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
IPR008661
8,661
L6 membrane
L6_membrane
Family
5,264
false
false
This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related ...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF05805", "PTHR14198" ]
[ "L6_membrane", "" ]
[ 5264, 5181 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011362", "PUB00011577", "PUB00011578" ]
[ "10975581", "1565644", "9479038" ]
[ "The L6 membrane proteins--a new four-transmembrane superfamily.", "Cloning and expression of the tumor-associated antigen L6.", "Identification of a new tumour-associated antigen TM4SF5 and its expression in human cancer." ]
[ 2000, 1992, 1998 ]
3
[]
[]
0
0
null
[ "Vertebrata" ]
[ 5264 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 16, 9, 16 ]
4
true
Family
L6 membrane
L6 membrane
L6_membrane
6
IPR008662
8,662
Torsin-1A-interacting protein 1/2
TOIP1/2
Family
2,777
false
false
This entry represents Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) also known as LAP1 proteins (Lamina-associated polypeptide 1), which are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane [ , , ]. These proteins interact with and activate Torsin A, an AAA+ ATP...
[ "GO:0001671" ]
[ "ATPase activator activity" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR18843" ]
[ "" ]
[ 2777 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9013405", "R-BTA-9035034", "R-HSA-9013405", "R-HSA-9035034", "R-MMU-9013405", "R-MMU-9035034", "R-RNO-9013405", "R-RNO-9035034" ]
[ "REACTOME:R-BTA-9013405", "REACTOME:R-BTA-9035034", "REACTOME:R-HSA-9013405", "REACTOME:R-HSA-9035034", "REACTOME:R-MMU-9013405", "REACTOME:R-MMU-9035034", "REACTOME:R-RNO-9013405", "REACTOME:R-RNO-9035034" ]
8
[ "4tvs", "5j1s", "5j1t" ]
3
[ "PUB00011363", "PUB00098431", "PUB00098432" ]
[ "12061773", "25149450", "27490483" ]
[ "Molecular cloning of one isotype of human lamina-associated polypeptide 1s and a topological analysis using its deletion mutants.", "How lamina-associated polypeptide 1 (LAP1) activates Torsin.", "Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dy...
[ 2002, 2014, 2016 ]
3
[]
[]
0
0
null
[ "Metazoa", "Pacific salmon nidovirus" ]
[ 2776, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 22, 1, 6, 5, 10 ]
6
true
Family
Torsin-1A-interacting protein 1/2
Torsin-1A-interacting protein 1/2
TOIP1/2
7
IPR008663
8,663
Leukocyte cell-derived chemotaxin 2
LECT2
Family
1,372
false
false
This family consists of several leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown [ ]. It contains an M23 metalloendopeptidase fold, but was found to be catalytically inactive ...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11329" ]
[ "" ]
[ 1372 ]
1
[]
[]
[]
0
[ "5b0h" ]
1
[ "PUB00011365", "PUB00089535" ]
[ "10355968", "27334921" ]
[ "Expression pattern of a newly recognized protein, LECT2, in hepatocellular carcinoma and its premalignant lesion.", "Crystal Structure of Human Leukocyte Cell-derived Chemotaxin 2 (LECT2) Reveals a Mechanistic Basis of Functional Evolution in a Mammalian Protein with an M23 Metalloendopeptidase Fold." ]
[ 1999, 2016 ]
2
[]
[ "IPR017381" ]
0
1
0
[ "Eukaryota", "Pseudomonadati", "metagenomes" ]
[ 1303, 64, 5 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 7, 4, 3, 3 ]
5
true
Family
Leukocyte cell-derived chemotaxin 2
Leukocyte cell-derived chemotaxin 2
LECT2
9
IPR008665
8,665
LRV FeS4 cluster
LRV_FeS
Domain
494
false
false
This iron sulphur cluster is found at the N terminus of some proteins containing leucine-repeat variant (LRV) repeats ( ). These proteins have a two-domain structure, composed of a small N-terminal domain containing a cluster of four Cys residues that houses the 4Fe:4S cluster, and a larger C-terminal domain containing...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05484" ]
[ "LRV_FeS" ]
[ 494 ]
1
[]
[]
[]
0
[ "1lrv" ]
1
[ "PUB00003936" ]
[ "8946850" ]
[ "A leucine-rich repeat variant with a novel repetitive protein structural motif." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Bacteria", "unclassified sequences" ]
[ 486, 8 ]
2
[]
[]
0
true
Domain
LRV FeS4 cluster
LRV FeS4 cluster
LRV_FeS
2
IPR008668
8,668
Virion infectivity factor, Lentivirus
Vir_infectivity_fact_Lentivir
Family
157
false
false
This family consists of several feline-specific Lentivirus virion infectivity factor (VIF) proteins. VIF is essential for productive Feline immunodeficiency virus infection of host target cells in vitro [ ].
[ "GO:0019058" ]
[ "viral life cycle" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05851" ]
[ "Lentivirus_VIF" ]
[ 157 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011368" ]
[ "10441553" ]
[ "The feline immunodeficiency virus vif gene is required for productive infection of feline peripheral blood mononuclear cells and monocyte-derived macrophages." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Lentivirus" ]
[ 157 ]
1
[]
[]
0
true
Family
Virion infectivity factor, Lentivirus
Virion infectivity factor, Lentivirus
Vir_infectivity_fact_Lentivir
6
IPR008669
8,669
LSM-interacting domain
LSM_interact
Domain
1,477
false
false
This short motif is found at the C terminus of Prp24 protein, Spliceosome associated factor 3, U4/U6 recycling protein (SART3) and their Drosophila orthologue, the RNA-binding protein 4F. It probably interacts with the Lsm proteins to promote U4/U6 formation [ ]. Prp24 is an RNA-binding protein with four well conserved...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05391" ]
[ "Lsm_interact" ]
[ 1477 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-SPO-72163", "R-SPO-72203" ]
[ "REACTOME:R-SPO-72163", "REACTOME:R-SPO-72203" ]
2
[ "5vsu", "6aso" ]
2
[ "PUB00011369", "PUB00056283", "PUB00065995", "PUB00082867", "PUB00082892", "PUB00082893", "PUB00082895", "PUB00082896", "PUB00083474" ]
[ "12458792", "21653550", "20181740", "11477570", "12578909", "11959860", "15314151", "10463607", "15811912" ]
[ "A conserved Lsm-interaction motif in Prp24 required for efficient U4/U6 di-snRNP formation.", "A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.", "Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24.", "Binding of ...
[ 2002, 2011, 2010, 2001, 2003, 2002, 2004, 1999, 2005 ]
9
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1477 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 9, 1, 2, 3, 1, 3, 1, 1 ]
8
true
Domain
LSM-interacting domain
LSM-interacting domain
LSM_interact
4
IPR008670
8,670
Long-chain-fatty-acyl-CoA reductase, LuxC
CoA_reduct_LuxC
Family
4,023
false
false
This family consists of several bacterial Acyl-CoA reductase (also known as long-chain-fatty-acyl-CoA reductase) LuxC proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalysed by a fatty acid reductase multienzyme complex, which channels fatty aci...
[ "GO:0003995", "GO:0008218" ]
[ "acyl-CoA dehydrogenase activity", "bioluminescence" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "CDD" ]
[ "PF05893", "PIRSF009414", "cd07080" ]
[ "LuxC", "LuxC", "ALDH_Acyl-CoA-Red_LuxC" ]
[ 4023, 671, 792 ]
3
[ "EC", "METACYC" ]
[ "1.2.1.50", "PWY-7723" ]
[ "EC:1.2.1.50", "METACYC:PWY-7723" ]
2
[ "7xc6" ]
1
[ "PUB00011370", "PUB00028002" ]
[ "9128139", "2030669" ]
[ "Cysteine-286 as the site of acylation of the Lux-specific fatty acyl-CoA reductase.", "Molecular biology of bacterial bioluminescence." ]
[ 1997, 1991 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Linnemannia gamsii", "metagenomes" ]
[ 37, 3943, 1, 42 ]
4
[]
[]
0
true
Family
Long-chain-fatty-acyl-CoA reductase, LuxC
Long-chain-fatty-acyl-CoA reductase, LuxC
CoA_reduct_LuxC
4
IPR008672
8,672
Spindle assembly checkpoint component Mad1
Mad1
Family
5,142
false
false
This family consists of pindle assembly checkpoint protein Mad1. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint hav...
[ "GO:0007094" ]
[ "mitotic spindle assembly checkpoint signaling" ]
[ "biological_process" ]
1
[ "PFAM", "PANTHER" ]
[ "PF05557", "PTHR23168" ]
[ "MAD", "" ]
[ 4817, 4946 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-141444", "R-HSA-2467813", "R-HSA-2500257", "R-HSA-5663220", "R-HSA-68877", "R-HSA-9648025", "R-MMU-141444", "R-MMU-2467813", "R-MMU-2500257", "R-MMU-5663220", "R-MMU-68877", "R-MMU-9648025" ]
[ "REACTOME:R-HSA-141444", "REACTOME:R-HSA-2467813", "REACTOME:R-HSA-2500257", "REACTOME:R-HSA-5663220", "REACTOME:R-HSA-68877", "REACTOME:R-HSA-9648025", "REACTOME:R-MMU-141444", "REACTOME:R-MMU-2467813", "REACTOME:R-MMU-2500257", "REACTOME:R-MMU-5663220", "REACTOME:R-MMU-68877", "REACTOME:R-MM...
12
[ "1go4", "4dzo", "7b1f", "7b1h", "7b1j" ]
5
[ "PUB00011371" ]
[ "12574116" ]
[ "Mad2 phosphorylation regulates its association with Mad1 and the APC/C." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halorubrum pallidum", "Streptococcus phage MM1" ]
[ 8, 5132, 1, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 3, 2, 7, 2, 1, 3, 4, 1, 2, 19 ]
12
true
Family
Spindle assembly checkpoint component Mad1
Spindle assembly checkpoint component Mad1
Mad1
6
IPR008674
8,674
Chromosomal protein MC1
MC1
Family
545
false
false
This entry represents the chromosomal protein MC1, which protects DNA against thermal denaturation and shapes DNA by binding to it [ , ]. Its global fold consists of a pseudo barrel with an extension of the β-sheet (beta4-beta5) forming an arm (LP5) [ ]. Some uncharacterised virus proteins are also included in this ent...
[ "GO:0042262" ]
[ "DNA protection" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05854" ]
[ "MC1" ]
[ 545 ]
1
[]
[]
[]
0
[ "1t23", "2khl", "2nbj" ]
3
[ "PUB00011373", "PUB00086556", "PUB00086557" ]
[ "2503033", "24558431", "25212183" ]
[ "Primary structure of the chromosomal protein MC1 from the archaebacterium Methanosarcina sp. CHTI 55.", "Model of a DNA-protein complex of the architectural monomeric protein MC1 from Euryarchaea.", "Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex...
[ 1989, 2014, 2015 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "ecological metagenomes" ]
[ 519, 3, 2, 14, 7 ]
5
[]
[]
0
true
Family
Chromosomal protein MC1
Chromosomal protein MC1
MC1
2
IPR008675
8,675
Mating factor alpha precursor, N-terminal
Mating_factor_alpha_N
Domain
209
false
false
This entry contains the N-terminal regions of the Saccharomyces mating factor alpha precursor protein. All proteins in this family contain one or more copies of further toward their C terminus.
[ "GO:0007618", "GO:0005576" ]
[ "mating", "extracellular region" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05436" ]
[ "MF_alpha_N" ]
[ 209 ]
1
[]
[]
[]
0
[ "6krl", "6krn", "7aft", "7xoi", "8s2y", "9l3d", "9l3j", "9l3o", "9l3p" ]
9
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Eukaryota" ]
[ 209 ]
1
[ "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 1, 2 ]
2
true
Domain
Mating factor alpha precursor, N-terminal
Mating factor alpha precursor, N-terminal
Mating_factor_alpha_N
4
IPR008676
8,676
MRG
MRG
Family
9,101
false
false
This entry represents MRG protein family, whose members include MORF4L1/2 (MRG15/MRGX) and MSL3L1/2 from humans, ESA1-associated factor 3 (Eaf3) from yeasts and male-specific lethal 3 (MSL3) from flies. They contain an N-terminal chromodomain that binds H3K36me3, a histone mark associated with transcription elongation ...
[ "GO:0006325", "GO:0006355", "GO:0005634" ]
[ "chromatin organization", "regulation of DNA-templated transcription", "nucleus" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PIRSF", "PANTHER" ]
[ "PIRSF038133", "PTHR10880" ]
[ "HAT_Nua4_EAF3/MRG15", "" ]
[ 3948, 9101 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-3214847", "R-HSA-3214847", "R-MMU-3214847" ]
[ "REACTOME:R-DME-3214847", "REACTOME:R-HSA-3214847", "REACTOME:R-MMU-3214847" ]
3
[ "2aql", "2efi", "2f5j", "2f5k", "2k3x", "2k3y", "2lkm", "2lrq", "2n1d", "2y0n", "3e9f", "3e9g", "3m9q", "3oa6", "3ob9", "4pl6", "4pli", "4pll", "5in1", "6ago", "6ine", "6k5w", "7s4a", "7yi0", "7yi1", "7yi2", "7yi3", "7yi4", "7yi5", "8bpa", "8c60", "8hxx"...
55
[ "PUB00017120", "PUB00035439", "PUB00060508", "PUB00060510", "PUB00060511", "PUB00060512", "PUB00074561", "PUB00074562", "PUB00074563", "PUB00074565" ]
[ "12773392", "14966270", "20332121", "2662307", "16364921", "20536842", "17173057", "22421046", "20657587", "22285924" ]
[ "Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity.", "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans.", "MRG15 binds directly to PALB2 and stimulates homology-directed repair of chromo...
[ 2003, 2004, 2010, 1989, 2005, 2010, 2007, 2012, 2010, 2012 ]
10
[]
[]
0
0
null
[ "Eukaryota", "Parachitinimonas caeni" ]
[ 9100, 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...
[ 9, 3, 2, 5, 36, 17, 2, 10, 26, 1, 1, 9 ]
12
true
Family
MRG
MRG
MRG
6
IPR008677
8,677
MRVI1
MRVI1
Family
3,723
false
false
This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expressi...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05781", "PTHR15352" ]
[ "MRVI1", "" ]
[ 3458, 3674 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-418457", "R-HSA-6798695", "R-MMU-418457" ]
[ "REACTOME:R-HSA-418457", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-418457" ]
3
[ "7z8y", "8b46", "8b5x" ]
3
[ "PUB00011374", "PUB00011375", "PUB00011376", "PUB00094245" ]
[ "10321731", "10724174", "8021504", "16990611" ]
[ "Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a protein with homology to a lymphoid-restricted membrane protein Jaw1.", "Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta.", "Jaw1, A lymphoid-restricted membrane protein localized t...
