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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR053912 | 53,912 | PGAP2IP, first transmembrane domain | PGAP2IP_TM_1nd | Domain | 2,523 | false | false | This domain is found in the human PGAP2-interacting protein (PGAP2IP) and its homologues in yeast CWH43. PGAP2IP is composed of three domains. Two of these domains are predicted to adopt very similar structure consisting of six transmembrane helices, which suggests a possible duplication event in these proteins. These ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23022"
] | [
"6TM_1st_PGAP2IP"
] | [
2523
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00063839"
] | [
"17761529"
] | [
"Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2523
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
5,
1,
1,
5,
1,
1
] | 6 | true | Domain | PGAP2IP, first transmembrane domain | PGAP2IP, first transmembrane domain | PGAP2IP_TM_1nd | 9 |
IPR053913 | 53,913 | DarT1-associated NADAR antitoxin | NADAR-DarT1 | Family | 404 | false | false | This entry, previously known as DUF6977, represents DarT1-associated NADAR antitoxin and related proteins. The DarT-NADAR system is a TA system catalysing the specific and reversible ADP-ribosylation of guanosine bases in which DarT1-associated NADARs reverse guanine ADP-ribosylation catalysed by DarT1. DarT1-associate... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22397"
] | [
"NADAR-DarT1"
] | [
404
] | 1 | [] | [] | [] | 0 | [
"8bat"
] | 1 | [
"PUB00154386"
] | [
"37390817"
] | [
"Molecular basis for the reversible ADP-ribosylation of guanosine bases."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
397,
7
] | 2 | [] | [] | 0 | true | Family | DarT1-associated NADAR antitoxin | DarT1-associated NADAR antitoxin | NADAR-DarT1 | 9 |
IPR053914 | 53,914 | Dispersed gene family protein 1, N-terminal domain | DGF-1_N | Domain | 1,408 | false | false | This entry represents the N-terminal domain present in DGF-1 (Dispersed gene family protein 1) from Trypanosoma, one of the most abundant proteins in T. cruzi genome [ ]. It seems to have a preferential expression in amastigotes (intracellular replicative forms that develop in the mammalian host) [ ]. The function of t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22279"
] | [
"DGF-1_N"
] | [
1408
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153905",
"PUB00153906"
] | [
"36839564",
"19841080"
] | [
"The Elusive <i>Trypanosoma cruzi</i> Disperse Gene Protein Family (DGF-1).",
"Localization and developmental regulation of a dispersed gene family 1 protein in Trypanosoma cruzi."
] | [
2023,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Metakinetoplastina"
] | [
1408
] | 1 | [] | [] | 0 | true | Domain | Dispersed gene family protein 1, N-terminal domain | Dispersed gene family protein 1, N-terminal domain | DGF-1_N | 5 |
IPR053915 | 53,915 | Dispersed gene family protein 1, beta-sheet domain | DGF-1_b-sheet_dom | Domain | 1,368 | false | false | This entry represents a β-sheet domain present in DGF-1 from Trypanosoma proteins, one of the most abundant proteins in T. cruzi genome [ ]. This domain adopts a pectin lyase-like fold. The function of this protein is not yet clear, however, it is likely to play a role in cell-to-cell interactions or signal transductio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22274"
] | [
"DGF-1_beta-sheet"
] | [
1368
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153905"
] | [
"36839564"
] | [
"The Elusive <i>Trypanosoma cruzi</i> Disperse Gene Protein Family (DGF-1)."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1368
] | 1 | [] | [] | 0 | true | Domain | Dispersed gene family protein 1, beta-sheet domain | Dispersed gene family protein 1, beta-sheet domain | DGF-1_b-sheet_dom | 7 |
IPR053916 | 53,916 | Protein of unknown function DUF6978 | DUF6978 | Family | 450 | false | false | This is a family of uncharacterised proteins. They are predicted to adopt a globular α/β structure consisting of a meander β-sheet and two α-helices packed on one side on the sheet. These proteins contain three highly conserved histidines that in the predicted structure cluster close in space and could potentially form... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22398"
] | [
"DUF6978"
] | [
450
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Methanobacteriota",
"Rhizophagus irregularis",
"metagenomes"
] | [
427,
4,
13,
1,
5
] | 5 | [] | [] | 0 | true | Family | Protein of unknown function DUF6978 | Protein of unknown function DUF6978 | DUF6978 | 2 |
IPR053917 | 53,917 | Protein of unknown function DUF6979 | DUF6979 | Family | 208 | false | false | This is a family of uncharacterised proteins. They are predicted to fold into a globular structure consisting mainly of α-helices. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22399"
] | [
"DUF6979"
] | [
208
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Escherichia phage 4A7",
"Methanomicrobia"
] | [
205,
1,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF6979 | Protein of unknown function DUF6979 | DUF6979 | 3 |
IPR053918 | 53,918 | Domain of unknown function DUF6980 | DUF6980 | Domain | 347 | false | false | This is a domain found in uncharacterised bacterial proteins. This domain occurs either standalone or in combination with other domains. It contains conserved cysteines and histidine that may be involved in Zn2 coordination. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22400"
] | [
"DUF6980"
] | [
347
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Glomeromycetes",
"Peduoviridae",
"hydrothermal vent metagenome"
] | [
336,
7,
3,
1
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF6980 | Domain of unknown function DUF6980 | DUF6980 | 6 |
IPR053919 | 53,919 | Treslin, N-terminal domain | Treslin_N | Domain | 920 | false | false | This entry represents the N-terminal domain of Treslin, the metazoan counterpart of Sld3 from yeast, which are the hub proteins mediating protein associations critical for the helicase formation [ , ]. Treslin, as Sld3, interacts with TopBP1 in a Cdk2-dependent manner, which then collaborate in the Cdk2-mediated loadin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21854"
] | [
"Treslin_N"
] | [
920
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-69273",
"R-HSA-69273",
"R-MMU-69273"
] | [
"REACTOME:R-DRE-69273",
"REACTOME:R-HSA-69273",
"REACTOME:R-MMU-69273"
] | 3 | [] | 0 | [
"PUB00103954",
"PUB00103961",
"PUB00103962"
] | [
"35091422",
"25126958",
"22380713"
] | [
"Refining the domain architecture model of the replication origin firing factor Treslin/TICRR.",
"Crystal structure of the homology domain of the eukaryotic DNA replication proteins Sld3/Treslin.",
"Treslin, DUE-B, and GEMC1 cannot complement Sld3 mutants in fission yeast."
] | [
2022,
2014,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
920
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
6,
2
] | 4 | true | Domain | Treslin, N-terminal domain | Treslin, N-terminal domain | Treslin_N | 3 |
IPR053920 | 53,920 | Treslin, STD domain | Treslin_STD | Domain | 1,036 | false | false | This entry represents the STD (Sld3-Treslin domain) domain from Treslin, the metazoan counterpart of Sld3 from yeast, which are the hub proteins mediating protein associations critical for the helicase formation [ , ]. Treslin, as Sld3, interacts with TopBP1 in a Cdk2-dependent manner, which then collaborate in the Cdk... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21855"
] | [
"Treslin_STD"
] | [
1036
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-69273",
"R-HSA-69273",
"R-MMU-69273"
] | [
"REACTOME:R-DRE-69273",
"REACTOME:R-HSA-69273",
"REACTOME:R-MMU-69273"
] | 3 | [] | 0 | [
"PUB00103954",
"PUB00103961",
"PUB00103962"
] | [
"35091422",
"25126958",
"22380713"
] | [
"Refining the domain architecture model of the replication origin firing factor Treslin/TICRR.",
"Crystal structure of the homology domain of the eukaryotic DNA replication proteins Sld3/Treslin.",
"Treslin, DUE-B, and GEMC1 cannot complement Sld3 mutants in fission yeast."
] | [
2022,
2014,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1036
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
4,
3
] | 5 | true | Domain | Treslin, STD domain | Treslin, STD domain | Treslin_STD | 6 |
IPR053923 | 53,923 | Replication protein RepB, C-terminal domain | RepB_C | Domain | 539 | false | false | This entry represents the C-terminal oligomerisation domain (OD) of plasmid replication proteins, such as RepB. These proteins are essential for replication of plasmids, the Rep proteins are topoisomerases that nick the positive stand at the plus origin of replication and also at the single-strand conversion sequence [... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21861"
] | [
"RepB_C"
] | [
539
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00097405",
"PUB00154199",
"PUB00160031"
] | [
"26875695",
"36688326",
"17267412"
] | [
"Conformational plasticity of RepB, the replication initiator protein of promiscuous streptococcal plasmid pMV158.",
"Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein.",
"Interactions between the RepB initiator protein of plasmid pMV158 and two distant... | [
2016,
2023,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ecdysozoa",
"Inoviridae",
"uncultured prokaryote"
] | [
498,
5,
2,
34
] | 4 | [] | [] | 0 | true | Domain | Replication protein RepB, C-terminal domain | Replication protein RepB, C-terminal domain | RepB_C | 2 |
IPR053924 | 53,924 | RecX, second three-helical domain | RecX_HTH_2nd | Domain | 20,444 | false | false | This entry represents the second three-helical domain (HTH-like) found in RecX family of proteins. RecX functions as a regulator of DNA recombination and repair pathways in bacterial cells [ ]. RecX protein is known to inhibit the activity of RecA protein in DNA recombination [ , ]. It contains three HTH-like domains, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02631"
] | [
"RecX_HTH2"
] | [
20444
] | 1 | [] | [] | [] | 0 | [
"3c1d",
"3d5l",
"3dfg",
"3e3v"
] | 4 | [
"PUB00050856",
"PUB00154197",
"PUB00154198"
] | [
"18650935",
"23284295",
"35730924"
] | [
"Structural basis for inhibition of homologous recombination by the RecX protein.",
"RecX facilitates homologous recombination by modulating RecA activities.",
"A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions."
] | [
2008,
2012,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctj8j9",
"unclassified sequences"
] | [
19528,
585,
1,
330
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
4,
7
] | 4 | true | Domain | RecX, second three-helical domain | RecX, second three-helical domain | RecX_HTH_2nd | 3 |
IPR053925 | 53,925 | RecX, third three-helical domain | RecX_HTH_3rd | Domain | 17,668 | false | false | This entry represents the third three-helical domain (HTH-like) found in RecX family of proteins. RecX functions as a regulator of DNA recombination and repair pathways in bacterial cells [ ]. RecX protein is known to inhibit the activity of RecA protein in DNA recombination [ , ]. It contains three HTH-like domains, f... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21981"
] | [
"RecX_HTH3"
] | [
17668
] | 1 | [] | [] | [] | 0 | [
"3c1d",
"3d5l",
"3dfg",
"3e3v"
] | 4 | [
"PUB00050856",
"PUB00154197",
"PUB00154198"
] | [
"18650935",
"23284295",
"35730924"
] | [
"Structural basis for inhibition of homologous recombination by the RecX protein.",
"RecX facilitates homologous recombination by modulating RecA activities.",
"A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions."
] | [
2008,
2012,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
16948,
438,
282
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
4,
7
] | 4 | true | Domain | RecX, third three-helical domain | RecX, third three-helical domain | RecX_HTH_3rd | 9 |
IPR053926 | 53,926 | RecX, first three-helical domain | RecX_HTH_1st | Domain | 14,807 | false | false | This entry represents the first three-helix domain (HTH-like) found in RecX family of proteins. RecX functions as a regulator of DNA recombination and repair pathways in bacterial cells [ ]. RecX protein is known to inhibit the activity of RecA protein in DNA recombination [ , ]. It contains three HTH-like domains, fir... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21982"
] | [
"RecX_HTH1"
] | [
14807
] | 1 | [] | [] | [] | 0 | [
"3c1d",
"3d5l",
"3dfg",
"3e3v"
] | 4 | [
"PUB00050856",
"PUB00154197",
"PUB00154198"
] | [
"18650935",
"23284295",
"35730924"
] | [
"Structural basis for inhibition of homologous recombination by the RecX protein.",
"RecX facilitates homologous recombination by modulating RecA activities.",
"A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions."
] | [
2008,
2012,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctj8j9",
"unclassified sequences"
] | [
14218,
344,
1,
244
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Zea mays"
] | [
4,
1,
6
] | 3 | true | Domain | RecX, first three-helical domain | RecX, first three-helical domain | RecX_HTH_1st | 8 |
IPR053927 | 53,927 | Flagellar hook-associated protein FlgK, helical domain | FlgK_helical | Domain | 14,278 | false | false | This entry represents a mainly helical domain found in flagellar hook-associated protein FlgK (also called Flagellar hook-associated protein 1) and related proteins mostly from bacteria. FlgK is one of three hook associated proteins that form the hook-filament junction. This domain adopts a broken antiparallel helical ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22638"
] | [
"FlgK_D1"
] | [
14278
] | 1 | [] | [] | [] | 0 | [
"2d4y",
"4ut1",
"5xbj",
"9go6",
"9gsx"
] | 5 | [
"PUB00076713",
"PUB00153951"
] | [
"25645451",
"29147015"
] | [
"From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook-associated protein FlgK.",
"Structure of FlgK reveals the divergence of the bacterial Hook-Filament Junction of Campylobacter."
