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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR058969 | 58,969 | Putative phage tail fibre, N-terminal domain | Phage_phiTE_241_N | Domain | 113 | false | false | This entry represents the N-terminal region of a putative phage tail fibre protein. Members of this group are found in tailed bacteriophages and bacterial prophages, including Phage PhiTE protein phiTE_241 . These proteins are predicted to form a homotrimeric arrangement. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26208"
] | [
"Phage_phiTE_241_N"
] | [
113
] | 1 | [] | [] | [] | 0 | [
"9cuy",
"9mjn"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Betaproteobacteria",
"Viruses"
] | [
4,
109
] | 2 | [] | [] | 0 | true | Domain | Putative phage tail fibre, N-terminal domain | Putative phage tail fibre, N-terminal domain | Phage_phiTE_241_N | 9 |
IPR058970 | 58,970 | Putative phage tail fibre, C-terminal domain | Phage_phiTE_241_C | Domain | 275 | false | false | This entry represents the C-terminal β sandwich domain of a putative phage tail fibre protein. Members of this group are found in tailed bacteriophages and bacterial prophages, including Phage PhiTE protein phiTE_241 . These proteins are predicted to form a homotrimeric arrangement. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26209"
] | [
"Phage_phiTE_241_C"
] | [
275
] | 1 | [] | [] | [] | 0 | [
"9cuy",
"9mjn"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"metagenomes"
] | [
111,
140,
24
] | 3 | [] | [] | 0 | true | Domain | Putative phage tail fibre, C-terminal domain | Putative phage tail fibre, C-terminal domain | Phage_phiTE_241_C | 3 |
IPR058971 | 58,971 | Rok, N-terminal oligomerisation domain | Rok_N_oligomerisation | Domain | 222 | false | false | This entry represents the N-terminal oligomerisation domain of the Rok (regulator of ComK) protein. The N-terminal domain is involved in protein dimerisation and contributes to the formation of DNA bridges, allowing Rok to compact DNA and silence genes [ , ]. Rok is a nucleoid-associated protein that functions as a tra... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26513"
] | [
"Rok_N"
] | [
222
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161446",
"PUB00161447",
"PUB00161448"
] | [
"21085634",
"15743949",
"11849533"
] | [
"The transcriptional regulator Rok binds A+T-rich DNA and is involved in repression of a mobile genetic element in Bacillus subtilis.",
"The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions.",
"Rok (YkuW) regulates genetic competence in Bacillus subtilis by directly ... | [
2010,
2005,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Bastillevirinae"
] | [
218,
4
] | 2 | [] | [] | 0 | true | Domain | Rok, N-terminal oligomerisation domain | Rok, N-terminal oligomerisation domain | Rok_N_oligomerisation | 7 |
IPR058973 | 58,973 | BanI/HgiCI, C-terminal domain | RE_BanI/HgiCI_C | Domain | 114 | false | false | This entry represents the C-terminal domain in BanI and HgiCI and similar bacterial proteins. P subtype restriction enzyme BanI and Type II restriction enzyme HgiCl recognise the double-stranded sequence 5'-GGYRCC-3' and cleave after G-1 [ ]. They contain an N-terminal represented by and a C-terminal represented by . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26568"
] | [
"RE_BanI_C"
] | [
114
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00099965"
] | [
"12654995"
] | [
"A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
109,
2,
3
] | 3 | [] | [] | 0 | true | Domain | BanI/HgiCI, C-terminal domain | BanI/HgiCI, C-terminal domain | RE_BanI/HgiCI_C | 8 |
IPR058974 | 58,974 | BanI/HgiCI, N-terminal domain | RE_BanI/HgiCI_N | Domain | 83 | false | false | This entry represents the N-terminal domain in P subtype restriction enzyme BanI, Type II restriction enzyme HgiCI and similar bacterial proteins. P subtype restriction enzyme BanI and Type II restriction enzyme HgiCl recognise the double-stranded sequence 5'-GGYRCC-3' and cleave after G-1 [ ]. They contain an N-termin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF24447"
] | [
"RE_BanI"
] | [
83
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00099965"
] | [
"12654995"
] | [
"A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
81,
2
] | 2 | [] | [] | 0 | true | Domain | BanI/HgiCI, N-terminal domain | BanI/HgiCI, N-terminal domain | RE_BanI/HgiCI_N | 8 |
IPR058975 | 58,975 | Inner membrane protein CbrB | CbrB | Family | 394 | false | false | This entry represents Inner membrane protein CbrB from Escherichia coli and related enterobacterial proteins. CbrB (also known as YieI) is predicted to be an integral inner membrane protein [ ]. The specific function of CbrB remains to be determined, but it is conserved among various E. coli strains including pathogeni... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF007334",
"PF26516"
] | [
"PRK09823.1",
"CBRB"
] | [
338,
394
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042652"
] | [
"15919996"
] | [
"Global topology analysis of the Escherichia coli inner membrane proteome."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
394
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Inner membrane protein CbrB | Inner membrane protein CbrB | CbrB | 8 |
IPR058976 | 58,976 | SusF, first starch specific CBM | CBM_1st_SusF | Domain | 208 | false | false | This domain is found in the Outer membrane protein SusF from Bacteroides thetaiotaomicron and related proteins from bacteroidales. This entry represents the first of the tandem CBMs. SusF is a multidomain protein and contains three starch specific carbohydrate binding modules (CBMs). Each of this CBMs differ in the way... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26120"
] | [
"CBM_1st_SusF"
] | [
208
] | 1 | [] | [] | [] | 0 | [
"4fe9"
] | 1 | [
"PUB00016547",
"PUB00055601",
"PUB00059168",
"PUB00062486",
"PUB00075681"
] | [
"11717282",
"20532204",
"9006015",
"22910908",
"10986238"
] | [
"Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron.",
"Expansion of the protein repertoire in newly explored environments: human gut microbiome specific protein families.",
"Characterization of four outer membrane proteins ... | [
2001,
2010,
1997,
2012,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteroidota",
"metagenomes"
] | [
201,
7
] | 2 | [] | [] | 0 | true | Domain | SusF, first starch specific CBM | SusF, first starch specific CBM | CBM_1st_SusF | 2 |
IPR058977 | 58,977 | RNA-editing substrate-binding complex 8 protein, HEAT repeats | RESC8_HEAT | Domain | 249 | false | false | This domain is found in the RNA-editing substrate-binding complex 8 protein (RESC8, ) from Trypanosoma brucei, a component of RESC which together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs [ ]. RESC stabilises gRNAs... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26172"
] | [
"RESC8"
] | [
249
] | 1 | [] | [] | [] | 0 | [
"8fnc",
"8fnf",
"8fni",
"8fnk"
] | 4 | [
"PUB00160174"
] | [
"37410820"
] | [
"Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Orientia tsutsugamushi"
] | [
248,
1
] | 2 | [] | [] | 0 | true | Domain | RNA-editing substrate-binding complex 8 protein, HEAT repeats | RNA-editing substrate-binding complex 8 protein, HEAT repeats | RESC8_HEAT | 6 |
IPR058978 | 58,978 | Gasdermin, bacterial-type | GSDM_bact-type | Family | 124 | false | false | This entry represents a group of gasdermin proteins mainly found in bacteria. Gasodermin is involved in defence against bacteriophages [ ]. Members of this family are precursors of pore-forming proteins that, upon activation by specific proteases, release an active N-terminal moiety. This active form inserts into membr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26164"
] | [
"Bact_GSDM"
] | [
124
] | 1 | [] | [] | [] | 0 | [
"7n50",
"7n51",
"7n52",
"8sl0"
] | 4 | [
"PUB00100796",
"PUB00161134"
] | [
"35025633",
"38509367"
] | [
"Bacterial gasdermins reveal an ancient mechanism of cell death.",
"Structure and assembly of a bacterial gasdermin pore."
