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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054706 | 54,706 | Methyltransferase double-selenoprotein MduS | MT_CxxU_and_UXX | Family | 5 | false | false | This entry represents a group of proteins from Thermodesulfobacteriota with an N-terminal SAM-dependent methyltransferase domain with two selenocysteine (U)-containing motifs in the C-terminal region, typically CDPU about 70 amino acids from the C-terminal, and UGX as the last three amino acids. The name MduS derives f... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045649"
] | [
"2X_seleno_MduS"
] | [
5
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Thermodesulfobacteriota"
] | [
5
] | 1 | [] | [] | 0 | true | Family | Methyltransferase double-selenoprotein MduS | Methyltransferase double-selenoprotein MduS | MT_CxxU_and_UXX | 9 |
IPR054707 | 54,707 | 2,6-dihydroxypyridine 3-monooxygenase, substrate binding domain-like | DhpH_subs-bd | Domain | 2,158 | false | false | This domain is found in a number of FAD-binding enzymes from bacteria and eukaryotes including 2,6-dihydroxypyridine 3-monooxygenase from Paenarthrobacter nicotinovorans (DhpH), which catalyses the conversion of 2,6-dihydroxypyridine into 2,3,6-trihydroxypyridine in the nicotine degradation pathway [ ]. This protein is... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22607"
] | [
"FAD_binding-like"
] | [
2158
] | 1 | [] | [] | [] | 0 | [
"2vou"
] | 1 | [
"PUB00015973",
"PUB00049835"
] | [
"11514508",
"18440023"
] | [
"Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase.",
"Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway."
] | [
2001,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"freshwater metagenome"
] | [
1162,
940,
47,
9
] | 4 | [] | [] | 0 | true | Domain | 2,6-dihydroxypyridine 3-monooxygenase, substrate binding domain-like | 2,6-dihydroxypyridine 3-monooxygenase, substrate binding domain-like | DhpH_subs-bd | 9 |
IPR054708 | 54,708 | Poly(A) RNA polymerase, mitochondrial-like, central palm domain | MTPAP-like_central | Domain | 28,420 | false | false | This domain is found centrally in human Poly(A) RNA polymerase, mitochondrial (MTPAP) and similar proteins from eukaryotes. MTPAP is a noncanonical polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. It plays a role in the replication-dependent histone mRNA degradation. MTPAP may be involved in th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22600"
] | [
"MTPAP-like_central"
] | [
28420
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7",
"2.7.7.19",
"R-HSA-429947",
"R-HSA-6802952",
"R-HSA-9819196",
"R-HSA-9820865",
"R-HSA-9930044",
"R-HSA-9937008"
] | [
"EC:2.7.7",
"EC:2.7.7.19",
"REACTOME:R-HSA-429947",
"REACTOME:R-HSA-6802952",
"REACTOME:R-HSA-9819196",
"REACTOME:R-HSA-9820865",
"REACTOME:R-HSA-9930044",
"REACTOME:R-HSA-9937008"
] | 8 | [
"2b4v",
"2b51",
"2b56",
"2ikf",
"2nom",
"2q0c",
"2q0d",
"2q0e",
"2q0f",
"2q0g",
"3hiy",
"3hj1",
"3hj4",
"3nyb",
"3pq1",
"4e7x",
"4e80",
"4e8f",
"4ep7",
"4fh3",
"4fh5",
"4fhp",
"4fhv",
"4fhw",
"4fhx",
"4fhy",
"4nkt",
"4nku",
"4ud4",
"4ud5",
"4zrl",
"5a2v"... | 76 | [
"PUB00030151",
"PUB00039518",
"PUB00058875",
"PUB00117867",
"PUB00154846",
"PUB00154847"
] | [
"15328606",
"16281058",
"21292163",
"15769737",
"18172165",
"20970105"
] | [
"Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase.",
"Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei.",
"Structural basis for dimerization and activity of human PAPD1, a noncanonical poly(A) polymerase.",
"H... | [
2004,
2005,
2011,
2005,
2008,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermococcus",
"bird metagenome"
] | [
15,
28402,
2,
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... | [
68,
15,
13,
13,
26,
18,
3,
34,
32,
2,
6,
76
] | 12 | true | Domain | Poly(A) RNA polymerase, mitochondrial-like, central palm domain | Poly(A) RNA polymerase, mitochondrial-like, central palm domain | MTPAP-like_central | 8 |
IPR054709 | 54,709 | Cilia- and flagella-associated protein 107 | CFAP107 | Family | 812 | false | false | This family includes cilia and flagella associated protein 107 (CFAP107, also known as C1orf158 in human) and its homologues. CFAP107 is a microtubule inner protein (MIP) part of the doublet microtubules (DMTs) in cilia and sperm axoneme. CFAP107 belongs to the core MIPs and binds to protofilaments A10-A11 of the sperm... | [
"GO:0030317"
] | [
"flagellated sperm motility"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF22595"
] | [
"CFAP107"
] | [
812
] | 1 | [] | [] | [] | 0 | [
"7rro",
"7ung",
"8i7r",
"8iyj",
"8j07",
"8otz",
"8snb",
"8to0",
"9cpb",
"9cpc",
"9fqr"
] | 11 | [
"PUB00151496"
] | [
"37327785"
] | [
"Structural specializations of the sperm tail."
] | [
2023
] | 1 | [
"IPR037662"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
812
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
1,
2
] | 4 | true | Family | Cilia- and flagella-associated protein 107 | Cilia- and flagella-associated protein 107 | CFAP107 | 2 |
IPR054710 | 54,710 | Trichothecene 3-O-acetyltransferase-like, N-terminal | Tri101-like_N | Domain | 2,804 | false | false | This entry represents the N-terminal domain of trichothecene 3-O-acetyltransferase from Gibberella zeae (Tri101, ) and similar fungal sequences. Some members of this entry consist of N- and C-terminal domains arranged in a doughnut-form. The active site lies in the doughnut-hole formed by the interface between these do... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22664"
] | [
"TRI-like_N"
] | [
2804
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
"PWY-5794"... | [
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"METACYC:PWY-53... | 219 | [
"2rkt",
"2rkv",
"2zba",
"3b2s",
"3b30"
] | 5 | [
"PUB00049412"
] | [
"17923480"
] | [
"Structural and functional characterization of the TRI101 trichothecene 3-O-acetyltransferase from Fusarium sporotrichioides and Fusarium graminearum: kinetic insights to combating Fusarium head blight."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2804
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Trichothecene 3-O-acetyltransferase-like, N-terminal | Trichothecene 3-O-acetyltransferase-like, N-terminal | Tri101-like_N | 9 |
IPR054711 | 54,711 | eIF3a, PCI domain, TPR-like region | eIF3a_PCI_TPR-like | Domain | 5,301 | false | false | This entry represents the TPR-like region of the PCI domain of the Eukaryotic translation initiation factor 3 subunit A from Saccharomyces cerevisiae (eIF3a) and similar eukaryotic sequences. eIF3a is the RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in prote... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22591"
] | [
"eIF3a_PCI_TPR-like"
] | [
5301
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-156827",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-DDI-156827",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DME-156827",
"R-DME-72649",
"R-DME-72689",
"R-DME-72695",
"R-DME-72702",
"R-DRE-156827",
"R-DRE-72689",
"R-DRE-72695",
"R-DRE-72702",
"R-HSA... | [
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL-72702",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72695",
"REACTOME:R-DDI-72702",
"REACTOME:R-DME-156827",
"REACTOME:R-DME-72649",
"REACTOME:R-DME-72689",
"... | 49 | [
"3j8b",
"3j8c",
"3jap",
"4k51",
"4u1c",
"4u1d",
"4uer",
"5a5t",
"6fec",
"6fyx",
"6fyy",
"6gsm",
"6gsn",
"6w2s",
"6w2t",
"6yam",
"6ybd",
"6ybt",
"6zce",
"6zmw",
"6zon",
"6zp4",
"6zu9",
"6zvj",
"7a09",
"7qp6",
"7qp7",
"8cah",
"8cas",
"8oz0",
"8pj1",
"8pj2"... | 42 | [
"PUB00091244",
"PUB00114394",
"PUB00146069",
"PUB00153922",
"PUB00153923",
"PUB00154848",
"PUB00154849"
] | [
"26344199",
"25664723",
"25171412",
"26212456",
"24423867",
"18765792",
"9694884"
] | [
"Structure of mammalian eIF3 in the context of the 43S preinitiation complex.",
"Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex.",
"Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex.",
"Conformational Differences between Open and Closed States of the Eukaryotic Tran... | [
2015,
2015,
2014,
2015,
2014,
2008,
1998
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5301
] | 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,
2,
1,
8,
7,
1,
7,
3,
1,
1,
15
] | 12 | true | Domain | eIF3a, PCI domain, TPR-like region | eIF3a, PCI domain, TPR-like region | eIF3a_PCI_TPR-like | 7 |
IPR054712 | 54,712 | CRISPR-associated nuclease/helicase Cas3 domain | Cas3-like_dom | Domain | 10,246 | false | false | This entry represents a domain of CRISPR-associated nuclease/helicase Cas3 subtype I-F/YPEST from Pseudomonas aeruginosa (Cas3) and similar prokaryotic sequences. Cas3 is a DNA-degradation enzyme that forms part of the CRISPR-Cas bacterial immune system. Cas3 contains a Cas2 domain, an HD nuclease domain ( ), RecA1, Re... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22590"
] | [
"Cas3-like_C_2"
] | [
10246
] | 1 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"4q2c",
"4q2d",
"4qqw",
"4qqx",
"4qqy",
"4qqz",
"5b7i",
"5gqh",
"6c66",
"7r2k",
"7tr8",
"7tr9",
"7tra",
"8flj",
"8g9u",
"8k22",
"8k23",
"8k24",
"8wtk",
"8wtl",
"8zns",
"9p11",
"9p1d"
] | 23 | [
"PUB00148147"
] | [
"27455460"
] | [
"Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Vibrio phage ICP1_2004_A",
"unclassified sequences"
] | [
585,
9554,
9,
1,
97
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | CRISPR-associated nuclease/helicase Cas3 domain | CRISPR-associated nuclease/helicase Cas3 domain | Cas3-like_dom | 2 |
IPR054713 | 54,713 | GMIP/FCHO2-like, FCH domain | GMIP/FCHO2-like_FCH | Domain | 7,948 | false | false | This entry represents the FCH (FER-CIP4 homology) domain (part of the F-BAR domain) found at the N-terminal of GEM-interacting protein from humans (GMIP) [ ] and F-BAR domain only proteins 1 and 2 (FCHO1/2) [ ]. This domain is also found in Rho GTPase-activating protein 29 and 45. This domain mediates dimerisation and ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22699"
] | [
"GMIP-like_FCH"
] | [
7948
] | 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-8980692",
"R-BTA-9013148",
"R-BTA-9013149",
"R-DRE-8980692",
"R-DRE-9013148",
"R-DRE-9013149",
"R-HSA-6798695",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-8980692",
"R-HSA-9013148",
"R-HSA-9013149",
"R-MMU-6798695",
"R-MMU-8856825",
"R-MMU-8856828",
"R-MMU-8980692",
"R-MMU-90131... | [
"REACTOME:R-BTA-8980692",
"REACTOME:R-BTA-9013148",
"REACTOME:R-BTA-9013149",
"REACTOME:R-DRE-8980692",
"REACTOME:R-DRE-9013148",
"REACTOME:R-DRE-9013149",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013148",
"REACTOM... | 23 | [
"2v0o",
"3qwe"
] | 2 | [
"PUB00040395",
"PUB00043263",
"PUB00054433",
"PUB00057692",
"PUB00076229",
"PUB00117357"
] | [
"17512409",
"17540576",
"20404169",
"19713939",
"20188097",
"12093360"
] | [
"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.",
"Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.",
"Molecular basis for SH3 domain regulation of F-BAR-mediated membrane d... | [
2007,
2007,
2010,
2009,
2010,
2002
] | 6 | [
"IPR031160"
] | [
"IPR030122",
"IPR042735"
] | 1 | 2 | 0 | [
"Ancylobacter polymorphus",
"Eukaryota",
"bird metagenome"
] | [
1,
7946,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
60,
3,
37,
17,
20
] | 6 | true | Domain | GMIP/FCHO2-like, FCH domain | GMIP/FCHO2-like, FCH domain | GMIP/FCHO2-like_FCH | 5 |
IPR054714 | 54,714 | GPR158/179, extracellular domain | GPR158_179_extracellular | Domain | 3,470 | false | false | This entry represents the extracellular domain of GPR158 (also known as metabotropic glycine receptor, mGlyR), GRP179 and similar animal sequences. GPR158 is a metabotropic receptor for glycine that controls synapse formation and function in the brain [ , ]. It functions in cognition, stress-induced mood control, and s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22572"
] | [
"GPR158_179_EC"
] | [
3470
] | 1 | [] | [] | [] | 0 | [
"7ewl",
"7ewp",
"7ewr",
"7she",
"7shf",
"8d1b",
"8irj"
] | 7 | [
"PUB00077266",
"PUB00151535",
"PUB00151536",
"PUB00151537",
"PUB00154850",
"PUB00154851",
"PUB00154852",
"PUB00154853",
"PUB00154854"
] | [
"22325362",
"36996198",
"34793198",
"34815401",
"24114537",
"24790204",
"30282023",
"31189666",
"33922602"
] | [
"GPR179 is required for depolarizing bipolar cell function and is mutated in autosomal-recessive complete congenital stationary night blindness.",
"Orphan receptor GPR158 serves as a metabotropic glycine receptor: mGlyR.",
"Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex.",
... | [
2012,
2023,
2022,
2021,
2013,
2014,
2018,
2019,
2021
] | 9 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
3470
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
2,
4,
5,
8
] | 5 | true | Domain | GPR158/179, extracellular domain | GPR158/179, extracellular domain | GPR158_179_extracellular | 9 |
IPR054715 | 54,715 | Digeranylgeranylglycerophospholipid reductase, catalytic domain | GGR_cat | Domain | 1,942 | false | false | This entry represents the catalytic domain of a group of geranylgeranyl reductases (GGR) mainly found in prokaryotes, including Digeranylgeranylglycerophospholipid reductase from from Sulfolobus acidocaldarius [ , ]. This domain contains the PxxYxWxFP sequence motif, which defines a specificity pocket in the structure,... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22578"
] | [
"GGR_cat"
] | [
1942
] | 1 | [] | [] | [] | 0 | [
"3atq",
"3atr",
"3oz2",
"4opc",
"4opd",
"4opg",
"4opi",
"4opl",
"4opt",
"4opu"
] | 10 | [
"PUB00106162",
"PUB00106211",
"PUB00153969"
] | [
"21515284",
"20869368",
"24954619"
] | [
"Structure and mutation analysis of archaeal geranylgeranyl reductase.",
"Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids.",
"Constructing tailored iso... | [
2011,
2010,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1095,
435,
318,
94
] | 4 | [] | [] | 0 | true | Domain | Digeranylgeranylglycerophospholipid reductase, catalytic domain | Digeranylgeranylglycerophospholipid reductase, catalytic domain | GGR_cat | 9 |
IPR054716 | 54,716 | Soluble Rieske-type ferredoxin domain | Sol_Rieske_ferrdox_dom | Domain | 2,191 | false | false | This entry represents a Rieske-type ferredoxin domain from soluble animal, plant and fungi sequences, referred to as MRF and HRF for the mouse and human proteins, respectively, whose function is not yet known [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22543"
] | [
"Rieske_4"
] | [
2191
] | 1 | [] | [] | [] | 0 | [
"3d89"
] | 1 | [
"PUB00051288"
] | [
"18703841"
] | [
"X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus."