] | [
2015,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
14095,
33,
150
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Flagellar hook-associated protein FlgK, helical domain | Flagellar hook-associated protein FlgK, helical domain | FlgK_helical | 6 |
IPR053928 | 53,928 | Nonstructural protein NS-S, N-terminal, bunyaviral | NS-S_N_bunyaviral | Domain | 605 | false | false | This entry represents the N-terminal domain of Nonstructural protein NS-S from the tospovirus Tomato spotted wilt virus and related sequences from related Bunyavirales. Bunyavirus has three genomic segments: small (S), middle-sized (M), and large (L). The S segment encodes the nucleocapsid and a non-structural protein.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03231"
] | [
"Tospov_NS-S_N"
] | [
605
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034463",
"PUB00034464",
"PUB00034465",
"PUB00034466",
"PUB00034467",
"PUB00154426",
"PUB00154427"
] | [
"1826573",
"8445364",
"11209062",
"12133999",
"12829839",
"12502849",
"31206553"
] | [
"The nonstructural protein (NSs) encoded by the ambisense S RNA segment of tomato spotted wilt virus is associated with fibrous structures in infected plant cells.",
"Multiplication of tomato spotted wilt virus in its insect vector, Frankliniella occidentalis.",
"Bunyamwera bunyavirus nonstructural protein NSs ... | [
1991,
1993,
2001,
2002,
2003,
2003,
2019
] | 7 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
605
] | 1 | [] | [] | 0 | true | Domain | Nonstructural protein NS-S, N-terminal, bunyaviral | Nonstructural protein NS-S, N-terminal, bunyaviral | NS-S_N_bunyaviral | 6 |
IPR053929 | 53,929 | Nonstructural protein NS-S, WIV domain, bunyaviral | NS-S_WIV_bunyaviral | Domain | 568 | false | false | This entry represents the WIV domain [ ] of Nonstructural protein NS-S from the tospovirus Tomato spotted wilt virus and related sequences from related Bunyavirales. Bunyavirus has three genomic segments: small (S), middle-sized (M), and large (L). The S segment encodes the nucleocapsid and a non-structural protein. Th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23017"
] | [
"WIV_2"
] | [
568
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034463",
"PUB00034464",
"PUB00034465",
"PUB00034466",
"PUB00034467",
"PUB00154424",
"PUB00154426",
"PUB00154427"
] | [
"1826573",
"8445364",
"11209062",
"12133999",
"12829839",
"38193819",
"12502849",
"31206553"
] | [
"The nonstructural protein (NSs) encoded by the ambisense S RNA segment of tomato spotted wilt virus is associated with fibrous structures in infected plant cells.",
"Multiplication of tomato spotted wilt virus in its insect vector, Frankliniella occidentalis.",
"Bunyamwera bunyavirus nonstructural protein NSs ... | [
1991,
1993,
2001,
2002,
2003,
2024,
2003,
2019
] | 8 | [] | [] | 0 | 0 | null | [
"Bunyaviricetes"
] | [
568
] | 1 | [] | [] | 0 | true | Domain | Nonstructural protein NS-S, WIV domain, bunyaviral | Nonstructural protein NS-S, WIV domain, bunyaviral | NS-S_WIV_bunyaviral | 1 |
IPR053930 | 53,930 | RapZ-like, N-terminal domain | RapZ-like_N | Domain | 17,895 | false | false | This entry represents the N-terminal P-loop kinase domain of RNase adapter protein RapZ and related proteins. RapZ plays a central role in RNA-mediated regulation of amino-sugar metabolism [ , , ]. It is a RNA-binding protein that recruits the major endoribonuclease RNase E to sRNAs GlmZ [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03668"
] | [
"RapZ-like_N"
] | [
17895
] | 1 | [] | [] | [] | 0 | [
"5o5o",
"5o5q",
"8b0i",
"8b0j",
"9m1q",
"9m1v"
] | 6 | [
"PUB00075613",
"PUB00150969",
"PUB00153826"
] | [
"23475961",
"28977623",
"36968430"
] | [
"Targeted decay of a regulatory small RNA by an adaptor protein for RNase E and counteraction by an anti-adaptor RNA.",
"Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.",
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic proces... | [
2013,
2017,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
17519,
19,
357
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RapZ-like, N-terminal domain | RapZ-like, N-terminal domain | RapZ-like_N | 5 |
IPR053931 | 53,931 | RapZ, C-terminal domain | RapZ_C | Domain | 19,546 | false | false | This entry represents the C-terminal domain of RapZ which belongs to the Rhodanese-Phosphatase superfamily. It has been shown to bind multiple ligands as part of the regulation of glucosamine-6-phosphate (GlcN6P) levels, which is a precursor to the bacterial cell wall polymer peptidoglycan. Assignment to the greater Rh... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22740"
] | [
"PapZ_C"
] | [
19546
] | 1 | [] | [] | [] | 0 | [
"5o5o",
"5o5q",
"5o5s",
"8b0i",
"8b0j"
] | 5 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
18709,
419,
26,
392
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RapZ, C-terminal domain | RapZ, C-terminal domain | RapZ_C | 9 |
IPR053933 | 53,933 | Glabrous enhancer-binding protein-like, C-terminal domain | GeBP-like_C | Domain | 531 | false | false | This entry represents the C-terminal domain present in GLABROUS1 enhancer-binding protein (GeBP) and GeBP-like proteins, such as storekeeper and storekeeper-like (STKL) transcription factors. GeBP and GeBP-like proteins play a redundant role in cytokinin hormone pathway regulation [ , , ]. Storekeeper was identified as... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22757"
] | [
"GeBP-like_C"
] | [
531
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00081457",
"PUB00081459",
"PUB00081460",
"PUB00153966",
"PUB00153967"
] | [
"18162594",
"27031427",
"12028578",
"12535344",
"35890483"
] | [
"GeBP and GeBP-like proteins are noncanonical leucine-zipper transcription factors that regulate cytokinin response in Arabidopsis.",
"Regulation of Arabidopsis thaliana plasma membrane glucose-responsive regulator (AtPGR) expression by A. thaliana storekeeper-like transcription factor, AtSTKL, modulates glucose ... | [
2008,
2016,
2002,
2003,
2022
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
531
] | 1 | [
"Arabidopsis thaliana"
] | [
53
] | 1 | true | Domain | Glabrous enhancer-binding protein-like, C-terminal domain | Glabrous enhancer-binding protein-like, C-terminal domain | GeBP-like_C | 3 |
IPR053934 | 53,934 | HTTM domain | HTTM_dom | Domain | 4,753 | false | false | This entry represents the HTTM (for horizontally transferred transmembrane) domain found at the N-terminal in metazoan Vitamin K-dependent gamma-carboxylase and in diverse domain architectures in bacterial proteins. This domain contains four transmembrane regions [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF05090"
] | [
"HTTM"
] | [
4753
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.90",
"PWY-7999",
"R-BTA-159740",
"R-HSA-159740",
"R-HSA-9673240",
"R-MMU-159740",
"R-RNO-159740"
] | [
"EC:4.1.1.90",
"METACYC:PWY-7999",
"REACTOME:R-BTA-159740",
"REACTOME:R-HSA-159740",
"REACTOME:R-HSA-9673240",
"REACTOME:R-MMU-159740",
"REACTOME:R-RNO-159740"
] | 7 | [
"9bum",
"9bur",
"9bux",
"9bvk",
"9bvl",
"9bvm",
"9bvo",
"9bvp",
"9bvq",
"9bvr",
"9l1y",
"9l20",
"9l21",
"9l23",
"9l24",
"9l25",
"9l54",
"9l6q",
"9l6r",
"9l6s",
"9mqb",
"9mqc",
"9mqe"
] | 23 | [
"PUB00010243",
"PUB00055033",
"PUB00154019"
] | [
"10748045",
"12817086",
"14729325"
] | [
"Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase.",
"Cannibalism by sporulating bacteria.",
"HTTM, a horizontally transferred transmembrane domain."
] | [
2000,
2003,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
266,
2737,
1723,
27
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
16,
6,
7
] | 5 | true | Domain | HTTM domain | HTTM domain | HTTM_dom | 9 |
IPR053935 | 53,935 | Vitamin K-dependent gamma-carboxylase, lumenal domain | VKGC_lumenal_dom | Domain | 3,239 | false | false | Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase (VKGC) post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22777"
] | [
"VKGC_lumenal_dom"
] | [
3239
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.90",
"PWY-7999",
"R-BTA-159740",
"R-HSA-159740",
"R-HSA-9673240",
"R-MMU-159740",
"R-RNO-159740"
] | [
"EC:4.1.1.90",
"METACYC:PWY-7999",
"REACTOME:R-BTA-159740",
"REACTOME:R-HSA-159740",
"REACTOME:R-HSA-9673240",
"REACTOME:R-MMU-159740",
"REACTOME:R-RNO-159740"
] | 7 | [
"9bum",
"9bur",
"9bux",
"9bvk",
"9bvl",
"9bvm",
"9bvo",
"9bvp",
"9bvq",
"9bvr",
"9l1y",
"9l20",
"9l21",
"9l23",
"9l24",
"9l25",
"9l54",
"9l6q",
"9l6r",
"9l6s",
"9mqb",
"9mqc",
"9mqe"
] | 23 | [
"PUB00010243",
"PUB00154019"
] | [
"10748045",
"14729325"
] | [
"Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase.",
"HTTM, a horizontally transferred transmembrane domain."
] | [
2000,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrosopumilus maritimus (strain SCM1)",
"metagenomes"
] | [
1635,
1582,
1,
21
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
11,
4,
4
] | 5 | true | Domain | Vitamin K-dependent gamma-carboxylase, lumenal domain | Vitamin K-dependent gamma-carboxylase, lumenal domain | VKGC_lumenal_dom | 3 |
IPR053936 | 53,936 | Wntless, GOLD domain | WLS_GOLD | Domain | 2,156 | false | false | This entry represents the GOLD domain from wntless (WLS) proteins. WLS are membrane trafficking and secretion chaperones for lipidated Wnt signaling proteins. They are homologous to GPR180, TMEM145, and TMEM181, which have been described as GOST proteins (for GOLD domain seven-transmembrane helix proteins) together wit... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21883"
] | [
"WLS_GOLD"
] | [
2156
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-3238698",
"R-DME-3238698",
"R-HSA-3238698",
"R-MMU-3238698",
"R-RNO-3238698"
] | [
"REACTOME:R-CEL-3238698",
"REACTOME:R-DME-3238698",
"REACTOME:R-HSA-3238698",
"REACTOME:R-MMU-3238698",
"REACTOME:R-RNO-3238698"
] | 5 | [
"7drt",
"7kc4",
"8tzo",
"8tzp",
"8tzr",
"8tzs"
] | 6 | [
"PUB00151072"
] | [
"36373655"
] | [
"Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2156
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
1,
10,
2,
3
] | 6 | true | Domain | Wntless, GOLD domain | Wntless, GOLD domain | WLS_GOLD | 6 |
IPR053937 | 53,937 | GOST, seven transmembrane domain | GOST_TM | Domain | 12,844 | false | false | This entry represents the transmembrane domain of a group of related proteins that share the same domain architecture, termed GOST (GOLD domain seven-transmembrane helix) proteins, including TMEM87A/B, GPR107/GPR108 from human and the homologues from yeast, PTM1 [ ]. This entry also includes plant proteins, CAND6/7 [ ]... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06814"
] | [
"GOST_TM"
] | [
12844
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-8980692",
"R-MMU-8980692"
] | [
"REACTOME:R-HSA-8980692",
"REACTOME:R-MMU-8980692"
] | 2 | [
"8ctj",
"8hsi",
"8htt",
"8kb4"
] | 4 | [
"PUB00151072",
"PUB00153986"
] | [
"36373655",
"33878345"
] | [
"Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A.",
"A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis."
] | [
2022,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
12844
] | 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... | [
39,
2,
13,
2,
26,
12,
1,
29,
14,
2,
2,
75
] | 12 | true | Domain | GOST, seven transmembrane domain | GOST, seven transmembrane domain | GOST_TM | 1 |
IPR053938 | 53,938 | PTM1-like, N-terminal domain | PTM1-like_N | Domain | 1,768 | false | false | This entry represents the N-terminal domain of fungal proteins, such as PTM1 from S.cerevisiae and its closely homologues from S.pombe. They have been identified as orthologues of TMEM87A/B from human. Structure predictions suggest that these proteins has the same domain architecture as GOST (GOLD seven-transmembrane h... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21902"
] | [
"PTM1-like_N"
] | [
1768
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035466",
"PUB00151072"
] | [
"16107716",
"36373655"
] | [
"Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments.",
"Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A."
] | [
2005,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1768
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
2
] | 3 | true | Domain | PTM1-like, N-terminal domain | PTM1-like, N-terminal domain | PTM1-like_N | 4 |
IPR053939 | 53,939 | UTP25, C-terminal domain | UTP25_C | Domain | 4,652 | false | false | UTP25 is a family of eukaryotic proteins. The family displays limited sequence similarity to DEAD-box RNA helicases, having alternative residues at the Walker A and DEAD-box sites, but conservation of structural and other key residues [ ]. This entry represents the C-terminal domain that is required and sufficient for ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06862"
] | [
"Utp25_C"
] | [
4652
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-RNO-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-RNO-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 6 | [] | 0 | [
"PUB00074620",
"PUB00109164"
] | [
"21941128",
"20884785"
] | [
"The nucleolar protein Nop19p interacts preferentially with Utp25p and Dhr2p and is essential for the production of the 40S ribosomal subunit in Saccharomyces cerevisiae.",
"The DEAD-box RNA helicase-like Utp25 is an SSU processome component."