] | [
2022,
2024
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobium antiquum"
] | [
107,
16,
1
] | 3 | [] | [] | 0 | true | Family | Gasdermin, bacterial-type | Gasdermin, bacterial-type | GSDM_bact-type | 7 |
IPR058980 | 58,980 | Glycosyltransferase, N-terminal domain | Glyco_transf_N | Domain | 15,011 | false | false | This domain is found at the N-terminal end of glycosyltransferase sequences from plants. This domain is often found associated with and shows a five stranded β-sheet with α-helices on both sides [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26168"
] | [
"Glyco_transf_N"
] | [
15011
] | 1 | [
"EC"
] | [
"2.4.1"
] | [
"EC:2.4.1"
] | 1 | [
"6l8w",
"6l8z",
"6l90",
"7c2x",
"7w09",
"7w0k",
"7w0z",
"7w10",
"7w11",
"7w1b",
"7w1h",
"8hjf",
"8hjg",
"8hjh",
"8hjk",
"8hjl",
"8hjn",
"8hjo",
"8hjp",
"8hjq",
"8in7",
"8ina",
"8ind",
"8inh",
"8inj",
"8ino",
"8inv",
"8j66",
"8jzq",
"8k08",
"8k09",
"8wrj"... | 38 | [
"PUB00042397",
"PUB00095588",
"PUB00097197",
"PUB00161247",
"PUB00161248",
"PUB00161249",
"PUB00161250",
"PUB00161251",
"PUB00161252",
"PUB00161253",
"PUB00161254",
"PUB00161255"
] | [
"17553523",
"32688778",
"27227328",
"15342621",
"18702669",
"12644686",
"15352060",
"12900416",
"30893500",
"35819080",
"39080270",
"37123177"
] | [
"Crystal structure of Medicago truncatula UGT85H2--insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase.",
"A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels.",
"Two UGT84 Family Glycosyltransferases Catalyze a Criti... | [
2007,
2008,
2016,
2004,
2008,
2003,
2004,
2003,
2019,
2022,
2024,
2023
] | 12 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
15011
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
90,
100,
96
] | 3 | true | Domain | Glycosyltransferase, N-terminal domain | Glycosyltransferase, N-terminal domain | Glyco_transf_N | 6 |
IPR058981 | 58,981 | MGRN1/RNF157-like, N-terminal domain | MGRN1/RNF157-like_N | Domain | 6,382 | false | false | This entry describes the N-terminal domain in E3 ubiquitin ligases, including MGNR1, LUL1-4, RNF157 and LOG2. E3 ubiquitin ligase proteins are involved in the ubiquitination process, where ubiquitin is transferred to substrate proteins, marking them for degradation or altering their cellular functions. MGRN1 is involve... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26192"
] | [
"RNF157-like_N"
] | [
6382
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.27",
"PWY-7511",
"R-HSA-983168",
"R-MMU-983168",
"R-RNO-983168"
] | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-983168",
"REACTOME:R-RNO-983168"
] | 5 | [] | 0 | [
"PUB00064253",
"PUB00088714",
"PUB00090853",
"PUB00098239",
"PUB00098240",
"PUB00098241",
"PUB00098244",
"PUB00161443",
"PUB00161444"
] | [
"15644464",
"29290584",
"22291198",
"19737927",
"17229889",
"19703557",
"25342469",
"12560552",
"28655764"
] | [
"Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis.",
"CRISPR Screens Uncover Genes that Regulate Target Cell Sensitivity to the Morphogen Sonic Hedgehog.",
"The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE DUMPER1-induced amino acid secretion in Arabidopsis.",
"Mahogun... | [
2005,
2018,
2012,
2009,
2007,
2009,
2015,
2003,
2017
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6382
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
23,
1,
14,
6,
9,
4,
11,
15,
16
] | 9 | true | Domain | MGRN1/RNF157-like, N-terminal domain | MGRN1/RNF157-like, N-terminal domain | MGRN1/RNF157-like_N | 8 |
IPR058982 | 58,982 | AprE-like, beta-barrel domain | Beta-barrel_AprE | Domain | 23,522 | false | false | This domain is found in the Alkaline protease secretion protein AprE from Pseudomonas aeruginosa and related bacterial proteins, including Type I secretion system membrane fusion protein PrsE from Rhizobium meliloti. AprE is involved in the secretion of alkaline protease while PrsE mediates secretion of glycanase ExsH ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26002"
] | [
"Beta-barrel_AprE"
] | [
23522
] | 1 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"5nen",
"7sgr",
"8dck"
] | 3 | [
"PUB00001820",
"PUB00161136"
] | [
"1427098",
"11902715"
] | [
"Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways.",
"The Rhizobium meliloti exoK gene and prsD/prsE/exsH genes are components of independent degradative pathways which contribute to production of low-molec... | [
1992,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Peduovirinae sp. ctGB41",
"unclassified sequences"
] | [
3,
23335,
44,
1,
139
] | 5 | [
"Mus musculus"
] | [
1
] | 1 | true | Domain | AprE-like, beta-barrel domain | AprE-like, beta-barrel domain | Beta-barrel_AprE | 2 |
IPR058983 | 58,983 | Terminal beta-(1->2)-arabinofuranosyltransferase, C-terminal domain | AftB_C | Domain | 1,114 | false | false | This entry represents the C-terminal domain of Terminal beta-(1->2)-arabinofuranosyltransferase from Mycobacterium tuberculosis (AftB) and similar proteins mainly found in actinomycetes. AftB is involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26371"
] | [
"AftB_C"
] | [
1114
] | 1 | [] | [] | [] | 0 | [
"9dlf",
"9dlh"
] | 2 | [
"PUB00151340"
] | [
"17387176"
] | [
"Identification of a novel arabinofuranosyltransferase AftB involved in a terminal step of cell wall arabinan biosynthesis in Corynebacterianeae, such as Corynebacterium glutamicum and Mycobacterium tuberculosis."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"freshwater metagenome"
] | [
1110,
4
] | 2 | [] | [] | 0 | true | Domain | Terminal beta-(1->2)-arabinofuranosyltransferase, C-terminal domain | Terminal beta-(1->2)-arabinofuranosyltransferase, C-terminal domain | AftB_C | 2 |
IPR058984 | 58,984 | PD-(D/E)XK nuclease-like, halobacteria | PDDEXK-like_halobact | Family | 96 | false | false | This entry represents a family of uncharacterised proteins in halobacteria. The proteins in this family typically range from 190 to 220 amino acids in length. These proteins are structurally related to the PD-(D/E)XK nuclease superfamily. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26437"
] | [
"PDDEXK_18"
] | [
96
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
96
] | 1 | [] | [] | 0 | true | Family | PD-(D/E)XK nuclease-like, halobacteria | PD-(D/E)XK nuclease-like, halobacteria | PDDEXK-like_halobact | 5 |
IPR058985 | 58,985 | Putative Fic antitoxin, halobacterial | Antitox_halobact | Family | 130 | false | false | This entry represents a family of uncharacterised proteins found in halobacteria. Proteins in this family adopt a helical hairpin structure according to structure predictions. This family is found in operonic contexts adjacent to Fic/doc domains suggesting that this family represents a set of novel antitoxins that bind... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26044"
] | [
"Antitox_halo"
] | [
130
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
130