] | [
2008
] | 1 | [
"IPR017941"
] | [] | 1 | 0 | 1 | [
"Actinomadura rubrisoli",
"Eukaryota"
] | [
1,
2190
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
3,
1,
2
] | 4 | true | Domain | Soluble Rieske-type ferredoxin domain | Soluble Rieske-type ferredoxin domain | Sol_Rieske_ferrdox_dom | 8 |
IPR054718 | 54,718 | YhfS-like, C-terminal domain | YhfS-like_C | Domain | 747 | false | false | This entry represents the C-terminal domain of the uncharacterised protein YhfS from E.coli and similar bacterial sequences. This is an α/β domain commonly found in PLP-dependent enzymes. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22475"
] | [
"YhfS-like_C"
] | [
747
] | 1 | [] | [] | [] | 0 | [
"4j8l"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
739,
2,
6
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | YhfS-like, C-terminal domain | YhfS-like, C-terminal domain | YhfS-like_C | 7 |
IPR054719 | 54,719 | Tubulin-like protein TubZ-like, C-terminal domain | TubZ-like_C | Domain | 56 | false | false | This entry represents the C-terminal domain of TubZ from Bacillus thuringiensis and similar proteins from firmicutes. The structure of TubZ consists of an N-terminal GTPase domain and a C-terminal domain. TubZ is part of the polymerising cytomotive filament, a complex that drives newly replicated plasmids to opposite e... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22453"
] | [
"TubZ-like_C"
] | [
56
] | 1 | [] | [] | [] | 0 | [
"2xka",
"2xkb",
"3j4s",
"3j4t",
"3m89",
"3m8k"
] | 6 | [
"PUB00058650",
"PUB00059888",
"PUB00154307"
] | [
"20534443",
"20974911",
"24550513"
] | [
"Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition.",
"Filament structure of bacterial tubulin homologue TubZ.",
"Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate and a four-stranded filament upon GTP h... | [
2010,
2010,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome",
"uncultured Caudovirales phage"
] | [
54,
1,
1
] | 3 | [] | [] | 0 | true | Domain | Tubulin-like protein TubZ-like, C-terminal domain | Tubulin-like protein TubZ-like, C-terminal domain | TubZ-like_C | 8 |
IPR054720 | 54,720 | HpiC1 cyclase | HpiC1 | Family | 318 | false | false | This entry represents HpiC1, a Stig cyclase that catalyses the formation of 12-epi-hapalindole U. This enzyme folds into a β-sandwich with jelly-roll topology that is distantly related to galactose-binding domains. HpiC1 has two integral Ca2 ions, each with octahedral coordination geometry. Ca2 ions are required for ca... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22825"
] | [
"HpiC1-like"
] | [
318
] | 1 | [] | [] | [] | 0 | [
"5wpp",
"5wpr",
"5wps",
"5wpu",
"5yvk",
"5yvl",
"5yvp",
"5z53",
"5z54",
"5zfj",
"6a8x",
"6a92",
"6a98",
"6a99",
"6a9f",
"6adu",
"6al6",
"6al7",
"6al8",
"6j03"
] | 20 | [
"PUB00154015"
] | [
"29531360"
] | [
"Structural basis of the Cope rearrangement and cyclization in hapalindole biogenesis."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosopumilus koreensis AR1",
"Salpingoecidae",
"ecological metagenomes"
] | [
297,
1,
12,
8
] | 4 | [] | [] | 0 | true | Family | HpiC1 cyclase | HpiC1 cyclase | HpiC1 | 1 |
IPR054721 | 54,721 | GEO12453p1-like | GEO12453p1-like | Family | 542 | false | false | This protein family includes GEO12453p1 from Drosophila melanogaster ( , also known as CG13067) and similar sequences from insects. CG13067 is the product of a small open reading frame (small ORFs) contained in a long noncoding RNA (lncRNA) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22861"
] | [
"GEO12453p1-like"
] | [
542
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153968"
] | [
"36316320"
] | [
"Translation and natural selection of micropeptides from long non-canonical RNAs."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Endopterygota"
] | [
542
] | 1 | [
"Drosophila melanogaster"
] | [
14
] | 1 | true | Family | GEO12453p1-like | GEO12453p1-like | GEO12453p1-like | 8 |
IPR054722 | 54,722 | Retrovirus-related Pol polyprotein from transposon TNT 1-94-like, beta-barrel domain | PolX-like_BBD | Domain | 76,851 | false | false | This domain is found in retrovirus-related Pol polyproteins from transposon TNT 1-94 (PolX) from Nicotiana tabacum and similar retrovirus-related Pol polyprotein from transposons found in eukaryotes, mainly plant, fungi and arthropods. It is predicted to adopt a β-barrel fold with significant similarity to retroviral a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22936"
] | [
"Pol_BBD"
] | [
76851
] | 1 | [
"EC",
"EC",
"EC",
"EC"
] | [
"2.7.7.49",
"2.7.7.7",
"3.1.26.4",
"3.4.23.-"
] | [
"EC:2.7.7.49",
"EC:2.7.7.7",
"EC:3.1.26.4",
"EC:3.4.23.-"
] | 4 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Atrato Retro-like virus",
"Bacteria",
"Eukaryota"
] | [
2,
19,
76830
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
188,
1,
5,
2,
619,
17,
43
] | 7 | true | Domain | Retrovirus-related Pol polyprotein from transposon TNT 1-94-like, beta-barrel domain | Retrovirus-related Pol polyprotein from transposon TNT 1-94-like, beta-barrel domain | PolX-like_BBD | 3 |
IPR054724 | 54,724 | DNA (cytosine-5)-methyltransferase, N-terminal | DNM3A_N | Domain | 1,954 | false | false | This entry represents the N-terminal region of DNA (cytosine-5)-methyltransferase 3A (DNMT3A) from mouse and its homologues, a protein that is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. The dimethylation of lysine 44 (K44) in this ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22855"
] | [
"DNM3A_N"
] | [
1954
] | 1 | [
"EC",
"EC",
"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.-",
"2.1.1.37",
"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"... | [
"EC:2.1.1.-",
"EC:2.1.1.37",
"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",... | 157 | [
"6pa7",
"8qzm",
"8u5h",
"8uw1",
"9lq1",
"9mp0",
"9mpo",
"9mpp"
] | 8 | [
"PUB00057018",
"PUB00152671"
] | [
"22086334",
"32968275"
] | [
"MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a.",
"Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B."
] | [
2011,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1954
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
5,
12,
3
] | 4 | true | Domain | DNA (cytosine-5)-methyltransferase, N-terminal | DNA (cytosine-5)-methyltransferase, N-terminal | DNM3A_N | 2 |
IPR054726 | 54,726 | DUF569 associated ubiquitin-like domain | Ubiq_DUF569-assoc | Domain | 2,641 | false | false | This entry represents a small domain with a ubiquitin like fold found in plants, that is often associated with . The function of this domain is not known. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22932"
] | [
"Ubiq_DUF_assoc"
] | [
2641
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
2641
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
27,
51,
65
] | 3 | true | Domain | DUF569 associated ubiquitin-like domain | DUF569 associated ubiquitin-like domain | Ubiq_DUF569-assoc | 1 |
IPR054727 | 54,727 | Protein bicaudal C homolog 1, KH-like domain | BICC1_KH | Domain | 2,295 | false | false | This domain is found in human protein bicaudal C homolog 1 (Bicc1) and its homologues. Bicc1 is an RNA-binding protein composed of three KH and two KH-like domains that are linked by an intervening sequence to a C-terminal SAM domain. Bicc1 acts as a negative regulator of Wnt signalling [ ]. It is also involved in regu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22985"
] | [
"KH_BICC1"
] | [
2295
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00103533",
"PUB00148472"
] | [
"21922595",
"26217012"
] | [
"Two mutations in human BICC1 resulting in Wnt pathway hyperactivity associated with cystic renal dysplasia.",
"Bicc1 Polymerization Regulates the Localization and Silencing of Bound mRNA."
