sensing in bacteria.", "The autoregulatory role of EsaR, a quorum-sensing regulator in Pantoea stewartii ssp. stewartii: evidence for a repressor function.", "The crystal structure of the quorum sensing p...
[ 2002, 2001, 2002, 2002, 2001, 2004 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 12708, 13, 65 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Transcription factor LuxR-like, autoinducer-binding domain
Transcription factor LuxR-like, autoinducer-binding domain
TF_LuxR_autoind-bd_dom
9
IPR005144
5,144
ATP-cone domain
ATP-cone_dom
Domain
51,236
false
false
The ATP-cone is an evolutionarily mobile, ATP-binding regulatory domain which is found in a variety of proteins including ribonucleotide reductases, phosphoglycerate kinases and transcriptional regulators [ ]. In ribonucleotide reductase protein R1 ( ) from Escherichia coli this domain is located at the N terminus, and...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF03477", "PS51161" ]
[ "ATP-cone", "ATP_CONE" ]
[ 48887, 51145 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC51161", "R-CEL-499943", "R-DDI-499943", "R-DME-499943", "R-DRE-499943", "R-HSA-499943", "R-MMU-499943", "R-SCE-499943", "R-SPO-499943" ]
[ "PROSITEDOC:PDOC51161", "REACTOME:R-CEL-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTOME:R-DRE-499943", "REACTOME:R-HSA-499943", "REACTOME:R-MMU-499943", "REACTOME:R-SCE-499943", "REACTOME:R-SPO-499943" ]
9
[ "1r1r", "1rlr", "1zyz", "1zzd", "2cvs", "2cvt", "2cvu", "2cvv", "2cvw", "2cvx", "2cvy", "2eud", "2r1r", "2x0x", "2xak", "2xap", "2xav", "2xaw", "2xax", "2xay", "2xaz", "2xo4", "2xo5", "2zlf", "2zlg", "3hnc", "3hnd", "3hne", "3hnf", "3k8t", "3paw", "3r1r"...
79
[ "PUB00005953", "PUB00005954", "PUB00007748" ]
[ "9309223", "8052308", "10939243" ]
[ "Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.", "Structure of ribonucleotide reductase protein R1.", "The ATP-cone: an evolutionarily mobile, ATP-binding regulatory domain." ]
[ 1997, 1994, 2000 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1034, 41822, 5655, 1762, 963 ]
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",...
[ 4, 1, 2, 1, 3, 6, 3, 1, 5, 5, 2, 1, 6 ]
13
true
Domain
ATP-cone domain
ATP-cone domain
ATP-cone_dom
8
IPR005145
5,145
Threonylcarbamoyl-AMP synthase, C-terminal domain
Sua5_C
Domain
13,817
false
false
This domain can be found in the C terminus of threonylcarbamoyl-AMP synthases, including Sua5 from Saccharomyces cerevisiae and YwlC from Bacillus subtilis. Threonylcarbamoyl-AMP synthase is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning w...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03481" ]
[ "Sua5_C" ]
[ 13817 ]
1
[ "EC" ]
[ "2.7.7.87" ]
[ "EC:2.7.7.87" ]
1
[ "2eqa", "2yv4", "3aje", "4e1b", "6f87", "6f89", "6f8y", "8ide", "9dg5", "9dsq", "9dsv", "9dsw" ]
12
[ "PUB00043826", "PUB00054278", "PUB00063366" ]
[ "18004774", "19287007", "23072323" ]
[ "X-ray crystal structure of a hypothetical Sua5 protein from Sulfolobus tokodaii strain 7.", "The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.", "Mechanism of N6-Threonylcarbamoyladenonsine (t(6)A) Biosynthesis: Isolation and Characterization of the Intermediat...
[ 2008, 2009, 2012 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Pandoravirus", "unclassified sequences" ]
[ 282, 11088, 2178, 6, 263 ]
5
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1 ]
3
true
Domain
Threonylcarbamoyl-AMP synthase, C-terminal domain
Threonylcarbamoyl-AMP synthase, C-terminal domain
Sua5_C
8
IPR005149
5,149
Transcription regulator PadR, N-terminal
Tscrpt_reg_PadR_N
Domain
76,713
false
false
Phenolic acids, also called substituted hydroxycinnamic acids, are abundant in the plant kingdom because they are involved in the structure of plant cell walls and are present in some vacuoles. In plant-soil ecosystems they are released as free acids by hemicellulases produced by several fungi and bacteria. Of these we...
[]
[]
[]
0
[ "PFAM" ]
[ "PF03551" ]
[ "PadR" ]
[ 76713 ]
1
[ "REACTOME" ]
[ "R-HSA-9638334" ]
[ "REACTOME:R-HSA-9638334" ]
1
[ "1xma", "1yg2", "2dql", "2e1n", "2esh", "2zfw", "3elk", "3f8b", "3f8c", "3f8f", "3hhh", "3l7w", "3l9f", "4ejo", "4esb", "4esf", "4zzd", "5dym", "5h20", "5x11", "5x12", "5x13", "5x14", "5y8t", "5z7b", "5zhc", "5zhv", "5zi8", "5zqh", "6abq", "6abt", "6do0"...
76
[ "PUB00014956" ]
[ "15066807" ]
[ "Cloning, deletion, and characterization of PadR, the transcriptional repressor of the phenolic acid decarboxylase-encoding padA gene of Lactobacillus plantarum." ]
[ 2004 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3916, 72184, 13, 22, 578 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Transcription regulator PadR, N-terminal
Transcription regulator PadR, N-terminal
Tscrpt_reg_PadR_N
5
IPR005150
5,150
Cellulose synthase
Cellulose_synth
Domain
23,647
false
false
Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterised gen...