] | [
2011,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4652
] | 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... | [
5,
1,
1,
3,
3,
2,
1,
3,
3,
1,
1,
7
] | 12 | true | Domain | UTP25, C-terminal domain | UTP25, C-terminal domain | UTP25_C | 1 |
IPR053940 | 53,940 | UTP25, NTP hydrolase-like domain | UTP25_NTPase-like | Domain | 4,976 | false | false | UTP25 (U3 small nucleolar RNA-associated protein 25) is a DEAD-box RNA helicase-like protein component of the ribosomal small subunit processome for the biogenesis of ribosomes, which functions in pre-ribosomal RNA (pre-rRNA) processing [ ]. U3 small nucleolar RNA-associated protein 25 homologue (UTP25, also known as D... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22916"
] | [
"UTP25_NTPase-like"
] | [
4976
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-RNO-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-RNO-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 6 | [] | 0 | [
"PUB00074620",
"PUB00097919",
"PUB00097921",
"PUB00097922",
"PUB00109164"
] | [
"21941128",
"25007945",
"27657329",
"23357851",
"20884785"
] | [
"The nucleolar protein Nop19p interacts preferentially with Utp25p and Dhr2p and is essential for the production of the 40S ribosomal subunit in Saccharomyces cerevisiae.",
"MiR-195 affects cell migration and cell proliferation by down-regulating DIEXF in Hirschsprung's disease.",
"Phosphorylation of Def Regula... | [
2011,
2014,
2016,
2013,
2010
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4976
] | 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... | [
5,
1,
1,
3,
4,
3,
1,
4,
3,
1,
1,
7
] | 12 | true | Domain | UTP25, NTP hydrolase-like domain | UTP25, NTP hydrolase-like domain | UTP25_NTPase-like | 6 |
IPR053941 | 53,941 | Csm6, HEPN domain | Csm6_HEPN | Domain | 539 | false | false | This entry represents the HEPN domain of CRISPR system endoribonuclease Csm6 from Enterococcus italicus and similar bacterial sequences. Csm6 is a Cas (CRISPR-associated) protein from type III-A CRISPR-Cas system. It consists of a CARF domain at the N-terminal ( ), a six-helix domain and a C-terminal HEPN domain at the... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09659"
] | [
"Cas_Csm6_HEPN"
] | [
539
] | 1 | [] | [] | [] | 0 | [
"4rgp",
"5yjc",
"6tug",
"8pcw",
"8pe3"
] | 5 | [
"PUB00153857"
] | [
"32221291"
] | [
"Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1)",
"bioreactor metagenome"
] | [
537,
1,
1
] | 3 | [] | [] | 0 | true | Domain | Csm6, HEPN domain | Csm6, HEPN domain | Csm6_HEPN | 3 |
IPR053943 | 53,943 | Ribosomal RNA large subunit methyltransferase K/L-like, conserved site | RlmKL-like_Mtase_CS | Conserved_site | 11,962 | false | false | This entry represents a conserved site found in ribosomal RNA large subunit methyltransferase K/L from Escherichia coli (RmlKL) and related proteins. RmlKL specifically methylates the guanine in positions 2445 and 2069 of 23S rRNA before its assembly into 50S subunits [ , , , ]. This conserved site is defined by a D-P-... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01261"
] | [
"UPF0020"
] | [
11962
] | 1 | [
"EC",
"EC",
"EC"
] | [
"2.1.1",
"2.1.1.173",
"2.1.1.264"
] | [
"EC:2.1.1",
"EC:2.1.1.173",
"EC:2.1.1.264"
] | 3 | [
"3k0b",
"3ldu",
"3tlj",
"3tm4",
"3tm5",
"3v8v",
"3v97",
"6zxv",
"6zxw",
"6zxy"
] | 10 | [
"PUB00039897",
"PUB00100798",
"PUB00100799"
] | [
"16343540",
"22362734",
"17010378"
] | [
"Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain.",
"Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA.",
"Identification of Escherichia coli m2G methyl... | [
2006,
2012,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ct9mC1",
"metagenomes"
] | [
546,
9950,
1345,
1,
120
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
2,
1,
3
] | 5 | true | Conserved_site | Ribosomal RNA large subunit methyltransferase K/L-like, conserved site | Ribosomal RNA large subunit methyltransferase K/L-like, conserved site | RlmKL-like_Mtase_CS | 5 |
IPR053944 | 53,944 | Shieldin complex subunit 2, second OB fold domain | SHLD2_OB2 | Domain | 816 | false | false | This entry represents the second OB fold domain found in the middle of Shieldin complex subunit 2 (SHLD2, formerly known as FAM35A) and in similar sequences mainly found in vertebrates. SHLD2 is a component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs) [ , ]. In s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22779"
] | [
"OB_SHLD2_2nd"
] | [
816
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00089626",
"PUB00101857"
] | [
"29656893",
"29789392"
] | [
"DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity.",
"FAM35A associates with REV7 and modulates DNA damage responses of normal and BRCA1-defective cells."
] | [
2018,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
816
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
3,
5
] | 4 | true | Domain | Shieldin complex subunit 2, second OB fold domain | Shieldin complex subunit 2, second OB fold domain | SHLD2_OB2 | 2 |
IPR053945 | 53,945 | Phosphoinositide phospholipase C beta 1-4-like, EF-hand domain | PLCB1-4-like_EFh | Domain | 7,213 | false | false | This entry represents the first EF-hand domain found in 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1-4 (PLCB1-4) from human and related animal proteins. PLC-beta isoforms mediate the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) to propagate... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22631"
] | [
"PLCB1-4-like_EFh"
] | [
7213
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.4.11",
"PWY-6351",
"PWY-6367",
"PWY-7039",
"PWY-8052",
"R-BTA-112043",
"R-BTA-1855204",
"R-BTA-399997",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418217",
"R-BTA-434316",
"R-BTA-500657",
"R-CEL-112043",
"R-CEL-1855204",
"R-CEL-416476",
"R-DME-112043",
"R-DME-1855204",
"R-DME-3... | [
"EC:3.1.4.11",
"METACYC:PWY-6351",
"METACYC:PWY-6367",
"METACYC:PWY-7039",
"METACYC:PWY-8052",
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418217",
"REACTOME:R-BTA-434316",
"REACTOME:R-BTA-5006... | 46 | [
"2fju",
"2zkm",
"3qr0",
"3qr1",
"4gnk",
"4qj3",
"4qj4",
"4qj5",
"7sq2",
"8emv",
"8emw",
"8emx",
"8uqn",
"8uqo"
] | 14 | [
"PUB00040695",
"PUB00093065",
"PUB00112989",
"PUB00137701",
"PUB00137702"
] | [
"17115053",
"23377541",
"21822282",
"25435326",
"20966218"
] | [
"Crystal structure of Rac1 bound to its effector phospholipase C-beta2.",
"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain.",
"An autoinhibitory helix in the C-terminal region of phospholipase C-β mediates Gαq activation.",
"Molecular mechanisms of phosph... | [
2006,
2013,
2011,
2014,
2010
] | 5 | [] | [
"IPR028400",
"IPR046969"
] | 0 | 2 | 0 | [
"Eumetazoa"
] | [
7213
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
23,
19,
4,
37,
19,
24
] | 6 | true | Domain | Phosphoinositide phospholipase C beta 1-4-like, EF-hand domain | Phosphoinositide phospholipase C beta 1-4-like, EF-hand domain | PLCB1-4-like_EFh | 3 |
IPR053946 | 53,946 | YscD-like, Bon-like domain 3 | YscD_ppl_3rd | Domain | 1,187 | false | false | This entry represents the third of three periplasmic BON domains. YscD is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD contains an N-terminal cytoplasmic domain ( ), a transmembrane linker and a large peripl... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21934"
] | [
"Yop-YscD_ppl_3rd"
] | [
1187
] | 1 | [] | [] | [] | 0 | [
"4alz"
] | 1 | [
"PUB00020581",
"PUB00076172"
] | [
"1860816",
"23908767"
] | [
"Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica.",
"In situ structural analysis of the Yersinia enterocolitica injectisome."
] | [
1991,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"invertebrate metagenome"
] | [
1183,
3,
1
] | 3 | [] | [] | 0 | true | Domain | YscD-like, Bon-like domain 3 | YscD-like, Bon-like domain 3 | YscD_ppl_3rd | 4 |
IPR053947 | 53,947 | YscD-like, Bon-like domain 2 | YscD_ppl__2nd | Domain | 992 | false | false | This entry represents the second of three periplasmic BON domains in YscD proteins from proteobacteria. YscD is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD contains an N-terminal cytoplasmic domain ( ), a t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21937"
] | [
"Yop-YscD_ppl_2nd"
] | [
992
] | 1 | [] | [] | [] | 0 | [
"4alz"
] | 1 | [
"PUB00020581",
"PUB00076172"
] | [
"1860816",
"23908767"
] | [
"Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica.",
"In situ structural analysis of the Yersinia enterocolitica injectisome."
] | [
1991,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bracon brevicornis",
"invertebrate metagenome"
] | [
990,
1,
1
] | 3 | [] | [] | 0 | true | Domain | YscD-like, Bon-like domain 2 | YscD-like, Bon-like domain 2 | YscD_ppl__2nd | 5 |
IPR053948 | 53,948 | SBE2/SBE22, N-terminal domain | SBE2/SBE22_N | Domain | 95 | false | false | This entry represents a domain found at the N-terminal of SBE2 and its paralogue, SBE22 from budding yeast. These proteins are involved in bud growth and yeast cell wall formation [ ]. They may be also involved in the transport of cell wall components from the Golgi apparatus to the cell surface periphery [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22876"
] | [
"SBE2_N"
] | [
95
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075790",
"PUB00114131"
] | [
"10679005",
"12045225"
] | [
"Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell wall formation.",
"Mechanisms for targeting of the Saccharomyces cerevisiae GPI-anchored cell wall protein Crh2p to polarised growth sites."
] | [
2000,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
95
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2
] | 1 | true | Domain | SBE2/SBE22, N-terminal domain | SBE2/SBE22, N-terminal domain | SBE2/SBE22_N | 7 |
IPR053949 | 53,949 | SBE2/SBE22, middle domain | SBE2/SBE22_M | Domain | 1,051 | false | false | This entry represents a domain found central in SBE2, its paralogue, SBE22 from budding yeast, and similar proteins from ascomycetes. These proteins are involved in bud growth and yeast cell wall formation [ ]. They may be also involved in the transport of cell wall components from the Golgi apparatus to the cell surfa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22874"
] | [
"SBE2_M"
] | [
1051
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075790",
"PUB00114131"
] | [
"10679005",
"12045225"
] | [
"Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell wall formation.",
"Mechanisms for targeting of the Saccharomyces cerevisiae GPI-anchored cell wall protein Crh2p to polarised growth sites."
] | [
2000,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"saccharomyceta"
] | [
1051
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
2
] | 2 | true | Domain | SBE2/SBE22, middle domain | SBE2/SBE22, middle domain | SBE2/SBE22_M | 2 |
IPR053950 | 53,950 | CAP, N-terminal domain | CAP_N | Domain | 6,586 | false | false | Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that regulate actin remodelling in response to cellular signals [ ]. They consist of an N-terminal conserved motif ( ) followed... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21938"
] | [
"CAP_N"
] | [
6586
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-6798695",
"R-HSA-114608",
"R-HSA-428890",
"R-HSA-6798695",
"R-MMU-6798695",
"R-RNO-6798695",
"R-SCE-6798695",
"R-SPO-6798695"
] | [
"REACTOME:R-DDI-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-428890",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-6798695",
"REACTOME:R-SCE-6798695",
"REACTOME:R-SPO-6798695"
] | 8 | [
"1s0p",
"1tjf",
"6rsq",
"6rsw"
] | 4 | [
"PUB00022651",
"PUB00031477",
"PUB00153848"
] | [
"12962635",
"15558566",
"31757941"
] | [
"Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.",
"Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).",
"Mechanism of synergistic actin filament pointed end depolymerization by cyclase... | [
2003,
2005,
2019
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6586
] | 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... | [
5,
4,
3,
3,
23,
10,
1,
6,
9,
1,
1,
21
] | 12 | true | Domain | CAP, N-terminal domain | CAP, N-terminal domain | CAP_N | 5 |
IPR053951 | 53,951 | K+ potassium transporter, integral membrane domain | K_trans_N | Domain | 28,232 | false | false | This is a family of K+ potassium transporters that are conserved across phyla, including bacterial (KUP) [ ], yeast (HAK) [ ], and plant (AtKT) [ ]. This entry represents the N-terminal integral membrane domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02705"
] | [
"K_trans"
] | [
28232
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007570",
"PUB00007571",
"PUB00007572"
] | [
"8226635",
"7621817",
"9350997"
] | [
"Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus.",
"A potassium transporter of the yeast Schwanniomyces occidentalis homologous to the Kup system of E... | [
1993,
1995,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Chlorovirus",
"Eukaryota",
"Methanomicrobia",
"unclassified sequences"
] | [
12768,
2,
15293,
50,
119
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
59,
1,
1,
65,
234
] | 5 | true | Domain | K+ potassium transporter, integral membrane domain | K+ potassium transporter, integral membrane domain | K_trans_N | 8 |