] | [
2012,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2295
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
2,
3,
2,
4
] | 5 | true | Domain | Protein bicaudal C homolog 1, KH-like domain | Protein bicaudal C homolog 1, KH-like domain | BICC1_KH | 4 |
IPR054728 | 54,728 | Ribosomal RNA small subunit methyltransferase B-like, ferredoxin-like domain | RsmB-like_ferredoxin | Domain | 21,566 | false | false | This entry represents a central ferredoxin-like domain found in SAM-dependent methyltransferases RsmB and related sequences ( , [ , ]). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22458"
] | [
"RsmF-B_ferredox"
] | [
21566
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"2.1.1.176",
"R-HSA-6790901",
"R-HSA-8869496"
] | [
"EC:2.1.1.176",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-8869496"
] | 3 | [
"1sqf",
"1sqg",
"2yxl",
"5zvd",
"5zve",
"5zvg",
"5zvh",
"8esq",
"8esr",
"8fkt",
"8fku",
"8fkv",
"8fkw",
"8fkx",
"8fky",
"8i9r",
"8i9t",
"8i9v",
"8i9w",
"8i9x",
"8i9y",
"8i9z",
"8ia0"
] | 23 | [
"PUB00014204",
"PUB00026173",
"PUB00036064",
"PUB00072551",
"PUB00094475"
] | [
"14656444",
"14997580",
"16793063",
"21123870",
"30541086"
] | [
"The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.",
"Crystal structure of human p120 homologue protein PH1374 from Pyrococcus horikoshii.",
"The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals... | [
2003,
2004,
2006,
2010,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
398,
17874,
3078,
216
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
2,
1,
2,
2,
2,
2,
1,
20
] | 9 | true | Domain | Ribosomal RNA small subunit methyltransferase B-like, ferredoxin-like domain | Ribosomal RNA small subunit methyltransferase B-like, ferredoxin-like domain | RsmB-like_ferredoxin | 5 |
IPR054729 | 54,729 | Telomere ends associated, middle domain | Tea_mid | Domain | 99 | false | false | This entry represents a presumed domain, mostly α-helical, found near the middle region of protein telomere ends associated (Tea) found in Drosophila species and related fly sequences. Tea protects telomeres from fusion and it likely functions as a component of the MTV complex along with moi and ver. The complex binds ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22889"
] | [
"Tea_mid"
] | [
99
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154269"
] | [
"27835648"
] | [
"MTV, an ssDNA Protecting Complex Essential for Transposon-Based Telomere Maintenance in Drosophila."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Schizophora"
] | [
99
] | 1 | [
"Drosophila melanogaster"
] | [
5
] | 1 | true | Domain | Telomere ends associated, middle domain | Telomere ends associated, middle domain | Tea_mid | 5 |
IPR054730 | 54,730 | Telomere ends associated, C-terminal domain | Tea_C | Domain | 64 | false | false | This entry represents the C-terminal domain of protein telomere ends associated (Tea) found in Drosophila species and related fly sequences. The function of this domain is still unknown. According to structure predictions, it adopts and α/β structure consisting of 7 β-strands and 3 α-helices. Tea protects telomeres fro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22884"
] | [
"Tea_C"
] | [
64
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154269"
] | [
"27835648"
] | [
"MTV, an ssDNA Protecting Complex Essential for Transposon-Based Telomere Maintenance in Drosophila."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Schizophora"
] | [
64
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Domain | Telomere ends associated, C-terminal domain | Telomere ends associated, C-terminal domain | Tea_C | 9 |
IPR054731 | 54,731 | Histidine Kinase domain observed in conflict contexts | HisKin-conflict | Domain | 65 | false | false | This histidine kinase domain is predicted to function in signal transduction during effector activation in at least a subset of (TOTE TPR, OB, TBP, Effector) biological conflict systems [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22561"
] | [
"HisKin-conflict"
] | [
65
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"metagenomes"
] | [
62,
3
] | 2 | [] | [] | 0 | true | Domain | Histidine Kinase domain observed in conflict contexts | Histidine Kinase domain observed in conflict contexts | HisKin-conflict | 9 |
IPR054732 | 54,732 | NACHT C-terminal Alpha/Beta 2 | NCAB2 | Domain | 87 | false | false | This is a domain containing α-helices and β-strands, found at the C-terminal of certain bacterial NACHT conflict systems [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22726"
] | [
"NCAB2"
] | [
87
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154095"
] | [
"37160116"
] | [
"Bacterial NLR-related proteins protect against phage."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
87
] | 1 | [] | [] | 0 | true | Domain | NACHT C-terminal Alpha/Beta 2 | NACHT C-terminal Alpha/Beta 2 | NCAB2 | 8 |
IPR054733 | 54,733 | Coenzyme PQQ synthesis protein F, C-terminal lobe, domain 3 | PqqF_C_3 | Domain | 902 | false | false | This entry represents domain 3 from the C-terminal lobe of Coenzyme PQQ synthesis protein F (PqqF), a protein required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. It consists of four structurally similar domains organised in N-terminal (domain 1 represented by and domain 2) and C-terminal (domain 3 repres... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22455"
] | [
"PqqF_C_3"
] | [
902
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.24.-",
"PWY-8119"
] | [
"EC:3.4.24.-",
"METACYC:PWY-8119"
] | 2 | [
"5cio"
] | 1 | [
"PUB00154178"
] | [
"27231346"
] | [
"Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
902
] | 1 | [] | [] | 0 | true | Domain | Coenzyme PQQ synthesis protein F, C-terminal lobe, domain 3 | Coenzyme PQQ synthesis protein F, C-terminal lobe, domain 3 | PqqF_C_3 | 3 |
IPR054734 | 54,734 | Coenzyme PQQ synthesis protein F-like, C-terminal lobe, domain 4 | PqqF-like_C_4 | Domain | 14,519 | false | false | This entry represents domain 4 from the C-terminal lobe of Coenzyme PQQ synthesis protein F (PqqF,) a protein required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. It consists of four structurally similar domains organised in N-terminal (domain 1 represented by and domain 2) and C-terminal (domain 3 repres... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22456"
] | [
"PqqF-like_C_4"
] | [
14519
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24",
"R-BTA-5689880",
"R-BTA-77387",
"R-BTA-9033241",
"R-DDI-9033241",
"R-HSA-5689880",
"R-HSA-77387",
"R-HSA-9033241",
"R-MMU-5689880",
"R-MMU-77387",
"R-MMU-9033241",
"R-RNO-5689880",
"R-RNO-77387",
"R-RNO-9033241",
"R-SCE-9033241",
"R-SPO-5689880",
"R-SPO-9033241"
] | [
"EC:3.4.24",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-9033241",
"REACTOME:R-DDI-9033241",
"REACTOME:R-HSA-5689880",
"REACTOME:R-HSA-77387",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-5689880",
"REACTOME:R-MMU-77387",
"REACTOME:R-MMU-9033241",
"REACTOME:R-RNO-5689880",
... | 17 | [
"1q2l",
"2g47",
"2g48",
"2g49",
"2g54",
"2g56",
"2jbu",
"2jg4",
"2wby",
"2wc0",
"2wk3",
"2ypu",
"3cww",
"3e4a",
"3e4z",
"3e50",
"3h44",
"3hgz",
"3n56",
"3n57",
"3ofi",
"3p7l",
"3p7o",
"3qz2",
"3tuv",
"4dtt",
"4dwk",
"4gs8",
"4gsc",
"4gsf",
"4ifh",
"4iof"... | 66 | [
"PUB00154178",
"PUB00154858"
] | [
"27231346",
"29596046"
] | [
"Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway.",
"Ensemble cryoEM elucidates the mechanism of insulin capture and degradation by human insulin degrading enzyme."
] | [
2016,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
4813,
9650,
18,
38
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
19,
1,
9,
1,
1,
10,
2,
1,
16,
6,
1,
1,
36
] | 13 | true | Domain | Coenzyme PQQ synthesis protein F-like, C-terminal lobe, domain 4 | Coenzyme PQQ synthesis protein F-like, C-terminal lobe, domain 4 | PqqF-like_C_4 | 7 |
IPR054736 | 54,736 | NACHT C-terminal Helical domain 3 | NCH3 | Domain | 19 | false | false | This entry represents an helical domain found at the C-terminal of bacterial NACHT conflict systems [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22729"
] | [
"NCH3"
] | [
19
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154095"
] | [
"37160116"
] | [
"Bacterial NLR-related proteins protect against phage."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
19
] | 1 | [] | [] | 0 | true | Domain | NACHT C-terminal Helical domain 3 | NACHT C-terminal Helical domain 3 | NCH3 | 1 |
IPR054737 | 54,737 | NACHT N-terminal Helical domain 6 | NNH6 | Domain | 52 | false | false | This is the helical domain found at the N-terminal of bacterial NACHT conflict systems. This position is frequently occupied by an effector domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22737"
] | [
"NNH6"
] | [
52
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154095"
] | [
"37160116"
] | [
"Bacterial NLR-related proteins protect against phage."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
52
] | 1 | [] | [] | 0 | true | Domain | NACHT N-terminal Helical domain 6 | NACHT N-terminal Helical domain 6 | NNH6 | 9 |
IPR054738 | 54,738 | Siphovirus-type tail component, C-terminal domain | Siphovirus-type_tail_C | Domain | 2,733 | false | false | This entry consists of several phage tail component proteins, including bacteriophage SPP1 distal tail protein Dit (also known as Gp19.1 or Gp19) [ ], as well as some bacterial proteins of unknown function. This entry represents the C-terminal domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22768"
] | [
"SPP1_Dit"
] | [
2733
] | 1 | [] | [] | [] | 0 | [
"2x8k"
] | 1 | [
"PUB00082619"
] | [
"20843802"
] | [
"Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in gram-positive infecting phages."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomada group",
"Viruses",
"metagenomes"
] | [
2231,
9,
462,
31
] | 4 | [] | [] | 0 | true | Domain | Siphovirus-type tail component, C-terminal domain | Siphovirus-type tail component, C-terminal domain | Siphovirus-type_tail_C | 1 |
IPR054739 | 54,739 | LEM-3-like, GIY-YIG domain | LEM-3_GIY-YIG | Domain | 2,218 | false | false | This is the C-terminal domain of ANKL1/LEM-3 from metazoans and its homologues from bacteria. Ankyrin repeat and LEM domain-containing protein 1 (ANKL1, also known as LEM-domain containing protein 3) is an endonuclease that probably plays a role in the DNA damage response and DNA repair [ , ]. LEM-3 processes chromatin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22945"
] | [
"LEM-3_GIY-YIG"
] | [
2218
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00084814",
"PUB00084815",
"PUB00154034"
] | [
"22399800",
"27245214",
"29463814"
] | [
"The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo.",
"Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals.",
"LEM-3 is a midbody-tethered DNA nuclease... | [
2012,
2016,
2018
] | 3 | [] | [
"IPR060771",
"IPR060772"
] | 0 | 2 | 0 | [
"Bacteria",
"Caudoviricetes",
"Metazoa",
"Methanobrevibacter gottschalkii",
"metagenomes"
] | [
742,
19,
1437,
1,
19
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
1,
3,
7,
1,
3
] | 6 | true | Domain | LEM-3-like, GIY-YIG domain | LEM-3-like, GIY-YIG domain | LEM-3_GIY-YIG | 7 |
IPR054741 | 54,741 | DNA double-strand break repair protein Mre11, second domain | Mre11_dom | Domain | 30 | false | false | This entry represents the second calcineurin-like nuclease domain of DNA double-strand break repair protein Mre11 from Pyrococcus furiosus and similar archaeal proteins. Mre11, also known as Mre11 nuclease, is part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22411"
] | [
"Mre11_2nd"
] | [
30
] | 1 | [] | [] | [] | 0 | [
"1ii7",
"1s8e",
"3dsc",
"3dsd",
"4hd0"
] | 5 | [
"PUB00022670",
"PUB00026038",
"PUB00052836",
"PUB00064229"
] | [
"15047855",
"11371344",
"18854158",
"23080121"
] | [
"Structural and functional analysis of Mre11-3.",
"Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase.",
"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair.",
"Mre11 ATLD17/18 mutation retains ... | [
2004,
2001,
2008,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
30
] | 1 | [] | [] | 0 | true | Domain | DNA double-strand break repair protein Mre11, second domain | DNA double-strand break repair protein Mre11, second domain | Mre11_dom | 8 |
IPR054742 | 54,742 | Autotransporter adhesin NhhA, Trp-ring domain | NhhA_Tpr-ring_dom | Domain | 84 | false | false | This domain is found in autotransporter adhesin NhhA from Haemophilus influenzae (also known as Hia) and similar proteins predominantly from proteobacteria. Hia is a trimeric autotransporter that mediates bacterial adherence to the respiratory epithelium. This protein shows a modular architecture with repeats of struct... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22414"
] | [
"Hia_Tpr_ring_dom"
] | [
84
] | 1 | [] | [] | [] | 0 | [
"3emi",
"5lnl"
] | 2 | [
"PUB00051735",
"PUB00154004"
] | [
"18948113",
"28177321"
] | [
"Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.",
"The crystal structure of PD1, a Haemophilus surface fibril domain."
] | [
2008,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
84
] | 1 | [] | [] | 0 | true | Domain | Autotransporter adhesin NhhA, Trp-ring domain | Autotransporter adhesin NhhA, Trp-ring domain | NhhA_Tpr-ring_dom | 1 |
IPR054743 | 54,743 | PA2794-like, C-terminal | PA2794-like_C | Domain | 7 | false | false | This domain is found at the C-terminal of Exo-alpha-sialidase from Pseudomonas aeruginosa (PA2794, ), which adopts a trimeric structure, partly held together by an immunoglobulin-like trimerisation domain, represented in this entry, that is C-terminal to the sialidase domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22432"
] | [
"PA2794-like_C"
] | [
7
] | 1 | [] | [] | [] | 0 | [
"2w38",
"3h6j"
] | 2 | [
"PUB00050022"
] | [
"19166860"
] | [
"Structural studies on the Pseudomonas aeruginosa sialidase-like enzyme PA2794 suggest substrate and mechanistic variations."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
7
] | 1 | [] | [] | 0 | true | Domain | PA2794-like, C-terminal | PA2794-like, C-terminal | PA2794-like_C | 9 |
IPR054745 | 54,745 | DNA double-strand break repair protein Mre11, thermococcales | Mre11_thermococcales | Family | 30 | false | false | This entry represents DNA double-strand break repair protein Mre11 from Pyrococcus furiosus and similar proteins mainly found in thermococcales. Mre11, also known as Mre11 nuclease, is part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair [ , ]. | [
"GO:0000729"
] | [
"DNA double-strand break processing"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"NF041029"
] | [
"Mre11_Pyroc"
] | [
30
] | 1 | [] | [] | [] | 0 | [
"1ii7",
"1s8e",
"3dsc",
"3dsd",
"4hd0"
] | 5 | [
"PUB00064229",
"PUB00104144"
] | [
"23080121",
"11029422"
] | [
"Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair.",
"Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine."