[ 1999, 2000, 1994, 2007 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2, 3721 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 44, 15, 18, 10 ]
4
true
Family
MRVI1
MRVI1
MRVI1
2
IPR008680
8,680
Mastadenovirus early E4 13kDa
M_adenovirusE4
Family
225
false
false
This family consists of Homo sapiens and simian mastadenovirus early E4 13kDa proteins. Human adenovirus 9 (HAdV-9) is unique in eliciting exclusively estrogen-dependent mammary tumours in Rattus spp. and in not requiring viral E1 region transforming genes for tumorigenicity. E4 codes for an oncoprotein essential for t...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05385" ]
[ "Adeno_E4" ]
[ 225 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011378" ]
[ "11134268" ]
[ "Several E4 region functions influence mammary tumorigenesis by human adenovirus type 9." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Mastadenovirus" ]
[ 225 ]
1
[]
[]
0
true
Family
Mastadenovirus early E4 13kDa
Mastadenovirus early E4 13kDa
M_adenovirusE4
2
IPR008681
8,681
Negative regulator of genetic competence, MecA
Neg-reg_MecA
Family
4,653
false
false
Competence is the ability of a cell to take up exogenous DNA from its environment, resulting in transformation. It is widespread among bacteria and is probably an important mechanism for the horizontal transfer of genes. DNA usually becomes available by the death and lysis of other cells. Competent bacteria use compone...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PIRSF", "PANTHER" ]
[ "MF_01124", "PF05389", "PIRSF029008", "PTHR39161" ]
[ "MecA", "MecA", "MecA", "" ]
[ 2796, 4653, 3732, 4553 ]
4
[]
[]
[]
0
[ "2mk6", "2y1r", "3j3r", "3j3s", "3j3t", "3j3u", "3jtn", "3jto", "3jtp", "3pxg", "3pxi", "6emw", "9goq", "9rai" ]
14
[ "PUB00011574", "PUB00011575", "PUB00011576", "PUB00052316" ]
[ "11004200", "12028382", "8412687", "8901420" ]
[ "Identification in Listeria monocytogenes of MecA, a homologue of the Bacillus subtilis competence regulatory protein.", "Spx (YjbD), a negative effector of competence in Bacillus subtilis, enhances ClpC-MecA-ComK interaction.", "Sequence and properties of mecA, a negative regulator of genetic competence in Bac...
[ 2000, 2002, 1993, 1996 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 4641, 2, 10 ]
3
[]
[]
0
true
Family
Negative regulator of genetic competence, MecA
Negative regulator of genetic competence, MecA
Neg-reg_MecA
5
IPR008685
8,685
Centromere protein Mis12
Centromere_Mis12
Family
3,655
false
false
Kinetochores are the chromosomal sites for spindle interaction and play a vital role for chromosome segregation. Fission Saccharomyces cerevisiae kinetochore protein Mis12, is required for correct spindle morphogenesis, determining metaphase spindle length [ ]. Thirty-five to sixty percent extension of metaphase spindl...
[ "GO:0000278", "GO:0000775", "GO:0005634" ]
[ "mitotic cell cycle", "chromosome, centromeric region", "nucleus" ]
[ "biological_process", "cellular_component", "cellular_component" ]
3
[ "PFAM", "PANTHER" ]
[ "PF05859", "PTHR14527" ]
[ "Mis12", "" ]
[ 3639, 3474 ]
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-141444", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-5663220", "R-BTA-68877", "R-BTA-9648025", "R-HSA-141444", "R-HSA-2467813", "R-HSA-2500257", "R-HSA-5663220", "R-HSA-68877", "R-HSA-9648025", "R-MMU-141444", "R-MMU-2467813", "R-MMU-2500257", "R-MMU-5663220", "R-MMU-68877", "R...
[ "REACTOME:R-BTA-141444", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-5663220", "REACTOME:R-BTA-68877", "REACTOME:R-BTA-9648025", "REACTOME:R-HSA-141444", "REACTOME:R-HSA-2467813", "REACTOME:R-HSA-2500257", "REACTOME:R-HSA-5663220", "REACTOME:R-HSA-68877", "REACTOME:R-HS...
24
[ "5lsj", "5lsk", "5t51", "5t58", "5t59", "5wwl", "8ppr", "8q5h" ]
8
[ "PUB00011382", "PUB00011383" ]
[ "10398680", "12242294" ]
[ "Proper metaphase spindle length is determined by centromere proteins Mis12 and Mis6 required for faithful chromosome segregation.", "The mal2p protein is an essential component of the fission yeast centromere." ]
[ 1999, 2002 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 9, 3646 ]
2
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (st...
[ 2, 1, 3, 1, 1, 2, 2, 1, 1, 10 ]
10
true
Family
Centromere protein Mis12
Centromere protein Mis12
Centromere_Mis12
7
IPR008686
8,686
RNA-dependent RNA polymerase, mitoviral
RNA_pol_mitovir
Family
1,637
false
false
This family consists of several Mitovirus RNA-dependent RNA polymerase proteins. The family also contains fragment matches in the mitochondria of Arabidopsis thaliana [ ].
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05919", "PTHR34456" ]
[ "Mitovir_RNA_pol", "" ]
[ 1588, 1312 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011573" ]
[ "9657003" ]
[ "Evolutionary relationships among putative RNA-dependent RNA polymerases encoded by a mitochondrial virus-like RNA in the Dutch elm disease fungus, Ophiostoma novo-ulmi, by other viruses and virus-like RNAs and by the Arabidopsis mitochondrial genome." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Eukaryota", "Riboviria", "Roseicella aquatilis", "unclassified sequences" ]
[ 705, 906, 2, 24 ]
4
[ "Arabidopsis thaliana" ]
[ 12 ]
1
true
Family
RNA-dependent RNA polymerase, mitoviral
RNA-dependent RNA polymerase, mitoviral
RNA_pol_mitovir
4
IPR008687
8,687
Bacterial mobilisation
MobC
Domain
3,273
false
false
This family consists of several bacterial MobC-like, mobilisation proteins. MobC proteins belong to the group of relaxases. Together with MobA and MobB they bind to a single cis-active site of a mobilising plasmid, the origin of transfer (oriT) region [ ]. The absence of MobC has several different effects on oriT DNA. ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05713" ]
[ "MobC" ]
[ 3273 ]
1
[]
[]
[]
0
[ "6qeq" ]
1
[ "PUB00011384", "PUB00011385" ]
[ "11976306", "9302013" ]
[ "Characterization of two cryptic Helicobacter pylori plasmids: a putative source for horizontal gene transfer and gene shuffling.", "The relaxosome protein MobC promotes conjugal plasmid mobilization by extending DNA strand separation to the nick site at the origin of transfer." ]
[ 2002, 1997 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "plasmids", "unclassified sequences" ]
[ 3227, 4, 3, 39 ]
4
[]
[]
0
true
Domain
Bacterial mobilisation
Bacterial mobilisation
MobC
6
IPR008688
8,688
ATP synthase, F0 complex, subunit B/MI25
ATP_synth_Bsub_B/MI25
Family
5,842
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0015078", "GO:0015986" ]
[ "proton transmembrane transporter activity", "proton motive force-driven ATP synthesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF05405" ]
[ "Mt_ATP-synt_B" ]
[ 5842 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-163210", "R-BTA-8949613", "R-CEL-163210", "R-CEL-8949613", "R-DME-163210", "R-DME-8949613", "R-HSA-163210", "R-HSA-8949613", "R-MMU-163210", "R-MMU-8949613", "R-RNO-163210", "R-RNO-8949613" ]
[ "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-8949613", "REACTOME:R-DME-163210", "REACTOME:R-DME-8949613", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-RNO-163210", "REACTOME:R-RN...
12
[ "2cly", "2wss", "4b2q", "5ara", "5are", "5arh", "5ari", "5fij", "5fik", "5fil", "5lqx", "5lqy", "5lqz", "6b2z", "6b8h", "6cp3", "6cp5", "6cp6", "6cp7", "6j54", "6j5a", "6j5i", "6j5j", "6j5k", "6tt7", "6wtd", "6yy0", "6z1r", "6z1u", "6za9", "6zbb", "6ziq"...
102
[ "PUB00009752", "PUB00016657", "PUB00020603", "PUB00020604", "PUB00020607", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789", "PUB00081956" ]
[ "11309608", "12681508", "15473999", "15078220", "16045926", "20450191", "18937357", "1385979", "9741106", "22864911" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/A...
[ 2001, 2003, 2004, 2004, 2005, 2010, 2008, 1992, 1998, 2012 ]
10
[]
[ "IPR013837", "IPR044988" ]
0
2
0
[ "Bacteria", "Eukaryota", "bioreactor metagenome" ]
[ 9, 5832, 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...
[ 3, 2, 1, 1, 5, 6, 1, 4, 7, 1, 1, 8 ]
12
true
Family
ATP synthase, F0 complex, subunit B/MI25
ATP synthase, F0 complex, subunit B/MI25
ATP_synth_Bsub_B/MI25
8
IPR008689
8,689
ATP synthase, F0 complex, subunit D, mitochondrial
ATP_synth_F0_dsu_mt
Family
4,898
false
false
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ...
[ "GO:0015078", "GO:0015986" ]
[ "proton transmembrane transporter activity", "proton motive force-driven ATP synthesis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF05873", "PIRSF005514", "PTHR12700" ]
[ "Mt_ATP-synt_D", "ATPase_F0_D_mt", "" ]
[ 4808, 3603, 4603 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-163210", "R-BTA-8949613", "R-BTA-9837999", "R-DME-163210", "R-DME-8949613", "R-DME-9837999", "R-HSA-163210", "R-HSA-8949613", "R-HSA-9837999", "R-MMU-163210", "R-MMU-8949613", "R-MMU-9837999", "R-RNO-163210", "R-RNO-8949613", "R-RNO-9837999", "R-SCE-9837999", "R-SPO-9837999" ]
[ "REACTOME:R-BTA-163210", "REACTOME:R-BTA-8949613", "REACTOME:R-BTA-9837999", "REACTOME:R-DME-163210", "REACTOME:R-DME-8949613", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-163210", "REACTOME:R-HSA-8949613", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-163210", "REACTOME:R-MMU-8949613", "REACTOME:R-...
17
[ "2cly", "2wss", "4b2q", "5ara", "5are", "5arh", "5ari", "5fij", "5fik", "5fil", "5lqx", "5lqy", "5lqz", "6b2z", "6b8h", "6cp3", "6cp5", "6cp6", "6cp7", "6j54", "6j5a", "6j5i", "6j5j", "6j5k", "6tt7", "6wtd", "6ynx", "6yny", "6ynz", "6yo0", "6yy0", "6za9"...
104
[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020607", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]
[ "11309608", "15473999", "15078220", "16045926", "20450191", "18937357", "1385979", "9741106" ]
[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "Structure of the F1-binding...
[ 2001, 2004, 2004, 2005, 2010, 2008, 1992, 1998 ]
8
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4898 ]
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, 1, 1, 4, 3, 2, 1, 2, 9, 1, 1, 7 ]
12
true
Family
ATP synthase, F0 complex, subunit D, mitochondrial
ATP synthase, F0 complex, subunit D, mitochondrial
ATP_synth_F0_dsu_mt
3
IPR008690
8,690
Tetrahydromethanopterin S-methyltransferase subunit B
MtrB_MeTrfase
Family
223
false
false
Members of this protein family are the MtrB protein of the tetrahydromethanopterin S-methyltransferase complex. This system is universal in archaeal methanogens [ ]. The N5-methyltetrahydromethanopterin: coenzyme M ( ) of Methanosarcina mazei Go1 is a membrane-associated, corrinoid-containing protein that uses a transm...
[ "GO:0030269", "GO:0015948", "GO:0016020" ]
[ "tetrahydromethanopterin S-methyltransferase activity", "methanogenesis", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PIRSF", "NCBIFAM" ]
[ "MF_01094", "PF05440", "PIRSF005518", "TIGR04166" ]
[ "MtrB", "MtrB", "MtrB", "methano_MtrB" ]
[ 197, 223, 215, 221 ]
4
[ "EC", "GP", "GP" ]
[ "7.2.1.4", "GenProp0288", "GenProp0722" ]
[ "EC:7.2.1.4", "GP:GenProp0288", "GP:GenProp0722" ]
3
[ "8q3v", "8q54" ]
2
[ "PUB00005738", "PUB00009902" ]
[ "7737157", "9559648" ]
[ "The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits.", "Cloning, sequencing and expression of the genes encoding the sodium translocating N5-methyltetrahydromethanopterin : coenzyme M methylt...
[ 1995, 1998 ]
2
[]
[]
0
0
null
[ "Archaea", "ecological metagenomes" ]
[ 218, 5 ]
2
[]
[]
0
true
Family
Tetrahydromethanopterin S-methyltransferase subunit B
Tetrahydromethanopterin S-methyltransferase subunit B
MtrB_MeTrfase
9
IPR008691
8,691
19kDa lipoprotein antigen
LpqH
Family
1,805
false
false
Most of the antigens of Mycobacterium leprae and Mycobacterium tuberculosis that have been identified are members of stress protein families, which are highly conserved throughout many diverse species. Of the M. leprae and M. tuberculosis antigens identified by monoclonal antibodies, all except the 18kDa M. leprae anti...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF05481" ]
[ "Myco_19_kDa" ]
[ 1805 ]
1
[]
[]
[]
0
[ "4xin", "4zjm", "7fds" ]
3
[ "PUB00011569", "PUB00011570" ]
[ "8454357", "2230723" ]
[ "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium tuberculosis 19-kilodalton antigens in other mycobacteria.", "Cloning and characterization of the gene for the '19 kDa' antigen of Mycobacterium bovis." ]
[ 1993, 1990 ]
2
[]
[]
0
0
null
[ "Bacillati" ]
[ 1805 ]
1
[]
[]
0
true
Family
19kDa lipoprotein antigen
19kDa lipoprotein antigen
LpqH
4
IPR008692
8,692
Haemagglutinin, Mycoplasma
Hemogglutn_Mycoplasma
Domain
317
false
false
This family consists of several haemagglutinin sequences from Mycoplasma gallisepticum. The major plasma membrane proteins, pMGAs, of Mycoplasma gallisepticum are cell adhesin (hemagglutinin) molecules. It has been shown that the genetic determinants that code for the haemagglutinins are organised into a large family o...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05692" ]
[ "Myco_haema" ]
[ 317 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011564", "PUB00011565" ]
[ "9784576", "7925999" ]
[ "A protein (M9) associated with monoclonal antibody-mediated agglutination of Mycoplasma gallisepticum is a member of the pMGA family.", "The organisation of the multigene family which encodes the major cell surface protein, pMGA, of Mycoplasma gallisepticum." ]
[ 1998, 1994 ]
2
[]
[]
0
0
null
[ "Loa loa", "Mycoplasmatota" ]
[ 1, 316 ]
2
[]
[]
0
true
Domain
Haemagglutinin, Mycoplasma
Haemagglutinin, Mycoplasma
Hemogglutn_Mycoplasma
5
IPR008693
8,693
Transport accessory protein MmpS
MmpS
Family
5,202
false
false
This entry represents a group of putative transport accessory proteins, including MmpS1-5 from Mycobacterium tuberculosis [ ] and Divisome factor lamA. MmpS1-S5 and IamA are part of an export system required for biosynthesis and secretion of siderophores and are essential for virulence of Mycobacterium tuberculosis [ ]...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05423" ]
[ "Mycobact_memb" ]
[ 5202 ]
1
[]
[]
[]
0
[ "2lw3", "8em5", "8zkp", "8zkq", "9mvz", "9rfu", "9rgb" ]
7
[ "PUB00011563", "PUB00066028" ]
[ "11891304", "23431276" ]
[ "A new evolutionary scenario for the Mycobacterium tuberculosis complex.", "Discovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosis." ]
[ 2002, 2013 ]
2
[]
[]
0
0
null
[ "Bacteria", "Gordonia phage Walrus", "marine sediment metagenome" ]
[ 5200, 1, 1 ]
3
[]
[]
0
true
Family
Transport accessory protein MmpS
Transport accessory protein MmpS
MmpS
5
IPR008698
8,698
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7
NDUB7
Family
3,492
false
false
This family consists of the accessory subunit of complex I NADH-ubiquinone oxidoreductase NDUB7 (or NDUFB7, also known as B18), which is not involved in catalysis [ , ].
[ "GO:0005739" ]
[ "mitochondrion" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF05676", "PTHR20900" ]
[ "NDUF_B7", "" ]
[ 3456, 3334 ]
2
[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1230", "GenProp1637", "R-BTA-611105", "R-BTA-6799198", "R-HSA-611105", "R-HSA-6799198", "R-MMU-611105", "R-MMU-6799198" ]
[ "GP:GenProp1230", "GP:GenProp1637", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-6799198" ]
8
[ "5gup", "5lc5", "5ldw", "5ldx", "5lnk", "5o31", "5xtc", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6gcs", "6q9b", "6qa9", "6qbx", "6qc2", "6qc3", "6qc4", "6qc5", "6qc6", "6qc7", "6qc8", "6qc9", "6qca", "6qcf", "6rfq", "6rfr", "6rfs", "6y79", "6yj4", "6zka"...