] | 1 | [] | [] | 0 | true | Family | Putative Fic antitoxin, halobacterial | Putative Fic antitoxin, halobacterial | Antitox_halobact | 8 |
IPR058986 | 58,986 | Swc3, C-terminal domain | Swc3_C | Domain | 192 | false | false | This is the C-terminal domain of Swc3, a component of the SWR1 complex, which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodelling [ , ]. Proteins in this entry are mainly found in Pichiomycetes and Saccharomycetes. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26242"
] | [
"Swc3_C"
] | [
192
] | 1 | [] | [] | [] | 0 | [
"9b1e"
] | 1 | [
"PUB00018537",
"PUB00046116",
"PUB00046117"
] | [
"14645854",
"14690608",
"15045029"
] | [
"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex.",
"A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1.",
"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
] | [
2004,
2003,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
192
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Swc3, C-terminal domain | Swc3, C-terminal domain | Swc3_C | 9 |
IPR058987 | 58,987 | MPN635, N-terminal domain | MPN635_N | Domain | 114 | false | false | This entry represents a domain found at the N-terminal end of MPN_635 from Mycoplasma pneumoniae. It is also found at the C-terminal end of MPN633 and in similar prokaryotic sequences. The specific function of this domain remains to be determined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25856"
] | [
"MPN635_N"
] | [
114
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
85,
2,
2,
16,
9
] | 5 | [] | [] | 0 | true | Domain | MPN635, N-terminal domain | MPN635, N-terminal domain | MPN635_N | 4 |
IPR058988 | 58,988 | Cysteine protease effector IpaJ | IpaJ | Family | 130 | false | false | This entry represents the invasion plasmid antigen J (IpaJ) family of cysteine proteases found in proteobacterial pathogens such as Shigella flexneri. IpaJ functions as a virulence factor that is secreted via the type III secretion system and delivered into host cells. It has a unique proteolytic activity that cleaves ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25855"
] | [
"IpaJ_protease"
] | [
130
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161308"
] | [
"23535599"
] | [
"Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
130
] | 1 | [] | [] | 0 | true | Family | Cysteine protease effector IpaJ | Cysteine protease effector IpaJ | IpaJ | 4 |
IPR058990 | 58,990 | Primase-associated, winged helix domain | WH_Primase-assoc | Domain | 129 | false | false | This entry represents the third domain found in a family of uncharacterised proteins from halobacteria that are found adjacent to a DNA primase-like protein. This domain adopts a winged helix fold. Proteins in this group are typically around 500 amino acids in length. Many of these proteins are encoded on plasmids, sug... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26462"
] | [
"WH_Halo_primase"
] | [
129
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Stenosarchaea group"
] | [
129
] | 1 | [] | [] | 0 | true | Domain | Primase-associated, winged helix domain | Primase-associated, winged helix domain | WH_Primase-assoc | 1 |
IPR058991 | 58,991 | Lin-66-like, winged helix domain | Lin-66-like_WHD | Domain | 167 | false | false | This entry represents a winged helix domain (WHD) found in Lin-66 and related proteins from nematodes. This domain is usually the N-terminal domain of a pair of adjacent winged helix domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26288"
] | [
"WHD_lin-66"
] | [
167
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Nematoda"
] | [
167
] | 1 | [
"Caenorhabditis elegans"
] | [
5
] | 1 | true | Domain | Lin-66-like, winged helix domain | Lin-66-like, winged helix domain | Lin-66-like_WHD | 7 |
IPR058992 | 58,992 | DUF7961, N-terminal domain | DUF7961_N | Domain | 99 | false | false | This domain, found in a family of uncharacterised proteins from halobacteria, has a restriction endonuclease-like structure, suggesting these protein may function as endonucleases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25902"
] | [
"DUF7961_N"
] | [
99
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteria"
] | [
99
] | 1 | [] | [] | 0 | true | Domain | DUF7961, N-terminal domain | DUF7961, N-terminal domain | DUF7961_N | 9 |
IPR058994 | 58,994 | Ig domain-containing, halobacteria | Ig-containing_halobact | Family | 88 | false | false | This entry represents a family of uncharacterised proteins in halophilic archaea. The protein contains an N-terminal transmembrane helix followed by an immunoglobulin-like domain. This Ig domain unusually has a small three β stranded subdomain inserted between the second and third strands of the Ig domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26515"
] | [
"Ig_halo_2"
] | [
88
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
88
] | 1 | [] | [] | 0 | true | Family | Ig domain-containing, halobacteria | Ig domain-containing, halobacteria | Ig-containing_halobact | 1 |
IPR058995 | 58,995 | YolC/YozM-like | YolC/YozM-like | Family | 115 | false | false | This entry represents a family of uncharacterised proteins from tailed bacteriophages and prophages from bacillales. Structure prediction suggests that these proteins are likely to dimerise. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26328"
] | [
"YolC_YozM"
] | [
115
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Bacillus phage SPbeta"
] | [
114,
1
] | 2 | [] | [] | 0 | true | Family | YolC/YozM-like | YolC/YozM-like | YolC/YozM-like | 6 |
IPR058996 | 58,996 | RelE toxin-related domain | Toxin-rel_dom | Domain | 89 | false | false | This entry represents a domain fond at the N-terminal end in a family of uncharacterised proteins in halobacteria. The domain is approximately 100-130 amino acids in length. This domain shows structural similarity to the ribonuclease Colicin-E5 and RelE-like toxins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26442"
] | [
"Halo_toxin"
] | [
89
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales",
"Halorubrum virus BJ1"
] | [
88,
1
] | 2 | [] | [] | 0 | true | Domain | RelE toxin-related domain | RelE toxin-related domain | Toxin-rel_dom | 8 |
IPR058997 | 58,997 | YycE-like, C-terminal domain | YycE-like_C | Domain | 2,550 | false | false | This entry represents a VOC-like domain found at the C-terminal of a group of uncharacterised sequences from bacteria and fungi, such as YycE from Bacillus subtilis ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22659"
] | [
"YycE-like_C"
] | [
2550
] | 1 | [] | [] | [] | 0 | [
"1twu"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
2263,
287
] | 2 | [] | [] | 0 | true | Domain | YycE-like, C-terminal domain | YycE-like, C-terminal domain | YycE-like_C | 9 |