] | [
2012,
2000
] | 2 | [
"IPR032885"
] | [] | 1 | 0 | 1 | [
"Methanobacteriota"
] | [
30
] | 1 | [] | [] | 0 | true | Family | DNA double-strand break repair protein Mre11, thermococcales | DNA double-strand break repair protein Mre11, thermococcales | Mre11_thermococcales | 6 |
IPR054746 | 54,746 | GLMA-like, second domain | GLMA-like_second | Domain | 440 | false | false | This entry represents the second domain of exo-beta-D-glucosaminidase (GLMA) from Thermococcus kodakarensis and similar archaeal and bacterial proteins, just before the C-terminal domain ( ). It is an exo-type enzyme that specifically cleaves the non-reducing terminal glycosidic bond of chitooligosaccharides, being inv... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22369"
] | [
"GLMA_2nd"
] | [
440
] | 1 | [] | [] | [] | 0 | [
"5gsl",
"5gsm",
"6jow",
"7vkw",
"7vkx",
"7vky",
"7vkz",
"7vl0",
"7vl1",
"7vl2",
"7vl3",
"7vl4",
"7vl5",
"7vl6",
"7vl7",
"7x87",
"8oug"
] | 17 | [
"PUB00153978",
"PUB00160296"
] | [
"28130448",
"35065074"
] | [
"The Structure of an Archaeal β-Glucosaminidase Provides Insight into Glycoside Hydrolase Evolution.",
"Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages."
] | [
2017,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cladocopium goreaui",
"marine sediment metagenome"
] | [
27,
411,
1,
1
] | 4 | [] | [] | 0 | true | Domain | GLMA-like, second domain | GLMA-like, second domain | GLMA-like_second | 8 |
IPR054747 | 54,747 | GLMA-like, C-terminal | GLMA-like_C | Domain | 17 | false | false | This entry represents a β-sandwich domain found at the C-terminal of exo-beta-D-glucosaminidase from Thermococcus kodakarensis (GLMA) and similar archaeal proteins. It is an exo-type enzyme that specifically cleaves the non-reducing terminal glycosidic bond of chitooligosaccharides, being involved in chitin degradation... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22345"
] | [
"GLMA_C"
] | [
17
] | 1 | [] | [] | [] | 0 | [
"5gsl",
"5gsm",
"6jow",
"8oug"
] | 4 | [
"PUB00153977",
"PUB00153978"
] | [
"15136574",
"28130448"
] | [
"Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.",
"The Structure of an Archaeal β-Glucosaminidase Provides Insight into Glycoside Hydrolase Evolution."
] | [
2004,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
17
] | 1 | [] | [] | 0 | true | Domain | GLMA-like, C-terminal | GLMA-like, C-terminal | GLMA-like_C | 4 |
IPR054748 | 54,748 | NAD(P)H:rubredoxin oxidoreductase, C-terminal domain | NROR-like_C | Domain | 31 | false | false | This domain is found at the C-terminal end of NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus (NROR) and similar sequences mainly found in archaea. NROR catalyses the NADH -dependent reduction of rubredoxin (Rd), a small iron-containing redox protein [ , , ]. This domain, likely to be involved in dimerisatio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22353"
] | [
"PF1197-like_C"
] | [
31
] | 1 | [] | [] | [] | 0 | [
"1xhc"
] | 1 | [
"PUB00154859",
"PUB00154860",
"PUB00154861"
] | [
"10464233",
"11398485",
"15746356"
] | [
"A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus.",
"NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus.",
"In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus."
] | [
1999,
2001,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Thermococcaceae",
"Thermotoga"
] | [
26,
5
] | 2 | [] | [] | 0 | true | Domain | NAD(P)H:rubredoxin oxidoreductase, C-terminal domain | NAD(P)H:rubredoxin oxidoreductase, C-terminal domain | NROR-like_C | 3 |
IPR054749 | 54,749 | PF0095-like, C-terminal domain | PF0095-like_C | Domain | 42 | false | false | This domain is found at the C-terminal end of the transcription factor PF0095 from Pyrococcus furiosus ( ) and similar archaeal sequences. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22315"
] | [
"PF0095-like_C"
] | [
42
] | 1 | [] | [] | [] | 0 | [
"2qlz",
"2quf"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
42
] | 1 | [] | [] | 0 | true | Domain | PF0095-like, C-terminal domain | PF0095-like, C-terminal domain | PF0095-like_C | 5 |
IPR054750 | 54,750 | DNA polymerase II small subunit, N-terminal domain | PolB_N | Domain | 43 | false | false | This domain is found at the N-terminal of DNA polymerase II small subunit from Pyrococcus horikoshii (PolB) and similar sequences from thermococcales. PolB possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. This domain folds... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22317"
] | [
"PolB_N"
] | [
43
] | 1 | [
"EC",
"EC"
] | [
"2.7.7.7",
"3.1.11.1"
] | [
"EC:2.7.7.7",
"EC:3.1.11.1"
] | 2 | [
"2kxe",
"6knb",
"6knc",
"6t8h",
"7e15",
"8ppt",
"8ppu",
"8ppv",
"9f29",
"9f2a"
] | 10 | [
"PUB00059681",
"PUB00154174",
"PUB00154175",
"PUB00154176"
] | [
"20598295",
"33115459",
"32221299",
"34568951"
] | [
"Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.",
"Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy.",
"Structural basis for... | [
2010,
2020,
2020,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Thermococcaceae",
"marine sediment metagenome"
] | [
42,
1
] | 2 | [] | [] | 0 | true | Domain | DNA polymerase II small subunit, N-terminal domain | DNA polymerase II small subunit, N-terminal domain | PolB_N | 6 |
IPR054751 | 54,751 | NBAS subunit of NRZ tethering complex, C-terminal | NBAS_C | Domain | 1,509 | false | false | This domain is found towards the C-terminal of human NBAS subunit of NRZ tethering complex (NBAS) and similar sequences mainly found in vertebrates. NBAS (also known as Neuroblastoma-amplified sequence) is involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport [ ]. This domain is predicted to adopt an all... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22913"
] | [
"NBAS_11th"
] | [
1509
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-DRE-6811434",
"R-HSA-6811434"
] | [
"REACTOME:R-DRE-6811434",
"REACTOME:R-HSA-6811434"
] | 2 | [] | 0 | [
"PUB00154864"
] | [
"19369418"
] | [
"Identification of the neuroblastoma-amplified gene product as a component of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum retrograde transport."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1509
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
6,
7,
5
] | 4 | true | Domain | NBAS subunit of NRZ tethering complex, C-terminal | NBAS subunit of NRZ tethering complex, C-terminal | NBAS_C | 5 |
IPR054752 | 54,752 | Interferon-gamma receptor, N-terminal domain | CR4_N | Domain | 97 | false | false | This domain is found at the N-terminal of Interferon-gamma receptor from Ectromelia virus (C4R, ) and similar viral sequences. CR4 consists of two fibronectin type III domains (FBNIII) containing seven conserved β-strands each: this entry and [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22325"
] | [
"CR4_N"
] | [
97
] | 1 | [] | [] | [] | 0 | [
"3bes"
] | 1 | [
"PUB00050609"
] | [
"18252829"
] | [
"Structure and mechanism of IFN-gamma antagonism by an orthopoxvirus IFN-gamma-binding protein."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Chordopoxvirinae"
] | [
97
] | 1 | [] | [] | 0 | true | Domain | Interferon-gamma receptor, N-terminal domain | Interferon-gamma receptor, N-terminal domain | CR4_N | 8 |
IPR054753 | 54,753 | E3 SUMO-protein ligase MMS21, N-terminal domain | MMS21_N | Domain | 64 | false | false | This domain is found at the N-terminal of E3 SUMO-protein ligase MMS21 from Saccharomyces cerevisiae and similar proteins specific to Saccharomycetales. MMS21 acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22326"
] | [
"MMS21_N"
] | [
64
] | 1 | [
"REACTOME"
] | [
"R-SCE-3108214"
] | [
"REACTOME:R-SCE-3108214"
] | 1 | [
"3htk",
"7p47",
"7qcd",
"7ylm",
"7yqh",
"8i13",
"8i21",
"8i4u",
"8i4v",
"8i4x",
"8wjl",
"8wjo"
] | 12 | [
"PUB00154072"
] | [
"19748359"
] | [
"Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycetes",
"Salipaludibacillus keqinensis"
] | [
63,
1
] | 2 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | E3 SUMO-protein ligase MMS21, N-terminal domain | E3 SUMO-protein ligase MMS21, N-terminal domain | MMS21_N | 4 |
IPR054754 | 54,754 | U8 snoRNA-decapping enzyme NudT16 | NudT16 | Family | 1,501 | false | false | This entry represents a group of proteins mainly found in animals that contain the NUDIX hydrolase domain, including U8 snoRNA -decapping enzyme NudT16 [ ]. NudT16 was initially described as an RNA-binding and decapping enzyme but it was later reported to be specialised in the removal of hazardous (deoxy)inosine diphos... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF22327",
"PTHR31699"
] | [
"Nudt16-like",
""
] | [
1500,
1471
] | 2 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.1.62",
"3.6.1.64",
"R-BTA-2393930",
"R-HSA-2393930",
"R-MMU-2393930"
] | [
"EC:3.6.1.62",
"EC:3.6.1.64",
"REACTOME:R-BTA-2393930",
"REACTOME:R-HSA-2393930",
"REACTOME:R-MMU-2393930"
] | 5 | [
"1u20",
"2a8p",
"2a8q",
"2a8r",
"2a8s",
"2a8t",
"2xsq",
"3cou",
"3kvh",
"3mgm",
"4zg0",
"5vy2",
"5w6x",
"5w6z",
"5wji",
"5z78",
"5zcj",
"6b09",
"6co1",
"6co2",
"6d0l",
"6x7u",
"6x7v",
"8u3s"
] | 24 | [
"PUB00154125",
"PUB00154127"
] | [
"26121039",
"30976021"
] | [
"Structural Basis for the Specificity of Human NUDT16 and Its Regulation by Inosine Monophosphate.",
"Structural analyses of NudT16-ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins."
] | [
2015,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota"
] | [
17,
23,
1461
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
9,
9,
11
] | 4 | true | Family | U8 snoRNA-decapping enzyme NudT16 | U8 snoRNA-decapping enzyme NudT16 | NudT16 | 8 |
IPR054755 | 54,755 | Sas-6-like, oligomerization domain | Sas-6-like_oligomerization | Domain | 22 | false | false | This entry represents the coiled-coil region of Sas-6 from Chlamydomonas reinhardtii ( ), which mediates oligomerisation [ , ]. In human, Sas-6 is essential for the onset of procentriole formation and accumulates on the torus where Plk4 has focused. This entry is specific to Chlorophyta. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22331"
] | [
"Sas-6-like_oligomerization"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"3q0x",
"6zz8",
"6zzc"
] | 3 | [
"PUB00058831",
"PUB00154220"
] | [
"21277013",
"34155202"
] | [
"Structural basis of the 9-fold symmetry of centrioles.",
"Tuning SAS-6 architecture with monobodies impairs distinct steps of centriole assembly."
] | [
2011,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"core chlorophytes"
] | [
22
] | 1 | [] | [] | 0 | true | Domain | Sas-6-like, oligomerization domain | Sas-6-like, oligomerization domain | Sas-6-like_oligomerization | 4 |
IPR054756 | 54,756 | Tubulin-like protein TubZ, C-terminal domain, clostridia-type | TubZ_C_clostridia | Domain | 9 | false | false | This domain is found at the C-terminal end of Tubulin-like protein TubZ from Clostridium botulinum C phage and similar sequences found in tailed bacteriophages and prophages from Clostridium species. TubZ is a tubulin-like, filament forming GTPase. This protein adopts a tubulin/FtsZ protein family fold organised into t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22340"
] | [
"TubZ_C_3"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"3v3t",
"4xcq"
] | 2 | [
"PUB00059542"
] | [
"22538818"
] | [
"Tubulin homolog TubZ in a phage-encoded partition system."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Clostridia",
"Clostridium botulinum C phage"
] | [
8,
1
] | 2 | [] | [] | 0 | true | Domain | Tubulin-like protein TubZ, C-terminal domain, clostridia-type | Tubulin-like protein TubZ, C-terminal domain, clostridia-type | TubZ_C_clostridia | 5 |
IPR054757 | 54,757 | Type II secretion system protein E, N1E domain | GSPE_N1E | Domain | 4,506 | false | false | Type II secretion system protein E (GSPE) is an ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. This entry represents its N-terminal N1E domain, which associates with the cytoplasmic domain of the inne... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22341"
] | [
"GSPE_N1E"
] | [
4506
] | 1 | [
"EC"
] | [
"7.4.2.8"
] | [
"EC:7.4.2.8"
] | 1 | [
"2bh1",
"4pht"
] | 2 | [
"PUB00033663",
"PUB00094003"
] | [
"15843017",
"25092625"
] | [
"The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae.",
"Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL."