IPR053952 | 53,952 | K+ potassium transporter, C-terminal domain | K_trans_C | Domain | 26,179 | false | false | This is a family of K+ potassium transporters that are conserved across phyla, including bacterial (KUP) [ ], yeast (HAK) [ ], and plant (AtKT) [ ]. This entry represents the C-terminal non-membrane domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22776"
] | [
"K_trans_C"
] | [
26179
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007570",
"PUB00007571",
"PUB00007572"
] | [
"8226635",
"7621817",
"9350997"
] | [
"Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus.",
"A potassium transporter of the yeast Schwanniomyces occidentalis homologous to the Kup system of E... | [
1993,
1995,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Chlorovirus",
"Eukaryota",
"Methanomicrobia",
"unclassified sequences"
] | [
12549,
2,
13462,
47,
119
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
60,
1,
1,
1,
55,
194
] | 6 | true | Domain | K+ potassium transporter, C-terminal domain | K+ potassium transporter, C-terminal domain | K_trans_C | 4 |
IPR053953 | 53,953 | Siroheme decarboxylase NirL-like, HTH domain | NirdL-like_HTH | Domain | 4,947 | false | false | This entry represents the helix-turn-helix (HTH) domain found in siroheme decarboxylase NirdL from Hydrogenobacter thermophilus and related sequences, from bacteria and archaea [ , , , , ]. NirdL is involved in heme d1 biosynthesis. It catalyses the decarboxylation of siroheme into didecarboxysiroheme. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22451"
] | [
"NirdL-like_HTH"
] | [
4947
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.1.111",
"PWY-7552",
"PWY-7554"
] | [
"EC:4.1.1.111",
"METACYC:PWY-7552",
"METACYC:PWY-7554"
] | 3 | [
"4ch7",
"4czc",
"4czd",
"4un1"
] | 4 | [
"PUB00014071",
"PUB00022604",
"PUB00050396",
"PUB00059696",
"PUB00154102"
] | [
"11230123",
"14976242",
"19004003",
"21338611",
"25083922"
] | [
"Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus.",
"The archaeal feast/famine regulatory protein: potential roles of its assembly forms for regulating transcription.",
"Interactions between the archaeal transcription repressor FL11 and its coregulators lysine a... | [
2001,
2004,
2009,
2011,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Metazoa",
"unclassified sequences"
] | [
922,
3882,
8,
135
] | 4 | [] | [] | 0 | true | Domain | Siroheme decarboxylase NirL-like, HTH domain | Siroheme decarboxylase NirL-like, HTH domain | NirdL-like_HTH | 5 |
IPR053954 | 53,954 | Domain of unknown function DUF7023 | DUF7023 | Domain | 966 | false | false | This domain is found in human Protein dispatched homolog 3 (DISP3) and related proteins mainly from vertebrates. DISP3 (PTCHD2), a sterol-sensing domain- containing protein, is highly expressed in neural tissue, promotes cell proliferation and alters expression of genes that are involved in tumorigenesis. The function ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22894"
] | [
"DUF7023"
] | [
966
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Chordata"
] | [
966
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
2,
2
] | 4 | true | Domain | Domain of unknown function DUF7023 | Domain of unknown function DUF7023 | DUF7023 | 8 |
IPR053955 | 53,955 | Csm6, CARF domain | Csm6_CARF | Domain | 256 | false | false | This entry represents the CARF domain of CRISPR system endoribonuclease Csm6 from Enterococcus italicus and similar bacterial sequences. Csm6 is a Cas (CRISPR-associated) protein from type III-A CRISPR-Cas system. It consists of a CARF domain at the N-terminal, a six-helix domain and a C-terminal HEPN domain at the C-t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22208"
] | [
"Cas_Csm6_CARF"
] | [
256
] | 1 | [] | [] | [] | 0 | [
"6tug",
"8pcw",
"8pe3"
] | 3 | [
"PUB00153857"
] | [
"32221291"
] | [
"Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobrevibacter millerae",
"bioreactor metagenome"
] | [
254,
1,
1
] | 3 | [] | [] | 0 | true | Domain | Csm6, CARF domain | Csm6, CARF domain | Csm6_CARF | 9 |
IPR053956 | 53,956 | NPC1, middle luminal domain | NPC1_MLD | Domain | 7,601 | false | false | NPC intracellular cholesterol transporter 1 (NPC1) is a endosomal/lysosomal membrane protein that facilitates the trafficking of cholesterol and other cargo from lysosomes and is involved in cholesterol homeostasis [ , , , ]. Mutations in the NPC1 gene cause the rare neurodegenerative disease Niemann-Pick Type C (NPC).... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22314"
] | [
"NPC1_MLD"
] | [
7601
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-8963678",
"R-CEL-8964038",
"R-DME-8963678",
"R-HSA-8963678",
"R-HSA-8964038",
"R-MMU-8963678",
"R-MMU-8964038",
"R-RNO-8963678",
"R-SCE-8963678",
"R-SCE-8964038"
] | [
"REACTOME:R-CEL-8963678",
"REACTOME:R-CEL-8964038",
"REACTOME:R-DME-8963678",
"REACTOME:R-HSA-8963678",
"REACTOME:R-HSA-8964038",
"REACTOME:R-MMU-8963678",
"REACTOME:R-MMU-8964038",
"REACTOME:R-RNO-8963678",
"REACTOME:R-SCE-8963678",
"REACTOME:R-SCE-8964038"
] | 10 | [
"3jd8",
"5f18",
"5f1b",
"5hns",
"5jnx",
"5kwy",
"5u73",
"5u74",
"6r4l",
"6uox",
"6v3f",
"6v3h",
"6w5r",
"6w5s",
"6w5t",
"6w5u",
"6w5v",
"7df8",
"7dfw",
"7dfz",
"7n4u",
"7n4v",
"7n4x",
"8eus",
"8qeb",
"8qec",
"8qed",
"8qee",
"9dz2"
] | 29 | [
"PUB00154113",
"PUB00154114",
"PUB00154115",
"PUB00154116",
"PUB00154117"
] | [
"31543266",
"26771495",
"26846330",
"27551080",
"28784760"
] | [
"Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins.",
"Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1.",
"Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.",
"Clues to the mechanism of chole... | [
2019,
2016,
2016,
2016,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
7601
] | 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... | [
13,
2,
8,
5,
11,
7,
1,
4,
6,
1,
6
] | 11 | true | Domain | NPC1, middle luminal domain | NPC1, middle luminal domain | NPC1_MLD | 5 |
IPR053957 | 53,957 | DUF2089, zinc ribbon | DUF2089_Zn_ribbon | Domain | 1,382 | false | false | This entry represents the zinc ribbon found at the N-terminal of a group of hypothetical prokaryotic proteins that often contain ( ). In some members, it occurs as a fusion of ZnR+HTH+SHOCT-like. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22747"
] | [
"Zn_ribbon_DUF2089"
] | [
1382
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacterium",
"ecological metagenomes"
] | [
1347,
2,
9,
24
] | 4 | [] | [] | 0 | true | Domain | DUF2089, zinc ribbon | DUF2089, zinc ribbon | DUF2089_Zn_ribbon | 8 |
IPR053958 | 53,958 | HMGCR/SNAP/NPC1-like, sterol-sensing domain | HMGCR/SNAP/NPC1-like_SSD | Domain | 24,045 | false | false | This entry represents the sterol-sensing domain found in a group of proteins related to cholesterol metabolism and transport, such as HMG-CoA reductase (HMGCR), Sterol regulatory element-binding protein cleavage-activating protein (SCAP), NPC1, patched and related proteins, which are membrane-bound transcription factor... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12349"
] | [
"Sterol-sensing"
] | [
24045
] | 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-191273",
"R-CEL-5632684",
"R-CEL-8963678",
"R-CEL-8964038",
"R-DME-191273",
"R-DME-209338",
"R-DME-209471",
"R-DME-5610787",
"R-DME-5632681",
"R-DME-5632684",
"R-DME-8963678",
"R-HSA-1655829",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-373080",
"R-HSA-5610787",
... | [
"REACTOME:R-BTA-191273",
"REACTOME:R-CEL-5632684",
"REACTOME:R-CEL-8963678",
"REACTOME:R-CEL-8964038",
"REACTOME:R-DME-191273",
"REACTOME:R-DME-209338",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-5610787",
"REACTOME:R-DME-5632681",
"REACTOME:R-DME-5632684",
"REACTOME:R-DME-8963678",
"REACTOME:R-... | 39 | [
"3jd8",
"5jnx",
"5u73",
"5u74",
"6dmb",
"6dmo",
"6dmy",
"6e1h",
"6m49",
"6mg8",
"6n7g",
"6n7h",
"6n7k",
"6oeu",
"6oev",
"6r4l",
"6rmg",
"6rvd",
"6tbu",
"6td6",
"6uox",
"6v3f",
"6v3h",
"6w5r",
"6w5s",
"6w5t",
"6w5u",
"6w5v",
"6xe6",
"7df8",
"7dfw",
"7dfz"... | 57 | [
"PUB00062075",
"PUB00109796",
"PUB00109797",
"PUB00152323",
"PUB00154366",
"PUB00154389"
] | [
"12482938",
"9488713",
"17604677",
"9242699",
"29954986",
"27238017"
] | [
"Three mutations in sterol-sensing domain of SCAP block interaction with insig and render SREBP cleavage insensitive to sterols.",
"Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies.",
... | [
2002,
1998,
2007,
1997,
2018,
2016
] | 6 | [
"IPR000731"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"ecological metagenomes"
] | [
67,
23964,
2,
12
] | 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... | [
13,
9,
23,
12,
33,
22,
3,
4,
28,
3,
2,
6
] | 12 | true | Domain | HMGCR/SNAP/NPC1-like, sterol-sensing domain | HMGCR/SNAP/NPC1-like, sterol-sensing domain | HMGCR/SNAP/NPC1-like_SSD | 8 |
IPR053959 | 53,959 | YvlB/LiaX, N-terminal domain | YvlB/LiaX_N | Domain | 2,802 | false | false | This entry represents a small domain found at the N-terminal of the uncharacterised protein YvlB from Bacillus subtilis, the putative adhesin domain-containing protein LiaX from Enterococcus faecalis and similar prokaryotic sequences. In some members, this domain occurs as a fusion of ZnR+DUF2089-HTH+SHOCT-like, where ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22746"
] | [
"SHOCT-like_DUF2089-C"
] | [
2802
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105524"
] | [
"31818937"
] | [
"Antimicrobial sensing coupled with cell membrane remodeling mediates antibiotic resistance and virulence in <i>Enterococcus faecalis</i>."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
13,
2763,
26
] | 3 | [] | [] | 0 | true | Domain | YvlB/LiaX, N-terminal domain | YvlB/LiaX, N-terminal domain | YvlB/LiaX_N | 4 |
IPR053961 | 53,961 | XRCC4, N-terminal domain | XRCC4_N | Domain | 2,113 | false | false | This represents the N-terminal β-sandwich domain of a family consisting of several eukaryotic DNA double-strand break repair and V(D)J recombination protein XRCC4 sequences. In the non-homologous end joining pathway of DNA double-strand break repair, the ligation step is catalysed by a complex of XRCC4 and DNA ligase I... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06632"
] | [
"XRCC4"
] | [
2113
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-5693571",
"R-HSA-164843",
"R-HSA-3108214",
"R-HSA-5693571",
"R-MMU-3108214",
"R-MMU-5693571"
] | [
"REACTOME:R-DDI-5693571",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-5693571",
"REACTOME:R-MMU-3108214",
"REACTOME:R-MMU-5693571"
] | 6 | [
"1fu1",
"1ik9",
"3ii6",
"3mud",
"3q4f",
"3rwr",
"3sr2",
"3w03",
"4xa4",
"5chx",
"5cj0",
"5cj4",
"5wj7",
"5wlz",
"6abo",
"7lsy",
"7lt3",
"7m3p",
"7nfc",
"7nfe",
"8bh3",
"8bhv",
"8bhy",
"8bot",
"8eza",
"8ezb",
"9cq3",
"9cq6",
"9cqc",
"9gd7",
"9n81",
"9n82"... | 33 | [
"PUB00012766",
"PUB00147236",
"PUB00154391"
] | [
"12517771",
"10757784",
"15385968"
] | [
"Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro.",
"Ku recruits the XRCC4-ligase IV complex to DNA ends.",
"Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV."
] | [
2003,
2000,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2113
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
2,
1,
1,
5,
3,
7,
4
] | 8 | true | Domain | XRCC4, N-terminal domain | XRCC4, N-terminal domain | XRCC4_N | 9 |
IPR053962 | 53,962 | XRCC4, coiled-coil domain | XRCC4_CC | Domain | 1,923 | false | false | This entry represents the dimeric coiled-coil region from the XRCC4 protein. The complex of two proteins, XRCC4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination [ ]. The BRCT domains of DNA ligase IV... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21924"
] | [
"XRCC4_CC"
] | [
1923
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-164843",
"R-HSA-3108214",
"R-HSA-5693571",
"R-MMU-3108214",
"R-MMU-5693571"
] | [
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-5693571",
"REACTOME:R-MMU-3108214",
"REACTOME:R-MMU-5693571"
] | 5 | [
"1fu1",
"1ik9",
"3ii6",
"3q4f",
"3rwr",
"3sr2",
"3w03",
"4xa4",
"5cj0",
"5cj4",
"6abo",
"7lsy",
"7lt3",
"7m3p",
"7nfc",
"7nfe",
"8bh3",
"8bhv",
"8bhy",
"8bot",
"8eza",
"8ezb",
"9cq3",
"9cq6",
"9cqc",
"9gd7",
"9n81",
"9n82",
"9n83"
] | 29 | [
"PUB00012766",
"PUB00013254",
"PUB00147236",
"PUB00154391"
] | [
"12517771",
"11702069",
"10757784",
"15385968"
] | [
"Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro.",
"Crystal structure of an Xrcc4-DNA ligase IV complex.",
"Ku recruits the XRCC4-ligase IV complex to DNA ends.",
"Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligat... | [
2003,
2001,
2000,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1923
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
2,
1,
3,
1,
3,
7,
2
] | 7 | true | Domain | XRCC4, coiled-coil domain | XRCC4, coiled-coil domain | XRCC4_CC | 2 |
IPR053963 | 53,963 | XRCC4, C-terminal domain | XRCC4_C | Domain | 794 | false | false | This entry represents the C-terminal disordered region from the XRCC4 protein. This domain acts as an activator of the phospholipid scramblase activity of XKR4 [ ]. Upon apoptotic stimuli, XRCC4 is cleaved by caspases, and its C-terminal fragment with an intrinsically disordered region is released into the cytoplasm. T... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21925"
] | [
"XRCC4_C"
] | [
794
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-164843",