IPR058999 | 58,999 | EIF3CL-like, C-terminal domain | EIF3CL_C | Domain | 3,749 | false | false | This domain is found at the C-terminal end of human Eukaryotic translation initiation factor 3 subunit C-like protein (EIF3CL) and similar proteins. EIF3CL is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex. This domain is predicted to adopt an α-helical configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26569"
] | [
"EIF3CL_C"
] | [
3749
] | 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-156827",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-CEL-156827",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-DDI-156827",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DME-156827",
"R-DME-72649",
"R-DME-72689",
"R-DME-72695",
"R-DME... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL-72702",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-72689",
"... | 44 | [
"5a5t",
"6fec",
"6w2s",
"6w2t",
"6yam",
"6ybd",
"6ybw",
"6zmw",
"6zon",
"6zp4",
"6zvj",
"7a09",
"7qp6",
"7qp7",
"8oz0",
"8pj1",
"8pj2",
"8pj3",
"8pj4",
"8pj5",
"8pj6",
"8ppl",
"8rg0",
"8xxn",
"9bln",
"9cpa"
] | 26 | [
"PUB00056124",
"PUB00091244",
"PUB00146055",
"PUB00155621"
] | [
"17581632",
"26344199",
"25849773",
"27462815"
] | [
"Reconstitution reveals the functional core of mammalian eIF3.",
"Structure of mammalian eIF3 in the context of the 43S preinitiation complex.",
"eIF3 targets cell-proliferation messenger RNAs for translational activation or repression.",
"eIF3d is an mRNA cap-binding protein that is required for specialized ... | [
2007,
2015,
2015,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
3748,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
1,
3,
2,
9,
2,
1,
5,
3,
2
] | 10 | true | Domain | EIF3CL-like, C-terminal domain | EIF3CL-like, C-terminal domain | EIF3CL_C | 3 |
IPR059000 | 59,000 | P-type ATPase, A domain | ATPase_P-type_domA | Domain | 264,635 | false | false | This entry represents the actuator (A) domain, and some transmembrane helices found in P-type ATPases [ ]. It contains the TGES-loop which is essential for the metal ion binding which results in tight association between the A and P (phosphorylation) domains [ ]. It does not contain the phosphorylation site. It is thou... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00122"
] | [
"E1-E2_ATPase"
] | [
264635
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"7.2.2",
"R-BTA-418359",
"R-BTA-5578775",
"R-BTA-936837",
"R-CEL-418359",
"R-CEL-5578775",
"R-CEL-936837",
"R-CFA-418359",
"R-CFA-5578775",
"R-CFA-936837",
"R-DDI-418359",
"R-DDI-5578775",
"R-DDI-936837",
"R-DME-418359",
"R-DME-5578775",
"R-DME-936837",
"R-DRE-936837",
"R-GGA-41835... | [
"EC:7.2.2",
"REACTOME:R-BTA-418359",
"REACTOME:R-BTA-5578775",
"REACTOME:R-BTA-936837",
"REACTOME:R-CEL-418359",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-936837",
"REACTOME:R-CFA-418359",
"REACTOME:R-CFA-5578775",
"REACTOME:R-CFA-936837",
"REACTOME:R-DDI-418359",
"REACTOME:R-DDI-5578775",
"... | 51 | [
"1iwo",
"1kju",
"1mhs",
"1su4",
"1t5s",
"1t5t",
"1vfp",
"1wpg",
"1xp5",
"2agv",
"2by4",
"2c88",
"2c8k",
"2c8l",
"2c9m",
"2dqs",
"2ear",
"2eat",
"2eau",
"2hc8",
"2kij",
"2o9j",
"2oa0",
"2voy",
"2xzb",
"2yfy",
"2yn9",
"2zbd",
"2zbe",
"2zbf",
"2zbg",
"2zxe"... | 392 | [
"PUB00002805",
"PUB00009616",
"PUB00038122",
"PUB00039927",
"PUB00050553",
"PUB00052687",
"PUB00055017",
"PUB00055886",
"PUB00160065",
"PUB00160066"
] | [
"8226755",
"9419228",
"15448704",
"16710301",
"18075584",
"19645496",
"18930923",
"19917612",
"37264943",
"37838176"
] | [
"Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium.",
"Evolution of substrate specificities in the P-type ATPase superfamily.",
"Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues.",
"Modulatory and catalytic modes o... | [
1993,
1998,
2004,
2006,
2007,
2009,
2008,
2010,
2023,
2023
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4118,
132059,
126935,
21,
1502
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
185,
36,
175,
62,
4,
126,
111,
15,
121,
174,
13,
9,
333
] | 13 | true | Domain | P-type ATPase, A domain | P-type ATPase, A domain | ATPase_P-type_domA | 9 |
IPR059001 | 59,001 | STX17-like, N-terminal domain | STX17_N | Domain | 1,501 | false | false | This domain is found at the N-terminal end of human Syntaxin-17 (STX17), a SNARE protein (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) of the autophagosome that is involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane [ , , , ]. This domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26585"
] | [
"STX17_N"
] | [
1501
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-204005",
"R-HSA-204005",
"R-MMU-204005",
"R-RNO-204005"
] | [
"REACTOME:R-BTA-204005",
"REACTOME:R-HSA-204005",
"REACTOME:R-MMU-204005",
"REACTOME:R-RNO-204005"
] | 4 | [] | 0 | [
"PUB00065300",
"PUB00068997",
"PUB00091390",
"PUB00095356",
"PUB00101002"
] | [
"23217709",
"21545355",
"28504273",
"25686604",
"28306502"
] | [
"The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes.",
"Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi.",
"Legionella effector Lpg1137 shuts down ER-mitochondria communication through cleavag... | [
2012,
2011,
2017,
2015,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1501
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
9,
3,
3
] | 6 | true | Domain | STX17-like, N-terminal domain | STX17-like, N-terminal domain | STX17_N | 6 |
IPR059003 | 59,003 | At1g61900-like, C-terminal | At1g61900_C | Domain | 1,909 | false | false | This domain is found towards the C-terminal end of the uncharacterised GPI-anchored protein At1g61900 from Arabidopsis thaliana and similar plant sequences. This domain is predicted to adopt an all-α configuration. There are several C, Q and Y conserved residues. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26584"
] | [
"At1g61900"
] | [
1909
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
1909
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
12,
12
] | 3 | true | Domain | At1g61900-like, C-terminal | At1g61900-like, C-terminal | At1g61900_C | 6 |
IPR059004 | 59,004 | Unconventional myosin-XV-like domain | MYO15 | Domain | 2,135 | false | false | This domain is found in human Unconventional myosin-XV (MYO15) and similar animal proteins. Mutations in MYO15 are associated with human deafness [ ]. This domain is often found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26570"
] | [
"MYO15"
] | [
2135
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9662360",
"R-HSA-9662361"
] | [
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361"
] | 2 | [] | 0 | [
"PUB00086480",
"PUB00121380",
"PUB00127959"
] | [
"9603736",
"15654330",
"14610277"
] | [
"Association of unconventional myosin MYO15 mutations with human nonsyndromic deafness DFNB3.",
"Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia.",
"Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase f... | [
1998,
2005,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
2135
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
10,
2,
3,
6,
4