] | [
2005,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4434,
8,
64
] | 3 | [] | [] | 0 | true | Domain | Type II secretion system protein E, N1E domain | Type II secretion system protein E, N1E domain | GSPE_N1E | 1 |
IPR054758 | 54,758 | Putative surface anchored protein-like, helical insertion domain | Lrp-like_ins_dom | Domain | 17 | false | false | This entry represents the helical insertion domain found in surface proteins in certain pathogens, such as Putative surface anchored protein from Streptococcus pneumoniae (Lrp, , [ ]). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22343"
] | [
"Surface-like_ins_dom"
] | [
17
] | 1 | [] | [] | [] | 0 | [
"5a0n"
] | 1 | [
"PUB00104999"
] | [
"26032562"
] | [
"An internal thioester in a pathogen surface protein mediates covalent host binding."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
17
] | 1 | [] | [] | 0 | true | Domain | Putative surface anchored protein-like, helical insertion domain | Putative surface anchored protein-like, helical insertion domain | Lrp-like_ins_dom | 9 |
IPR054759 | 54,759 | RickCE-like, catalytic domain | RickCE_cat | Domain | 105 | false | false | This entry represents the catalytic domain of a subset of ubiquitin-like proteases from the CE clan, including RickCE from Rickettsia bellii ( , [ , ]). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22179"
] | [
"RickCE_cat"
] | [
105
] | 1 | [] | [] | [] | 0 | [
"5ham",
"6ups",
"6upu",
"8efx"
] | 4 | [
"PUB00117515",
"PUB00154209"
] | [
"27425412",
"32393759"
] | [
"The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.",
"A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi."
] | [
2016,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota"
] | [
27,
78
] | 2 | [] | [] | 0 | true | Domain | RickCE-like, catalytic domain | RickCE-like, catalytic domain | RickCE_cat | 4 |
IPR054760 | 54,760 | Transcriptional regulator DIP2311-like, C-terminal domain | DIP2311-like_C | Domain | 211 | false | false | This domain is found at the C-terminal of transcriptional regulator DIP2311 from Corynebacterium diphtheriae ( ) and similar bacterial sequences. This domain, which shows a winged helix fold, is normally found associated to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22168"
] | [
"DIP2311-like_C"
] | [
211
] | 1 | [] | [] | [] | 0 | [
"3lmm"
] | 1 | [] | [] | [] | [] | 0 | [
"IPR011991"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanobacteriota",
"ecological metagenomes"
] | [
205,
4,
2
] | 3 | [] | [] | 0 | true | Domain | Transcriptional regulator DIP2311-like, C-terminal domain | Transcriptional regulator DIP2311-like, C-terminal domain | DIP2311-like_C | 4 |
IPR054761 | 54,761 | Glutathione S-transferase, C-terminal domain, proteobacteria | GST_C_proteobact | Domain | 196 | false | false | This domain is found at the C-terminal of Glutathione S-transferase from Agrobacterium fabrum (Atu5508, ) and similar sequences mainly found in proteobacteria. This domain adopts an α-helical configuration [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22119"
] | [
"GST_C_8"
] | [
196
] | 1 | [] | [] | [] | 0 | [
"2fno"
] | 1 | [
"PUB00040747"
] | [
"16988933"
] | [
"Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
188,
8
] | 2 | [] | [] | 0 | true | Domain | Glutathione S-transferase, C-terminal domain, proteobacteria | Glutathione S-transferase, C-terminal domain, proteobacteria | GST_C_proteobact | 6 |
IPR054762 | 54,762 | Terminase, large subunit, ribonuclease H-like domain | Gp19_RNaseH-like | Domain | 1,503 | false | false | This entry represents the C-terminal ribonuclease (RNase) H-like domain in the terminase, large subunit from Escherichia phage T7 (Gp19), which functions as an ATP-powered molecular motor essential for the translocation of viral DNA into empty capsids. It also acts as an endonuclease, cleaving the viral genome at a spe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22530"
] | [
"Terminase-T7_RNaseH-like"
] | [
1503
] | 1 | [] | [] | [] | 0 | [
"4bij",
"4bil",
"8dgc"
] | 3 | [
"PUB00095692"
] | [
"23632014"
] | [
"Large terminase conformational change induced by connector binding in bacteriophage T7."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
392,
2,
1100,
9
] | 4 | [] | [] | 0 | true | Domain | Terminase, large subunit, ribonuclease H-like domain | Terminase, large subunit, ribonuclease H-like domain | Gp19_RNaseH-like | 3 |
IPR054763 | 54,763 | Argonaute, middle domain | Ago_mid | Domain | 24 | false | false | This domain is found in protein argonaute from Thermus thermophilus (Ago), a site-specific DNA-guided endoRNase organised into four domains: N ( ), PAZ ( ), Mid (this entry) and PIWI ( ). This domain contains residues that have been reported to be critical for cleavage activity. It folds into an α-β three layered sandw... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22474"
] | [
"Ago_Mid"
] | [
24
] | 1 | [] | [] | [] | 0 | [
"3dlb",
"3dlh",
"3f73",
"3hjf",
"3hk2",
"3hm9",
"3ho1",
"3hvr",
"3hxm",
"4kpy",
"4n41",
"4n47",
"4n76",
"4nca",
"4ncb",
"5gq9",
"5xou",
"5xow",
"5xp8",
"5xpa",
"5xpg",
"5xq2"
] | 22 | [
"PUB00051412",
"PUB00054729"
] | [
"18754009",
"19812667"
] | [
"Structure of the guide-strand-containing argonaute silencing complex.",
"Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes."
] | [
2008,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Thermus"
] | [
24
] | 1 | [] | [] | 0 | true | Domain | Argonaute, middle domain | Argonaute, middle domain | Ago_mid | 5 |
IPR054764 | 54,764 | Argonaute, N-terminal domain, thermus | Ago_N_thermus | Domain | 19 | false | false | This domain is found at the N-terminal of protein argonaute from Thermus thermophilus (Ago), a site-specific DNA-guided endoRNase organised into four domain: N (this entry), PAZ ( ), Mid ( ) and PIWI ( ). This domain shows a mixed α-β structure [ ]. This group of proteins is specific to Thermus species. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22472"
] | [
"Ago_N_2"
] | [
19
] | 1 | [] | [] | [] | 0 | [
"3dlb",
"3dlh",
"3f73",
"3hjf",
"3hk2",
"3hm9",
"3ho1",
"3hvr",
"3hxm",
"4kpy",
"4n41",
"4n47",
"4n76",
"4nca",
"4ncb",
"5gq9",
"5xou",
"5xow",
"5xp8",
"5xpa",
"5xpg",
"5xq2"
] | 22 | [
"PUB00051412",
"PUB00054729"
] | [
"18754009",
"19812667"
] | [
"Structure of the guide-strand-containing argonaute silencing complex.",
"Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes."
] | [
2008,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Thermus"
] | [
19
] | 1 | [] | [] | 0 | true | Domain | Argonaute, N-terminal domain, thermus | Argonaute, N-terminal domain, thermus | Ago_N_thermus | 7 |
IPR054765 | 54,765 | SLBB domain | SLBB_dom | Domain | 25,693 | false | false | This entry represents a set of soluble ligand-binding β-grasp domain (SLBB) domains from bacterial and eukaryotic NADH:ubiquinone oxidoreductases, including human NDUFV1 [ , ], and bacterial polysaccharide export proteins, such as Wza from Escherichia coli [ , ]. This domain has been proposed to bind soluble cofactors ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22461"
] | [
"SLBB_2"
] | [
25693
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1",
"R-DDI-6799198",
"R-DDI-9837999",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9837999",
"R-MMU-611105",
"R-MMU-6799198",
"R-MMU-9837999",
"R-SPO-9837999"
] | [
"EC:7.1.1",
"REACTOME:R-DDI-6799198",
"REACTOME:R-DDI-9837999",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-6799198",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-611105",
"REACTOME:R-MMU-6799198",
"REACTOME:R-MMU-9837999",
"REACTOME:R-SPO-9837999"
] | 10 | [
"2j58",
"2w8h",
"2w8i",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6q9d",
"6qa9",
"6qbx",
"6qc2",
"6qc3",
"6qc4",
"6qc5",
"6qc6",
"6qc7",
"6qc8",
"6qc9",
"6qca",
"6qcf",
"6rfq",
"6rfr"... | 271 | [
"PUB00040815",
"PUB00041878",
"PUB00044948",
"PUB00050072",
"PUB00098488",
"PUB00098489",
"PUB00149920",
"PUB00154862"
] | [
"16469879",
"17086202",
"17250770",
"19294709",
"28844695",
"27595392",
"27509854",
"32625172"
] | [
"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.",
"Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein.",
"A novel superfamily containing the beta-grasp fold involved in binding diverse soluble ligands.",
"PELDOR spectroscopy... | [
2006,
2006,
2007,
2009,
2017,
2016,
2016,
2020
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"unclassified sequences"
] | [
20582,
4816,
6,
289
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
2,
1,
1,
7,
2,
9,
3,
1,
5,
4,
1,
10
] | 12 | true | Domain | SLBB domain | SLBB domain | SLBB_dom | 5 |
IPR054766 | 54,766 | Initiator protein NS1-like, N-terminal domain, Bocavirus | BoV_NS1-like_N | Domain | 404 | false | false | This entry represents the N-terminal domain of the Human bocavirus 1 (HBoV1) nonstructural protein 1 (NS1) and similar sequences specific to bocavirus. HBoV-NS1 is a member of the histidine-hydrophobic-histidine (HUH) superfamily of endonucleases [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22419"
] | [
"HBoV_NS1-like_N"
] | [
404
] | 1 | [
"EC",
"EC"
] | [
"3.1.21.-",
"3.6.4.12"
] | [
"EC:3.1.21.-",
"EC:3.6.4.12"
] | 2 | [
"4kw3"
] | 1 | [
"PUB00153286"
] | [
"23966383"
] | [
"Structure of the NS1 protein N-terminal origin recognition/nickase domain from the emerging human bocavirus."