246
[ "PUB00005074", "PUB00043561", "PUB00045437", "PUB00086570", "PUB00097152" ]
[ "1470679", "10940377", "18394423", "27626371", "31485716" ]
[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.", "Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).", "Accessory subunits are in...
[ 1992, 2000, 2008, 2016, 2020 ]
5
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3492 ]
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", "Zea mays" ]
[ 2, 3, 1, 1, 1, 1, 1, 5, 2, 2 ]
10
true
Family
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7
NDUB7
3
IPR008699
8,699
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8
NDUFB8
Family
3,369
false
false
This family consists of several eukaryotic NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 proteins. NADH:ubiquinone oxidoreductase (complex I) is an extremely complicated multiprotein complex located in the inner mitochondrial membrane. Its main function is the transport of electrons from NADH to ubiquinon...
[ "GO:0005739" ]
[ "mitochondrion" ]
[ "cellular_component" ]
1
[ "PFAM", "PANTHER" ]
[ "PF05821", "PTHR12840" ]
[ "NDUF_B8", "" ]
[ 3270, 3265 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-1268020", "R-BTA-611105", "R-BTA-6799198", "R-HSA-1268020", "R-HSA-611105", "R-HSA-6799198", "R-MMU-1268020", "R-MMU-611105", "R-MMU-6799198" ]
[ "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-6799198", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-MMU-1268020", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-6799198" ]
9
[ "5gup", "5lnk", "5xtc", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6q9b", "6qa9", "6qbx", "6qc2", "6qc3", "6qc4", "6qc5", "6qc6", "6qc7", "6qc8", "6qc9", "6qca", "6qcf", "6rfq", "6rfr", "6rfs", "6y79", "6yj4", "6zka", "6zkb", "6zkc", "6zkd", "6zke", "6zkf"...
222
[ "PUB00011390", "PUB00086570", "PUB00097152" ]
[ "9878551", "27626371", "31485716" ]
[ "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed.", "Accessory subunits are integral for assembly and function of human mitochondrial complex I.", "Insights from Drosophila on mitochondrial complex I." ]
[ 1998, 2016, 2020 ]
3
[]
[ "IPR016551" ]
0
1
0
[ "Eukaryota", "Runella salmonicolor" ]
[ 3368, 1 ]
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" ]
[ 2, 1, 3, 4, 5, 1, 4 ]
7
true
Family
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8
NDUFB8
3
IPR008700
8,700
RIN4, pathogenic type III effector avirulence factor Avr cleavage site
TypeIII_avirulence_cleave
Domain
6,533
false
false
This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found in the plant RIN4 (RPM1-interacting protein 4) where it appears to contribute to the binding of the protein to RCS (AvrRpt2 auto-cleavage sit...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05627" ]
[ "AvrRpt-cleavage" ]
[ 6533 ]
1
[]
[]
[]
0
[ "2nud", "8two", "8tws", "8txf" ]
4
[ "PUB00043295", "PUB00045050" ]
[ "15845764", "16478045" ]
[ "The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation.", "Membrane release and destabilization of Arabidopsis RIN4 following cleavage by Pseudomonas syringae AvrRpt2." ]
[ 2005, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria", "Embryophyta" ]
[ 2, 6531 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 67, 50, 75 ]
3
true
Domain
RIN4, pathogenic type III effector avirulence factor Avr cleavage site
RIN4, pathogenic type III effector avirulence factor Avr cleavage site
TypeIII_avirulence_cleave
1
IPR008701
8,701
Necrosis inducing protein
NPP1
Family
6,102
false
false
This family consists of several NPP1-like necrosis inducing proteins from oomycetes, fungi and bacteria. Infiltration of NPP1 into leaves of Arabidopsis thaliana plants result in transcript accumulation of pathogenesis-related (PR) genes, production of ROS and ethylene, callose apposition, and HR-like cell death [ ]. M...
[]
[]
[]
0
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF05630", "PIRSF029958", "PTHR33657" ]
[ "NPP1", "Necrosis-inducing_protein", "" ]
[ 6095, 4173, 5655 ]
3
[]
[]
[]
0
[ "3gnu", "3gnz", "3st1", "5nnw", "5no9", "6qbd", "6qbe", "9wsc" ]
8
[ "PUB00011391", "PUB00101908" ]
[ "12410815", "35152834" ]
[ "NPP1, a Phytophthora-associated trigger of plant defense in parsley and Arabidopsis.", "Functional analysis of the Nep1-like proteins from <i>Plasmopara viticola</i>." ]
[ 2002, 2022 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Argoarchaeum ethanivorans", "Eukaryota", "marine sediment metagenome" ]
[ 1440, 2, 4659, 1 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Family
Necrosis inducing protein
Necrosis inducing protein
NPP1
7
IPR008702
8,702
Nucleopolyhedrovirus P10
NPV_P10
Family
176
false
false
This family consists of several nucleopolyhedrovirus P10 proteins which play a role in the proper virion occlusion of the polyhedra and is involved in the liberation of polyhedra from infected insect cells [ , ].
[ "GO:0039679" ]
[ "viral occlusion body" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF05531" ]
[ "NPV_P10" ]
[ 176 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011392", "PUB00096305" ]
[ "9634101", "19264658" ]
[ "The single-nucleocapsid nucleopolyhedrovirus of Buzura suppressaria encodes a P10 protein.", "Characterization of a virion occlusion-defective Autographa californica multiple nucleopolyhedrovirus mutant lacking the p26, p10 and p74 genes." ]
[ 1998, 2009 ]
2
[]
[]
0
0
null
[ "Bacteria", "Baculoviridae", "Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)" ]
[ 36, 139, 1 ]
3
[]
[]
0
true
Family
Nucleopolyhedrovirus P10
Nucleopolyhedrovirus P10
NPV_P10
2
IPR008703
8,703
Na(+)-translocating NADH-quinone reductase subunit A
NqrA
Family
4,727
false
false
This family consists of several bacterial Na + -translocating NADH-quinone reductase subunit A (NQRA) proteins. The Na + -translocating NADH: ubiquinone oxidoreductase (Na + -NQR) generates an electrochemical Na + potential driven by aerobic respiration [ ].
[ "GO:0016655", "GO:0006814" ]
[ "oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor", "sodium ion transport" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00425", "PTHR37839", "TIGR01936" ]
[ "NqrA", "", "nqrA" ]
[ 4450, 4727, 4428 ]
3
[ "EC", "GP" ]
[ "7.2.1.1", "GenProp0129" ]
[ "EC:7.2.1.1", "GP:GenProp0129" ]
2
[ "4u9o", "4u9q", "7xk3", "7xk4", "7xk5", "7xk6", "7xk7", "8a1t", "8a1u", "8a1v", "8a1w", "8a1x", "8a1y", "8acw", "8acy", "8ad0", "8evu", "8ew3", "9lrr", "9u5g", "9ud2", "9ud3", "9ud4", "9ud5", "9ud6", "9ud8", "9ud9", "9uda", "9udf", "9udg", "9uuu" ]
31
[ "PUB00011393" ]
[ "10587447" ]
[ "Sequencing and preliminary characterization of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio harveyi." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 4611, 10, 106 ]
3
[]
[]
0
true
Family
Na(+)-translocating NADH-quinone reductase subunit A
Na(+)-translocating NADH-quinone reductase subunit A
NqrA
3
IPR008704
8,704
Zinc-binding loop region of homing endonuclease
Endonuclease_Zinc-binding_loop
Domain
501
false
false
This domain [ ] is the short zinc-binding loops region of a number of much longer chain homing endonucleases. Such loops are probably stabilised by the zinc and may be viewed as small but separate domains. The common structural feature of these domains is that at least three zinc ligands lie very close to each other in...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05551" ]
[ "zf-His_Me_endon" ]
[ 501 ]
1
[]
[]
[]
0
[ "1a73", "1a74", "1cz0", "1evw", "1evx", "1ipp", "8vmo", "8vmp", "8vmq", "8vmr", "8vms", "8vmt", "8vmu", "8vmv", "8vmw", "8vmx", "8vmy", "8vmz", "8vn0", "8vn1", "8vn2", "8vn3", "8vn4", "8vn5", "8vn6", "8vn7", "8vn8", "8vn9", "8vna", "8vnb", "8vnc", "8vnd"...
46
[ "PUB00028315", "PUB00053732" ]
[ "10581547", "12527760" ]
[ "A novel endonuclease mechanism directly visualized for I-PpoI.", "Structural classification of zinc fingers: survey and summary." ]
[ 1999, 2003 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "organismal metagenomes" ]
[ 21, 452, 23, 5 ]
4
[]
[]
0
true
Domain
Zinc-binding loop region of homing endonuclease
Zinc-binding loop region of homing endonuclease
Endonuclease_Zinc-binding_loop
8
IPR008705
8,705
Nanos/Xcat2
Nanos/Xcar2
Family
2,963
false
false
In Drosophila melanogaster, Nanos functions as a localised determinant of posterior pattern. Nanos RNA is localised to the posterior pole of the maturing egg cell and encodes a protein that emanates from this localised source. Nanos acts as a translational repressor and thereby establishes a gradient of the morphogen H...
[ "GO:0003723", "GO:0008270" ]
[ "RNA binding", "zinc ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PANTHER" ]
[ "PTHR12887" ]
[ "" ]
[ 2963 ]
1
[ "REACTOME" ]
[ "R-HSA-9827857" ]
[ "REACTOME:R-HSA-9827857" ]
1
[ "3alr", "5kl1", "5kl8" ]
3
[ "PUB00011394", "PUB00011395", "PUB00055538" ]
[ "7601003", "8223259", "20948543" ]
[ "nanos is an evolutionarily conserved organizer of anterior-posterior polarity.", "A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a protein with a nanos-like zinc finger domain.", "Crystal structure of zinc-finger domain of Nanos and its functional implications." ]
[ 1995, 1993, 2010 ]
3
[]
[]
0
0
null
[ "Metazoa", "viral metagenome" ]
[ 2953, 10 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 10, 4, 5, 5 ]
6
true
Family
Nanos/Xcat2
Nanos/Xcat2
Nanos/Xcar2
8
IPR008706
8,706
Nanovirus component 8
Nanovirus_C8
Family
185
false
false
This family consists of a group of 17.4kDa nanovirus proteins which are highly related to the Faba bean necrotic yellows virus component 8 protein whose function is unknown [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF05629" ]
[ "Nanovirus_C8" ]
[ 185 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011396" ]
[ "9880028" ]
[ "Ten distinct circular ssDNA components, four of which encode putative replication-associated proteins, are associated with the faba bean necrotic yellows virus genome." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Camellia lanceoleosa", "Nanoviridae" ]
[ 1, 184 ]
2
[]
[]
0
true
Family
Nanovirus component 8
Nanovirus component 8
Nanovirus_C8
5
IPR008708
8,708
TspB virulence factor
Neisseria_TspB
Family
317
false
false
This family consists mainly of Neisseria meningitidis TspB virulence factor proteins. Proteins in this family also include attachment protein G3P from Pseudomonas phage Pf3. G3P plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process [ ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05616" ]
[ "Neisseria_TspB" ]
[ 317 ]
1
[]
[]
[]
0
[]
0
[ "PUB00075530" ]
[ "16298408" ]
[ "Identification and specificity of pilus adsorption proteins of filamentous bacteriophages infecting Pseudomonas aeruginosa." ]
[ 2006 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Inoviridae", "ecological metagenomes" ]
[ 301, 6, 8, 2 ]
4
[]
[]
0
true
Family
TspB virulence factor
TspB virulence factor
Neisseria_TspB
2
IPR008709
8,709
Neurochondrin
Neurochondrin
Family
3,188
false
false
This family contains several eukaryotic neurochondrin proteins. Neurochondrin induces hydroxyapatite resorptive activity in bone marrow cells resistant to bafilomycin A1, an inhibitor of macrophage- and osteoclast-mediated resorption. Expression of the gene is localised to chondrocyte, osteoblast, and osteocyte in the ...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05536", "PTHR13109" ]
[ "Neurochondrin", "" ]
[ 3142, 3111 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011398" ]
[ "10231559" ]
[ "Induction of hydroxyapatite resorptive activity in bone marrow cell populations resistant to bafilomycin A1 by a factor with restricted expression to bone and brain, neurochondrin." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3188 ]
1
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Ze...
[ 7, 2, 2, 5, 1, 2, 4, 2, 1, 16 ]
10
true
Family
Neurochondrin
Neurochondrin
Neurochondrin
9
IPR008710
8,710
Nicastrin
Nicastrin
Family
3,553
false
false
Nicastrin and presenilin are two major components of the gamma-secretase complex, which executes the intramembrane proteolysis of type I integral membrane proteins such as the amyloid precursor protein (APP) and Notch. Nicastrin is synthesised in fibroblasts and neurons as an endoglycosidase-H-sensitive glycosylated pr...
[ "GO:0016485", "GO:0016020" ]
[ "protein processing", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PANTHER" ]
[ "PTHR21092" ]
[ "" ]
[ 3553 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2017", "R-CEL-1251985", "R-CEL-3928665", "R-CEL-6798695", "R-DDI-6798695", "R-DME-1251985", "R-DME-3928665", "R-DME-6798695", "R-HSA-1251985", "R-HSA-1474228", "R-HSA-193692", "R-HSA-205043", "R-HSA-2122948", "R-HSA-2644606", "R-HSA-2894862", "R-HSA-2979096", "R-HSA-3928665",...
[ "GP:GenProp2017", "REACTOME:R-CEL-1251985", "REACTOME:R-CEL-3928665", "REACTOME:R-CEL-6798695", "REACTOME:R-DDI-6798695", "REACTOME:R-DME-1251985", "REACTOME:R-DME-3928665", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-1251985", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-193692", "REACTOME:R-HSA-2...
39
[ "4r12", "4uis", "5a63", "5fn2", "5fn3", "5fn4", "5fn5", "6idf", "6iyc", "6lqg", "6lr4", "7c9i", "7d8x", "7y5t", "7y5x", "7y5z", "8im7", "8k8e", "8kco", "8kcp", "8kcs", "8kct", "8kcu", "8oqy", "8oqz", "8x52", "8x53", "8x54", "9k95" ]
29
[ "PUB00011399" ]
[ "12584255" ]
[ "gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3553 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 7, 2, 1, 4, 20, 7, 2, 5, 16 ]
9
true
Family
Nicastrin
Nicastrin
Nicastrin
1
IPR008711
8,711
Recombinase NinB
Recombinase_NinB
Family
2,053
false
false
The ninR region of Bacteriophage lambda contains two recombination genes, ninB and ninG (rap), that have roles when the RecF and RecBCD recombination pathways of Escherichia coli, respectively, operate on phage lambda [ ]. Genetic recombination in phage lambda relies on DNA end processing by Exo to expose 3'-tailed str...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05772" ]
[ "NinB" ]
[ 2053 ]
1
[]
[]
[]
0
[ "1pc6" ]
1
[ "PUB00011400", "PUB00037361" ]
[ "11952832", "16076958" ]
[ "Gene products encoded in the ninR region of phage lambda participate in Red-mediated recombination.", "Functional similarities between phage lambda Orf and Escherichia coli RecFOR in initiation of genetic exchange." ]
[ 2002, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 1864, 3, 177, 9 ]
4
[]
[]
0
true
Family
Recombinase NinB
Recombinase NinB
Recombinase_NinB
2
IPR008712
8,712
NinF
NinF
Family
831
false
false
This family consists of several bacteriophage NinF proteins as well as related sequences from prophages mainly found in enterobacterales.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05810" ]
[ "NinF" ]
[ 831 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Viruses", "ecological metagenomes" ]
[ 760, 51, 20 ]
3
[]
[]
0
true
Family
NinF
NinF
NinF
2
IPR008713
8,713
Bacteriophage lambda NinG
Phage_lambda_NinG
Family
3,049
false
false
The ninR region of phage lambda contains two recombination genes, ninB (also known as orf) and ninG (also known as rap). These genes are involved in the RecF and RecBCD recombination pathways of Escherichia coli that operate on phage lambda [ , ]. NinB and NinG participate in Red recombination, the primary pathway oper...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05766" ]
[ "NinG" ]
[ 3049 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011400", "PUB00043650" ]
[ "11952832", "2142940" ]
[ "Gene products encoded in the ninR region of phage lambda participate in Red-mediated recombination.", "Analysis of mutations in the ninR region of bacteriophage lambda that bypass a requirement for lambda N antitermination." ]
[ 2002, 1990 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 2721, 4, 225, 99 ]
4
[]
[]
0
true
Family
Bacteriophage lambda NinG
Bacteriophage lambda NinG
Phage_lambda_NinG
1
IPR008715
8,715
SAM-dependent methyltransferase, NodS-like
SAM-MeTfrase_NodS-like
Family
3,036
false
false
This entry consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involve...