] | 6 | true | Domain | Unconventional myosin-XV-like domain | Unconventional myosin-XV-like domain | MYO15 | 7 |
IPR059005 | 59,005 | LETM1-like, C-terminal domain | LETM1_C | Domain | 2,186 | false | false | This domain is found at the C-terminal end of human Mitochondrial proton/calcium exchanger protein (LETM1) and similar animal proteins. LETM1 plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport [ , , , , , , ]. This domain seems to be exclusive... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26561"
] | [
"LETM1_C"
] | [
2186
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8949215",
"R-HSA-9013408",
"R-HSA-9865881",
"R-MMU-9013408",
"R-RNO-9013408",
"R-XTR-9013408"
] | [
"REACTOME:R-HSA-8949215",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9865881",
"REACTOME:R-MMU-9013408",
"REACTOME:R-RNO-9013408",
"REACTOME:R-XTR-9013408"
] | 6 | [] | 0 | [
"PUB00063313",
"PUB00095494",
"PUB00161314",
"PUB00161315",
"PUB00161316",
"PUB00161317",
"PUB00161318",
"PUB00161319",
"PUB00161320",
"PUB00161321"
] | [
"18628306",
"19797662",
"24898248",
"24344246",
"29123128",
"32139798",
"36321428",
"36055214",
"23716663",
"27669901"
] | [
"Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L.",
"Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter.",
"NCLX protein, but not LETM1, mediates mitochondrial Ca2+ extrusion, thereby limiti... | [
2008,
2009,
2014,
2014,
2017,
2020,
2022,
2022,
2013,
2016
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2186
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
9,
1,
1,
1,
4
] | 6 | true | Domain | LETM1-like, C-terminal domain | LETM1-like, C-terminal domain | LETM1_C | 9 |
IPR059007 | 59,007 | At1g04390, ARM repeat | ARM_At1g04390 | Domain | 641 | false | false | This entry represents a repeat from a set of uncharacterised plant proteins, including At1g04390 from Arabidopsis thaliana. The proteins containing this domain are predominantly found in the eudicotyledons and monocots, specifically within the Magnoliopsida and Liliopsida classes. The At1g04390 protein may act as a sub... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26522"
] | [
"ARM_6"
] | [
641
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
641
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
4,
9
] | 3 | true | Domain | At1g04390, ARM repeat | At1g04390, ARM repeat | ARM_At1g04390 | 5 |
IPR059008 | 59,008 | ABTB2/3, histone-like domain | ABTB2/3_histone | Domain | 3,109 | false | false | This entry represents a histone-like domain found towards the N-terminal of Ankyrin repeat and BTB (POZ) domain containing proteins (ABTB2/3). The Ankyrin repeat and BTB/POZ domain-containing protein family is characterised by the presence of ankyrin repeats and a BTB/POZ domain. These proteins may play a role in cellu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26281"
] | [
"Histone_ABTB"
] | [
3109
] | 1 | [] | [] | [] | 0 | [
"2jss",
"4m6b",
"6ae8",
"6k00",
"6k03",
"6k09",
"6k0c",
"7dlx",
"7ybf"
] | 9 | [
"PUB00139584",
"PUB00139585",
"PUB00139586",
"PUB00139587",
"PUB00139588",
"PUB00139589",
"PUB00139590"
] | [
"26916519",
"25568138",
"24076025",
"27482213",
"19930467",
"18459963",
"18429817"
] | [
"BPOZ-2 Gene Delivery Ameliorates Alpha-Synucleinopathy in A53T Transgenic Mouse Model of Parkinson's Disease.",
"Deficiency of BPOZ2 Decreases Liver Fibrosis After Chronic Carbon Tetrachloride Administration in Mice.",
"Ankyrin repeat and BTB/POZ domain containing protein-2 inhibits the aggregation of alpha-sy... | [
2016,
2015,
2013,
2016,
2009,
2008,
2008
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3109
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
2,
2,
6,
8
] | 5 | true | Domain | ABTB2/3, histone-like domain | ABTB2/3, histone-like domain | ABTB2/3_histone | 1 |
IPR059009 | 59,009 | C2H2-domain containing protein, first zinc finger domain | Znf_C2H2_17_1st | Domain | 2,139 | false | false | This entry represents the first C2H2 zinc finger domain in C2H2 domain-containing proteins found in fungi. C2H2 zinc fingers contain a short β-hairpin and an α-helix (β/β/α structure), where a single zinc atom is held in place by Cys(2)His(2) (C2H2) residues in a tetrahedral array. C2H2 zinc fingers are the most common... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26177"
] | [
"zf_C2H2_17_1st"
] | [
2139
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161554",
"PUB00161555",
"PUB00161556"
] | [
"25258363",
"27596598",
"29294058"
] | [
"Wilms tumor protein recognizes 5-carboxylcytosine within a specific DNA sequence.",
"Denys-Drash syndrome associated WT1 glutamine 369 mutants have altered sequence-preferences and altered responses to epigenetic modifications.",
"Role for first zinc finger of WT1 in DNA sequence specificity: Denys-Drash syndr... | [
2014,
2016,
2018
] | 3 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2139
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
3
] | 1 | true | Domain | C2H2-domain containing protein, first zinc finger domain | C2H2-domain containing protein, first zinc finger domain | Znf_C2H2_17_1st | 9 |
IPR059010 | 59,010 | Transmembrane protein 179/179B | TMEM179-179B | Family | 2,582 | false | false | This entry represents the Transmembrane proteins 179/179B and related proteins mostly found in animals. Their precise functions are not fully understood. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26158"
] | [
"Claudin_TMEM179-179B"
] | [
2582
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-6798695",
"R-HSA-6798695",
"R-MMU-6798695"
] | [
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695"
] | 3 | [] | 0 | [] | [] | [] | [] | 0 | [] | [
"IPR029673",
"IPR029776"
] | 0 | 2 | 0 | [
"Opisthokonta"
] | [
2582
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
1,
7,
3,
7
] | 5 | true | Family | Transmembrane protein 179/179B | Transmembrane protein 179/179B | TMEM179-179B | 9 |
IPR059011 | 59,011 | PTRR, N-terminal domain | PTPRR_N | Domain | 889 | false | false | This entry represents the N-terminal domain in Receptor-type tyrosine-protein phosphatase R (PTRRR) proteins. The N-terminal domain has hydrophobic regions that may help anchor receptor-type isoforms to membranes [ ]. It contains a β-sheet structure surrounded by α-helices. This domain is found next to the PTPase domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26155"
] | [
"PTPRR_N"
] | [
889
] | 1 | [
"EC"
] | [
"3.1.3.48"
] | [
"EC:3.1.3.48"
] | 1 | [] | 0 | [
"PUB00047013",
"PUB00142758",
"PUB00161424"
] | [
"16441242",
"19137382",
"23860656"
] | [
"Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.",
"PTPRR protein tyrosine phosphatase isoforms and locomotion of vesicles and mice.",
"Protein tyrosine phosphatases: structure, function, and implication in human disease.... | [
2006,
2009,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
889
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
5