] | [
2013
] | 1 | [
"IPR049901"
] | [] | 1 | 0 | 1 | [
"Parvoviridae"
] | [
404
] | 1 | [] | [] | 0 | true | Domain | Initiator protein NS1-like, N-terminal domain, Bocavirus | Initiator protein NS1-like, N-terminal domain, Bocavirus | BoV_NS1-like_N | 8 |
IPR054767 | 54,767 | Cas10/Cmr2, second palm domain | Cas10-Cmr2_palm2 | Domain | 2,751 | false | false | This entry represents the second palm domain of Cas10 subunit (named Csm1 in Type III-A and Cmr2 in III-B systems) from type III CRISPR-Cas systems [ ]. This domain contains a conserved GGDD motif that is important for DNA polymerase activity [ , , , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22335"
] | [
"Cas10-Cmr2_palm2"
] | [
2751
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.-",
"PWY-6322",
"PWY-6626",
"PWY-6749",
"PWY-6955",
"PWY-6998",
"PWY-7127",
"PWY-7419",
"PWY-7529",
"PWY-7706",
"PWY-7719",
"PWY-7735",
"PWY-7737",
"PWY-7769",
"PWY-7888",
"PWY-7904",
"PWY-8117",
"PWY-8179"
] | [
"EC:2.7.7.-",
"METACYC:PWY-6322",
"METACYC:PWY-6626",
"METACYC:PWY-6749",
"METACYC:PWY-6955",
"METACYC:PWY-6998",
"METACYC:PWY-7127",
"METACYC:PWY-7419",
"METACYC:PWY-7529",
"METACYC:PWY-7706",
"METACYC:PWY-7719",
"METACYC:PWY-7735",
"METACYC:PWY-7737",
"METACYC:PWY-7769",
"METACYC:PWY-7... | 18 | [
"3ung",
"3ur3",
"3w2v",
"3w2w",
"3x1l",
"4doz",
"4h4k",
"4uw2",
"4w8y",
"6ifk",
"6ifl",
"6ifn",
"6ifr",
"6ifu",
"6ify",
"6ifz",
"6ig0",
"6iqw",
"6kbd",
"6kc0",
"6mua",
"6mur",
"6mus",
"6mut",
"6muu",
"6nud",
"6nue",
"6o73",
"6o74",
"6o75",
"6o78",
"6o79"... | 77 | [
"PUB00065747",
"PUB00065812",
"PUB00091420",
"PUB00097430",
"PUB00150948",
"PUB00151629"
] | [
"22405013",
"23395183",
"25773141",
"22449983",
"23583914",
"33352158"
] | [
"Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex.",
"Structure of the cmr2-cmr3 subcomplex of the cmr RNA silencing complex.",
"Crystal structure of the Csm1 subunit of the Csm complex and its single-stranded DNA-specific nuclease activity.",
"Crystal structure of Cmr2 suggests a nucleot... | [
2012,
2013,
2015,
2012,
2013,
2021
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
241,
2472,
38
] | 3 | [] | [] | 0 | true | Domain | Cas10/Cmr2, second palm domain | Cas10/Cmr2, second palm domain | Cas10-Cmr2_palm2 | 5 |
IPR054768 | 54,768 | Phage tubulin-like protein, C-terminal domain | PhuZ_C | Domain | 19 | false | false | This domain is found at the C-terminal of phage tubulin-like protein from the Pseudomonas phage phiKZ (PhuZ, also known as TubZ) and similar viral sequences. TubZ is a tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replicatio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22334"
] | [
"TubZ_C_2"
] | [
19
] | 1 | [
"EC"
] | [
"3.6.5.-"
] | [
"EC:3.6.5.-"
] | 1 | [
"3j5v",
"3r4v",
"3rb8",
"3zbp",
"3zbq"
] | 5 | [
"PUB00063970",
"PUB00154308",
"PUB00154309",
"PUB00154310"
] | [
"22726436",
"23528827",
"28813669",
"24631461"
] | [
"A phage tubulin assembles dynamic filaments by an atypical mechanism to center viral DNA within the host cell.",
"Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ.",
"The Phage Nucleus and Tubulin Spindle Are Conserved among Large Pseudomonas Phages.",
"The structure and ass... | [
2012,
2013,
2017,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
19
] | 1 | [] | [] | 0 | true | Domain | Phage tubulin-like protein, C-terminal domain | Phage tubulin-like protein, C-terminal domain | PhuZ_C | 6 |
IPR054769 | 54,769 | Internalin J, EF-hand domain | InlJ_EF-hand | Domain | 110 | false | false | This entry represents the N-terminal EF-hand domain present in Internalin J proteins from Listeria species [ ]. InlJ is involved in several steps of L.monocytogenes infection by both intravenous and oral infection [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22350"
] | [
"Int_EF-hand"
] | [
110
] | 1 | [] | [] | [] | 0 | [
"3bz5"
] | 1 | [
"PUB00050832",
"PUB00094688",
"PUB00154863"
] | [
"18343406",
"16177371",
"18227172"
] | [
"Crystal structure and standardized geometric analysis of InlJ, a listerial virulence factor and leucine-rich repeat protein with a novel cysteine ladder.",
"LPXTG protein InlJ, a newly identified internalin involved in Listeria monocytogenes virulence.",
"The Listeria monocytogenes virulence factor InlJ is spe... | [
2008,
2005,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
110
] | 1 | [] | [] | 0 | true | Domain | Internalin J, EF-hand domain | Internalin J, EF-hand domain | InlJ_EF-hand | 1 |
IPR054770 | 54,770 | SgrA-like, Ig-like domain | SgrA-like_Ig-like | Domain | 32 | false | false | This entry represents a Immunoglobulin-like (Ig-like) domain present in the Serine-glutamate repeat protein A (SgrA, ), also known as LPXTG family cell surface protein Fms2 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22312"
] | [
"SgrA_ig-like"
] | [
32
] | 1 | [] | [] | [] | 0 | [
"5fce"
] | 1 | [
"PUB00154230"
] | [
"27334767"
] | [
"The crystal structure of the ligand-binding region of serine-glutamate repeat containing protein A (SgrA) of Enterococcus faecium reveals a new protein fold: functional characterization and insights into its adhesion function."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Enterococcus"
] | [
32
] | 1 | [] | [] | 0 | true | Domain | SgrA-like, Ig-like domain | SgrA-like, Ig-like domain | SgrA-like_Ig-like | 5 |
IPR054772 | 54,772 | Lmo2445-like, C-terminal domain | Lmo2445-like_C | Domain | 29 | false | false | This domain is found at the C-terminal of the Lmo2445 protein from Listeria monocytogenes ( ). This domain shows a immunoglobulin-like fold. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22416"
] | [
"Lmo2445-like_C"
] | [
29
] | 1 | [] | [] | [] | 0 | [
"5hzl"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Listeria"
] | [
29
] | 1 | [] | [] | 0 | true | Domain | Lmo2445-like, C-terminal domain | Lmo2445-like, C-terminal domain | Lmo2445-like_C | 5 |
IPR054773 | 54,773 | Protein P1-like, N-terminal domain | P1-like_N | Domain | 11 | false | false | This domain is found at the N-terminal of Protein P1 from Acyrthosiphon pisum virus ( ) and similar proteins from arthropod-infecting viruses. This region has been named the 'Widespread, Intriguing, Versatile' (WIV) domain. This region is likely to play a role in viral infection of arthropods. It is often found associa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22533"
] | [
"WIV_dom_3"
] | [
11
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
11
] | 1 | [] | [] | 0 | true | Domain | Protein P1-like, N-terminal domain | Protein P1-like, N-terminal domain | P1-like_N | 2 |
IPR054774 | 54,774 | 2-Component system ADP-ribose glycohydrolase domain | 2CompARG | Domain | 16 | false | false | This entry represents the 2CompARG domain, which coupled with its partner 2CompART (represented by ), forms a two-domain T-A-like association in the duplex-forming systems likely functioning as the principal effector of these systems in bacteroidetes. One is likely to function as the antitoxin, regulating the toxin act... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22545"
] | [
"2CompARG"
] | [
16
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteroidota"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | 2-Component system ADP-ribose glycohydrolase domain | 2-Component system ADP-ribose glycohydrolase domain | 2CompARG | 1 |
IPR054775 | 54,775 | 2-Component system ADP-ribosyltransferase domain | 2CompART | Domain | 32 | false | false | This entry represents the 2CompART domain, which coupled with its partner 2CompARG (represented by ), forms a two-domain T-A-like association in the duplex-forming systems likely functioning as the principal effector of these systems in bacteroidetes. One is likely to function as the antitoxin, regulating the toxin act... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22546"
] | [
"2CompART"
] | [
32
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
32
] | 1 | [] | [] | 0 | true | Domain | 2-Component system ADP-ribosyltransferase domain | 2-Component system ADP-ribosyltransferase domain | 2CompART | 3 |
IPR054776 | 54,776 | Virilizer, yeast | VIR1_yeast | Family | 65 | false | false | This entry includes virilizer (VIR1), the yeast homologue of human virilizer (VIRMA) [ ]. VIR1 is a component of the MIS complex, a complex that mediates N6-methyladenosine (m6A) methylation of meiotic mRNAs and is required for initiation of meiosis, progression through the meiotic divisions and sporulation. In the com... | [
"GO:0045944",
"GO:0051321"
] | [
"positive regulation of transcription by RNA polymerase II",
"meiotic cell cycle"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF22575"
] | [
"Vir1p"
] | [
65
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154326"
] | [
"36930734"
] | [
"Vir1p, the yeast homolog of virilizer, is required for mRNA m6A methylation and meiosis."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
65
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Virilizer, yeast | Virilizer, yeast | VIR1_yeast | 2 |
IPR054777 | 54,777 | BARF1, second Ig-like domain | BARF1_Ig_2 | Domain | 33 | false | false | This entry represents the second immunoglobulin-like domain present in the BARF1 protein from Epstein-Barr virus and similar proteins from Herpesvirales. BARF1 plays diverse functions in immunomodulation and oncogenicity, maybe by acting as a functional receptor for human CSF1. It may also inhibit interferon secretion ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22305"
] | [
"BARF1_ig2"
] | [
33
] | 1 | [] | [] | [] | 0 | [
"2ch8",
"3uez",
"4adf",
"4adq",
"4fa8"
] | 5 | [
"PUB00040015",
"PUB00065878",
"PUB00153831"
] | [
"16647084",
"22826234",
"22902366"
] | [
"Structure of the Epstein-Barr virus oncogene BARF1.",
"Multipronged attenuation of macrophage-colony stimulating factor signaling by Epstein-Barr virus BARF1.",
"Allosteric competitive inactivation of hematopoietic CSF-1 signaling by the viral decoy receptor BARF1."
] | [
2006,
2012,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Lymphocryptovirus"
] | [
33
] | 1 | [] | [] | 0 | true | Domain | BARF1, second Ig-like domain | BARF1, second Ig-like domain | BARF1_Ig_2 | 1 |
IPR054778 | 54,778 | Regulatory protein SIR3, C-terminal domain | SIR3_C | Domain | 17 | false | false | This domain is found at the C-terminal of Regulatory protein SIR3 from Saccharomyces cerevisiae and similar fungal proteins. SIR3 is essential for gene silencing. It is organised into a highly conserved N-terminal BAH domain ( ), a C-terminal AAA+ ATPase-like domain ( ), plus an extreme C-terminal domain (this entry). ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22344"
] | [
"SIR3_C"
] | [
17
] | 1 | [] | [] | [] | 0 | [
"3zco"
] | 1 | [
"PUB00154233"
] | [
"23299941"
] | [
"Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomyces"
] | [
17
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Regulatory protein SIR3, C-terminal domain | Regulatory protein SIR3, C-terminal domain | SIR3_C | 2 |
IPR054779 | 54,779 | Cysteine peptidase, putative, mycoplasmatota | Cys_pept_put_mycoplasmatota | Domain | 97 | false | false | This entry represents a region about 240 amino acids long with local similarity to C39 and C10 families of cysteine peptidases, including the region of the active site Cys. Members of this group occur in Mycoplasmatota. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045837"
] | [
"Mplas_Cys_pep"
] | [
97
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
97
] | 1 | [] | [] | 0 | true | Domain | Cysteine peptidase, putative, mycoplasmatota | Cysteine peptidase, putative, mycoplasmatota | Cys_pept_put_mycoplasmatota | 8 |
IPR054780 | 54,780 | Cytochrome c550, firmicutes | Cytochro_C550_firm | Family | 795 | false | false | C-type cytochrome c550 (also known as CccA) differs from its close homologue cytochrome c551 (also known as CccB) in having a regular rather than lipoprotein signal peptide [ , , ]. Cytochrome c550 is dispensable for growth and sporulation, however, it may play an important role for initiation of sporulation [ ]. Membe... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045773"
] | [
"cytochro_C550"
] | [
795
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154706",
"PUB00154707",
"PUB00154708",
"PUB00154709",
"PUB00154710"
] | [
"10473570",
"15995641",
"11361075",
"19222757",
"10024472"
] | [
"Bacillus subtilis contains two small c-type cytochromes with homologous heme domains but different types of membrane anchors.",
"Cytochrome c550 is related to initiation of sporulation in Bacillus subtilis.",
"Catabolite regulation of the cytochrome c550-encoding Bacillus subtilis cccA gene.",
"Two small c-t... | [
1999,
2005,
2001,
2009,
1999
] | 5 | [
"IPR012218"
] | [] | 1 | 0 | 1 | [
"Bacillales"
] | [
795
] | 1 | [] | [] | 0 | true | Family | Cytochrome c550, firmicutes | Cytochrome c550, firmicutes | Cytochro_C550_firm | 6 |
IPR054781 | 54,781 | Asp23-related | Asp23-rel | Family | 152 | false | false | This family, restricted to the phylum Mycoplasmatota, shows evidence of homology to some members of the Asp23 family ( ), which was named for a Staphylococcus aureus stress protein called alkaline shock protein 23. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045836"
] | [
"MMB_0454_fam"
] | [
152
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
152
] | 1 | [] | [] | 0 | true | Family | Asp23-related | Asp23-related | Asp23-rel | 9 |
IPR054783 | 54,783 | HinT-interacting membrane complex lipoprotein P60-like | P60-like | Family | 141 | false | false | This entry represents a group of proteins from Mycoplasmatota, including lipoprotein P60 from Metamycoplasma hominis. This protein is part of a complex that interacts with HinT, a lineage-specific subgroup of the cytosolic histidine triad (HIT) family of proteins [ , ]. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045835",
"PF28251"
] | [
"P60_lipo",
"P60-like"
] | [
127,
141
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035586",
"PUB00154805"
] | [
"15904496",
"15579213"
] | [
"HinT proteins and their putative interaction partners in Mollicutes and Chlamydiaceae.",
"P80, the HinT interacting membrane protein, is a secreted antigen of Mycoplasma hominis."
] | [
2005,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
141
] | 1 | [] | [] | 0 | true | Family | HinT-interacting membrane complex lipoprotein P60-like | HinT-interacting membrane complex lipoprotein P60-like | P60-like | 1 |
IPR054784 | 54,784 | HpyAIV-type II restriction enzyme | HpyAIV-type_restriction_enz | Family | 137 | false | false | This entry represents a group of bacterial proteins, inluding HP1351 from Helicobacter pylori ( ), designated HpyAIV by the restriction enzyme database REBASE. It is a type II restriction enzyme that recognises GANTC. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045832"
] | [
"restrict_HpyAIV"
] | [
137
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
2,
133,
2
] | 3 | [] | [] | 0 | true | Family | HpyAIV-type II restriction enzyme | HpyAIV-type II restriction enzyme | HpyAIV-type_restriction_enz | 9 |
IPR054785 | 54,785 | Type II restriction enzyme HinfI | HinfI | Family | 32 | false | false | This entry represents a group of bacterial type II restriction enzymes, including Type II restriction enzyme HinfI from Haemophilus influenzae, which recognises the double-stranded sequence 5'-GANTC-3' and cleaves after G-1 [ , ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045831"
] | [
"restrict_HinfI"
] | [
32
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00081252",
"PUB00154748"
] | [
"18456708",
"3063606"
] | [
"Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses.",
"Cloning and sequencing the HinfI restriction and modification genes."