"R-HSA-3108214",
"R-HSA-5693571",
"R-MMU-3108214",
"R-MMU-5693571"
] | [
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-5693571",
"REACTOME:R-MMU-3108214",
"REACTOME:R-MMU-5693571"
] | 5 | [
"7lsy",
"7lt3",
"7nfc",
"7nfe",
"8bh3",
"8bhv",
"8bhy",
"8bot",
"8eza",
"8ezb",
"9cq3",
"9cq6",
"9cqc",
"9gd7",
"9n81",
"9n82",
"9n83"
] | 17 | [
"PUB00012766",
"PUB00147236",
"PUB00154390",
"PUB00154391"
] | [
"12517771",
"10757784",
"33725486",
"15385968"
] | [
"Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro.",
"Ku recruits the XRCC4-ligase IV complex to DNA ends.",
"Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane.",
"Xrcc4 physicall... | [
2003,
2000,
2021,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
794
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
3,
7
] | 4 | true | Domain | XRCC4, C-terminal domain | XRCC4, C-terminal domain | XRCC4_C | 9 |
IPR053964 | 53,964 | Integrator complex subunit 1, R3 domain | INT1_R3 | Domain | 1,806 | false | false | Integrator (INT) complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. It binds the C-terminal domain (CTD) of RNA polymerase II (Pol II) and functions as an RNA endonuclease to cleave different classes of RNAs, regulating the transcription of both prote... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22927"
] | [
"INT1_R3"
] | [
1806
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-6807505",
"R-DME-6807505",
"R-HSA-6807505",
"R-MMU-6807505"
] | [
"REACTOME:R-DDI-6807505",
"REACTOME:R-DME-6807505",
"REACTOME:R-HSA-6807505",
"REACTOME:R-MMU-6807505"
] | 4 | [
"7cun",
"7pks",
"7ycx",
"8rbx",
"8rbz",
"8rc4",
"8yjb",
"9vd9"
] | 8 | [
"PUB00152015"
] | [
"33243860"
] | [
"Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1806
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
1,
3,
4,
4
] | 5 | true | Domain | Integrator complex subunit 1, R3 domain | Integrator complex subunit 1, R3 domain | INT1_R3 | 2 |
IPR053965 | 53,965 | Integrator complex subunit 1, R4 domain | INTS1_R4 | Domain | 1,732 | false | false | Integrator (INT) complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. It binds the C-terminal domain (CTD) of RNA polymerase II (Pol II) and functions as an RNA endonuclease to cleave different classes of RNAs, regulating the transcription of both prote... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22928"
] | [
"INTS1_R4"
] | [
1732
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-6807505",
"R-DME-6807505",
"R-HSA-6807505",
"R-MMU-6807505"
] | [
"REACTOME:R-DDI-6807505",
"REACTOME:R-DME-6807505",
"REACTOME:R-HSA-6807505",
"REACTOME:R-MMU-6807505"
] | 4 | [
"7cun",
"7pks",
"7ycx",
"8rbx",
"8rbz",
"8rc4",
"8yjb",
"9vd9"
] | 8 | [
"PUB00152015"
] | [
"33243860"
] | [
"Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1732
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
1,
4,
3,
2
] | 6 | true | Domain | Integrator complex subunit 1, R4 domain | Integrator complex subunit 1, R4 domain | INTS1_R4 | 6 |
IPR053967 | 53,967 | Flagellar hook protein FlgE/F/G-like, D1 domain | LlgE_F_G-like_D1 | Domain | 38,062 | false | false | This entry represents the D1 domain found in three closely related flagellar proteins, usually denoted FlgE, FlgF and FlgG and related proteins. In FlgE, there is an additional domain D2 ( ) outside D1 [ , , , , ]. The flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the l... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22692"
] | [
"LlgE_F_G_D1"
] | [
38062
] | 1 | [] | [] | [] | 0 | [
"1wlg",
"2bgy",
"2bgz",
"3a69",
"5az4",
"5jxl",
"5npy",
"5wrh",
"6jf2",
"6jzr",
"6jzt",
"6k3i",
"6k9q",
"6kfk",
"6ndx",
"7bin",
"7cbm",
"7cgb",
"7cgo",
"7e80",
"7e82",
"7nvg",
"8wk3",
"8wki",
"8wkk",
"8wl2",
"8wlh",
"8wlp",
"8wlq",
"8wlt",
"8wo5",
"8woe"... | 39 | [
"PUB00032756",
"PUB00106064",
"PUB00151809",
"PUB00154040",
"PUB00154041"
] | [
"15657146",
"27759043",
"27811912",
"19913483",
"29083539"
] | [
"A partial atomic structure for the flagellar hook of Salmonella typhimurium.",
"Structural insights into bacterial flagellar hooks similarities and specificities.",
"Complete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions.",
"Specific arrangement of alpha-helical ... | [
2005,
2016,
2016,
2009,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
37573,
69,
2,
418
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Flagellar hook protein FlgE/F/G-like, D1 domain | Flagellar hook protein FlgE/F/G-like, D1 domain | LlgE_F_G-like_D1 | 7 |
IPR053968 | 53,968 | BF9343_1606-like, C-terminal | BF9343_1606-like_C | Domain | 25 | false | false | This domain is found at the C-terminal of BF9343_1606 from Bacteroides fragilis ( ). This domain, whose structure has been solved ( ), is associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22452"
] | [
"BF9343_1606-like_C"
] | [
25
] | 1 | [] | [] | [] | 0 | [
"3g3l"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroides"
] | [
25
] | 1 | [] | [] | 0 | true | Domain | BF9343_1606-like, C-terminal | BF9343_1606-like, C-terminal | BF9343_1606-like_C | 5 |
IPR053969 | 53,969 | Gag1-like, lock domain | Lock_Gag1-like | Domain | 40 | false | false | This domain found in Gag1 from Saccharomyces cerevisiae and similar fungal sequences. Gag1 interacts with Cka2, the fourth subunit of the eukaryotic kinase CK2. This protein is organised into three domains: lock (this entry), Gag and Clamp ( ) [ ]. This short domain is predicted to adopt a predominantly α-helical confi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22991"
] | [
"Lock_Gag1-like"
] | [
40
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153176"
] | [
"37968396"
] | [
"The social and structural architecture of the yeast protein interactome."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycetaceae"
] | [
40
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Gag1-like, lock domain | Gag1-like, lock domain | Lock_Gag1-like | 9 |
IPR053970 | 53,970 | RavZ, C-terminal PI3P-binding domain | RavZ_C | Domain | 16 | false | false | This entry represents the C-terminal in RavZ proteins. The intracellular pathogen Legionella pneumophila interferes with autophagy by delivering an effector protein, cysteine protease RavZ, into the host cytosol. This effector protein cleaves membrane-conjugated Atg8/LC3 proteins from pre-autophagosomal structures [ , ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22225"
] | [
"RavZ_C"
] | [
16
] | 1 | [] | [] | [] | 0 | [
"5cqc",
"5hzy",
"5io3",
"5izv",
"5ms2",
"5ms7",
"5ms8"
] | 7 | [
"PUB00154191",
"PUB00154192",
"PUB00154193",
"PUB00154418"
] | [
"26343456",
"27791457",
"28395732",
"32686895"
] | [
"The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs.",
"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane.",
"Elucidation of the anti-autophagy mechanism of the <i>Legionella</i> effector RavZ us... | [
2015,
2017,
2017,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Legionella"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | RavZ, C-terminal PI3P-binding domain | RavZ, C-terminal PI3P-binding domain | RavZ_C | 7 |
IPR053971 | 53,971 | CofB-like, beta-repeat domain | CofB-like_b-rpt_dom | Domain | 24 | false | false | CofB is a minor pilin involved in type IV pili assembly. It consists of a pilin domain at the N-terminal ( ), followed by a β-repeat hinge-like domain and a C-terminal β-sheet-rich lectin domain [ , ]. This entry represents the central β-repeat domain which has two three-stranded anti-parallel β-sheets [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22228"
] | [
"CofB_beta-rpt"
] | [
24
] | 1 | [] | [] | [] | 0 | [
"4qs4",
"5ax6",
"5ypz"
] | 3 | [
"PUB00151800",
"PUB00151801"
] | [
"26324721",
"26876601"
] | [
"Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.",
"Homo-trimeric Structure of the Type IVb Minor Pilin CofB Suggests Mechanism of CFA/III Pilus Assembly in Human Enterotoxigenic Escherichia coli."
] | [
2015,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
24
] | 1 | [] | [] | 0 | true | Domain | CofB-like, beta-repeat domain | CofB-like, beta-repeat domain | CofB-like_b-rpt_dom | 8 |
IPR053972 | 53,972 | CofB, C-terminal domain | CofB_C | Domain | 101 | false | false | CofB is a minor pilin involved in type IV pili assembly. It consists of a pilin domain at the N-terminal ( ), followed by a β-repeat hinge-like domain ( ) and a C-terminal β-sheet-rich domain, similar to H-type lectins [ , ]. This entry represents the C-terminal domain which is required for CofB to initiate pilus assem... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22229"
] | [
"CofB_C"
] | [
101
] | 1 | [] | [] | [] | 0 | [
"4qs4",
"5ax6",
"5ypz",
"6mic"
] | 4 | [
"PUB00151800",
"PUB00151801"
] | [
"26324721",
"26876601"
] | [
"Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.",
"Homo-trimeric Structure of the Type IVb Minor Pilin CofB Suggests Mechanism of CFA/III Pilus Assembly in Human Enterotoxigenic Escherichia coli."
] | [
2015,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
101
] | 1 | [] | [] | 0 | true | Domain | CofB, C-terminal domain | CofB, C-terminal domain | CofB_C | 2 |
IPR053973 | 53,973 | Endoplasmic reticulum metallopeptidase 1-like, C-terminal domain | ERMP1-like_C | Domain | 3,576 | false | false | Endoplasmic reticulum metallopeptidase 1 (ERMP1, also known as Felix-ina, FXNA or Fxna peptidase) is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, it may play a crucial role in processing proteins required for the organisation of somatic cells and oocytes into discrete follicul... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22248"
] | [
"ERMP1_C"
] | [
3576
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00116354",
"PUB00153927"
] | [
"17267443",
"24498434"
] | [
"Fxna, a novel gene differentially expressed in the rat ovary at the time of folliculogenesis, is required for normal ovarian histogenesis.",
"Structural and functional characterization of cargo-binding sites on the μ4-subunit of adaptor protein complex 4."
] | [
2007,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3576
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
11,
2,
1,
24,
10,
1,
4,
6,
11
] | 9 | true | Domain | Endoplasmic reticulum metallopeptidase 1-like, C-terminal domain | Endoplasmic reticulum metallopeptidase 1-like, C-terminal domain | ERMP1-like_C | 4 |
IPR053974 | 53,974 | Endoplasmic reticulum metallopeptidase 1/1-A, TM domain | ERMP1_1-A_TM | Domain | 2,735 | false | false | Endoplasmic reticulum metallopeptidase 1 (ERMP1, also known as Felix-ina, FXNA or Fxna peptidase) is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, it may play a crucial role in processing proteins required for the organisation of somatic cells and oocytes into discrete follicul... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22249"
] | [
"ERMP1-TM"
] | [
2735
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00116354"
] | [
"17267443"
] | [
"Fxna, a novel gene differentially expressed in the rat ovary at the time of folliculogenesis, is required for normal ovarian histogenesis."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2735
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
17,
12,
2,
7
] | 6 | true | Domain | Endoplasmic reticulum metallopeptidase 1/1-A, TM domain | Endoplasmic reticulum metallopeptidase 1/1-A, TM domain | ERMP1_1-A_TM | 3 |
IPR053975 | 53,975 | Vacuolar membrane protease, C-terminal domain | PFF1_C | Domain | 1,483 | false | false | This entry includes fungal vacuolar membrane proteases, such as PFF1 from yeast, which may be involved in vacuolar sorting and osmoregulation [ ]. It is an homologue of human ERMP1 [ ]. According to AlphaFold structure predictions, these proteins consist of a M28 peptidase domain ( ) at the N-terminal, a central transm... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22250"
] | [
"PFF1_C"
] | [
1483
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00101324",
"PUB00151250"
] | [
"35175277",
"23679341"
] | [
"A lysosomal biogenesis map reveals the cargo spectrum of yeast vacuolar protein targeting pathways.",
"Characterization of an M28 metalloprotease family member residing in the yeast vacuole."
] | [
2022,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1483
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1
] | 2 | true | Domain | Vacuolar membrane protease, C-terminal domain | Vacuolar membrane protease, C-terminal domain | PFF1_C | 3 |
IPR053977 | 53,977 | Thioredoxin-like reductase Rv2466c-like | Rv2466c-like | Family | 5,946 | false | false | This entry represents a family of proteins mainly found in actinomycetes, including thioredoxin-like reductase Rv2466c from Mycobacterium tuberculosis. Rv2466c is a key oxidoreductase that mediates the reductive activation of TP053, a thienopyrimidine derivative that kills replicating and non-replicating M.tuberculosis... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22234"
] | [
"Rv2466c-like"
] | [
5946
] | 1 | [] | [] | [] | 0 | [
"4nxi",
"4wkw",
"4zil",
"5xur"
] | 4 | [
"PUB00154217",
"PUB00154218",
"PUB00154219"
] | [
"26546681",
"24877756",
"29465985"
] | [
"The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.",
"Rv2466c mediates the activation of TP053 to kill replicating and non-replicating Mycobacterium tuberculosis.",
"Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis."
