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 |
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