] | [
2008,
1988
] | 2 | [
"IPR019045"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
32
] | 1 | [] | [] | 0 | true | Family | Type II restriction enzyme HinfI | Type II restriction enzyme HinfI | HinfI | 1 |
IPR054786 | 54,786 | MYPU_1760-like | MYPU_1760-like | Family | 111 | false | false | This entry represents a group of proteins from Mycoplasmatota, including MYPU_1760 from Mycoplasmopsis pulmoni ( ). Members of this family average over 600 amino acids in length, and contain a region similar to a region of the zinc metalloproteases from , including the signature motif HEYxH. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045830",
"PF28253"
] | [
"MYPU_1760_HExxH",
"MYPU_1760"
] | [
93,
111
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
111
] | 1 | [] | [] | 0 | true | Family | MYPU_1760-like | MYPU_1760-like | MYPU_1760-like | 7 |
IPR054787 | 54,787 | TrlF AAA-like ATPase | TrlF_ATPase | Family | 1,742 | false | false | This entry represents TrlF from Photorhabdus laumondii ( ) and similar bacterial sequences. TrlF was described as an 875-amino acid protein encoded in a small genomic island operon next to TrlG, whose mutation and loss of function restores an ability to grow at 36 degrees [ , ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045780"
] | [
"TrlF_fam_ATP"
] | [
1742
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154665",
"PUB00154666"
] | [
"22529932",
"33101227"
] | [
"Complete genome and transcriptomes of Streptococcus parasanguinis FW213: phylogenic relations and potential virulence mechanisms.",
"Temperature Restriction in Entomopathogenic Bacteria."
] | [
2012,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Thelohanellus kitauei",
"Yersinia phage vB_YenM_42.18",
"metagenomes"
] | [
1697,
32,
1,
1,
11
] | 5 | [] | [] | 0 | true | Family | TrlF AAA-like ATPase | TrlF AAA-like ATPase | TrlF_ATPase | 5 |
IPR054788 | 54,788 | MSC_0620/UU052-like | MSC_0620_UU052-like | Family | 192 | false | false | This entry represents a group of proteins from Mycoplasmatota, including MSC_0620 from Mycoplasma mycoides ( ) and UU052 from Ureaplasma parvum ( ). Neighbouring proteins include paralogues to the alpha, beta, gamma, and epsilon subunits of the F1 ATPase, and are subunits of a related complex found only in the Mycoplas... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045829",
"PF28258"
] | [
"UU052_fam",
"MSC_0620_UU052"
] | [
169,
192
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154868"
] | [
"22685606"
] | [
"Specific evolution of F1-like ATPases in mycoplasmas."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
192
] | 1 | [] | [] | 0 | true | Family | MSC_0620/UU052-like | MSC_0620/UU052-like | MSC_0620_UU052-like | 6 |
IPR054789 | 54,789 | P97 adhesin, N-terminal domain | P97_adhes_N | Domain | 225 | false | false | This entry represents a region found at the N-terminal of a group of P97-like proteins mainly found in Mesomycoplasma species, including Mhp107 ( , [ ]) and Mhp385 ( , [ ]). | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045828",
"PF28259"
] | [
"P97_adhes_Nterm",
"P97_adhes_N"
] | [
218,
225
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105392",
"PUB00154779",
"PUB00154780",
"PUB00154781",
"PUB00154782",
"PUB00154783"
] | [
"30395255",
"24804907",
"21245147",
"7868222",
"16369004",
"22229926"
] | [
"VFDB 2019: a comparative pathogenomic platform with an interactive web interface.",
"Cilium adhesin P216 (MHJ_0493) is a target of ectodomain shedding and aminopeptidase activity on the surface of Mycoplasma hyopneumoniae.",
"Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae.... | [
2019,
2014,
2011,
1995,
2006,
2012
] | 6 | [] | [] | 0 | 0 | null | [
"Mesomycoplasma"
] | [
225
] | 1 | [] | [] | 0 | true | Domain | P97 adhesin, N-terminal domain | P97 adhesin, N-terminal domain | P97_adhes_N | 8 |
IPR054790 | 54,790 | N-acetylmuramate alpha-1-phosphate uridylyltransferase | MurU | Family | 4,161 | false | false | This family includes N-acetylmuramate alpha-1-phosphate uridylyltransferase (MurU) from beta and gammaproteobacteria. It catalyses the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P. It is involved in peptidoglycan recycling as ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045761"
] | [
"NAMPUrTaseMurU"
] | [
4161
] | 1 | [
"EC",
"METACYC"
] | [
"2.7.7.99",
"PWY-7883"
] | [
"EC:2.7.7.99",
"METACYC:PWY-7883"
] | 2 | [
"4y7t",
"4y7u",
"4y7v",
"8hhd"
] | 4 | [
"PUB00154740",
"PUB00154741",
"PUB00154742"
] | [
"23831760",
"24819062",
"25767118"
] | [
"A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis.",
"Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates intrinsic resistance to fosfomycin.",
"Crystal Structure of the N-Acetylmuramic Acid α-1-Phosphate (MurNAc-α1-P) Uridylyltransferase MurU, a Minimal Sugar Nu... | [
2013,
2014,
2015
] | 3 | [
"IPR050065"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
4078,
4,
79
] | 3 | [] | [] | 0 | true | Family | N-acetylmuramate alpha-1-phosphate uridylyltransferase | N-acetylmuramate alpha-1-phosphate uridylyltransferase | MurU | 2 |
IPR054792 | 54,792 | HSGNP motif-containing (seleno)protein TsoX | TsoX | Family | 17 | false | false | This entry represents a small group of short bacterial selenoproteins with a UxxC selenocysteine-containing motif immediately preceded by a signature motif HSGNPX. Most members contain selenocysteine. At least five members are fusion proteins with a C-terminal thioredoxin-disulfide reductase region ( ). Members of this... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045809",
"PF26315"
] | [
"seleno_TsoX",
"TsoX"
] | [
17,
17
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161499"
] | [
"40162776"
] | [
"Novel selenoprotein neighborhoods suggest specialized biochemical processes."
] | [
2025
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
17
] | 1 | [] | [] | 0 | true | Family | HSGNP motif-containing (seleno)protein TsoX | HSGNP motif-containing (seleno)protein TsoX | TsoX | 8 |
IPR054793 | 54,793 | HTH-type transcriptional regulator AlsR | AlsR | Family | 234 | false | false | This entry represents the HTH-type transcriptional regulator AlsR from Bacillus subtilis and similar proteins from Bacillales. AlsR is responsible for activating the expression of the acetoin operon (alsSD) in response to inducing signals such as glucose and acetate. Like many other LysR family proteins, AlsR is transc... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045775"
] | [
"acetoin_reg_AlsR"
] | [
234
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00086916",
"PUB00086917",
"PUB00154713"
] | [
"7685336",
"22178965",
"23695583"
] | [
"Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin.",
"The transcription factor AlsR binds and regulates the promoter of the alsSD operon responsible for acetoin formation in Bacillus subtilis.",
"Purification, crystallization and preliminary... | [
1993,
2012,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
234
] | 1 | [] | [] | 0 | true | Family | HTH-type transcriptional regulator AlsR | HTH-type transcriptional regulator AlsR | AlsR | 4 |
IPR054794 | 54,794 | Antitoxin TumA | TumA | Family | 127 | false | false | This family represents the antitoxin component TumA from the TumE-TumA toxin-antitoxin system [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045776"
] | [
"TumA"
] | [
127
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154744"
] | [
"37704037"
] | [
"Uncovering new families and folds in the natural protein universe."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
124,
3
] | 2 | [] | [] | 0 | true | Family | Antitoxin TumA | Antitoxin TumA | TumA | 3 |
IPR054795 | 54,795 | Toxin TumE | TumE | Family | 75 | false | false | This entry represents a small group of bacterial sequences, recently described as the toxin component TumE from the novel toxin-antitoxin system TumE-TumA [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045777"
] | [
"TumE"
] | [
75
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154744"
] | [
"37704037"
] | [
"Uncovering new families and folds in the natural protein universe."
] | [
2023
] | 1 | [
"IPR045397"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"marine sediment metagenome"
] | [
74,
1
] | 2 | [] | [] | 0 | true | Family | Toxin TumE | Toxin TumE | TumE | 2 |
IPR054796 | 54,796 | Gas vesicle protein GvpL | Gas_vesic_GvpL | Family | 151 | false | false | This entry includes gas vesicle protein L (GvpL) from archaea, mainly from halobacteria. A cluster of 12-14 gvp genes (gvpMLKJIHGFEDACNO) is responsible for gas vesicle synthesis in Halobacterium sp. [ ]. GvpL is essential for gas vesicle formation and displays sequence similarity to GvpF, both containing predicted coi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045778"
] | [
"gas_vesic_GvpL"
] | [
151
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014923"
] | [
"15126480"
] | [
"Complexity of gas vesicle biogenesis in Halobacterium sp. strain NRC-1: identification of five new proteins."
] | [
2004
] | 1 | [
"IPR009430"
] | [] | 1 | 0 | 1 | [
"Candidatus Hakubella thermalkaliphila",
"Halobacteriales"
] | [
3,
148
] | 2 | [] | [] | 0 | true | Family | Gas vesicle protein GvpL | Gas vesicle protein GvpL | Gas_vesic_GvpL | 7 |
IPR054797 | 54,797 | Gas vesicle protein GvpG, halobacteria | Gas_vesic_GvpG_halobact | Family | 143 | false | false | Gas vesicles are intracellular, protein-coated, and hollow organelles found in cyanobacteria and halophilic archaea [ ]. They are permeable to ambient gases by diffusion and provide buoyancy, enabling cells to move upwards in water to access oxygen and/or light , ]. This family represents Gas vesicle protein G from hal... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045779"
] | [
"gas_vesic_GvpG"
] | [
143
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014923",
"PUB00151154"
] | [
"15126480",
"33711860"
] | [
"Complexity of gas vesicle biogenesis in Halobacterium sp. strain NRC-1: identification of five new proteins.",
"Growth competition between <i>Halobacterium salinarium</i> strain PHH1 and mutants affected in gas vesicle synthesis."
] | [
2004,
1997
] | 2 | [
"IPR007804"
] | [] | 1 | 0 | 1 | [
"Halobacteriales"
] | [
143
] | 1 | [] | [] | 0 | true | Family | Gas vesicle protein GvpG, halobacteria | Gas vesicle protein GvpG, halobacteria | Gas_vesic_GvpG_halobact | 3 |
IPR054798 | 54,798 | AAA-like ATPase Spaf_1101-like | Spaf_1101-like | Family | 100 | false | false | This entry represents a family of AAA-like ATPases, including Spaf_1101 from Streptococcus parasanguinis ( ), which was found at one end of a reported transposon. The high frequency of pseudogenes related to the intact members of this family, typical for genes with higher than average potential costs to the host specie... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045781"
] | [
"Spaf1101_AAA_ATP"
] | [
100
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154665"
] | [
"22529932"
] | [
"Complete genome and transcriptomes of Streptococcus parasanguinis FW213: phylogenic relations and potential virulence mechanisms."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
100
] | 1 | [] | [] | 0 | true | Family | AAA-like ATPase Spaf_1101-like | AAA-like ATPase Spaf_1101-like | Spaf_1101-like | 2 |
IPR054799 | 54,799 | Nicotine blue oxidoreductase | NboR | Family | 60 | false | false | This entry represents nicotine blue oxidoreductase from Paenarthrobacter nicotinovorans (NboR) and similar sequences from actinomycetes. NboR catalyses the reduction of nicotine blue to its hydroquinone form. Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045782"
] | [
"NicBOxredNboR"
] | [
60
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154649"
] | [
"17293530"
] | [
"An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Micrococcaceae"
] | [
60
] | 1 | [] | [] | 0 | true | Family | Nicotine blue oxidoreductase | Nicotine blue oxidoreductase | NboR | 2 |
IPR054800 | 54,800 | Nigerythrin | Nigrythrn | Family | 64 | false | false | This entry represents Nigerythrin from Nitratidesulfovibrio vulgaris, a member of the rubrerythrin (Rbr) family that has NADH peroxidase activity [ , ], and similar sequences from actinomycetota. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045783"
] | [
"Nigrythrn"
] | [
64
] | 1 | [] | [] | [] | 0 | [
"1yux",
"1yuz",
"1yv1"
] | 3 | [
"PUB00038641",
"PUB00112472",
"PUB00154745",
"PUB00154865"
] | [
"15895271",
"8383040",
"9226272",
"21872605"
] | [
"High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins.",
"Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and tw... | [
2005,
1993,
1997,
2011
] | 4 | [
"IPR052753"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
64
] | 1 | [] | [] | 0 | true | Family | Nigerythrin | Nigerythrin | Nigrythrn | 9 |
IPR054801 | 54,801 | Styrene monooxygenase subunit StyA | StyMonoxStyA | Family | 110 | false | false | Styrene monooxygenase StyA catalyses the first step in the aerobic styrene degradation pathway by enantioselective epoxidation of the vinyl side chain. In a two-component system, StyB reductase utilizes NADH to reduce FAD, which is then transferred to the oxygenase; the electron transfer is proposed to occur via a diff... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045732"
] | [
"StyMonoxStyA"
] | [
110
] | 1 | [] | [] | [] | 0 | [
"3ihm"
] | 1 | [
"PUB00122405",
"PUB00154628"
] | [
"9172343",
"25187627"
] | [
"Sequencing and functional analysis of styrene catabolism genes from Pseudomonas fluorescens ST.",
"Styrene oxide isomerase of Sphingopyxis sp. Kp5.2."