] | [
2015,
2014,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhynchospora breviuscula",
"metagenomes"
] | [
5804,
1,
141
] | 3 | [] | [] | 0 | true | Family | Thioredoxin-like reductase Rv2466c-like | Thioredoxin-like reductase Rv2466c-like | Rv2466c-like | 1 |
IPR053978 | 53,978 | SO2946-like, C-terminal domain | SO2946-like_C | Domain | 33 | false | false | This entry represents the C-terminal domain of SO2946 from Shewanella oneidensis ( ). This protein consists of a short helical N-terminal domain and a large C-terminal domain with the jelly-roll topology, identified as a putative carbohydrate-binding module [ ]. This domain can also be found in other regions in bacteri... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22237"
] | [
"SO2946-like_C"
] | [
33
] | 1 | [] | [] | [] | 0 | [
"2a5z"
] | 1 | [
"PUB00047012"
] | [
"18566914"
] | [
"Structure of SO2946 orphan from Shewanella oneidensis shows \"jelly-roll\" fold with carbohydrate-binding module."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"metagenomes"
] | [
18,
4,
11
] | 3 | [] | [] | 0 | true | Domain | SO2946-like, C-terminal domain | SO2946-like, C-terminal domain | SO2946-like_C | 4 |
IPR053980 | 53,980 | Type ISP restriction-modification enzyme, coupler domain | ISP_coupler | Domain | 1,584 | false | false | Type ISP restriction-modification (RM) enzymes cleave random DNA between distant target sites when two enzymes collide following convergent ATP-driven translocation. This entry represents the all-helical coupler domain of type ISP RM enzymes, which links the ATPase to the MTase and the C-terminal TRD (target recognitio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22240"
] | [
"ISP_coupler"
] | [
1584
] | 1 | [] | [] | [] | 0 | [
"4xqk",
"5ffj",
"7lo5",
"7lvv"
] | 4 | [
"PUB00091657",
"PUB00154025",
"PUB00154026"
] | [
"26389736",
"26975655",
"33826880"
] | [
"Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes.",
"Structural insights into DNA sequence recognition by Type ISP restriction-modification enzymes.",
"Coordination of phage genome degradation versus host genome protection by a bifunctional restriction-modification enzyme vis... | [
2015,
2016,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta",
"Siphoviridae sp. ctBLh2",
"metagenomes"
] | [
3,
1558,
5,
1,
17
] | 5 | [] | [] | 0 | true | Domain | Type ISP restriction-modification enzyme, coupler domain | Type ISP restriction-modification enzyme, coupler domain | ISP_coupler | 6 |
IPR053981 | 53,981 | Baseplate hub protein gp44/GpP-like, second domain | Gp44/GpP-like_2nd | Domain | 2,308 | false | false | This domain is found in baseplate hub protein gp44 from Escherichia phage Mu, GpP from Shewanella oneidensis ( ) and similar proteins found in tailed bacteriophages and bacterial prophages. This domain is located C-terminal to and N-terminal to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22255"
] | [
"Gp44-like_2nd"
] | [
2308
] | 1 | [] | [] | [] | 0 | [
"1wru",
"3cdd",
"3d37",
"9ki1"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
2252,
34,
8,
14
] | 4 | [] | [] | 0 | true | Domain | Baseplate hub protein gp44/GpP-like, second domain | Baseplate hub protein gp44/GpP-like, second domain | Gp44/GpP-like_2nd | 6 |
IPR053982 | 53,982 | Baseplate hub protein gp44/GpP-like, C-terminal | Gp44/GpP-like_C | Domain | 1,817 | false | false | This domain is found in baseplate hub protein gp44 from Escherichia phage Mu, Mu phage baseplate assembly protein GpP from Shewanella oneidensis ( ) and similar sequences found in tailed bacteriophages and prophages from proteobacteria. It is normally found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21929"
] | [
"GpP_4th"
] | [
1817
] | 1 | [] | [] | [] | 0 | [
"1wru",
"3cdd",
"9ki1"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
1787,
11,
6,
13
] | 4 | [] | [] | 0 | true | Domain | Baseplate hub protein gp44/GpP-like, C-terminal | Baseplate hub protein gp44/GpP-like, C-terminal | Gp44/GpP-like_C | 8 |
IPR053983 | 53,983 | BDI_1685-like, C-terminal domain | BDI_1685-like_C | Domain | 51 | false | false | This domain is found at the C-terminal end of BDI_1685 from Parabacteroides distasonis ( ) and similar bacterial sequences. This domain is usually found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22256"
] | [
"BDI_1685-like_C"
] | [
51
] | 1 | [] | [] | [] | 0 | [
"5cd6"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
51
] | 1 | [] | [] | 0 | true | Domain | BDI_1685-like, C-terminal domain | BDI_1685-like, C-terminal domain | BDI_1685-like_C | 7 |
IPR053984 | 53,984 | GPR128, N-terminal domain | GPR128_N | Domain | 491 | false | false | GRP128, also known as Adhesion G-protein coupled receptor G7 (AGRG7), is an orphan receptor of the adhesion family (subclass B2) that belongs to class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance [ , ]. This entry represents the N-terminal dom... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22257"
] | [
"GPR128_N"
] | [
491
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00058430",
"PUB00137741",
"PUB00137742"
] | [
"22333914",
"24574718",
"19797732"
] | [
"A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.",
"Deletion of Gpr128 results in weight loss and increased intestinal contraction frequency.",
"TFG, a target of chromosome translocations in lymphoma and soft tissue tumors, fuses to GPR128 in healthy individuals."
] | [
2012,
2014,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Deuterostomia"
] | [
491
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
2,
1,
2
] | 4 | true | Domain | GPR128, N-terminal domain | GPR128, N-terminal domain | GPR128_N | 2 |
IPR053985 | 53,985 | GPR128, GAIN subdomain A | GPR128_GAIN_subdom_A | Domain | 604 | false | false | GRP128, also known as Adhesion G-protein coupled receptor G7 (AGRG7), is an orphan receptor of the adhesion family (subclass B2) that belongs to class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance [ , ]. It consists of an N-terminal HormR-like ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22259"
] | [
"GPR128_GAIN_subdomA"
] | [
604
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00058430",
"PUB00137741",
"PUB00137742"
] | [
"22333914",
"24574718",
"19797732"
] | [
"A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.",
"Deletion of Gpr128 results in weight loss and increased intestinal contraction frequency.",
"TFG, a target of chromosome translocations in lymphoma and soft tissue tumors, fuses to GPR128 in healthy individuals."
] | [
2012,
2014,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
604
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
1,
2
] | 4 | true | Domain | GPR128, GAIN subdomain A | GPR128, GAIN subdomain A | GPR128_GAIN_subdom_A | 8 |
IPR053986 | 53,986 | GPR128, GAIN subdomain B | GPR128_GAIN_subdom_B | Domain | 650 | false | false | GRP128, also known as Adhesion G-protein coupled receptor G7 (AGRG7), is an orphan receptor of the adhesion family (subclass B2) that belongs to class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance [ , ]. It consists of an N-terminal HormR-like ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22261"
] | [
"GPR128_GAIN_subdom_B"
] | [
650
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00058430",
"PUB00137741",
"PUB00137742"
] | [
"22333914",
"24574718",
"19797732"
] | [
"A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.",
"Deletion of Gpr128 results in weight loss and increased intestinal contraction frequency.",
"TFG, a target of chromosome translocations in lymphoma and soft tissue tumors, fuses to GPR128 in healthy individuals."
] | [
2012,
2014,
2010
] | 3 | [
"IPR057244"
] | [] | 1 | 0 | 1 | [
"Eumetazoa",
"Pontibacter"
] | [
648,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
5,
1,
2
] | 4 | true | Domain | GPR128, GAIN subdomain B | GPR128, GAIN subdomain B | GPR128_GAIN_subdom_B | 1 |
IPR053987 | 53,987 | Transcriptional regulator MlrA-like, C-terminal domain | MlrA-like_C | Domain | 2,581 | false | false | The HTH transcription regulator MlrA belongs to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by re configuring the spacer between the -35 and -10 promoter elements. MlrA it is also known as YehV, and has been shown to control cell-cell aggregation by co-regula... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22267"
] | [
"MlrA_C"
] | [
2581
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00115538",
"PUB00151466",
"PUB00154392"
] | [
"11489123",
"23708798",
"22783906"
] | [
"MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis by Escherichia coli and Salmonella enterica serovar Typhimurium.",
"The EAL domain protein YciR acts as a trigger enzyme in a c-di-GMP signalling cascade in E. coli biofilm control.",
"Molecular function and potential evolution of the bi... | [
2001,
2013,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Pseudomonadati",
"metagenomes"
] | [
5,
2574,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Transcriptional regulator MlrA-like, C-terminal domain | Transcriptional regulator MlrA-like, C-terminal domain | MlrA-like_C | 2 |
IPR053988 | 53,988 | Transcriptional regulator MlrA-like, helical domain | MlrA-like_helical | Domain | 2,524 | false | false | The HTH transcription regulator MlrA belongs to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by re configuring the spacer between the -35 and -10 promoter elements. MlrA it is also known as YehV, and has been shown to control cell-cell aggregation by co-regula... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22270"
] | [
"MlrA_helical"
] | [
2524
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00115538",
"PUB00151466",
"PUB00154392"
] | [
"11489123",
"23708798",
"22783906"
] | [
"MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis by Escherichia coli and Salmonella enterica serovar Typhimurium.",
"The EAL domain protein YciR acts as a trigger enzyme in a c-di-GMP signalling cascade in E. coli biofilm control.",
"Molecular function and potential evolution of the bi... | [
2001,
2013,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
2519,
5
] | 2 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Transcriptional regulator MlrA-like, helical domain | Transcriptional regulator MlrA-like, helical domain | MlrA-like_helical | 7 |
IPR053989 | 53,989 | Teichoic acid transporter subunit TagH, SH3-like domain | TagH_SH3-like | Domain | 166 | false | false | This domain is found in TagH from Staphylococcus epidermidis ( ), the ATPase subunit of the two-component transporter TagGH, which is involved in the synthesis of bacterial polysaccharides-wall teichoic acids. This entry represents the middle SH3-like subdomain that consists of a twisted antiparallel β-sheet and two β-... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22269"
] | [
"TagH_SH3-like"
] | [
166
] | 1 | [] | [] | [] | 0 | [
"5bnd"
] | 1 | [
"PUB00154255"
] | [
"27213893"
] | [
"SH3-like motif-containing C-terminal domain of staphylococcal teichoic acid transporter suggests possible function."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Staphylococcaceae",
"human gut metagenome"
] | [
165,
1
] | 2 | [] | [] | 0 | true | Domain | Teichoic acid transporter subunit TagH, SH3-like domain | Teichoic acid transporter subunit TagH, SH3-like domain | TagH_SH3-like | 4 |
IPR053990 | 53,990 | Teichoic acid transporter subunit TagH, C-terminal domain | TagH_C | Domain | 188 | false | false | TagH from Staphylococcus epidermidis ( ) is the ATPase subunit of the two-component transporter TagGH involved in the synthesis of bacterial polysaccharides-wall teichoic acids. This entry represents the C-terminal of TagH that adopts an α/β structure consisting of a central antiparallel mixed β-sheet packed on one sid... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22096"
] | [
"TagH_C"
] | [
188
] | 1 | [] | [] | [] | 0 | [
"5bnd"
] | 1 | [
"PUB00154255"
] | [
"27213893"
] | [
"SH3-like motif-containing C-terminal domain of staphylococcal teichoic acid transporter suggests possible function."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillales",
"human gut metagenome"
] | [
187,
1
] | 2 | [] | [] | 0 | true | Domain | Teichoic acid transporter subunit TagH, C-terminal domain | Teichoic acid transporter subunit TagH, C-terminal domain | TagH_C | 7 |
IPR053992 | 53,992 | ATR1, N-terminal domain | ATR1_N | Domain | 7 | false | false | Host-adapted plant pathogens secrete numerous effectors into the host extracellular spaces or inside cells. The A. thaliana TNL receptor RPP1 confers strain-specific immunity through recognition of H.arabidopsidis effector ATR1. ATR1 consists of two α-helical domains that are involved in interactions with the receptor.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22223"
] | [
"ATR1_N"
] | [
7
] | 1 | [] | [] | [] | 0 | [
"3rmr",
"7crb",
"7crc"
] | 3 | [
"PUB00098642"
] | [
"33273071"
] | [
"Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Peronosporaceae"
] | [
7
] | 1 | [] | [] | 0 | true | Domain | ATR1, N-terminal domain | ATR1, N-terminal domain | ATR1_N | 9 |
IPR053993 | 53,993 | Cas12a, PI domain | Cas12a_PI | Domain | 127 | false | false | This entry represents the PI (PAM-interacting) domain found in Cpf1, also known as CRISPR-associated endonuclease Cas12a. The CRISPR-Cpf1 system is a class 2 CRISPR-Cas system that mediates robust DNA interference. Cpf1 differ from Cas9 in many aspects, including the guide RNAs and substrate specificity. The Cpf1-crRNA... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22222"
] | [
"Cpf1_PI-like"
] | [
127
] | 1 | [] | [] | [] | 0 | [
"5id6",
"5mga",
"5nfv",
"5ng6",
"5xus",
"5xut",
"5xuu",
"5xuz",
"6gtc",
"6gtd",
"6gte",
"6gtf",
"6gtg",
"6i1k",
"6i1l",
"6iv6",
"6kl9",
"6klb",
"6nm9",
"6nma",
"6nmc",
"6nmd",
"6nme",
"6omv",
"6p7m",
"6p7n",
"8h9d",
"8i54",
"8kgf",
"8qwd",
"8qwe",
"8qwf"... | 44 | [
"PUB00087324",
"PUB00087325",
"PUB00153855",
"PUB00153885",
"PUB00153886"
] | [
"28431230",
"28562584",
"27096363",
"28781234",
"30503205"
] | [
"Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a.",
"Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage.",
"The crystal structure of Cpf1 in complex with CRISPR RNA.",
"Structural Basis for the Canonical and Non-canonical PAM Recognition by ... | [
2017,
2017,
2016,
2017,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomassiliicoccales",
"Potamilus streckersoni",
"bioreactor metagenome"
] | [
122,
3,
1,
1
] | 4 | [] | [] | 0 | true | Domain | Cas12a, PI domain | Cas12a, PI domain | Cas12a_PI | 2 |
IPR053994 | 53,994 | NigD-like, OB domain | NigD-like_OB | Domain | 93 | false | false | This entry represents an OB fold domain found in NigD and related proteins from bacteria. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22221"
] | [
"NigD_N-like"
] | [
93
] | 1 | [] | [] | [] | 0 | [
"5bmt"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidales",
"bioreactor metagenome"
] | [
92,
1
] | 2 | [] | [] | 0 | true | Domain | NigD-like, OB domain | NigD-like, OB domain | NigD-like_OB | 2 |
IPR053995 | 53,995 | Quiescin sulphydryl oxidase, pseudo-Erv domain | QSOX_pErv | Domain | 51 | false | false | Quiescin sulphydryl oxidase (QSOX) family of enzymes is the only known example of conserved concatenation of disulphide-generating and disulphide-transferring modules within a single polypeptide. Formation and transfer of disulphide bonds in QSOX are mediated by redox-active cysteine pairs in a canonical Cys-X-X-Cys pa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22220"
] | [
"QSOX_pErv"
] | [
51
] | 1 | [] | [] | [] | 0 | [
"3qcp",
"3qd9"
] | 2 | [
"PUB00061153"
] | [
"22801504"
] | [
"The dynamic disulphide relay of quiescin sulphydryl oxidase."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Metakinetoplastina"
] | [
51
] | 1 | [] | [] | 0 | true | Domain | Quiescin sulphydryl oxidase, pseudo-Erv domain | Quiescin sulphydryl oxidase, pseudo-Erv domain | QSOX_pErv | 1 |
IPR053996 | 53,996 | DUF3829-like, C-terminal domain | DUF3829-like_C | Domain | 137 | false | false | This domain is found at the C-terminal end of uncharacterised DUF3829-like proteins. It is often found associated to . Its function is unknown. It shows four α-helices. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22219"
] | [
"DUF3829_2nd"
] | [
137
] | 1 | [] | [] | [] | 0 | [
"3iee",
"3rh3"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidales"
] | [
137
] | 1 | [] | [] | 0 | true | Domain | DUF3829-like, C-terminal domain | DUF3829-like, C-terminal domain | DUF3829-like_C | 7 |
IPR053997 | 53,997 | SAS-6, C-terminal coiled coil | SAS-6_C_CC | Domain | 102 | false | false | This domain is found at the C-terminal end of Spindle assembly abnormal protein 6 (Sas-6). Sas-6 is a central scaffolding component of the centrioles ensuring their nine-fold symmetry. Sas-6 forms a dimer through this domain to then further homo-oligomerise to form a ring structure from which the CC domains emanate as ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF22216",
"PF22218"
] | [
"Sas-6_C_CC",
"SAS-6_C_CC_2"
] | [
61,
41
] | 2 | [] | [] | [] | 0 | [
"4ckn",
"4ckp",
"5al7"
] | 3 | [
"PUB00154221",
"PUB00154222"
] | [
"26002084",
"24596152"
] | [
"The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies.",
"Structure of the SAS-6 cartwheel hub from Leishmania major."