[ "GO:0016760", "GO:0030244", "GO:0016020" ]
[ "cellulose synthase (UDP-forming) activity", "cellulose biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF03552" ]
[ "Cellulose_synt" ]
[ 23647 ]
1
[ "CAZY", "EC" ]
[ "GT2", "2.4.1" ]
[ "CAZY:GT2", "EC:2.4.1" ]
2
[ "5jnp", "6wlb", "7ck1", "7ck2", "7ck3", "7d5k", "8dqk", "8g27", "8g2j", "8vht", "8vhz", "8vi0" ]
12
[ "PUB00008351" ]
[ "8901635" ]
[ "Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Chlorovirus", "Eukaryota", "metagenomes" ]
[ 6, 2117, 4, 21512, 8 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 139, 100, 342 ]
3
true
Domain
Cellulose synthase
Cellulose synthase
Cellulose_synth
7
IPR005151
5,151
Tail specific protease
Tail-specific_protease
Domain
70,044
false
false
This entry represents a domain found in the tail-specific proteases, such as retinol-binding protein 3 (also known as IRBP) from animals, C-terminal processing peptidases from algae and tricorn proteases from archaea. This domain share structural similarity with the crotonase fold that is formed from repeated β/β/α uni...
[ "GO:0008236", "GO:0006508" ]
[ "serine-type peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "SMART" ]
[ "PF03572", "SM00245" ]
[ "Peptidase_S41", "TSPc" ]
[ 69989, 60131 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21", "R-HSA-2187335", "R-HSA-2453902", "R-MMU-2187335", "R-MMU-2453902" ]
[ "EC:3.4.21", "REACTOME:R-HSA-2187335", "REACTOME:R-HSA-2453902", "REACTOME:R-MMU-2187335", "REACTOME:R-MMU-2453902" ]
5
[ "1fc6", "1fc7", "1fc9", "1fcf", "1j7x", "1k32", "1n6d", "1n6e", "1n6f", "3dja", "3dor", "3dpm", "3dpn", "3k50", "4c2c", "4c2d", "4c2e", "4c2f", "4c2g", "4c2h", "4ghn", "4l8k", "4lur", "4ql6", "4y68", "5wql", "6iqq", "6iqr", "6iqs", "6iqu", "6vbb", "7jti"...
42
[ "PUB00016215", "PUB00057844", "PUB00057845" ]
[ "11719810", "8702985", "1856173" ]
[ "Crystal structure of the tricorn protease reveals a protein disassembly line.", "Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants.", "Cloning, mapping, and characterization of the Escherichia coli prc gene, which is i...
[ 2001, 1996, 1991 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 94, 54929, 14179, 11, 831 ]
5
[ "Arabidopsis thaliana", "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)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 15, 3, 1, 1, 4, 1, 8, 11, 20 ]
9
true
Domain
Tail specific protease
Tail specific protease
Tail-specific_protease
6
IPR005152
5,152
Lipase, secreted
Lipase_secreted
Family
16,288
false
false
This entry represents a family of secreted lipases. Family members include the LIP lipases from Candida albicans, which are expressed and secreted during the infection cycle of these pathogens [ ]. This entry also includes trichothecene C-3 esterase (also known as Tri8) from Fusarium sporotrichioides. It is part of the...
[ "GO:0004806", "GO:0016042" ]
[ "triacylglycerol lipase activity", "lipid catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF03583", "PIRSF029171", "PTHR34853" ]
[ "LIP", "Esterase_LipA", "" ]
[ 13559, 12497, 16131 ]
3
[ "EC", "METACYC" ]
[ "3.1.1.3", "PWY-6857" ]
[ "EC:3.1.1.3", "METACYC:PWY-6857" ]
2
[ "2veo", "3guu", "3h2g", "3h2h", "3h2i", "3h2j", "3h2k", "3zpx", "4ezi", "9jc9", "9jca", "9jcb" ]
12
[ "PUB00008352", "PUB00017111", "PUB00087312", "PUB00088162" ]
[ "11131027", "11352533", "12039755", "27251547" ]
[ "Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members.", "A genetic and biochemical approach to study trichothecene diversity in Fusarium sporotrichioides and Fusarium graminearum.", "Fusarium Tri8 encodes a trichothecene C-3 este...
[ 2000, 2001, 2002, 2016 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 12011, 4150, 127 ]
3
[]
[]
0
true
Family
Lipase, secreted
Lipase, secreted
Lipase_secreted
1
IPR005153
5,153
MbtH-like domain
MbtH-like_dom
Domain
10,721
false
false
This domain is found in the MbtH protein as well as at the N terminus of the antibiotic synthesis protein NIKP1. This domain is about 70 amino acids long and contains 3 fully conserved tryptophan residues. Many of the members of this family are found in known antibiotic synthesis gene clusters.
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF03621", "SM00923" ]
[ "MbtH", "MbtH" ]
[ 10719, 10698 ]
2
[]
[]
[]
0
[ "2gpf", "2khr", "2lpd", "2myy", "2n6g", "2pst", "4gr4", "4gr5", "5ja1", "5ja2", "5u89", "5wmm", "6ea3", "6eby", "6n8e", "8gic", "8gj4", "8gjp", "8gkm", "8glc", "9dvh" ]
21
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Timema poppense", "metagenomes" ]
[ 10715, 1, 5 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
MbtH-like domain
MbtH-like domain
MbtH-like_dom
4