[ "GO:0008757", "GO:0009312" ]
[ "S-adenosylmethionine-dependent methyltransferase activity", "oligosaccharide biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF05401" ]
[ "NodS" ]
[ 3036 ]
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"...
[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...
[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...
146
[ "3ofj", "3ofk" ]
2
[ "PUB00011401" ]
[ "11344149" ]
[ "Rhizobial NodL O-acetyl transferase and NodS N-methyl transferase functionally interfere in production of modified Nod factors." ]
[ 2001 ]
1
[]
[ "IPR020944" ]
0
1
0
[ "Bacteria", "Opisthokonta", "Stenosarchaea group", "metagenomes" ]
[ 3009, 4, 5, 18 ]
4
[]
[]
0
true
Family
SAM-dependent methyltransferase, NodS-like
SAM-dependent methyltransferase, NodS-like
SAM-MeTfrase_NodS-like
8
IPR008716
8,716
Nodulation protein Z
NodZ
Family
732
false
false
The nodulation genes of Rhizobia are regulated by the nodD gene product in response to host-produced flavonoids and appear to encode enzymes involved in the production of a lipo-chitose signal molecule required for infection and nodule formation. NodZ is required for the addition of a 2-O-methylfucose residue to the te...
[ "GO:0016758", "GO:0009312" ]
[ "hexosyltransferase activity", "oligosaccharide biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF" ]
[ "PF05830", "PIRSF020513" ]
[ "NodZ", "6alphaFUT_NodZ" ]
[ 732, 98 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "2.4.1.-", "PWY-1901", "PWY-1961", "PWY-1981", "PWY-2021", "PWY-2881", "PWY-2901", "PWY-2902", "PWY-4421", "PWY-4801", "PWY-5094", "PWY-5105", "PWY-5129", "PWY-5139", "PWY-5160", "PWY-5161", "PWY-5268", "PWY-5284", "PWY-5286", "PWY-5310", "PWY-5312", "PWY-5313", "PWY-5317...
[ "EC:2.4.1.-", "METACYC:PWY-1901", "METACYC:PWY-1961", "METACYC:PWY-1981", "METACYC:PWY-2021", "METACYC:PWY-2881", "METACYC:PWY-2901", "METACYC:PWY-2902", "METACYC:PWY-4421", "METACYC:PWY-4801", "METACYC:PWY-5094", "METACYC:PWY-5105", "METACYC:PWY-5129", "METACYC:PWY-5139", "METACYC:PWY-5...
200
[ "2hhc", "2hlh", "2ocx", "3siw", "3six" ]
5
[ "PUB00011402" ]
[ "8300517" ]
[ "nodZ, a unique host-specific nodulation gene, is involved in the fucosylation of the lipooligosaccharide nodulation signal of Bradyrhizobium japonicum." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 694, 36, 2 ]
3
[]
[]
0
true
Family
Nodulation protein Z
Nodulation protein Z
NodZ
9
IPR008717
8,717
Noggin
Noggin
Family
2,089
false
false
Noggin was first discovered by its ability to induce secondary axis formation in Xenopus embryos [ ]. It is a secreted homodimeric glycoprotein that serves as a BMP (bone morphogenetic protein) antagonist [ , ]. It has been found that noggin arrests the differentiation of stromal cells, preventing cellular maturation [...
[ "GO:0030514", "GO:0045596" ]
[ "negative regulation of BMP signaling pathway", "negative regulation of cell differentiation" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF05806", "PIRSF008129", "PTHR10494" ]
[ "Noggin", "Noggin", "" ]
[ 2089, 1427, 1983 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DRE-201451", "R-HSA-201451", "R-HSA-9793380", "R-MMU-201451" ]
[ "REACTOME:R-DRE-201451", "REACTOME:R-HSA-201451", "REACTOME:R-HSA-9793380", "REACTOME:R-MMU-201451" ]
4
[ "1m4u", "7ag0" ]
2
[ "PUB00011403", "PUB00074874", "PUB00074875", "PUB00074876", "PUB00074878", "PUB00074879", "PUB00160729", "PUB00160730" ]
[ "12633782", "1339313", "21256973", "15951218", "15809086", "11163261", "24584029", "35357435" ]
[ "Noggin arrests stromal cell differentiation in vitro.", "Expression cloning of noggin, a new dorsalizing factor localized to the Spemann organizer in Xenopus embryos.", "Noggin.", "BMP antagonists: their roles in development and involvement in pathophysiology.", "Noggin and bFGF cooperate to maintain the p...
[ 2003, 1992, 2011, 2005, 2005, 2000, 2014, 2022 ]
8
[]
[]
0
0
null
[ "Metazoa" ]
[ 2089 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 1, 2, 2, 3 ]
5
true
Family
Noggin
Noggin
Noggin
3
IPR008718
8,718
NolX
NolX
Family
260
false
false
This family consists of Rhizobium NolX and Xanthomonas HrpF proteins. The interaction between the plant pathogen Xanthomonas campestris pv. vesicatoria (strain 85-10) and its host plants is controlled by hrp genes (hypersensitive reaction and pathogenicity), which encode a type III protein secretion system. Among type ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05819" ]
[ "NolX" ]
[ 260 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011404", "PUB00011405" ]
[ "11115117", "11790754" ]
[ "HrpB2 and HrpF from Xanthomonas are type III-secreted proteins and essential for pathogenicity and recognition by the host plant.", "NolX of Sinorhizobium fredii USDA257, a type III-secreted protein involved in host range determination, Iis localized in the infection threads of cowpea (Vigna unguiculata [L.] Wal...
[ 2000, 2002 ]
2
[]
[]
0
0
null
[ "Bacteria" ]
[ 260 ]
1
[]
[]
0
true
Family
NolX
NolX
NolX
3
IPR008719
8,719
Nitrous oxide reductase accessory protein NosL
N2O_reductase_NosL
Family
4,916
false
false
NosL is one of the accessory proteins of the nos (nitrous oxide reductase) gene cluster. NosL is a monomeric protein of 18,540 MW that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. It is possible th...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF05573", "PTHR41247" ]
[ "NosL", "" ]
[ 4734, 4480 ]
2
[]
[]
[]
0
[ "2hpu", "2hq3", "7og7", "7osf", "7osg", "7osh", "7osi", "7osj", "7znq" ]
9
[ "PUB00011406", "PUB00066868" ]
[ "11293413", "19168619" ]
[ "Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster.", "Copper acquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis." ]
[ 2001, 2009 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 724, 4109, 2, 81 ]
4
[]
[]
0
true
Family
Nitrous oxide reductase accessory protein NosL
Nitrous oxide reductase accessory protein NosL
N2O_reductase_NosL
2
IPR008720
8,720
Viral hemorrhagic septicemia virus non-virion
Novirhabdo_Nv
Family
96
false
false
This family consists of several viral hemorrhagic septicemia virus non-virion (Nv) proteins. The NV protein is a nonstructural protein absent from mature virions although it is present in infected cells. The function of this protein is unknown [ ].
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF05554", "PIRSF009530" ]
[ "Novirhabdo_Nv", "Novirhabdo_Nv" ]
[ 96, 94 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011407" ]
[ "7571446" ]
[ "Distant strains of the fish rhabdovirus VHSV maintain a sixth functional cistron which codes for a nonstructural protein of unknown function." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Novirhabdovirus piscine" ]
[ 96 ]
1
[]
[]
0
true
Family
Viral hemorrhagic septicemia virus non-virion
Viral hemorrhagic septicemia virus non-virion
Novirhabdo_Nv
5
IPR008721
8,721
ORC6, first cyclin-like domain
ORC6_cyclin_first
Domain
2,980
false
false
This entry represents the first cyclin-like domain of ORC6, a protein that directs DNA replication by binding to replication origins and is also involved in transcriptional silencing; interacts with Spp1 and with trimethylated histone H3; phosphorylated by Cdc28 [ , ]. The Origin Recognition Complex (ORC) is a six-subu...
[ "GO:0003677", "GO:0006260", "GO:0005664" ]
[ "DNA binding", "DNA replication", "nuclear origin of replication recognition complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF05460" ]
[ "ORC6" ]
[ 2980 ]
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-176187", "R-BTA-68616", "R-BTA-68689", "R-BTA-68949", "R-BTA-68962", "R-DDI-68616", "R-DDI-68689", "R-DDI-68962", "R-DME-176187", "R-DME-68616", "R-DME-68689", "R-DME-68949", "R-DME-68962", "R-HSA-113507", "R-HSA-176187", "R-HSA-68616", "R-HSA-68689", "R-HSA-68867", "R-HSA...
[ "REACTOME:R-BTA-176187", "REACTOME:R-BTA-68616", "REACTOME:R-BTA-68689", "REACTOME:R-BTA-68949", "REACTOME:R-BTA-68962", "REACTOME:R-DDI-68616", "REACTOME:R-DDI-68689", "REACTOME:R-DDI-68962", "REACTOME:R-DME-176187", "REACTOME:R-DME-68616", "REACTOME:R-DME-68689", "REACTOME:R-DME-68949", "R...
30
[ "5v8f", "5zr1", "6kvg", "6rqc", "6wgc", "6wgg", "6wgi", "7jgr", "7jgs", "7jk2", "7jk3", "7jk4", "7jk5", "7jk6", "7mca", "7tjf", "7tjh", "7tji", "7tjj", "7tjk", "8s0b", "8s0d", "8zp5", "9bcx", "9gjp", "9gjw", "9gm5", "9i3i" ]
28
[ "PUB00011408", "PUB00052559", "PUB00052560", "PUB00052561", "PUB00052562", "PUB00052563", "PUB00052564", "PUB00052565", "PUB00052566", "PUB00052567", "PUB00052568", "PUB00052569", "PUB00052570", "PUB00052571", "PUB00052572", "PUB00052573", "PUB00052574", "PUB00052575", "PUB000525...
[ "11914271", "17241905", "17825065", "1579162", "7585959", "16716188", "7892251", "7781615", "16228006", "10966477", "12045100", "15680967", "11572976", "11429609", "16024805", "8622770", "9171055", "9038340", "11459976", "15610739", "16387651", "17053779", "9442876", "1...
[ "The origin recognition complex: from simple origins to complex functions.", "Multiple functions of the origin recognition complex.", "Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.", "ATP-dependent ...
[ 2002, 2007, 2007, 1992, 1995, 2006, 1995, 1995, 2005, 2000, 2002, 2005, 2001, 2001, 2005, 1996, 1997, 1997, 2001, 2004, 2006, 2006, 1997, 2003, 2004, 2007, 2019, 2020 ]
28
[]
[]
0
0
null
[ "Eukaryota" ]
[ 2980 ]
1
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "...
[ 3, 1, 1, 5, 5, 1, 1, 4, 1, 1, 4 ]
11
true
Domain
ORC6, first cyclin-like domain
ORC6, first cyclin-like domain
ORC6_cyclin_first
3
IPR008722
8,722
Outer membrane porin F, N-terminal
OprF_membrane_N
Domain
1,106
false
false
This entry represents the N-terminal presumed membrane spanning domain of the outer membrane porin F (OprF) [ ]. This domain is involved in channel formation and is thought to form an 8-stranded β-barrel [ ]. OprF has porin activity and can form water-filled pores of variable size [ ]. Pseudomonas aeruginosa OprF exist...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05736" ]
[ "OprF" ]
[ 1106 ]
1
[]
[]
[]
0
[ "4rlc" ]
1
[ "PUB00011409", "PUB00071921", "PUB00071922", "PUB00071924" ]
[ "11034289", "2447060", "20978537", "22240095" ]
[ "Ion channel formation by N-terminal domain: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli.", "Sequence and transcriptional start site of the Pseudomonas aeruginosa outer membrane porin protein F gene.", "Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-dom...
[ 2000, 1988, 2010, 2012 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]
[ 1101, 3, 2 ]
3
[]
[]
0
true
Domain
Outer membrane porin F, N-terminal
Outer membrane porin F, N-terminal
OprF_membrane_N
8
IPR008724
8,724
Orthopoxvirus, Protein C1
Orthopox_C1
Family
74
false
false
This family consists of several sequences which are highly related to the C1 protein of the Vaccinia virus.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF003783" ]
[ "VAC_C1L" ]
[ 74 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[ "IPR022819" ]
[]
1
0
1
[ "Orthopoxvirus" ]
[ 74 ]
1
[]
[]
0
true
Family
Orthopoxvirus, Protein C1
Orthopoxvirus, Protein C1
Orthopox_C1
4
IPR008725
8,725
Orthopoxvirus F7
Orthopox_F7
Family
74
false
false
This entry represents Protein F7L from Vaccinia virus, also known as Protein OPG051, and similar sequences mainly found in orthopoxvirus. The function of the orthopoxvirus F7L proteins are unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05813" ]
[ "Orthopox_F7" ]
[ 74 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Araneus ventricosus", "Chordopoxvirinae" ]
[ 1, 73 ]
2
[]
[]
0
true
Family
Orthopoxvirus F7
Orthopoxvirus F7
Orthopox_F7
4
IPR008726
8,726
Poxvirus F8
Poxvirus_F8
Family
81
false
false
This family consists of several poxvirus F8 proteins. F8 is also known as Protein OPG052. The function of this family is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05886" ]
[ "Orthopox_F8" ]
[ 81 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Chordopoxvirinae" ]
[ 81 ]
1
[]
[]
0
true
Family
Poxvirus F8
Poxvirus F8
Poxvirus_F8
6
IPR008727
8,727
PAAR motif
PAAR_motif
Repeat
15,544
false
false
The PAAR motif is usually found in pairs in a family of bacterial membrane proteins.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05488" ]
[ "PAAR_motif" ]
[ 15544 ]
1
[]
[]
[]
0
[ "4jiv", "4jiw", "4ku0", "5iv5", "6ox6", "7pq5", "7q97", "8gra", "9f4b" ]
9
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 55, 15040, 19, 390, 40 ]
5
[]
[]
0
true
Repeat
PAAR motif
PAAR motif
PAAR_motif
5
IPR008728
8,728
Elongator complex protein 4
Elongator_complex_protein_4
Family
4,803
false
false
Elongator is a 6 subunit protein complex highly conserved in eukaryotes. The human Elongator six-subunit complex, known as holo-Elongator, has histone acetyltransferase activity directed against histone H3 and H4 [ , ]. It consists of two subcomplexes, a core subcomplex (ELP1-3), and an accessory subcomplex (ELP4-6) [ ...