] | [
1997,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
110
] | 1 | [] | [] | 0 | true | Family | Styrene monooxygenase subunit StyA | Styrene monooxygenase subunit StyA | StyMonoxStyA | 1 |
IPR054802 | 54,802 | NADH-dependent flavin reductase StyB | StyMonoxStyB | Family | 52 | false | false | This entry includes NADH-dependent flavin reductase StyB, the reductase component of a two-component system that catalyses the first step in the aerobic styrene degradation pathway by enantioselective epoxidation of the vinyl side chain. It utilizes NADH to reduce FAD, which is then transferred to the styrene monooxyge... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045733"
] | [
"StyMonoxStyB"
] | [
52
] | 1 | [] | [] | [] | 0 | [
"4f07"
] | 1 | [
"PUB00122405",
"PUB00154628"
] | [
"9172343",
"25187627"
] | [
"Sequencing and functional analysis of styrene catabolism genes from Pseudomonas fluorescens ST.",
"Styrene oxide isomerase of Sphingopyxis sp. Kp5.2."
] | [
1997,
2014
] | 2 | [
"IPR050268"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
52
] | 1 | [] | [] | 0 | true | Family | NADH-dependent flavin reductase StyB | NADH-dependent flavin reductase StyB | StyMonoxStyB | 4 |
IPR054803 | 54,803 | Styrene-oxide isomerase StyC | StyOxIsoStyC | Family | 84 | false | false | This entry represents Styrene-oxide isomerase StyC, an epoxystyrene isomerase that catalyses the second step in the aerobic styrene degradation pathway by converting epoxystyrene to phenylacetaldehyde [ , ]. | [
"GO:0018846",
"GO:0042207"
] | [
"styrene-oxide isomerase activity",
"styrene catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"NF045734"
] | [
"StyOxIsoStyC"
] | [
84
] | 1 | [] | [] | [] | 0 | [
"8pnu",
"8pnv"
] | 2 | [
"PUB00122405",
"PUB00154628"
] | [
"9172343",
"25187627"
] | [
"Sequencing and functional analysis of styrene catabolism genes from Pseudomonas fluorescens ST.",
"Styrene oxide isomerase of Sphingopyxis sp. Kp5.2."
] | [
1997,
2014
] | 2 | [
"IPR058965"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
69,
15
] | 2 | [] | [] | 0 | true | Family | Styrene-oxide isomerase StyC | Styrene-oxide isomerase StyC | StyOxIsoStyC | 7 |
IPR054805 | 54,805 | Phenylacetaldehyde dehydrogenase | StyD | Family | 105 | false | false | This entry includes phenylacetaldehyde dehydrogenase StyD, which catalyses the last step in the aerobic styrene degradation pathway by mediating oxidation of phenylacetaldehyde to phenylacetic acid [ , ]. Members of this group are mainly found in Betaproteobacteria. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045735"
] | [
"PaDhStyDPseudo"
] | [
105
] | 1 | [] | [] | [] | 0 | [
"4qyj"
] | 1 | [
"PUB00122405",
"PUB00154628"
] | [
"9172343",
"25187627"
] | [
"Sequencing and functional analysis of styrene catabolism genes from Pseudomonas fluorescens ST.",
"Styrene oxide isomerase of Sphingopyxis sp. Kp5.2."
] | [
1997,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
105
] | 1 | [] | [] | 0 | true | Family | Phenylacetaldehyde dehydrogenase | Phenylacetaldehyde dehydrogenase | StyD | 1 |
IPR054806 | 54,806 | NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon | PadH | Family | 45 | false | false | This entry includes NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon (PadH) from Aromatoleum evansii, which is involved in the anaerobic metabolism of phenylalanine and phenylacetate. The system catalyses the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly wit... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045765"
] | [
"PhenlGlyoxDHPadH"
] | [
45
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154629"
] | [
"9490067"
] | [
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii."
] | [
1998
] | 1 | [
"IPR050260"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati",
"mine drainage metagenome"
] | [
44,
1
] | 2 | [] | [] | 0 | true | Family | NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon | NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon | PadH | 7 |
IPR054807 | 54,807 | NADH-dependent phenylglyoxylate dehydrogenase subunit alpha | PadG | Family | 45 | false | false | This family represents NADH-dependent phenylglyoxylate dehydrogenase subunit alpha (PadG), which is involved in the anaerobic metabolism of phenylalanine and phenylacetate. It catalyses the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly with 2-oxo-3-methylbutanoate and us... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045764"
] | [
"PhenlGlyoxDHPadG"
] | [
45
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154629"
] | [
"9490067"
] | [
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii."
] | [
1998
] | 1 | [
"IPR050722"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati",
"mine drainage metagenome"
] | [
44,
1
] | 2 | [] | [] | 0 | true | Family | NADH-dependent phenylglyoxylate dehydrogenase subunit alpha | NADH-dependent phenylglyoxylate dehydrogenase subunit alpha | PadG | 1 |
IPR054808 | 54,808 | NADH-dependent phenylglyoxylate dehydrogenase subunit beta | PadI | Family | 42 | false | false | This family represents NADH-dependent phenylglyoxylate dehydrogenase subunit beta (PadI), which is involved in the anaerobic metabolism of phenylalanine and phenylacetate. This system catalyses the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly with 2-oxo-3-methylbutanoat... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045766"
] | [
"PhenlGlyoxDHPadI"
] | [
42
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154629"
] | [
"9490067"
] | [
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii."
] | [
1998
] | 1 | [
"IPR051479"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota",
"mine drainage metagenome"
] | [
41,
1
] | 2 | [] | [] | 0 | true | Family | NADH-dependent phenylglyoxylate dehydrogenase subunit beta | NADH-dependent phenylglyoxylate dehydrogenase subunit beta | PadI | 9 |
IPR054809 | 54,809 | PilM-like pilus complex protein Amuc_1101-like | Amuc_1101-like | Family | 46 | false | false | This entry represents a group of proteins from Verrucomicrobiota, including Amuc_1101 from Akkermansia muciniphila ( ), a PilM-like protein from a variant type of IV-pilin complex. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045709"
] | [
"Amuc_1101_fam"
] | [
46
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR005883"
] | [] | 1 | 0 | 1 | [
"Verrucomicrobiota"
] | [
46
] | 1 | [] | [] | 0 | true | Family | PilM-like pilus complex protein Amuc_1101-like | PilM-like pilus complex protein Amuc_1101-like | Amuc_1101-like | 3 |
IPR054811 | 54,811 | NADH-dependent phenylglyoxylate dehydrogenase subunit gamma | PadE | Family | 44 | false | false | This entry includes NADH-dependent phenylglyoxylate dehydrogenase subunit gamma (PadE) which is involved in the anaerobic metabolism of phenylalanine and phenylacetate. The system catalyzes the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly with 2-oxo-3-methylbutanoate an... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045762"
] | [
"PhenlGlyoxDHPadE"
] | [
44
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154629"
] | [
"9490067"
] | [
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii."
] | [
1998
] | 1 | [
"IPR051626"
] | [] | 1 | 0 | 1 | [
"Pseudomonadati",
"mine drainage metagenome"
] | [
43,
1
] | 2 | [] | [] | 0 | true | Family | NADH-dependent phenylglyoxylate dehydrogenase subunit gamma | NADH-dependent phenylglyoxylate dehydrogenase subunit gamma | PadE | 8 |
IPR054812 | 54,812 | NADH-dependent phenylglyoxylate dehydrogenase subunit delta | PadF | Family | 42 | false | false | This family includes NADH-dependent phenylglyoxylate dehydrogenase subunit delta (PadF), which is involved in the anaerobic metabolism of phenylalanine and phenylacetate. The pathway catalyses the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO2. It can also react slowly with 2-oxo-3-methylbutanoate... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045763"
] | [
"PhenlGlyoxDHPadF"
] | [
42
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154629"
] | [
"9490067"
] | [
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii."
] | [
1998
] | 1 | [
"IPR011898"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota",
"mine drainage metagenome"
] | [
41,
1
] | 2 | [] | [] | 0 | true | Family | NADH-dependent phenylglyoxylate dehydrogenase subunit delta | NADH-dependent phenylglyoxylate dehydrogenase subunit delta | PadF | 8 |
IPR054813 | 54,813 | Sulfate respiration complex hexadecaheme cytochrome HmcA | HmcA | Family | 88 | false | false | This entry represents a group of proteins mainly from Thermodesulfobacteriota, including HmcA (high molecular weight cytochrome complex protein A or high molecular weight cytochrome c), a periplasmic protein typically with 16 intact CxxCH motifs typical of c-type cytochromes. HmcA is encoded in a six-gene operon well-c... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045713"
] | [
"CxxCH_16_HmcA"
] | [
88
] | 1 | [] | [] | [] | 0 | [
"1gws",
"1h29",
"1z1n",
"2cvc",
"2e84"
] | 5 | [
"PUB00021717",
"PUB00025401"
] | [
"12356749",
"12467575"
] | [
"Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.",
"The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3)."
] | [
2002,
2002
] | 2 | [
"IPR002322"
] | [
"IPR011346"
] | 1 | 1 | 0 | [
"Bacteria"
] | [
88
] | 1 | [] | [] | 0 | true | Family | Sulfate respiration complex hexadecaheme cytochrome HmcA | Sulfate respiration complex hexadecaheme cytochrome HmcA | HmcA | 7 |
IPR054815 | 54,815 | DVU0259-like | DVU0259-like | Family | 108 | false | false | This entry represents a group of proteins mainly from Thermodesulfobacteriota, including DVU0259 from Nitratidesulfovibrio vulgaris ( , also known as DivK), a response regulator receiver domain protein apparently with no DNA-binding domain. The architecture suggests that DivK acts through protein-protein interaction ra... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045717"
] | [
"DVU0259_DivK"
] | [
108
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR050595"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
108
] | 1 | [] | [] | 0 | true | Family | DVU0259-like | DVU0259-like | DVU0259-like | 9 |
IPR054816 | 54,816 | Mollicutes-type lipoprotein signal peptide region | Lipoprotein_mollicutes-type_CS | Conserved_site | 2,068 | false | false | This entry represents a lipoprotein signal peptide predominantly found in Mollicutes, including Spiralin from Spiroplasma citri. | [] | [] | [] | 0 | [
"NCBIFAM",
"NCBIFAM"
] | [
"NF038029",
"NF045726"
] | [
"LP_plasma",
"XXplasma_LP"
] | [
1741,
870
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154736"
] | [
"16788201"
] | [
"Distinctive repertoire of contingency genes conferring mutation- based phase variation and combinatorial expression of surface lipoproteins in Mycoplasma capricolum subsp. capricolum of the Mycoplasma mycoides phylogenetic cluster."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
2044,
24
] | 2 | [] | [] | 0 | true | Conserved_site | Mollicutes-type lipoprotein signal peptide region | Mollicutes-type lipoprotein signal peptide region | Lipoprotein_mollicutes-type_CS | 9 |
IPR054817 | 54,817 | Glycosylhydrolase F510_1955-like | Glycosyl_F510_1955-like | Family | 1,535 | false | false | This entry represents a group of bacterial predicted glycosylhydrolases. This family is after for F510_1955, a lipoprotein from the Gram-positive bacterium Anoxybacillus gonensis [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045728"
] | [
"glycosyl_F510_1955"
] | [
1535
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154661"
] | [
"24603481"
] | [
"Analysis of anoxybacillus genomes from the aspects of lifestyle adaptations, prophage diversity, and carbohydrate metabolism."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Nitrososphaerota",
"ecological metagenomes"
] | [
1524,
3,
8
] | 3 | [] | [] | 0 | true | Family | Glycosylhydrolase F510_1955-like | Glycosylhydrolase F510_1955-like | Glycosyl_F510_1955-like | 2 |
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