] | 3 | true | Domain | PTRR, N-terminal domain | PTRR, N-terminal domain | PTPRR_N | 4 |
IPR059012 | 59,012 | Domain of unknown function (DUF8168), C-terminal domain | DUF8168_C | Domain | 50 | false | false | This entry represents the C-terminal domain from a family of uncharacterised proteins found predominantly in Proteobacteria that contain two domains the N-terminal represented by . The proteins are distributed among various orders including Burkholderiales, Rhodobacterales, and Hyphomicrobiales. The proteins in this fa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26504"
] | [
"DUF8168_C"
] | [
50
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Stenosarchaea group",
"mine drainage metagenome"
] | [
45,
4,
1
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF8168), C-terminal domain | Domain of unknown function (DUF8168), C-terminal domain | DUF8168_C | 2 |
IPR059013 | 59,013 | Domain of unknown function (DUF8168), N-terminal domain | DUF8168_N | Domain | 38 | false | false | This entry represents the N-terminal domain from a family of uncharacterised proteins found predominantly in Proteobacteria that contain two domains, the C-terminal is represented by . The proteins are distributed among various orders including Burkholderiales, Rhodobacterales, and Hyphomicrobiales. The proteins in thi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26505"
] | [
"DUF8168_N"
] | [
38
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Stenosarchaea group"
] | [
35,
3
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF8168), N-terminal domain | Domain of unknown function (DUF8168), N-terminal domain | DUF8168_N | 6 |
IPR059014 | 59,014 | Domain of unknown function (DUF8161), C-terminal domain | DUF8161_C | Domain | 54 | false | false | This entry represents the C-terminal domain from a family of uncharacterised proteins in archaea. The proteins are predominantly found in the class Halobacteria, which includes organisms from the orders Halobacteriales and families such as Haloferacaceae, Haloarculaceae, and Natrialbaceae. The proteins in this family a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26495"
] | [
"DUF8161_C"
] | [
54
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
54
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF8161), C-terminal domain | Domain of unknown function (DUF8161), C-terminal domain | DUF8161_C | 7 |
IPR059015 | 59,015 | Domain of unknown function (DUF8148), central domain | DUF8148_M | Domain | 44 | false | false | This entry represents a the central domain from a family of uncharacterised proteins found predominantly in archaea, specifically within the Halobacteria class. The domain is approximately 60-70 amino acids in length. The proteins in this family are typically found in species such as Halovenus, Halobellus, and Natrarch... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26474"
] | [
"DUF8148_M"
] | [
44
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphapleolipovirus",
"Halobacteriales"
] | [
2,
42
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF8148), central domain | Domain of unknown function (DUF8148), central domain | DUF8148_M | 9 |
IPR059016 | 59,016 | Domain of unknown function (DUF8148), C-terminal domain | DUF8148_C | Domain | 54 | false | false | This entry represents the C-terminal domain from a family of uncharacterised proteins found predominantly in archaea, specifically within the Halobacteria class. Additionally, some members are associated with viruses like the Pleolipoviridae family. The domain is approximately 60-70 amino acids in length. The proteins ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26475"
] | [
"DUF8148_C"
] | [
54
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphapleolipovirus",
"Methanobacteriota"
] | [
3,
51
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF8148), C-terminal domain | Domain of unknown function (DUF8148), C-terminal domain | DUF8148_C | 1 |
IPR059017 | 59,017 | PMEL/NMB, N-terminal domain | PMEL_NMB_N | Domain | 1,850 | false | false | This entry represents the N-terminal domain in PKD PMEL/NMB proteins, including Protein QNR-71. This domain contains an RGD motif, which mediates integrin binding. It also contains potential N-glycosylation sites and an Ig-like fold [ ]. This entry does not include the N-terminal in Transmembrane protein 130. PKD PMEL/... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26141"
] | [
"PMEL_NMB_N"
] | [
1850
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8857538",
"R-HSA-9824585",
"R-MMU-8857538",
"R-RNO-8857538"
] | [
"REACTOME:R-HSA-8857538",
"REACTOME:R-HSA-9824585",
"REACTOME:R-MMU-8857538",
"REACTOME:R-RNO-8857538"
] | 4 | [
"9jst",
"9jsu",
"9jsv",
"9jsw",
"9jsx"
] | 5 | [
"PUB00101280",
"PUB00161415",
"PUB00161416",
"PUB00161417",
"PUB00161418",
"PUB00161419",
"PUB00161420",
"PUB00161421",
"PUB00161422",
"PUB00161423"
] | [
"26694611",
"8022805",
"7706734",
"32445534",
"11694580",
"21962903",
"26387950",
"28272432",
"30988362",
"21949658"
] | [
"The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.",
"Identification of a human melanoma antigen recognized by tumor-infiltrating lymphocytes associated with in vivo tumor rejectio... | [
2016,
1994,
1995,
2020,
2001,
2011,
2015,
2017,
2019,
2011
] | 10 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
1850
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
20,
10,
9
] | 4 | true | Domain | PMEL/NMB, N-terminal domain | PMEL/NMB, N-terminal domain | PMEL_NMB_N | 4 |
IPR059018 | 59,018 | URB1, central HEAT repeat domain | HEAT_URB1 | Domain | 2,523 | false | false | This domain is found in URB1 and related proteins. This domain contains a HEAT repeat. Nucleolar pre-ribosomal-associated protein 1 (Npa1 or URB1) is required for ribosome biogenesis and operates in the same functional environment as Rsa3p and Dbp6p during early maturation of 60S ribosomal subunits [ ]. The protein par... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26140"
] | [
"HEAT_URB1"
] | [
2523
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044526",
"PUB00045128",
"PUB00053537"
] | [
"15226434",
"15242642",
"15208443"
] | [
"Npa1p, a component of very early pre-60S ribosomal particles, associates with a subset of small nucleolar RNPs required for peptidyl transferase center modification.",
"Exploration of essential gene functions via titratable promoter alleles.",
"Npa1p is an essential trans-acting factor required for an early st... | [
2004,
2004,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Xanthomonas campestris pv. badrii"
] | [
2522,
1
] | 2 | [
"Danio rerio",
"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)"
] | [
1,
1,
2,
1,
2,
1,
1
] | 7 | true | Domain | URB1, central HEAT repeat domain | URB1, central HEAT repeat domain | HEAT_URB1 | 7 |