] | [
2015,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
97
] | 2 | [
"Drosophila melanogaster"
] | [
1
] | 1 | true | Domain | SAS-6, C-terminal coiled coil | SAS-6, C-terminal coiled coil | SAS-6_C_CC | 3 |
IPR053998 | 53,998 | Acyl-CoA dehydrogenase 11-like C-terminal domain | ACDH-11_C | Domain | 1,215 | false | false | Acyl-CoA dehydrogenase 11 (ACDH-11) sequesters C11/C12-chain fatty acids and prevents these fatty acids from activating nuclear hormone receptors and driving fat-7 expression. This enzyme consists of four domains, of which the C-terminal folds into a four-helical up-and-down bundle [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22217"
] | [
"ACDH-11_C"
] | [
1215
] | 1 | [] | [] | [] | 0 | [
"4y9j",
"4y9l"
] | 2 | [
"PUB00082831"
] | [
"25981666"
] | [
"Acyl-CoA Dehydrogenase Drives Heat Adaptation by Sequestering Fatty Acids."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
173,
1005,
35,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio"
] | [
1,
3
] | 2 | true | Domain | Acyl-CoA dehydrogenase 11-like C-terminal domain | Acyl-CoA dehydrogenase 11-like C-terminal domain | ACDH-11_C | 7 |
IPR054000 | 54,000 | Mixed lineage kinase domain-like, N-terminal domain | MLKL_N | Domain | 2,791 | false | false | Mixed-lineage kinase domain-like (MLKL) is crucial for necroptosis, permeabilising membranes via its N-terminal domain upon phosphorylation of its kinase-like domain by RIP3. The MLKL N-terminal domain forms a four-helical up-and-down bundle that is sufficient to induce liposome leakage and a fifth C-terminal helix tha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22215"
] | [
"MLKL_N"
] | [
2791
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-3295583",
"R-HSA-5213460",
"R-HSA-5675482",
"R-HSA-9686347",
"R-MMU-3295583",
"R-MMU-5213460",
"R-MMU-5675482"
] | [
"REACTOME:R-HSA-3295583",
"REACTOME:R-HSA-5213460",
"REACTOME:R-HSA-5675482",
"REACTOME:R-HSA-9686347",
"REACTOME:R-MMU-3295583",
"REACTOME:R-MMU-5213460",
"REACTOME:R-MMU-5675482"
] | 7 | [
"2msv",
"4btf",
"6d74",
"6lk5",
"6ux8",
"6zle",
"6zpr",
"6zvo",
"6zz1",
"7nm2",
"7nm4",
"7nm5"
] | 12 | [
"PUB00146334",
"PUB00146335",
"PUB00154068",
"PUB00154069",
"PUB00154070"
] | [
"25220470",
"24012422",
"31031142",
"34158471",
"32234780"
] | [
"A plug release mechanism for membrane permeation by MLKL.",
"The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism.",
"Direct Activation of Human MLKL by a Select Repertoire of Inositol Phosphate Metabolites.",
"The MLKL kinase-like domain dimerization is an indispensable step of mammal... | [
2014,
2013,
2019,
2021,
2020
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2791
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
2,
5,
3,
3
] | 5 | true | Domain | Mixed lineage kinase domain-like, N-terminal domain | Mixed lineage kinase domain-like, N-terminal domain | MLKL_N | 2 |
IPR054001 | 54,001 | Degenerin mec-4/10, cytosolic domain | Mec-4/10_cyt | Domain | 132 | false | false | This entry represents the cytosolic domain found in Degenerin mec-4 and mec-10, the pore-forming subunits of the sensory mechanotransduction complex that mediates touch sensation [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22214"
] | [
"Mec-4_10_cyt"
] | [
132
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-CEL-2672351",
"R-CEL-9730628"
] | [
"REACTOME:R-CEL-2672351",
"REACTOME:R-CEL-9730628"
] | 2 | [
"2k2b",
"5ttt"
] | 2 | [
"PUB00154059"
] | [
"17261841"
] | [
"Gain-of-function mutations in the MEC-4 DEG/ENaC sensory mechanotransduction channel alter gating and drug blockade."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
132
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | Degenerin mec-4/10, cytosolic domain | Degenerin mec-4/10, cytosolic domain | Mec-4/10_cyt | 4 |
IPR054002 | 54,002 | RNA-directed RNA polymerase, C-terminal | RdRP_C | Domain | 62 | false | false | This domain is found at the C-terminal of RNA-directed RNA polymerase (RdRP). This protein adopts a closed cage-like structure consisting of a central polymerase domain sandwiched between N-terminal and C-terminal bracelet domains. This domain adopts a predominantly α-helical configuration [ , , , , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22213"
] | [
"CPV_RdRP_C"
] | [
62
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"3ja4",
"3ja5",
"3jb6",
"3jb7",
"5h0r",
"6k32",
"6ty8",
"6ty9",
"6tz0",
"6tz1",
"6tz2"
] | 11 | [
"PUB00152701",
"PUB00153887",
"PUB00153888",
"PUB00153889",
"PUB00153890"
] | [
"31629769",
"26383954",
"26503045",
"27914893",
"31695188"
] | [
"Structure of RdRps Within a Transcribing dsRNA Virus Provides Insights Into the Mechanisms of RNA Synthesis.",
"Cryo-EM shows the polymerase structures and a nonspooled genome within a dsRNA virus.",
"In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus.",
"Near-Atomic R... | [
2020,
2015,
2015,
2017,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
62
] | 1 | [] | [] | 0 | true | Domain | RNA-directed RNA polymerase, C-terminal | RNA-directed RNA polymerase, C-terminal | RdRP_C | 3 |
IPR054004 | 54,004 | Type six secretion immunity 3 domain | Tsi3 | Domain | 42 | false | false | This entry represents the Tsi3 domain. Tsi3 immunity protein prevents early activation of toxin Tse3. Three loops of Tsi3 deeply insert into the groove of Tse3, fully blocking its active site. This interaction serves as the structural basis for Tse3 inactivation [ , , ]. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF038331",
"PF22211"
] | [
"Tsi3_fam",
"Tsi3"
] | [
31,
40
] | 2 | [] | [] | [] | 0 | [
"3wa5",
"4luq",
"4m5f",
"4n7s",
"4n80",
"4n88",
"8ik0",
"8ik3"
] | 8 | [
"PUB00105729",
"PUB00105730",
"PUB00154253"
] | [
"24100309",
"24724564",
"24025333"
] | [
"Complex structure of type VI peptidoglycan muramidase effector and a cognate immunity protein.",
"Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3 complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-binding mechanism.",
"Structural Insights on the bacteriolytic and ... | [
2013,
2014,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
42
] | 1 | [] | [] | 0 | true | Domain | Type six secretion immunity 3 domain | Type six secretion immunity 3 domain | Tsi3 | 9 |
IPR054005 | 54,005 | VP17, central beta-barrel | VP17_central_barrel | Domain | 21 | false | false | This entry represents the central β-barrel of VP17, the large major capsid protein of of bacteriophage P23-77 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22210"
] | [
"VP17_central_barrel"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"3zmn",
"3zn6"
] | 2 | [
"PUB00067131"
] | [
"23623731"
] | [
"Bacteriophage p23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Deinococci",
"Hukuchivirus"
] | [
19,
2
] | 2 | [] | [] | 0 | true | Domain | VP17, central beta-barrel | VP17, central beta-barrel | VP17_central_barrel | 2 |
IPR054006 | 54,006 | RNA-directed RNA polymerase, N-terminal | RdRP_N | Domain | 129 | false | false | This domain is found at the N terminus of RNA-directed RNA polymerase (RdRP) found in reoviruses. This protein adopts a closed cage-like structure consisting of a central polymerase domain sandwiched between the N-terminal and the C-terminal bracelet domains. This domain adopts a predominantly α-helical configuration [... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22209"
] | [
"CPV_RdRP_N"
] | [
129
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"3ja4",
"3ja5",
"3jb6",
"3jb7",
"5h0r",
"6k32",
"6ty8",
"6ty9",
"6tz0",
"6tz1",
"6tz2"
] | 11 | [
"PUB00152701",
"PUB00153887",
"PUB00153888",
"PUB00153889",
"PUB00153890"
] | [
"31629769",
"26383954",
"26503045",
"27914893",
"31695188"
] | [
"Structure of RdRps Within a Transcribing dsRNA Virus Provides Insights Into the Mechanisms of RNA Synthesis.",
"Cryo-EM shows the polymerase structures and a nonspooled genome within a dsRNA virus.",
"In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus.",
"Near-Atomic R... | [
2020,
2015,
2015,
2017,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Apolygus lucorum",
"Viruses"
] | [
2,
127
] | 2 | [] | [] | 0 | true | Domain | RNA-directed RNA polymerase, N-terminal | RNA-directed RNA polymerase, N-terminal | RdRP_N | 8 |
IPR054007 | 54,007 | MCM3 winged helix domain | WHD_MCM3 | Domain | 50 | false | false | This entry represents the C-terminal winged helix domain found in yeast DNA replication licensing factor MCM3. This protein acts as a component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22207"
] | [
"WHD_MCM3"
] | [
50
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-SCE-176187",
"R-SCE-68867",
"R-SCE-68962",
"R-SCE-69052"
] | [
"REACTOME:R-SCE-176187",
"REACTOME:R-SCE-68867",
"REACTOME:R-SCE-68962",
"REACTOME:R-SCE-69052"
] | 4 | [
"3ja8",
"3jc5",
"3jc6",
"3jc7",
"5bk4",
"5u8s",
"5u8t",
"5v8f",
"5xf8",
"6eyc",
"6f0l",
"6hv9",
"6ptj",
"6ptn",
"6pto",
"6rqc",
"6skl",
"6sko",
"6wgc",
"6wgf",
"6wgg",
"6wgi",
"7p30",
"7p5z",
"7pmk",
"7pmn",
"7pt6",
"7pt7",
"7qhs",
"7v3u",
"7v3v",
"7w8g"... | 55 | [
"PUB00063043",
"PUB00138519",
"PUB00152060",
"PUB00154054"
] | [
"19896182",
"26222030",
"26854665",
"28191894"
] | [
"Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing.",
"Structure of the eukaryotic MCM complex at 3.8 A.",
"Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation.",
"Open-ringed structure of the Cdt1-Mcm2-7 complex as a p... | [
2009,
2015,
2016,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Saccharomycetaceae"
] | [
50
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | MCM3 winged helix domain | MCM3 winged helix domain | WHD_MCM3 | 5 |
IPR054008 | 54,008 | Csm6 6H domain | Csm6_6H | Domain | 185 | false | false | This entry represents the six-helix domain (6H) of CRISPR system endoribonuclease Csm6 from Thermus termophilus and related sequences [ ]. Csm6 is a ssRNA-specific endoribonuclease that provides an auxiliary RNA-targeting interference mechanism in type III-A CRISPR-Cas systems, working together with the RNA- and DNA-ta... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22205"
] | [
"Csm6_6H"
] | [
185
] | 1 | [] | [] | [] | 0 | [
"5fsh",
"8jbb",
"8jbc",
"8jh1"
] | 4 | [
"PUB00106708",
"PUB00153094",
"PUB00153854"
] | [
"31326273",
"33461211",
"26763118"
] | [
"CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA<sub>4</sub> Cleavage with ApA>p Formation Terminating RNase Activity.",
"The Card1 nuclease provides defence during type III CRISPR immunity.",
"Structural basis for the endoribonuclease activity of the type III-A CRISPR-associated pro... | [
2019,
2021,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"marine sediment metagenome"
] | [
32,
151,
2
] | 3 | [] | [] | 0 | true | Domain | Csm6 6H domain | Csm6 6H domain | Csm6_6H | 7 |
IPR054009 | 54,009 | CRISPR-associated endonuclease C2c1, wedge domain, second region | C2c1_WED-II | Domain | 16 | false | false | This entry represents the second region of the wedge domain (WED-II) of CRISPR-associated endonuclease C2c1 (also known as Cas12b). It adopts an oligonucleotide-binding (OB) fold with eight β-stranded distorted β-sheets flanked by two α-helices and one β-hairpin [ , ]. C2c1 is a class 2 type V-B effector protein that w... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22204"
] | [
"C2c1_WED-II"
] | [
16
] | 1 | [] | [] | [] | 0 | [
"5u30",
"5u31",
"5u33",
"5u34",
"5wqe",
"5wti"
] | 6 | [
"PUB00153840",
"PUB00153841"
] | [
"27984729",
"27989439"
] | [
"PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease.",
"C2c1-sgRNA Complex Structure Reveals RNA-Guided DNA Cleavage Mechanism."
] | [
2016,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease C2c1, wedge domain, second region | CRISPR-associated endonuclease C2c1, wedge domain, second region | C2c1_WED-II | 9 |
IPR054010 | 54,010 | CRISPR-associated endonuclease C2c1, Nuc-II domain | C2c1_Nuc-II | Domain | 18 | false | false | This entry represents the C-terminal second Nuc (Nuc-II) domain of C2c1 CRISPR-Cas endonuclease (also known as Cas12b). This domain folds into an open five-stranded β-barrel and an α-helix. Nuc-II is essential for cleavage activity. C2c1 is a class 2 type V-B effector protein that was shown to be active for target DNA ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22077"
] | [
"C2c1_Nuc-II"
] | [
18
] | 1 | [] | [] | [] | 0 | [
"5u30",
"5u31",
"5u33",
"5u34",
"5wqe",
"5wti"
] | 6 | [
"PUB00153840",
"PUB00153841"
] | [
"27984729",
"27989439"
] | [
"PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease.",
"C2c1-sgRNA Complex Structure Reveals RNA-Guided DNA Cleavage Mechanism."