[ "GO:0002098", "GO:0033588" ]
[ "tRNA wobble uridine modification", "elongator holoenzyme complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF05625", "PTHR12896" ]
[ "PAXNEB", "" ]
[ 4791, 4679 ]
2
[ "REACTOME" ]
[ "R-HSA-3214847" ]
[ "REACTOME:R-HSA-3214847" ]
1
[ "4a8j", "4ejs", "8asv", "8at6" ]
4
[ "PUB00008616", "PUB00019998", "PUB00043577", "PUB00043578", "PUB00074321", "PUB00074324", "PUB00074325", "PUB00086633", "PUB00086635" ]
[ "10024884", "11689709", "11904415", "15769872", "11714725", "19172991", "22556426", "22889844", "23165209" ]
[ "Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation.", "Characterization of a six-subunit holo-elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae.", "Elongator is a histone H3 and H4 acetyltransferase im...
[ 1999, 2001, 2002, 2005, 2002, 2009, 2012, 2012, 2012 ]
9
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4803 ]
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...
[ 7, 1, 5, 1, 23, 2, 1, 2, 5, 1, 1, 11 ]
12
true
Family
Elongator complex protein 4
Elongator complex protein 4
Elongator_complex_protein_4
3
IPR008729
8,729
Phenolic acid decarboxylase
PA_de_COase
Family
2,097
false
false
This family includes several bacterial phenolic acid decarboxylase proteins. Phenolic acids, also called substituted cinnamic acids, are important lignin-related aromatic acids and natural constituents of plant cell walls. These acids (particularly ferulic, p-coumaric, and caffeic acids) bind the complex lignin polymer...
[ "GO:0016831" ]
[ "carboxy-lyase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PIRSF", "PANTHER", "CDD" ]
[ "PF05870", "PIRSF011561", "PTHR40087", "cd14241" ]
[ "PA_decarbox", "PAD", "", "PAD" ]
[ 2039, 669, 2039, 1209 ]
4
[]
[]
[]
0
[ "2gc9", "2p8g", "2w2a", "2w2b", "2w2f", "2wsj", "3nad", "3nx1", "3nx2", "4alb", "4uu2", "4uu3", "8a85", "8adx", "8b30", "8c66" ]
16
[ "PUB00011411" ]
[ "9546183" ]
[ "Gene cloning, transcriptional analysis, purification, and characterization of phenolic acid decarboxylase from Bacillus subtilis." ]
[ 1998 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1269, 824, 4 ]
3
[]
[]
0
true
Family
Phenolic acid decarboxylase
Phenolic acid decarboxylase
PA_de_COase
9
IPR008730
8,730
Pheromone biosynthesis activating neuropeptide
PBAN
Family
155
false
false
This family consists of several moth pheromone biosynthesis activating neuropeptide (PBAN) sequences. Female moths produce and release species specific sex pheromones to attract males for mating. Pheromone biosynthesis is hormonally regulated by the Pheromone Biosynthesis Activating Neuropeptide (PBAN) which is biosynt...
[ "GO:0005184", "GO:0007218", "GO:0042811" ]
[ "neuropeptide hormone activity", "neuropeptide signaling pathway", "pheromone biosynthetic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM" ]
[ "PF05874" ]
[ "PBAN" ]
[ 155 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011412" ]
[ "12110297" ]
[ "A new member of the PBAN family in Spodoptera littoralis: molecular cloning and immunovisualisation in scotophase hemolymph." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Pancrustacea" ]
[ 155 ]
1
[]
[]
0
true
Family
Pheromone biosynthesis activating neuropeptide
Pheromone biosynthesis activating neuropeptide
PBAN
2
IPR008731
8,731
Phosphotransferase system, enzyme I N-terminal
PTS_EIN
Domain
29,817
false
false
This sequence identifies proteins which are a component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), a major carbohydrate active transport system. The PTS system is found throughout the bacterial kingdom, and is responsible for the coupled phosphorylation and translocation of numerous sugars across...
[ "GO:0009401" ]
[ "phosphoenolpyruvate-dependent sugar phosphotransferase system" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05524" ]
[ "PEP-utilisers_N" ]
[ 29817 ]
1
[ "EC", "GP" ]
[ "2.7.3.9", "GenProp1324" ]
[ "EC:2.7.3.9", "GP:GenProp1324" ]
2
[ "1eza", "1ezb", "1ezc", "1ezd", "1zym", "2eza", "2ezb", "2ezc", "2hro", "2hwg", "2kx9", "2l5h", "2mp0", "2n5t", "2wqd", "2xdf", "3eza", "3ezb", "3eze", "5t12", "5t1o", "5woy" ]
22
[ "PUB00003612", "PUB00028034", "PUB00028035" ]
[ "8246840", "1655788", "8031118" ]
[ "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium.", "Identification of the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:...
[ 1993, 1991, 1994 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 196, 29327, 38, 256 ]
4
[ "Escherichia coli (strain K12)" ]
[ 5 ]
1
true
Domain
Phosphotransferase system, enzyme I N-terminal
Phosphotransferase system, enzyme I N-terminal
PTS_EIN
8
IPR008732
8,732
Protein Pet122
Pet122
Family
65
false
false
Pet122 is a mitochondrial-localised protein that activates initiation of translation of the mitochondrial mRNA from the COX3 gene, which encodes subunit III of cytochrome c oxidase [ ].
[ "GO:0003743", "GO:0070131", "GO:0005743" ]
[ "translation initiation factor activity", "positive regulation of mitochondrial translation", "mitochondrial inner membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PIRSF" ]
[ "PF05476", "PIRSF003326" ]
[ "PET122", "PET122" ]
[ 65, 18 ]
2
[]
[]
[]
0
[]
0
[ "PUB00011413" ]
[ "10410243" ]
[ "Expression of the divergent transcription unit containing the yeast PET122 and OXA1 genes." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Saccharomycetes", "Sulfurospirillum" ]
[ 62, 3 ]
2
[ "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 1 ]
1
true
Family
Protein Pet122
Protein Pet122
Pet122
1
IPR008733
8,733
Peroxisomal biogenesis factor 11
PEX11
Family
11,432
false
false
This family consists of several peroxisomal biogenesis factor 11 (PEX11) proteins from several eukaryotic species. The PEX11 peroxisomal membrane proteins promote peroxisome division in multiple eukaryotes [ ]. PEX11 genes in rice have diversification not only in sequences but also in expression patterns under normal a...
[ "GO:0016559", "GO:0005778" ]
[ "peroxisome fission", "peroxisomal membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF05648" ]
[ "PEX11" ]
[ 11432 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9603798", "R-DDI-9603798", "R-HSA-1989781", "R-HSA-9603798", "R-HSA-9841922", "R-MMU-9603798", "R-SCE-9603798", "R-SPO-9603798" ]
[ "REACTOME:R-BTA-9603798", "REACTOME:R-DDI-9603798", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-9603798", "REACTOME:R-HSA-9841922", "REACTOME:R-MMU-9603798", "REACTOME:R-SCE-9603798", "REACTOME:R-SPO-9603798" ]
8
[]
0
[ "PUB00011611", "PUB00043392" ]
[ "12417726", "18291602" ]
[ "PEX11alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation.", "Comprehensive sequence and expression profile analysis of PEX11 gene family in rice." ]
[ 2002, 2008 ]
2
[]
[ "IPR026510" ]
0
1
0
[ "Catovirus CTV1", "Eukaryota", "bioreactor metagenome" ]
[ 1, 11430, 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...
[ 18, 1, 3, 5, 10, 7, 2, 8, 15, 2, 1, 20 ]
12
true
Family
Peroxisomal biogenesis factor 11
Peroxisomal biogenesis factor 11
PEX11
2
IPR008734
8,734
Phosphorylase kinase alpha/beta subunit
PHK_A/B_su
Family
10,033
false
false
This protein family is predominantly found in animals and bacteria. Phosphorylase kinase (PHK) is a hexadecameric enzyme complex consisting of four copies each of four different subunits: alpha, beta, delta and gamma [ , , ] that plays a role in glycogen metabolism. During activation of glycogenolysis, this protein com...
[ "GO:0005516", "GO:0005977" ]
[ "calmodulin binding", "glycogen metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR10749" ]
[ "" ]
[ 10033 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp2089", "R-CEL-70221", "R-DME-70221", "R-HSA-70221", "R-MMU-70221", "R-RNO-70221" ]
[ "GP:GenProp2089", "REACTOME:R-CEL-70221", "REACTOME:R-DME-70221", "REACTOME:R-HSA-70221", "REACTOME:R-MMU-70221", "REACTOME:R-RNO-70221" ]
6
[ "8jfk", "8jfl", "8xy7", "8xya", "8xyb", "8z5m", "8z5p", "8z5q", "8z5r", "8z5t" ]
10
[ "PUB00011612", "PUB00011613", "PUB00098854", "PUB00098855", "PUB00098856", "PUB00098857" ]
[ "9384616", "9835437", "29098736", "29098725", "10487978", "27845042" ]
[ "Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis.", "Clinical, biochemical and molecular findings in a patient with X-linked liver glycogenosis followed for 40 years.", "Structural characterization of the catalytic γ and regulatory β subuni...
[ 1998, 1998, 2018, 2018, 1999, 2017 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 355, 9678 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 20, 10, 16, 26, 21 ]
6
true
Family
Phosphorylase kinase alpha/beta subunit
Phosphorylase kinase alpha/beta subunit
PHK_A/B_su
2
IPR008737
8,737
Putative aspartic peptidase, DUF1758
DUF1758
Domain
2,241
false
false
This is a domain found in a group of proteins of unknown function. Most members of this entry are found in arthropods and nematodes [ , , ]. It seems likely that these proteins act as aspartic peptidases.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05585" ]
[ "DUF1758" ]
[ 2241 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011616", "PUB00100109", "PUB00100110" ]
[ "7525414", "28424974", "26251035" ]
[ "Tas, a retrotransposon from the parasitic nematode Ascaris lumbricoides.", "Transposable elements in the Anopheles funestus transcriptome.", "Trends in genome dynamics among major orders of insects revealed through variations in protein families." ]
[ 1994, 2017, 2015 ]
3
[]
[]
0
0
null
[ "Metazoa" ]
[ 2241 ]
1
[]
[]
0
true
Domain
Putative aspartic peptidase, DUF1758
Putative aspartic peptidase, DUF1758
DUF1758
9
IPR008738
8,738
Peptidase C27, rubella virus endopeptidase
Peptidase_C27
Domain
118
false
false
This group of cysteine peptidases belong to the MEROPS peptidase family C27 (clan CA). The type example is the rubella virus endopeptidase (Rubella virus), which is required for processing of the rubella virus replication protein. A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thi...
[ "GO:0004197" ]
[ "cysteine-type endopeptidase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF05407" ]
[ "Peptidase_C27" ]
[ 118 ]
1
[ "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.7.48", "3.4.22.-", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210" ]
[ "EC:2.7.7.48", "EC:3.4.22.-", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210" ]
9
[ "7fav" ]
1
[ "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
[ "Rubivirus" ]
[ 118 ]
1
[]
[]
0
true
Domain
Peptidase C27, rubella virus endopeptidase
Peptidase C27, rubella virus endopeptidase
Peptidase_C27
5
IPR008739
8,739
Peptidase C28, foot-and-mouth virus L-proteinase
Peptidase_C28
Domain
1,334
false
false
This group of cysteine peptidases belong to MEROPS peptidase family C28 (clan CA).The protein fold of the peptidase unit for members of this family resembles that of papain. The leader peptidase of Foot-and-mouth disease virus cleaves itself from the growing polyprotein and also cleaves the host translation initiation ...
[ "GO:0004197", "GO:0016032", "GO:0019082" ]
[ "cysteine-type endopeptidase activity", "viral process", "viral protein processing" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PROFILE" ]
[ "PF05408", "PS51887" ]
[ "Peptidase_C28", "APHTHOVIRUS_LPRO" ]
[ 1334, 1314 ]
2
[ "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.7.48", "3.4.22.28", "3.4.22.46", "3.6.1.15", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210" ]
[ "EC:2.7.7.48", "EC:3.4.22.28", "EC:3.4.22.46", "EC:3.6.1.15", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210" ]
9
[ "1qmy", "1qol", "2jqf", "2jqg", "4qbb", "6ffa" ]
6
[ "PUB00011620", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953" ]
[ "12297280", "11517925", "9891971", "14725770", "7044372" ]
[ "Foot-and-mouth disease virus leader proteinase: a papain-like enzyme requiring an acidic environment in the active site.", "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.", ...
[ 2002, 2001, 1998, 2004, 1982 ]
5
[]
[]
0
0
null
[ "Aphthovirus" ]
[ 1334 ]
1
[]
[]
0
true
Domain
Peptidase C28, foot-and-mouth virus L-proteinase
Peptidase C28, foot-and-mouth virus L-proteinase
Peptidase_C28
1
IPR008740
8,740
Peptidase C30, coronavirus
Peptidase_C30_CoV
Domain
7,847
false
false
This group of cysteine peptidases correspond to MEROPS peptidase family C30 (clan PA(C)). These peptidases are related to serine endopeptidases of family S1 and are restricted to coronaviruses, where they are involved in viral polyprotein processing during replication [ , , ]. This Coronavirus (CoV) domain, peptidase C...
[ "GO:0008233", "GO:0019082" ]
[ "peptidase activity", "viral protein processing" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "CDD" ]
[ "PF05409", "PS51442", "cd21666" ]
[ "Peptidase_C30", "M_PRO", "betaCoV_Nsp5_Mpro" ]
[ 7778, 7629, 5164 ]
3
[ "EC", "EC", "EC", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.7.50", "3.4.19.12", "3.4.22.-", "GenProp1009", "PWY-7375", "R-HSA-191859", "R-HSA-918233", "R-HSA-9679504", "R-HSA-9682706", "R-HSA-9682708", "R-HSA-9683439", "R-HSA-9684325", "R-HSA-9692916", "R-HSA-9694271", "R-HSA-9694301", "R-HSA-9694676", "R-HSA-9694686", "R-HSA-9694786",...
[ "EC:2.7.7.50", "EC:3.4.19.12", "EC:3.4.22.-", "GP:GenProp1009", "METACYC:PWY-7375", "REACTOME:R-HSA-191859", "REACTOME:R-HSA-918233", "REACTOME:R-HSA-9679504", "REACTOME:R-HSA-9682706", "REACTOME:R-HSA-9682708", "REACTOME:R-HSA-9683439", "REACTOME:R-HSA-9684325", "REACTOME:R-HSA-9692916", ...
21
[ "1lvo", "1p9s", "1p9u", "1q2w", "1uj1", "1uk2", "1uk3", "1uk4", "1wof", "1z1i", "1z1j", "2a5a", "2a5i", "2a5k", "2alv", "2amd", "2amp", "2amq", "2bx3", "2bx4", "2c3s", "2d2d", "2duc", "2gt7", "2gt8", "2gtb", "2gx4", "2gz7", "2gz8", "2gz9", "2h2z", "2hob"...
2,025
[ "PUB00011621", "PUB00011622", "PUB00011623", "PUB00022402", "PUB00048878", "PUB00051210", "PUB00094068", "PUB00099876", "PUB00099877" ]
[ "12093723", "10725411", "11842254", "12746549", "18094151", "18562531", "20021285", "34580920", "33811162" ]
[ "Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.", "Virus-encoded proteinases and proteolytic processing in the Nidovirales.", "Conservation of substrate specificities among coronavirus main proteases.", "Coronavirus main proteinase (3CLp...