IPR059019 | 59,019 | DNA-binding transcriptional repressor CapW, winged helix-turn-helix domain | WHD_CapW | Domain | 3,070 | false | false | This entry represents the N-terminal winged helix-turn-helix (wHTH) DNA-binding domain of BrxR family of transcriptional regulators including CapW and BrxR. This domain (approximately residues 1-94 in the prototypical BrxR from Escherichia fergusonii) is responsible for binding to inverted DNA repeats, enabling BrxR to... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26109"
] | [
"WHD_BrxR"
] | [
3070
] | 1 | [] | [] | [] | 0 | [
"7qfz",
"7t8k",
"7t8l",
"7tb5",
"7tb6",
"9c5g"
] | 6 | [
"PUB00153145",
"PUB00161156",
"PUB00161157"
] | [
"35536256",
"35511079",
"35544231"
] | [
"Control of bacterial immune signaling by a WYL domain transcription factor.",
"Identification and characterization of the WYL BrxR protein and its gene as separable regulatory elements of a BREX phage restriction system.",
"A widespread family of WYL-domain transcriptional regulators co-localizes with diverse ... | [
2022,
2022,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"IncJ plasmid R391",
"metagenomes"
] | [
3027,
3,
1,
39
] | 4 | [] | [] | 0 | true | Domain | DNA-binding transcriptional repressor CapW, winged helix-turn-helix domain | DNA-binding transcriptional repressor CapW, winged helix-turn-helix domain | WHD_CapW | 8 |
IPR059020 | 59,020 | DNA-binding transcriptional repressor CapW, C-terminal dimerisation domain | CapW_CTD | Domain | 2,936 | false | false | This entry represents the C-terminal dimerization domain of BrxR family of transcriptional regulators including CapW and BrxR. BrxR is a three-domain protein that regulates phage defense systems [ , , ]. The C-terminal domain (residues 200-295 in the prototypical BrxR from Escherichia fergusonii) is responsible for dim... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26107"
] | [
"BrxR_CTD"
] | [
2936
] | 1 | [] | [] | [] | 0 | [
"7qfz",
"7t8k",
"7t8l",
"7tb5",
"7tb6",
"9c5g"
] | 6 | [
"PUB00153145",
"PUB00161156",
"PUB00161157"
] | [
"35536256",
"35511079",
"35544231"
] | [
"Control of bacterial immune signaling by a WYL domain transcription factor.",
"Identification and characterization of the WYL BrxR protein and its gene as separable regulatory elements of a BREX phage restriction system.",
"A widespread family of WYL-domain transcriptional regulators co-localizes with diverse ... | [
2022,
2022,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"IncJ plasmid R391",
"metagenomes"
] | [
2893,
5,
1,
37
] | 4 | [] | [] | 0 | true | Domain | DNA-binding transcriptional repressor CapW, C-terminal dimerisation domain | DNA-binding transcriptional repressor CapW, C-terminal dimerisation domain | CapW_CTD | 6 |
IPR059021 | 59,021 | Epg5-like, C-terminal TPR repeats | TPR_Epg5_C | Domain | 1,690 | false | false | This is a region of tetratricopeptide (TPR)-like repeats found at the C-terminal end of Ectopic P granules protein 5 homolog from Drosophila melanogaster (Epg5) and similar proteins mainly from animals. Epg5 plays a role in late steps of autophagy [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26106"
] | [
"TPR_Epg5_C"
] | [
1690
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161491"
] | [
"26917586"
] | [
"EPG5-related Vici syndrome: a paradigm of neurodevelopmental disorders with defective autophagy."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1690
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
9,
2,
3
] | 5 | true | Domain | Epg5-like, C-terminal TPR repeats | Epg5-like, C-terminal TPR repeats | TPR_Epg5_C | 8 |
IPR059022 | 59,022 | MINDY4, N-terminal dimerisation domain | MINDY4_N | Domain | 1,244 | false | false | This domain is found at the N-terminal end of human Probable ubiquitin carboxyl-terminal hydrolase MINDY-4 and similar animal sequences. This domain is predicted to show an all-α structure. This domain is not present in MINDY-3 and MINDY-4B. Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated subst... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26038"
] | [
"Dimer_MINDY4_N"
] | [
1244
] | 1 | [
"EC"
] | [
"3.4.19.12"
] | [
"EC:3.4.19.12"
] | 1 | [] | 0 | [
"PUB00081935"
] | [
"27292798"
] | [
"MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1244
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3,
4
] | 4 | true | Domain | MINDY4, N-terminal dimerisation domain | MINDY4, N-terminal dimerisation domain | MINDY4_N | 3 |
IPR059023 | 59,023 | RNA helicase, C-terminal domain | RNA_hel_CTD | Domain | 9,980 | false | false | This domain is found in a number of DEAD and DExH box RNA helicases. In DExH box RNA helicases, in particular DHX36, this domain is involved in interactions with the HA2 and the OB domains. It is composed of three antiparallel β-strands and three α-helices. This domain is found central in 3'-5' RNA helicase YTHDC2. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26026"
] | [
"RNA_hel_CTD"
] | [
9980
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.4.13",
"R-BTA-3134963",
"R-HSA-3134963",
"R-HSA-9930044",
"R-MMU-3134963",
"R-MMU-9930044",
"R-RNO-3134963"
] | [
"EC:3.6.4.13",
"REACTOME:R-BTA-3134963",
"REACTOME:R-HSA-3134963",
"REACTOME:R-HSA-9930044",
"REACTOME:R-MMU-3134963",
"REACTOME:R-MMU-9930044",
"REACTOME:R-RNO-3134963"
] | 7 | [
"5vha",
"5vhc",
"5vhd",
"5vhe",
"6up2",
"6up3",
"6up4",
"8vv2",
"8vvd",
"8vx1",
"8vx8",
"9cpa"
] | 12 | [
"PUB00108303",
"PUB00161433",
"PUB00161434",
"PUB00161435",
"PUB00161436",
"PUB00161437",
"PUB00161438",
"PUB00161439",
"PUB00161440",
"PUB00161441"
] | [
"14731398",
"23651854",
"29899445",
"16150737",
"18279852",
"18842585",
"18854321",
"20472641",
"21149580",
"21586581"
] | [
"Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU.",
"The DEAH-box helicase DHX36 mediates dendritic localization of the neuronal precursor-microRNA-134.",
"Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36.",
"The DEXH protein product of the DHX36 g... | [
2004,
2013,
2018,
2005,
2008,
2008,
2008,
2010,
2011,
2011
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Nocardioides abyssi"
] | [
9979,
1
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
33,
9,
1,
9,
6,
1,
15,
13,
1,
45
] | 10 | true | Domain | RNA helicase, C-terminal domain | RNA helicase, C-terminal domain | RNA_hel_CTD | 7 |
IPR059024 | 59,024 | Synergin gamma, C-terminal domain | SYNRG_C | Domain | 3,790 | false | false | This domain is found at the C-terminal end of human SYNRG and similar proteins. This domain is predicted to adopt a mainly α configuration. Synergin gamma (SYNRG) plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network. It is a component of clathrin-coated vesicles and of the aftiphilin/p200/... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25999"
] | [
"SYNRG_C"
] | [
3790
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00069887",
"PUB00073158"
] | [
"15758025",
"12538641"
] | [
"The aftiphilin/p200/gamma-synergin complex.",
"EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking."