] | [
2016,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
18
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease C2c1, Nuc-II domain | CRISPR-associated endonuclease C2c1, Nuc-II domain | C2c1_Nuc-II | 4 |
IPR054011 | 54,011 | C2c1 CRISPR-Cas endonuclease, RuvC-like domain | C2c1_RuvC-like | Domain | 22 | false | false | This entry represents the RuvC-like domain of C2c1 CRISPR-Cas endonuclease (also known as Cas12b). C2c1 is a class 2 type V-B effector protein that was shown to be active for target DNA cleavage in vivo and in vitro. In contrast to Cpf1, this enzyme cleavage activity requires both crRNA and tracrRNA. The structure of C... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22126"
] | [
"C2c1_RuvC-like"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"5u30",
"5u31",
"5u33",
"5u34",
"5wqe",
"5wti",
"9kln",
"9klo",
"9klp",
"9klq"
] | 10 | [
"PUB00153840",
"PUB00153841",
"PUB00153842"
] | [
"27984729",
"27989439",
"28374750"
] | [
"PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease.",
"C2c1-sgRNA Complex Structure Reveals RNA-Guided DNA Cleavage Mechanism.",
"Structural basis of stringent PAM recognition by CRISPR-C2c1 in complex with sgRNA."
] | [
2016,
2017,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
22
] | 1 | [] | [] | 0 | true | Domain | C2c1 CRISPR-Cas endonuclease, RuvC-like domain | C2c1 CRISPR-Cas endonuclease, RuvC-like domain | C2c1_RuvC-like | 9 |
IPR054012 | 54,012 | CRISPR-associated endonuclease C2c1, second helical domain | C2c1_helical_2nd | Domain | 17 | false | false | This entry represents the second helical domain (REC2) from CRISPR-associated endonuclease C2c1 (also known as Cas12b). This domain, together with the first helical domain (helical-I or REC1) ( ) forms the α-recognition (REC) lobe, which recognises a 20bp guide:target heteroduplex in RNAs [ , ]. C2c1 is a class 2 type ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22172"
] | [
"C2c1_helical"
] | [
17
] | 1 | [] | [] | [] | 0 | [
"5u30",
"5u31",
"5u33",
"5u34",
"5wqe",
"5wti"
] | 6 | [
"PUB00153840",
"PUB00153841",
"PUB00153842"
] | [
"27984729",
"27989439",
"28374750"
] | [
"PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease.",
"C2c1-sgRNA Complex Structure Reveals RNA-Guided DNA Cleavage Mechanism.",
"Structural basis of stringent PAM recognition by CRISPR-C2c1 in complex with sgRNA."
] | [
2016,
2017,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
17
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease C2c1, second helical domain | CRISPR-associated endonuclease C2c1, second helical domain | C2c1_helical_2nd | 8 |
IPR054013 | 54,013 | CRISPR-associated endonuclease C2c1, first helical domain | C2c1_helical_1st | Domain | 20 | false | false | This entry represents the first helical domain (REC1) of CRISPR-associated endonuclease C2c1 (also known as Cas12b). This domain, together with the second helical domain ( ) forms the α-recognition (REC) lobe, which recognises a 20bp guide:target heteroduplex in RNAs [ , ]. C2c1 is a class 2 type V-B effector protein t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22202"
] | [
"C2c1_helical_1st"
] | [
20
] | 1 | [] | [] | [] | 0 | [
"5u30",
"5u31",
"5u33",
"5u34",
"5wqe",
"5wti"
] | 6 | [
"PUB00153840",
"PUB00153841",
"PUB00153842"
] | [
"27984729",
"27989439",
"28374750"
] | [
"PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease.",
"C2c1-sgRNA Complex Structure Reveals RNA-Guided DNA Cleavage Mechanism.",
"Structural basis of stringent PAM recognition by CRISPR-C2c1 in complex with sgRNA."
] | [
2016,
2017,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
20
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease C2c1, first helical domain | CRISPR-associated endonuclease C2c1, first helical domain | C2c1_helical_1st | 7 |
IPR054014 | 54,014 | Surface cell antigen Sca2 helical repeat | Sca2 | Repeat | 53 | false | false | Sca2 (surface cell antigen 2) is the only bacterial protein known to promote both actin filament nucleation and profilin-dependent elongation, mimicking eukaryotic formins to assemble actin comet tails for Rickettsia motility. Sca2's functional mimicry of formins is achieved through a unique mechanism. Unlike formins, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22203"
] | [
"Sca2"
] | [
53
] | 1 | [] | [] | [] | 0 | [
"4j7o"
] | 1 | [
"PUB00154223"
] | [
"23818602"
] | [
"Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Rickettsia"
] | [
53
] | 1 | [] | [] | 0 | true | Repeat | Surface cell antigen Sca2 helical repeat | Surface cell antigen Sca2 helical repeat | Sca2 | 6 |
IPR054015 | 54,015 | ExsA-like, N-terminal regulatory domain | ExsA-like_N | Domain | 3,809 | false | false | This entry represents the ExsA regulatory domain which mediates the ExsD binding. The structure of this domain closely resembles those of the regulatory domains of AraC and ToxT, having typical cupin-like fold [ ]. ExsA is an AraC-type transcriptional activator protein that is regulated through protein-protein interact... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22200"
] | [
"ExsA_N"
] | [
3809
] | 1 | [] | [] | [] | 0 | [
"4zua"
] | 1 | [
"PUB00153932",
"PUB00154393",
"PUB00154394"
] | [
"26317977",
"1624422",
"2644192"
] | [
"Structural Analysis of the Regulatory Domain of ExsA, a Key Transcriptional Regulator of the Type Three Secretion System in Pseudomonas aeruginosa.",
"Temperature sensing in Yersinia pestis: regulation of yopE transcription by lcrF.",
"Homology between virF, the transcriptional activator of the Yersinia virule... | [
2015,
1992,
1989
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3789,
5,
15
] | 3 | [] | [] | 0 | true | Domain | ExsA-like, N-terminal regulatory domain | ExsA-like, N-terminal regulatory domain | ExsA-like_N | 3 |
IPR054016 | 54,016 | FKBP26, IF domain | FKBP26_IF | Domain | 862 | false | false | This domain is centrally located in Long-type peptidyl-prolyl cis-trans isomerase from Methanocaldococcus jannaschii (FKBP26) and similar archaeal sequences. FKBP26 catalyses the cis-trans isomerisation of peptidyl prolyl bonds and exhibits chaperone-like activity. The latter activity requires a 50-residue insertion (I... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22199"
] | [
"FKBP26_IF"
] | [
862
] | 1 | [] | [] | [] | 0 | [
"3pr9",
"3pra",
"3prb",
"3prd"
] | 4 | [
"PUB00026168",
"PUB00065543"
] | [
"12729748",
"21262232"
] | [
"Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities.",
"Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26."
] | [
2003,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
832,
5,
25
] | 3 | [] | [] | 0 | true | Domain | FKBP26, IF domain | FKBP26, IF domain | FKBP26_IF | 7 |
IPR054017 | 54,017 | Glucokinase regulatory protein, second SIS domain | GKRP_SIS_2 | Domain | 686 | false | false | Glucokinase regulatory protein (GKRP) binds glucokinase (GK) mainly through hydrophobic interactions, functioning as an allosteric switch in blood glucose control by the liver [ ]. GKRP is trilobal in shape, consisting of two topologically identical sugar isomerase (SIS) domains capped by an α-helical lid domain ( ). T... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22198"
] | [
"GKRP_SIS_2"
] | [
686
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-170822",
"R-HSA-5619107",
"R-MMU-170822",
"R-RNO-170822"
] | [
"REACTOME:R-HSA-170822",
"REACTOME:R-HSA-5619107",
"REACTOME:R-MMU-170822",
"REACTOME:R-RNO-170822"
] | 4 | [
"3w0l",
"4bb9",
"4bba",
"4lc9",
"4ly9",
"4mqu",
"4mro",
"4msu",
"4ohk",
"4ohm",
"4oho",
"4ohp",
"4olh",
"4op1",
"4op2",
"4op3",
"4px2",
"4px3",
"4px5",
"4pxs"
] | 20 | [
"PUB00067028",
"PUB00069412",
"PUB00151607",
"PUB00152605"
] | [
"23621087",
"23733961",
"24226772",
"23957911"
] | [
"Crystal Structure of Glucokinase Regulatory Protein.",
"Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase.",
"Antidiabetic effects of glucokinase regulatory protein small-molecule disruptors.",
"Structural basis for regulation of human glucokinase by gluc... | [
2013,
2013,
2013,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
12,
672,
2
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
1,
4
] | 4 | true | Domain | Glucokinase regulatory protein, second SIS domain | Glucokinase regulatory protein, second SIS domain | GKRP_SIS_2 | 5 |
IPR054018 | 54,018 | HdrB-like C-terminal domain | HdrB-like_C | Domain | 279 | false | false | This entry represents a domain found at the C-terminal of poorly characterised bacterial proteins similar to HdrB from Helicobacter sp. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22196"
] | [
"HdrB-like_C"
] | [
279
] | 1 | [] | [] | [] | 0 | [
"3kwl"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Campylobacterales"
] | [
279
] | 1 | [] | [] | 0 | true | Domain | HdrB-like C-terminal domain | HdrB-like C-terminal domain | HdrB-like_C | 8 |
IPR054019 | 54,019 | Properdin, thrombospondin type 1 C-terminal | CFP_TSR_C | Repeat | 583 | false | false | This represents the C-terminal thrombospondin type I repeat (TSR_C) found in human Properdin (CFP) and similar proteins from vertebrates. Properdin is a glycoprotein constructed from a common pool of structure units or modules, which are homologous to the thrombospondin type 1 repeat, TSR. It is a positive regulator of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22195"
] | [
"TSP1_CFP_C"
] | [
583
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-173736",
"R-HSA-174577",
"R-HSA-5083635",
"R-HSA-5173214",
"R-HSA-6798695",
"R-HSA-977606",
"R-MMU-173736",
"R-MMU-174577",
"R-MMU-5173214",
"R-MMU-6798695",
"R-MMU-977606"
] | [
"REACTOME:R-HSA-173736",
"REACTOME:R-HSA-174577",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-173736",
"REACTOME:R-MMU-174577",
"REACTOME:R-MMU-5173214",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-977606"
] | 11 | [
"1w0r",
"1w0s",
"6rur",
"6rus",
"6ruv",
"6rv6",
"6s08",
"6s0a",
"6s0b",
"6sej",
"7b26",
"7noz",
"8q6r"
] | 13 | [
"PUB00027123",
"PUB00038006",
"PUB00138414",
"PUB00138415",
"PUB00153864",
"PUB00153865",
"PUB00153866",
"PUB00153867",
"PUB00153868"
] | [
"12391027",
"15491616",
"28366782",
"28069958",
"21821127",
"31507604",
"31552043",
"35031611",
"36173177"
] | [
"Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication.",
"The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling.",
"Identification and characterizati... | [
2002,
2004,
2017,
2017,
2011,
2019,
2019,
2022,
2022
] | 9 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
583
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
2,
3
] | 4 | true | Repeat | Properdin, thrombospondin type 1 C-terminal | Properdin, thrombospondin type 1 C-terminal | CFP_TSR_C | 7 |
IPR054020 | 54,020 | F93, winged-helix domain | WHD_F93 | Domain | 22 | false | false | This entry represents a WH-like domain ( ) found in a putative transcription factor called F-93 from Sulfolobus spindle-shaped viruses (SSVs) ( ) [ ] and related proteins. Members of this family appear to be related to MarR ( ) and PadR ( ) families of prokaryotic transcription factors. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22194"
] | [
"WHD_F93"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"1tbx"
] | 1 | [
"PUB00031401"
] | [
"15479795"
] | [
"Crystal structure of F-93 from Sulfolobus spindle-shaped virus 1, a winged-helix DNA binding protein."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Neisseria subflava",
"Viruses incertae sedis"
] | [
16,
1,
5
] | 3 | [] | [] | 0 | true | Domain | F93, winged-helix domain | F93, winged-helix domain | WHD_F93 | 6 |
IPR054021 | 54,021 | MvcA insertion domain | MvcA_ins | Domain | 22 | false | false | This entry represents the insertion domain of MvcA, the MavC paralogue A of bacterial effector MavC from Legionella pneumophila. MvcA catalyses the reverse reaction of MavC, removing Ub from Ube2N through hydrolysis which regulates MavC activity. MvcA is similar at sequence and structural levels to MavC, and it exhibit... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22193"
] | [
"MvcA_ins"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"5suj",
"5tsc",
"5ym9",
"6jky",
"6k11",
"6k3b",
"6kfp",
"6kg6",
"6kl4",
"6lp2",
"6lw4",
"6p5b",
"6p5h",
"6ulh",
"6ump",
"6ums",
"7bxf",
"7bxg",
"7bxh"
] | 19 | [
"PUB00154089",
"PUB00154090",
"PUB00154091",
"PUB00154092",
"PUB00154093"
] | [
"29642013",
"31825121",
"32286321",
"32596129",
"32398758"
] | [
"Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila.",
"Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.",
"Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector... | [
2018,
2020,
2020,
2020,
2020
] | 5 | [] | [] | 0 | 0 | null | [
"Legionella pneumophila"
] | [
22
] | 1 | [] | [] | 0 | true | Domain | MvcA insertion domain | MvcA insertion domain | MvcA_ins | 9 |
IPR054022 | 54,022 | RickCE N-terminal domain | RickCE_N | Domain | 44 | false | false | This is a presumed domain found at the N-terminal end of rickCE ubiquitin-like proteases, such as , which may have a Rossmann-like fold similar to that in glycosyltransferases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22189"
] | [
"RickCE_N"
] | [
44
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Rickettsieae"
] | [
44
] | 1 | [] | [] | 0 | true | Domain | RickCE N-terminal domain | RickCE N-terminal domain | RickCE_N | 8 |
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