[ 2002, 2000, 2002, 2003, 2008, 2008, 2010, 2021, 2021 ]
9
[]
[ "IPR044307", "IPR044308", "IPR044309" ]
0
3
0
[ "Bacteria", "Eukaryota", "Nidovirales", "marine sediment metagenome" ]
[ 40, 22, 7784, 1 ]
4
[]
[]
0
true
Domain
Peptidase C30, coronavirus
Peptidase C30, coronavirus
Peptidase_C30_CoV
8
IPR008741
8,741
Arterivirus papain-like cysteine protease alpha (PCPalpha) domain
AV_PCPalpha
Domain
1,565
false
false
Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries: Equine arteritis virus (EAV). Porcine reproductive and respiratory syndrome virus (PRRSV). Mice actate dehydrogenase-elevating virus. Simian hemorrhagic fever virus. Th...
[ "GO:0004197" ]
[ "cysteine-type endopeptidase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF05410", "PS51539" ]
[ "Peptidase_C31", "AV_PCP_ALPHA" ]
[ 1289, 1565 ]
2
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC" ]
[ "2.7.7.48", "3.4.21.-", "3.4.22.-", "3.6.4.12", "3.6.4.13", "4.6.1.-", "PWY-7884" ]
[ "EC:2.7.7.48", "EC:3.4.21.-", "EC:3.4.22.-", "EC:3.6.4.12", "EC:3.6.4.13", "EC:4.6.1.-", "METACYC:PWY-7884" ]
7
[ "3ifu" ]
1
[ "PUB00011622", "PUB00011704", "PUB00020025", "PUB00020037", "PUB00030423", "PUB00057981", "PUB00057982", "PUB00057983", "PUB00057984", "PUB00076953" ]
[ "10725411", "11517925", "9891971", "7769711", "14725770", "11172046", "20696193", "19706710", "20410261", "7044372" ]
[ "Virus-encoded proteinases and proteolytic processing in the Nidovirales.", "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.", "Processing and evolution of the N-terminal regi...
[ 2000, 2001, 1998, 1995, 2004, 2001, 2010, 2009, 2010, 1982 ]
10
[]
[]
0
0
null
[ "Arteriviridae", "Bacteria", "Eukaryota", "freshwater metagenome" ]
[ 1482, 55, 27, 1 ]
4
[]
[]
0
true
Domain
Arterivirus papain-like cysteine protease alpha (PCPalpha) domain
Arterivirus papain-like cysteine protease alpha (PCPalpha) domain
AV_PCPalpha
8
IPR008743
8,743
Arterivirus Nsp2, peptidase C33
Arterivirus_Nsp2_C33
Domain
2,550
false
false
Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries: Equine arteritis virus (EAV). Porcine reproductive and respiratory syndrome virus (PRRSV). Mice actate dehydrogenase-elevating virus. Simian hemorrhagic fever virus. Th...
[ "GO:0016032", "GO:0019082" ]
[ "viral process", "viral protein processing" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF05412", "PS51538" ]
[ "Peptidase_C33", "AV_CP" ]
[ 2538, 2549 ]
2
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC" ]
[ "2.7.7.48", "3.4.21.-", "3.4.22.-", "3.6.4.12", "3.6.4.13", "4.6.1.-", "PWY-7884" ]
[ "EC:2.7.7.48", "EC:3.4.21.-", "EC:3.4.22.-", "EC:3.6.4.12", "EC:3.6.4.13", "EC:4.6.1.-", "METACYC:PWY-7884" ]
7
[ "4ium", "8ehn", "8eho" ]
3
[ "PUB00011622", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00054019", "PUB00057979", "PUB00076953" ]
[ "10725411", "11517925", "9891971", "14725770", "9371590", "7622476", "7044372" ]
[ "Virus-encoded proteinases and proteolytic processing in the Nidovirales.", "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 transpep...
[ 2000, 2001, 1998, 2004, 1997, 1995, 1982 ]
7
[]
[]
0
0
null
[ "Arteriviridae", "Puccinia striiformis f. sp. tritici" ]
[ 2549, 1 ]
2
[]
[]
0
true
Domain
Arterivirus Nsp2, peptidase C33
Arterivirus Nsp2, peptidase C33
Arterivirus_Nsp2_C33
8
IPR008744
8,744
RNA-directed RNA polymerase, apple chlorotic leaf spot virus
RNA-dir_pol_ACLSV
Domain
115
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:0003723", "GO:0003968", "GO:0005524", "GO:0019079" ]
[ "RNA binding", "RNA-directed RNA polymerase activity", "ATP binding", "viral genome replication" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF05413" ]
[ "Peptidase_C34" ]
[ 115 ]
1
[]
[]
[]
0
[]
0
[ "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
[ "Methylosinus sporium", "Trichovirus" ]
[ 1, 114 ]
2
[]
[]
0
true
Domain
RNA-directed RNA polymerase, apple chlorotic leaf spot virus
RNA-directed RNA polymerase, apple chlorotic leaf spot virus
RNA-dir_pol_ACLSV
1
IPR008745
8,745
Domain of unknown function DUF1717
DUF1717
Domain
102
false
false
The domain is found towards the N terminus of the polyprotein of Apple stem grooving virus (strain P-209) (ASGV), Citrus tatter leaf virus and from Apple stem grooving virus (strain Korea) (ASGV) (Pear black necrotic leaf spot virus) [ , , ]. It is a putative RNA-directed RNA polymerase/helicase: replicates genomic RNA...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05414" ]
[ "DUF1717" ]
[ 102 ]
1
[]
[]
[]
0
[]
0
[ "PUB00005590", "PUB00011626", "PUB00098066" ]
[ "1413530", "8277280", "27507588" ]
[ "The nucleotide sequence of apple stem grooving capillovirus genome.", "Striking similarities between the nucleotide sequence and genome organization of citrus tatter leaf and apple stem grooving capilloviruses.", "Integrated analyses using RNA-Seq data reveal viral genomes, single nucleotide variations, the ph...
[ 1992, 1993, 2016 ]
3
[]
[]
0
0
null
[ "Capillovirus" ]
[ 102 ]
1
[]
[]
0
true
Domain
Domain of unknown function DUF1717
Domain of unknown function DUF1717
DUF1717
4
IPR008746
8,746
Peptidase C36, beet necrotic yellow vein furovirus-type papain-like endopeptidase
Peptidase_C36
Domain
23
false
false
This group of cysteine peptidases correspond to MEROPS peptidase family C36 (clan CA). The type example is beet necrotic yellow vein furovirus-type papain-like endopeptidase (beet necrotic yellow vein virus), which is involved in processing the viral polyprotein. A cysteine peptidase is a proteolytic enzyme that hydrol...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05415" ]
[ "Peptidase_C36" ]
[ 23 ]
1
[]
[]
[]
0
[]
0
[ "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
[ "Benyviridae" ]
[ 23 ]
1
[]
[]
0
true
Domain
Peptidase C36, beet necrotic yellow vein furovirus-type papain-like endopeptidase
Peptidase C36, beet necrotic yellow vein furovirus-type papain-like endopeptidase
Peptidase_C36
3
IPR008748
8,748
Hepatitis E virus, cysteine peptidase
Hepatitis-E_Cys-pept
Family
725
false
false
This entry represents the cysteine proteinase of hepatitis E virus (HEV), which is a papain-like protease that cleaves the viral polyprotein encoded by ORF1 of the hepatitis E virus [ , , , ]. A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nu...
[ "GO:0019082" ]
[ "viral protein processing" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05417" ]
[ "Peptidase_C41" ]
[ 725 ]
1
[ "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", ...
[ "2.1.1.-", "2.7.7.-", "2.7.7.48", "3.6.4.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975",...
[ "EC:2.1.1.-", "EC:2.7.7.-", "EC:2.7.7.48", "EC:3.6.4.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:...
164
[ "6nu9" ]
1
[ "PUB00011628", "PUB00011629", "PUB00011630", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953", "PUB00098818" ]
[ "10963340", "1518855", "8219799", "11517925", "9891971", "14725770", "7044372", "32039053" ]
[ "Expression of the hepatitis E virus ORF1.", "Computer-assisted assignment of functional domains in the nonstructural polyprotein of hepatitis E virus: delineation of an additional group of positive-strand RNA plant and animal viruses.", "Molecular organization and replication of hepatitis E virus (HEV).", "E...
[ 2000, 1992, 1993, 2001, 1998, 2004, 1982, 2019 ]
8
[]
[]
0
0
null
[ "Hepeviridae" ]
[ 725 ]
1
[]
[]
0
true
Family
Hepatitis E virus, cysteine peptidase
Hepatitis E virus, cysteine peptidase
Hepatitis-E_Cys-pept
8
IPR008749
8,749
Peptidase C42, beet yellows virus-type papain-like endopeptidase C42
Peptidase_C42
Domain
364
false
false
This group of cysteine peptidases correspond to MEROPS peptidase family C42. The type example is beet yellows virus-type papain-like endopeptidase (beet yellows virus) [ ]. A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysi...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05533" ]
[ "Peptidase_C42" ]
[ 364 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011631", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953" ]
[ "11711606", "11517925", "9891971", "14725770", "7044372" ]
[ "Functional specialization and evolution of leader proteinases in the family Closteroviridae.", "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,...
[ 2001, 2001, 1998, 2004, 1982 ]
5
[]
[]
0
0
null
[ "Closterovirus" ]
[ 364 ]
1
[]
[]
0
true
Domain
Peptidase C42, beet yellows virus-type papain-like endopeptidase C42
Peptidase C42, beet yellows virus-type papain-like endopeptidase C42
Peptidase_C42
8
IPR008750
8,750
Staphopain peptidase C47
Peptidase_C47
Family
189
false
false
Staphopains are one of four major families of proteinases secreted by the Gram-positive Staphylococcus aureus. These staphylococcal cysteine proteases are secreted as preproenzymes that are proteolytically cleaved to generate the mature enzyme [ , , ].
[ "GO:0008234", "GO:0006508" ]
[ "cysteine-type peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF05543" ]
[ "Peptidase_C47" ]
[ 189 ]
1
[ "EC" ]
[ "3.4.22" ]
[ "EC:3.4.22" ]
1
[ "1cv8", "1pxv", "1x9y", "1y4h", "8oig" ]
5
[ "PUB00011632", "PUB00011633", "PUB00011634" ]
[ "12437090", "11447146", "11767947" ]
[ "Extracellular proteases of Staphylococcus spp.", "Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases.", "Molecular cloning and biochemical characterisation of proteases from Staphylococcus ep...
[ 2002, 2001, 2001 ]
3
[]
[]
0
0
null
[ "Bacteria" ]
[ 189 ]
1
[]
[]
0
true
Family
Staphopain peptidase C47
Staphopain peptidase C47
Peptidase_C47
6
IPR008751
8,751
Peptidase C53, pestivirus Npro
Peptidase_C53
Domain
2,250
false
false
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic ...
[ "GO:0016032", "GO:0019082" ]
[ "viral process", "viral protein processing" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PROFILE" ]
[ "PF05550", "PS51876" ]
[ "Peptidase_C53", "PV_NPRO" ]
[ 2225, 2246 ]
2
[ "EC", "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.7.48", "3.4.21.113", "3.4.22.-", "3.6.1.15", "3.6.4.13", "4.6.1.19", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210" ]
[ "EC:2.7.7.48", "EC:3.4.21.113", "EC:3.4.22.-", "EC:3.6.1.15", "EC:3.6.4.13", "EC:4.6.1.19", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210" ]
11
[ "3zfn", "3zfo", "3zfp", "3zfq", "3zfr", "3zft", "3zfu", "4h9j", "4h9k" ]
9
[ "PUB00011631", "PUB00011635", "PUB00011636", "PUB00011637", "PUB00011704", "PUB00020025", "PUB00030423", "PUB00076953" ]
[ "11711606", "8972567", "9499122", "10864644", "11517925", "9891971", "14725770", "7044372" ]
[ "Functional specialization and evolution of leader proteinases in the family Closteroviridae.", "Expression in E. coli and purification of the active autoprotease P20 of classical swine fever virus.", "N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesi...
[ 2001, 1996, 1998, 2000, 2001, 1998, 2004, 1982 ]
8
[]
[]
0
0
null
[ "Lutzomyia longipalpis", "Orthornavirae" ]
[ 1, 2249 ]
2
[]
[]
0
true
Domain
Peptidase C53, pestivirus Npro
Peptidase C53, pestivirus Npro
Peptidase_C53
9
IPR008753
8,753
Peptidase M13, N-terminal domain
Peptidase_M13_N
Domain
42,235
false
false
This entry represents the N-terminal domain of M13 peptidases. This group of metallopeptidases belong to the MEROPS peptidase family M13 (neprilysin family, clan MA(E)). The M13 family includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, ), endothelin-converting enzyme I (ECE-1, ), erythrocyte s...
[ "GO:0006508" ]
[ "proteolysis" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05649" ]
[ "Peptidase_M13_N" ]
[ 42235 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24", "R-BTA-375276", "R-CEL-2022377", "R-CEL-5578768", "R-CEL-6798695", "R-DME-2022377", "R-DME-5578768", "R-DME-6798695", "R-HSA-2022377", "R-HSA-375276", "R-HSA-5578768", "R-HSA-6798695", "R-HSA-9927432", "R-MMU-2022377", "R-MMU-375276", "R-MMU-5578768", "R-MMU-6798695", "R-...
[ "EC:3.4.24", "REACTOME:R-BTA-375276", "REACTOME:R-CEL-2022377", "REACTOME:R-CEL-5578768", "REACTOME:R-CEL-6798695", "REACTOME:R-DME-2022377", "REACTOME:R-DME-5578768", "REACTOME:R-DME-6798695", "REACTOME:R-HSA-2022377", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-5578768", "REACTOME:R-HSA-6798695...
21
[ "1dmt", "1r1h", "1r1i", "1r1j", "1y8j", "2qpj", "2yb9", "3dwb", "3zuk", "4cth", "4iuw", "4xbh", "4zr5", "5jmy", "5v48", "6gid", "6row", "6sh1", "6sh2", "6suk", "6svy", "6thp", "6xly", "6xvp", "7k1v", "9eyg", "9kn2" ]
27
[ "PUB00000181", "PUB00001657", "PUB00003579", "PUB00011643", "PUB00080115" ]
[ "3555489", "8099556", "7674922", "11223883", "10849750" ]
[ "Molecular cloning and amino acid sequence of rat enkephalinase.", "Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11.", "Evolutionary families of metallopeptidases.", "The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and functi...
[ 1987, 1993, 1995, 2001, 2000 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 64, 14162, 27686, 25, 298 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 30, 26, 44, 77, 33, 37 ]
6
true
Domain
Peptidase M13, N-terminal domain
Peptidase M13, N-terminal domain
Peptidase_M13_N
4
IPR008754
8,754
Peptidase M43, pregnancy-associated plasma-A
Peptidase_M43
Domain
11,095
false
false
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase...
[]
[]
[]
0
[ "PFAM", "CDD" ]
[ "PF05572", "cd04275" ]
[ "Peptidase_M43", "ZnMc_pappalysin_like" ]
[ 11064, 8189 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME" ]
[ "3.4.24.-", "PWY-8119", "R-HSA-381426", "R-MMU-381426" ]
[ "EC:3.4.24.-", "METACYC:PWY-8119", "REACTOME:R-HSA-381426", "REACTOME:R-MMU-381426" ]
4
[ "2cki", "2j83", "3lum", "3lun", "6r7u", "6r7v", "6r7w", "7od0", "7ufg", "7y5n", "7y5q", "8a7d", "8a7e", "8cd8", "8cdb", "8d8o", "8hgg", "8hgh", "8sl1" ]
19
[ "PUB00003579", "PUB00011644", "PUB00011646", "PUB00011647", "PUB00020052", "PUB00040049" ]
[ "7674922", "10913121", "11713222", "11897673", "11161967", "16627477" ]
[ "Evolutionary families of metallopeptidases.", "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor.", "Pregnancy-associated plasma protein-A (PAPP-A) in ovine, bovine, porcine, and equine ovaria...
[ 1995, 2000, 2001, 2002, 2000, 2006 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 6, 5055, 5963, 27, 44 ]
5
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]
[ 14, 2, 3, 2, 7 ]
5
true
Domain
Peptidase M43, pregnancy-associated plasma-A
Peptidase M43, pregnancy-associated plasma-A
Peptidase_M43
5
IPR008756
8,756
Peptidase M56
Peptidase_M56
Domain
15,230
false
false
This domain is found in a group of metallopeptidases belonging to MEROPS peptidase family M56 (clan M-). The predicted active site residues for members of this family occur in the motif HEXXH. The type example is BlaR1 peptidase from Bacillus licheniformis. BlaR1 is a potential penicillin-binding protein required for i...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05569" ]
[ "Peptidase_M56" ]
[ 15230 ]
1
[]
[]
[]
0
[ "4qhf", "4qhg", "4qhh", "4qhi", "4qhj", "8exp", "8exq", "8exr", "8exs", "8ext" ]
10
[ "PUB00070837" ]
[ "2404938" ]
[ "Identification of BlaR, the signal transducer for beta-lactamase production in Bacillus licheniformis, as a penicillin-binding protein with strong homology to the OXA-2 beta-lactamase (class D) of Salmonella typhimurium." ]
[ 1990 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "unclassified Caudoviricetes" ]
[ 14, 15094, 11, 109, 2 ]
5
[]
[]
0
true
Domain
Peptidase M56
Peptidase M56
Peptidase_M56
2
IPR008757
8,757
Peptidase M6-like, domain
Peptidase_M6-like_domain
Domain
8,731
false
false
This group of metallopeptidases belong to MEROPS peptidase family M6 (immune inhibitor A family, clan MA(M)). The predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH. InhA of Bacillus thuringiensis (an entomopathogenic bacterium) specifically...
[ "GO:0008233", "GO:0006508" ]
[ "peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "NCBIFAM" ]
[ "PF05547", "TIGR03296" ]
[ "Peptidase_M6", "M6dom_TIGR03296" ]
[ 5755, 8441 ]
2
[ "EC", "METACYC" ]
[ "3.4.24.-", "PWY-8119" ]
[ "EC:3.4.24.-", "METACYC:PWY-8119" ]
2
[ "4yu5", "4yu6" ]
2
[ "PUB00000112", "PUB00003579", "PUB00011416", "PUB00014362", "PUB00014369", "PUB00014396", "PUB00014398", "PUB00014400", "PUB00014414", "PUB00015264" ]
[ "3318666", "7674922", "9371455", "6421577", "2089225", "992874", "11429458", "12029046", "10475957", "7140755" ]
[ "Cell-free immunity in insects.", "Evolutionary families of metallopeptidases.", "Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a protease gene downstream of the hly region.", "Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropin...
[ 1987, 1995, 1997, 1984, 1990, 1976, 2001, 2002, 1999, 1982 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 32, 7715, 904, 80 ]
4
[]
[]
0
true
Domain
Peptidase M6-like, domain
Peptidase M6-like, domain
Peptidase_M6-like_domain
1
IPR008758
8,758
Peptidase S28
Peptidase_S28
Family
18,611
false
false
This group of serine peptidases belong to MEROPS peptidase family S28 (clan SC). The predicted active site residues for members of this family and family S10 occur in the same order in the sequence: S, D, H. These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-p...
[ "GO:0070008", "GO:0006508" ]
[ "serine-type exopeptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF05577" ]
[ "Peptidase_S28" ]
[ 18611 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-6798695", "R-HSA-140837", "R-HSA-6798695", "R-MMU-140837", "R-MMU-6798695", "R-RNO-6798695" ]
[ "REACTOME:R-CEL-6798695", "REACTOME:R-HSA-140837", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-140837", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695" ]
6
[ "3jyh", "3n0t", "3n2z", "4ebb", "7wab", "8b57", "8bbx" ]
7
[ "PUB00000522", "PUB00003576", "PUB00011654", "PUB00011655", "PUB00011656", "PUB00011657" ]
[ "8439290", "7845208", "10527559", "11003393", "11139392", "11173530" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Cloning of a novel MHC-encoded serine peptidase highly expressed by cortical epithelial cells of the thymus.", "Chromosomal localization of two mouse genes encoding thymus-specific serine peptidase and thymus-expressed acidic protein."...
[ 1993, 1994, 1999, 2000, 2001, 2001 ]
6
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 18567, 44 ]
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", "Zea mays" ]
[ 50, 10, 9, 14, 32, 6, 2, 19, 11, 50 ]
10
true
Family
Peptidase S28
Peptidase S28
Peptidase_S28
8
IPR008760
8,760
Equine arteritis virus peptidase S32
EAV_peptidase_S32
Family
1,546
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[ "GO:0004252", "GO:0016032", "GO:0019082" ]
[ "serine-type endopeptidase activity", "viral process", "viral protein processing" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM" ]
[ "PF05579" ]
[ "Peptidase_S32" ]
[ 1546 ]
1
[ "EC", "EC", "EC", "EC", "EC", "EC", "EC", "METACYC" ]
[ "2.7.7.48", "3.4.19.12", "3.4.21.-", "3.4.22.-", "3.6.4.12", "3.6.4.13", "4.6.1.-", "PWY-7884" ]
[ "EC:2.7.7.48", "EC:3.4.19.12", "EC:3.4.21.-", "EC:3.4.22.-", "EC:3.6.4.12", "EC:3.6.4.13", "EC:4.6.1.-", "METACYC:PWY-7884" ]
8
[ "1mbm", "3fan", "3fao", "5y4l" ]
4
[ "PUB00000522", "PUB00003576", "PUB00011622" ]
[ "8439290", "7845208", "10725411" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Virus-encoded proteinases and proteolytic processing in the Nidovirales." ]
[ 1993, 1994, 2000 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Nidovirales" ]
[ 3, 5, 1538 ]
3
[]
[]
0
true
Family
Equine arteritis virus peptidase S32
Equine arteritis virus peptidase S32
EAV_peptidase_S32
3
IPR008761
8,761
Peptidase S37, tripeptidyl aminopeptidase
Peptidase_S37
Family
1,959
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05576" ]
[ "Peptidase_S37" ]
[ 1959 ]
1
[]
[]
[]
0
[]
0
[ "PUB00000522", "PUB00003576", "PUB00011854", "PUB00011855" ]
[ "8439290", "7845208", "8920189", "7487044" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Cloning and analysis of a gene from Streptomyces lividans 66 encoding a novel secreted protease exhibiting homology to subtilisin BPN'.", "Cloning and characterization of a gene encoding a secreted tripeptidyl aminopeptidase from Strep...
[ 1993, 1994, 1996, 1995 ]
4
[]
[]
0
0
null
[ "Bacteria", "candidate division MSBL1 archaeon SCGC-AAA382M17", "metagenomes" ]
[ 1947, 1, 11 ]
3
[]
[]
0
true
Family
Peptidase S37, tripeptidyl aminopeptidase
Peptidase S37, tripeptidyl aminopeptidase
Peptidase_S37
9
IPR008763
8,763
Peptidase S55, SpoIVB
Peptidase_S55
Domain
3,565
false
false
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF05580", "PS51494" ]
[ "Peptidase_S55", "SPOIVB" ]
[ 3393, 3563 ]
2
[]
[]
[]
0
[ "9lnf" ]
1
[ "PUB00000522", "PUB00003576", "PUB00011660", "PUB00011661" ]
[ "8439290", "7845208", "11418578", "11741860" ]
[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions.", "The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases." ]
[ 1993, 1994, 2001, 2002 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 3495, 7, 63 ]
3
[]
[]
0
true
Domain
Peptidase S55, SpoIVB
Peptidase S55, SpoIVB
Peptidase_S55
9
IPR008764
8,764
Peptidase U57, YabG
Peptidase_U57
Family
1,755
false
false
The peptidases families associated with clan U-have an unknown catalytic mechanism as the protein fold of the active site domain and the active site residues have not been reported. This is a group of peptidases belong to MEROPS peptidase family U57 (clan U-). The type example is the YabG protein of Bacillus subtilis. ...
[]
[]
[]
0
[ "PFAM", "PIRSF", "NCBIFAM" ]
[ "PF05582", "PIRSF011575", "TIGR02855" ]
[ "Peptidase_U57", "YabG", "spore_yabG" ]
[ 1755, 1663, 1640 ]
3
[ "GP" ]
[ "GenProp0610" ]
[ "GP:GenProp0610" ]
1
[]
0
[ "PUB00011662" ]
[ "11040425" ]
[ "The yabG gene of Bacillus subtilis encodes a sporulation specific protease which is involved in the processing of several spore coat proteins." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Bacteria", "Phytophthora kernoviae 00238/432", "metagenomes" ]
[ 1737, 1, 17 ]
3
[]
[]
0
true
Family
Peptidase U57, YabG
Peptidase U57, YabG
Peptidase_U57
7
IPR008765
8,765
Bacteriophage T4, Frd3
Phage_T4_Frd3
Family
220
false
false
This is a group of proteins of unknown function from bacteriophage T4 and related phages.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05798" ]
[ "Phage_FRD3" ]
[ 220 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Viruses" ]
[ 220 ]
1
[]
[]
0
true
Family
Bacteriophage T4, Frd3
Bacteriophage T4, Frd3
Phage_T4_Frd3
3
IPR008766
8,766
Replication gene A protein-like
Replication_gene_A-like
Domain
4,688
false
false
Replication gene A proteins (also known as GpA) are found in bacteriophages and in bacteria as part of a suspected prophage. These proteins function as endonucleases during DNA replication [ , , ]. This entry represents a domain found at the centre of these sequences, which may be a DNA-binding domain.
[ "GO:0006260" ]
[ "DNA replication" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05840" ]
[ "Phage_GPA" ]
[ 4688 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011664", "PUB00011665", "PUB00011666" ]
[ "1701261", "7997180", "8510152" ]
[ "Retron for the 67-base multicopy single-stranded DNA from Escherichia coli: a potential transposable element encoding both reverse transcriptase and Dam methylase functions.", "Identification of an HP1 phage protein required for site-specific excision.", "Studies of bacteriophage P2 DNA replication. The DNA se...
[ 1990, 1994, 1993 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanomicrobia", "Viruses", "unclassified sequences" ]
[ 4272, 67, 2, 334, 13 ]
5
[]
[]
0
true
Domain
Replication gene A protein-like
Replication gene A protein-like
Replication_gene_A-like
9
IPR008767
8,767
Bacteriophage SPP1, head-tail adaptor
Phage_SPP1_head-tail_adaptor
Family
8,728
false
false
This entry describes the head-tail adaptor protein of bacteriophage SPP1 and related proteins in other bacteriophage and prophage regions of bacterial genomes. Homologues are also found in Gene Transfer Agents (GTA) [ ], including ORFg7 (RCAP_rcc01689) of the GTA of Rhodobacter capsulatus (Rhodopseudomonas capsulata) [...
[]
[]
[]
0
[ "PFAM", "NCBIFAM" ]
[ "PF05521", "TIGR01563" ]
[ "Phage_HCP", "gp16_SPP1" ]
[ 8220, 6117 ]
2
[ "GP" ]
[ "GenProp0208" ]
[ "GP:GenProp0208" ]
1
[ "2kca", "2kz4", "5a20", "5a21", "6tba", "6te9", "6toa", "6tui", "7z4w", "8fwe", "8fxr", "9cc7", "9mjn" ]
13
[ "PUB00048313", "PUB00055430", "PUB00055431", "PUB00067867", "PUB00082571" ]
[ "19433794", "11382219", "12399927", "19895817", "25991862" ]
[ "Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating.", "The gene transfer agent of Rhodobacter capsulatus and \"constitutive transduction\" in prokaryotes.", "Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus...
[ 2009, 2001, 2002, 2010, 2015 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "metagenomes" ]
[ 7783, 8, 3, 775, 159 ]
5
[]
[]
0
true
Family
Bacteriophage SPP1, head-tail adaptor
Bacteriophage SPP1, head-tail adaptor
Phage_SPP1_head-tail_adaptor
8
IPR008768
8,768
Capsid assembly scaffolding protein-like
Gp9-like
Family
808
false
false
This family includes the capsid assembly protein Gp9 (scaffolding protein) of bacteriophage T7, similar viral proteins and prophages from Proteobacteria. Gp9 facilitates assembly by binding to Gp10 hexamers but not the pentamers and locking them into a morphogenically correct conformation [ , ].
[ "GO:0019069" ]
[ "viral capsid assembly" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF05396" ]
[ "Phage_T7_Capsid" ]
[ 808 ]
1
[ "GP" ]
[ "GenProp0208" ]
[ "GP:GenProp0208" ]
1
[]
0
[ "PUB00075344", "PUB00075345" ]
[ "13677051", "16211007" ]
[ "Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment.", "Maturation of phage T7 involves structural modification of both shell and inner core components." ]
[ 2003, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria", "Viruses", "metagenomes" ]
[ 246, 556, 6 ]
3
[]
[]
0
true
Family
Capsid assembly scaffolding protein-like
Capsid assembly scaffolding protein-like
Gp9-like
9
IPR008769
8,769
Poly granule associated
PhaF_PhaI
Family
4,421
false
false
Polyhydroxyalkanoates (PHAs) are storage polyesters synthesised by various bacteria as intracellular carbon and energy reserve material. PHAs are accumulated as water-insoluble inclusions within the cells. This family consists of the phasins PhaF and PhaI which act as a transcriptional regulator of PHA biosynthesis gen...
[]
[]
[]
0
[ "PFAM", "PANTHER", "NCBIFAM" ]
[ "PF05597", "PTHR38664", "TIGR01837" ]
[ "Phasin", "", "PHA_granule_1" ]
[ 3605, 3994, 2056 ]
3
[ "GP" ]
[ "GenProp0055" ]
[ "GP:GenProp0055" ]
1
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanosarcinales", "metagenomes" ]
[ 4322, 5, 65, 29 ]
4
[]
[]
0
true
Family
Poly granule associated
Poly granule associated
PhaF_PhaI
6
IPR008770
8,770
DNA terminal protein Gp3
DNA_terminal_Gp3
Family
44
false
false
The DNA terminal protein Gp3, found in a number of Bacillus phages, is linked to the 5' ends of both strands of the genome through a phosphodiester bond between the β-hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in ...
[ "GO:0006260", "GO:0006269" ]
[ "DNA replication", "DNA replication, synthesis of primer" ]
[ "biological_process", "biological_process" ]
2
[ "PFAM", "PIRSF" ]
[ "PF05435", "PIRSF004179" ]
[ "Phi-29_GP3", "Phi-29_GP3" ]
[ 44, 17 ]
2
[]
[]
[]
0
[ "2ex3" ]
1
[ "PUB00011418" ]
[ "6779279" ]
[ "Protein p3 is linked to the DNA of phage phi 29 through a phosphoester bond between serine and 5'-dAMP." ]
[ 1980 ]
1
[]
[]
0
0
null
[ "Caudoviricetes", "Lucilia cuprina" ]
[ 43, 1 ]
2
[]
[]
0
true
Family
DNA terminal protein Gp3
DNA terminal protein Gp3
DNA_terminal_Gp3
8
IPR008772
8,772
Bacterial phosphonate metabolism, PhnH
Phosphonate_metab_PhnH
Family
3,936
false
false
PhnH is an essential component of the C-P lyase core complex formed through the interaction with other Phn proteins (G, I and J). This core complex is involved in the C-P lyase pathway that converts phosphonate into 5-phosphoribosyl-alpha-1-diphosphate (PRPP) and is activated upon phosphate starvation in many bacterial...
[ "GO:0019634" ]
[ "organic phosphonate metabolic process" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF", "NCBIFAM" ]
[ "PF05845", "PIRSF020680", "TIGR03292" ]
[ "PhnH", "PhnH", "PhnH_redo" ]
[ 3935, 3460, 3824 ]
3
[ "GP", "GP", "GP", "GP" ]
[ "GenProp0232", "GenProp1165", "GenProp1381", "GenProp1630" ]
[ "GP:GenProp0232", "GP:GenProp1165", "GP:GenProp1381", "GP:GenProp1630" ]
4
[ "2fsu", "4xb6", "7z15", "7z16", "7z17", "7z18", "7z19" ]
7
[ "PUB00047471", "PUB00079189" ]
[ "17993513", "22089136" ]
[ "Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.", "Intermediates in the transformation of phosphonates to phosphate by bacteria." ]
[ 2008, 2011 ]
2
[]
[]
0
0
null
[ "Bacteria", "Chiloscyllium punctatum", "Methanobacteriota", "metagenomes" ]
[ 3891, 1, 34, 10 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Bacterial phosphonate metabolism, PhnH
Bacterial phosphonate metabolism, PhnH
Phosphonate_metab_PhnH
6
IPR008773
8,773
Phosphonate metabolism protein PhnI
PhnI
Family
4,083
false
false
This family consists of several proteobacterial phosphonate metabolism protein (PhnI) sequences. Bacteria that use phosphonates as a phosphorus source must be able to break the stable carbon-phosphorus bond. In Escherichia coli phosphonates are broken down by a C-P lyase that has a broad substrate specificity. The gene...
[ "GO:0019634" ]
[ "organic phosphonate metabolic process" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF" ]
[ "PF05861", "PIRSF007313" ]
[ "PhnI", "PhnI" ]
[ 4083, 3852 ]
2
[ "GP", "GP", "GP", "GP" ]
[ "GenProp0232", "GenProp1165", "GenProp1381", "GenProp1630" ]
[ "GP:GenProp0232", "GP:GenProp1165", "GP:GenProp1381", "GP:GenProp1630" ]
4
[ "4xb6", "7z15", "7z16", "7z17", "7z18", "7z19" ]
6
[ "PUB00011420" ]
[ "1335942" ]
[ "Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 4030, 4, 34, 15 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Phosphonate metabolism protein PhnI
Phosphonate metabolism protein PhnI
PhnI
1
IPR008775
8,775
Phytanoyl-CoA dioxygenase-like
Phytyl_CoA_dOase-like
Family
52,807
false
false
This family includes several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins as well as several bacterial deoxygenases. PhyH is a peroxisomal enzyme catalysing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD), which is an inherited neurological syndrome biochemically ch...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05721" ]
[ "PhyH" ]
[ 52807 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.11", "R-BTA-389599", "R-BTA-9033241", "R-CEL-389599", "R-HSA-389599", "R-HSA-9033241", "R-HSA-9033500", "R-MMU-389599", "R-MMU-9033241", "R-RNO-389599", "R-RNO-9033241", "R-SCE-389599", "R-SCE-9033241" ]
[ "EC:1.14.11", "REACTOME:R-BTA-389599", "REACTOME:R-BTA-9033241", "REACTOME:R-CEL-389599", "REACTOME:R-HSA-389599", "REACTOME:R-HSA-9033241", "REACTOME:R-HSA-9033500", "REACTOME:R-MMU-389599", "REACTOME:R-MMU-9033241", "REACTOME:R-RNO-389599", "REACTOME:R-RNO-9033241", "REACTOME:R-SCE-389599", ...
13
[ "2a1x", "2fct", "2fcu", "2fcv", "2opw", "2rdn", "2rdq", "2rdr", "2rds", "3emr", "3gja", "3gjb", "3nnf", "3nnj", "3nnl", "3nnm", "3obz", "4mhr", "4mhu", "4nao", "4nmi", "4q5o", "4xaa", "4xab", "4xac", "4xbz", "4xc9", "4xca", "4xcb", "4y5s", "4y5t", "4zpi"...
129
[ "PUB00011422", "PUB00090978", "PUB00100770" ]
[ "10767344", "22564006", "18849444" ]
[ "Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease.", "PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond.", "Synthesis and uptake of the compatible solutes ectoine and 5-hydroxyectoine by Streptomyces coe...
[ 2000, 2012, 2008 ]
3
[]
[ "IPR010092", "IPR012774", "IPR047128" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 59, 28325, 22820, 47, 1556 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 4, 4, 7, 2, 12, 12, 3, 3, 10, 1, 33 ]
11
true
Family
Phytanoyl-CoA dioxygenase-like
Phytanoyl-CoA dioxygenase-like
Phytyl_CoA_dOase-like
4
IPR008776
8,776
Phytoreovirus Pns9Pns10
Phyto_Pns9_10
Family
12
false
false
This family consists of the Phytoreovirus nonstructural proteins Pns9 and Pns10. The function of this family is unknown.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05878" ]
[ "Phyto_Pns9_10" ]
[ 12 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Phytoreovirus" ]
[ 12 ]
1
[]
[]
0
true
Family
Phytoreovirus Pns9Pns10
Phytoreovirus Pns9Pns10
Phyto_Pns9_10
2
IPR008777
8,777
Phytoreovirus Pns1011
Phytoreo_Pns
Family
9
false
false
This family consists of Phytoreovirus nonstructural proteins Pns10 and Pns11. Genome segment S11 of Rice gall dwarf virus (RGDV), a Phytoreovirus, encodes a putative protein of 40kDa that exhibits approximately 37% homology at the amino acid level to the nonstructural proteins Pns10 of rice dwarf and wound tumour virus...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05451" ]
[ "Phytoreo_Pns" ]
[ 9 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011423" ]
[ "10949951" ]
[ "Sequence analysis of Pns11, a nonstructural protein of rice gall dwarf virus, and its expression and detection in infected rice plants and vector insects." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Phytoreovirus" ]
[ 9 ]
1
[]
[]
0
true
Family
Phytoreovirus Pns1011
Phytoreovirus Pns1011
Phytoreo_Pns
6
IPR008778
8,778
Pirin, C-terminal domain
Pirin_C_dom
Domain
29,984
false
false
Eukaryotic pirins are highly conserved nuclear proteins that may function as transcriptional regulators with a role in apoptosis [ , ]. Prokaryotic homologues have also been identified. Both bacterial and human pirins have been shown to possess quercetinase activity [ ], although this is not universally true for all fa...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05726" ]
[ "Pirin_C" ]
[ 29984 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-8935690", "R-MMU-8935690", "R-RNO-8935690" ]
[ "REACTOME:R-HSA-8935690", "REACTOME:R-MMU-8935690", "REACTOME:R-RNO-8935690" ]
3
[ "1j1l", "2p17", "3acl", "4ero", "4ewa", "4ewd", "4ewe", "4gul", "4hlt", "5jct", "6d0g", "6d0p", "6h1h", "6h1i", "6n0j", "6n0k", "7te5", "7tfq", "7tg5" ]
19
[ "PUB00020125", "PUB00020127", "PUB00046681", "PUB00049698", "PUB00057391" ]
[ "11485202", "14573596", "15951572", "18561187", "21514450" ]
[ "A tomato homologue of the human protein PIRIN is induced during programmed cell death.", "Crystal structure of human pirin: an iron-binding nuclear protein and transcription cofactor.", "Structural and biochemical analysis reveal pirins to possess quercetinase activity.", "The crystal structure of the protei...
[ 2001, 2004, 2005, 2009, 2011 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 281, 24159, 5187, 357 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 18, 1, 1, 2, 1, 9, 4, 27 ]
8
true
Domain
Pirin, C-terminal domain
Pirin, C-terminal domain
Pirin_C_dom
5
IPR008779
8,779
Plasmodium histidine-rich
Plasmodium_HRP
Family
1,597
false
false
This family consists of several histidine-rich protein II and III sequence from Plasmodium falciparum [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF05403" ]
[ "Plasmodium_HRP" ]
[ 1597 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011672", "PUB00011673" ]
[ "8432609", "3016741" ]
[ "Conservation of antigen components from two recombinant hybrid proteins protective against malaria.", "Homologous genes encode two distinct histidine-rich proteins in a cloned isolate of Plasmodium falciparum." ]
[ 1993, 1986 ]
2
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati", "Red sea bream iridovirus" ]
[ 1594, 2, 1 ]
3
[]
[]
0
true
Family
Plasmodium histidine-rich
Plasmodium histidine-rich
Plasmodium_HRP
6
IPR008781
8,781
Pneumovirinae attachment membrane glycoprotein G
Pneumo_att_G
Family
335
false
false
This family of proteins contain the major surface glycoprotein of turkey rhinotracheitis virus (TRTV), avian pneumovirus (APV), the aetiological agent of turkey rhinotracheitis (TRT), and other Metapneumoviruses. The major surface glycoprotein is the attachment (G) protein, which, by analogy with other respiratory sync...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05539" ]
[ "Pneumo_att_G" ]
[ 335 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011548" ]
[ "11038385" ]
[ "Nucleotide sequences of the F, L and G protein genes of two non-A/non-B avian pneumoviruses (APV) reveal a novel APV subgroup." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "avian metapneumovirus" ]
[ 335 ]
1
[]
[]
0
true
Family
Pneumovirinae attachment membrane glycoprotein G
Pneumovirinae attachment membrane glycoprotein G
Pneumo_att_G
4
IPR008784
8,784
Podovirus DNA packaging protein
Podovirus_Gp16
Family
159
false
false
This family includes several DNA encapsidation protein sequences from the phi-29-like viruses (gene product 16, Gp16). Gp16 is the primary ATPase of the motor assembly of phi-29; it binds to the prohead RNA to form a pentameric ring to complete the assembly of the DNA packaging motor [ , , ]. The characteristics of the...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05894" ]
[ "Podovirus_Gp16" ]
[ 159 ]
1
[ "EC", "METACYC" ]
[ "3.6.4.-", "PWY-7250" ]
[ "EC:3.6.4.-", "METACYC:PWY-7250" ]
2
[ "5hd9", "6v1w", "7cnb", "7jq6", "7jq7", "7jqp", "7jqq" ]
7
[ "PUB00079177", "PUB00079178", "PUB00079179" ]
[ "18674782", "16376938", "22795974" ]
[ "DNA packaging motor assembly intermediate of bacteriophage phi29.", "Interaction of gp16 with pRNA and DNA for genome packaging by the motor of bacterial virus phi29.", "Detailed kinetic analysis of the φ29 DNA packaging motor providing evidence for coordinated intersubunit ATPase activity of gp16." ]
[ 2008, 2006, 2012 ]
3
[]
[]
0
0
null
[ "Bacteria", "Lucilia cuprina", "Viruses", "metagenomes" ]
[ 20, 2, 135, 2 ]
4
[]
[]
0
true
Family
Podovirus DNA packaging protein
Podovirus DNA packaging protein
Podovirus_Gp16
1
IPR008785
8,785
Poxvirus A14, virion envelope
Poxvirus_A14
Family
96
false
false
This entry represents Protein A14 from Vaccinia virus, also known as Virion membrane protein OPG140, and similar sequences from poxvirus. A14 is a component of the virion membrane and has been found to be an H1 phosphatase substrate in vivo and in vitro . A14 is hyperphosphorylated on serine residues in the absence of ...
[ "GO:0019031" ]
[ "viral envelope" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF05767" ]
[ "Pox_A14" ]
[ 96 ]
1
[]
[]
[]
0
[]
0
[ "PUB00011428", "PUB00103644" ]
[ "10729144", "9445029" ]
[ "Elucidating the essential role of the A14 phosphoprotein in vaccinia virus morphogenesis: construction and characterization of a tetracycline-inducible recombinant.", "Vaccinia virus 15-kilodalton (A14L) protein is essential for assembly and attachment of viral crescents to virosomes." ]
[ 2000, 1998 ]
2
[]
[]
0
0
null
[ "Poxviridae", "hydrothermal vent metagenome" ]
[ 95, 1 ]
2
[]
[]
0
true
Family
Poxvirus A14, virion envelope
Poxvirus A14, virion envelope
Poxvirus_A14
9
IPR008786
8,786
Poxvirus A31
Poxvirus_A31
Family
118
false
false
This family contains the vaccinia virus A31R protein, also known as Protein OPG159, the function of which is not known.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05771" ]
[ "Pox_A31" ]
[ 118 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Poxviridae" ]
[ 118 ]
1
[]
[]
0
true
Family
Poxvirus A31
Poxvirus A31
Poxvirus_A31
4
IPR008787
8,787
Poxvirus G7-like
Poxvirus_G7
Family
143
false
false
This family of proteins which include vaccinia virus G7L and fowlpox virus FPV120 are associated with the intracellualar mature virus particle. The function of this family of proteins is not known.
[]
[]
[]
0
[ "PFAM" ]
[ "PF05503" ]
[ "Pox_G7" ]
[ 143 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Poxviridae" ]
[ 143 ]
1
[]
[]
0
true
Family
Poxvirus G7-like
Poxvirus G7-like
Poxvirus_G7
6
IPR008789
8,789
Poxvirus intermediate transcription factor
Poxvirus_intermed-TF
Family
132
false
false
This family consists of several highly related Poxvirus sequences which are thought to be intermediate transcription factors [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF05718" ]
[ "Pox_int_trans" ]
[ 132 ]
1
[]
[]
[]
0
[ "8p0j", "8p0k", "8p0n" ]
3
[ "PUB00011686" ]
[ "1660196" ]
[ "Sequence and analysis of a portion of the genomes of Shope fibroma virus and malignant rabbit fibroma virus that is important for viral replication in lymphocytes." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Ascobolus immersus RN42", "Poxviridae" ]
[ 1, 131 ]
2
[]
[]
0
true
Family
Poxvirus intermediate transcription factor
Poxvirus intermediate transcription factor
Poxvirus_intermed-TF
7
IPR008791
8,791
Orthopoxvirus interleukin 18 binding
Orthopox_IL18-bd
Family
87
false
false
Interleukin-18 (IL-18) is a proinflammatory cytokine that plays a key role in the activation of natural killer and T helper 1 cell responses principally by inducing interferon-gamma (IFN-gamma). Several poxvirus genes encode proteins with sequence similarity to IL-18BPs. It has been shown that vaccinia, ectromelia and ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF05566" ]
[ "Pox_vIL-18BP" ]
[ 87 ]
1
[]
[]
[]
0
[ "3f62" ]
1
[ "PUB00011430" ]
[ "10769064" ]
[ "Ectromelia, vaccinia and cowpox viruses encode secreted interleukin-18-binding proteins." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Paenibacillus polymyxa", "Viruses" ]
[ 1, 86 ]
2
[]
[]
0
true
Family
Orthopoxvirus interleukin 18 binding
Orthopoxvirus interleukin 18 binding
Orthopox_IL18-bd
3
IPR008792
8,792
Coenzyme PQQ synthesis protein D
PQQD
Family
11,705
false
false
This family contains several bacterial coenzyme PQQ synthesis protein D (PqqD) sequences. This protein is required for coenzyme pyrrolo-quinoline-quinone (PQQ) biosynthesis [ , ]. PqqD functions as a PqqA binding protein that would serve as a chaperone to deliver PqqA to PqqE [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF05402" ]
[ "PqqD" ]
[ 11705 ]
1
[]
[]
[]
0
[ "3g2b", "5sxy", "5v1u", "5v1v", "5vrd", "6jx3" ]
6
[ "PUB00010477", "PUB00020172", "PUB00091346" ]
[ "12437981", "8002620", "25817994" ]
[ "PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone.", "Transcriptional analysis of pqqD and study of the regulation of pyrroloquinoline quinone biosynthesis in Methylobacterium extorquens AM1.", "PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adeno...
[ 2002, 1995, 2015 ]
3
[]
[ "IPR022479", "IPR026342", "IPR027569" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 350, 11147, 3, 205 ]
4
[]
[]
0
true
Family
Coenzyme PQQ synthesis protein D
Coenzyme PQQ synthesis protein D
PQQD
1