] | [
2005,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3790
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
13,
1,
19,
2,
4,
7,
7,
8
] | 8 | true | Domain | Synergin gamma, C-terminal domain | Synergin gamma, C-terminal domain | SYNRG_C | 7 |
IPR059025 | 59,025 | STB6-like, N-terminal domain | STB6_N | Domain | 1,606 | false | false | This domain is found at the N-terminal end of Protein STB2 and STB6 from Saccharomyces cerevisiae, which interacts with SIN3. This domain is predicted to adopt an α-β configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25995"
] | [
"STB6_N"
] | [
1606
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1606
] | 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 | STB6-like, N-terminal domain | STB6-like, N-terminal domain | STB6_N | 7 |
IPR059026 | 59,026 | Lipoprotein LpqB, N-terminal domain | LpqB_N | Domain | 4,337 | false | false | This domain is found at the N-terminal end of LpqB from Mycobacterium tuberculosis. This domain is predicted to adopt an α-β configuration. LpqB may modulate activity of the MtrAB system in controlling homeostasis of the cell wall and cell division. It partially restores antibiotic resistance to M.smegmatis in which th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25976"
] | [
"LpqB_N"
] | [
4337
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00104902"
] | [
"20233304"
] | [
"A lipoprotein modulates activity of the MtrAB two-component system to provide intrinsic multidrug resistance, cytokinetic control and cell wall homeostasis in Mycobacterium."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4287,
2,
48
] | 3 | [] | [] | 0 | true | Domain | Lipoprotein LpqB, N-terminal domain | Lipoprotein LpqB, N-terminal domain | LpqB_N | 4 |
IPR059027 | 59,027 | DDX21/DDX50 dimerisation domain | DD_DDX21-DDX50 | Domain | 3,942 | false | false | This entry represents the dimerisation domain in DEAD box helicase DDX21/DDX50 proteins. DDX21/DDX50 are involved in various aspects of RNA metabolism, including ribosomal RNA processing, pre-mRNA splicing, and RNA folding. These proteins act as sensors of transcriptional status for RNA polymerase I and II, promoting r... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26142"
] | [
"DD_DDX21-DDX50"
] | [
3942
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.4.13",
"R-HSA-5250924",
"R-HSA-6791226",
"R-MMU-5250924",
"R-MMU-6791226",
"R-RNO-5250924",
"R-RNO-6791226"
] | [
"EC:3.6.4.13",
"REACTOME:R-HSA-5250924",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-5250924",
"REACTOME:R-MMU-6791226",
"REACTOME:R-RNO-5250924",
"REACTOME:R-RNO-6791226"
] | 7 | [] | 0 | [
"PUB00130323",
"PUB00143349",
"PUB00161205",
"PUB00161206",
"PUB00161207",
"PUB00161208",
"PUB00161209",
"PUB00161210",
"PUB00161211",
"PUB00161212",
"PUB00161213",
"PUB00161214"
] | [
"11823437",
"12027455",
"22576849",
"23227895",
"25043599",
"9461305",
"39764852",
"28181036",
"35215908",
"21703541",
"12851405",
"36608661"
] | [
"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription.",
"Expression, cellular localization, and enzymatic activities of RNA helicase II/Gu(beta).",
"Chloroplast RH3 DEAD box RNA helicases in maize and Arabidopsis function in splicing of specific group II introns and affect chlor... | [
2002,
2002,
2012,
2013,
2014,
1997,
2025,
2017,
2022,
2011,
2003,
2023
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
78,
3864
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
10,
2,
10,
8,
6,
8,
52
] | 7 | true | Domain | DDX21/DDX50 dimerisation domain | DDX21/DDX50 dimerisation domain | DD_DDX21-DDX50 | 4 |
IPR059028 | 59,028 | PhiTE_239 | PhiTE_239 | Family | 25 | false | false | This entry represents a small family of phage integral membrane proteins that have 6 predicted transmembrane helices. Structure prediction suggests that one face contains a potential ligand binding pocket. This family includes Phage PhiTE protein phiTE_239 . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26221"
] | [
"Phage_phiTE_239"
] | [
25
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caudoviricetes"
] | [
25
] | 1 | [] | [] | 0 | true | Family | PhiTE_239 | PhiTE_239 | PhiTE_239 | 2 |
IPR059029 | 59,029 | FAM13A-like domain | FAM13A_dom | Domain | 5,763 | false | false | Several copies of this domain are found in human Protein FAM13A and similar sequences. This domain is predicted to show an all-α structure. The function of FAM13 family members is not clear. They contain a bipartite nuclear-localisation signal and two coil-coiled domains [ ]. FAM13A and FAM13B (but not FAM13C) each con... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26116"
] | [
"FAM13A"
] | [
5763
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-8980692",
"R-HSA-9013148",
"R-HSA-9013149",
"R-MMU-8980692",
"R-MMU-9013148",
"R-MMU-9013149"
] | [
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013149",
"REACTOME:R-MMU-8980692",
"REACTOME:R-MMU-9013148",
"REACTOME:R-MMU-9013149"
] | 6 | [] | 0 | [
"PUB00088933",
"PUB00147316",
"PUB00161227"
] | [
"15234000",
"22730300",
"32193374"
] | [
"Cloning and characterization of FAM13A1--a gene near a milk protein QTL on BTA6: evidence for population-wide linkage disequilibrium in Israeli Holsteins.",
"The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif.",
"FAM13A affects body fat distribution and adipocyte function."... | [
2004,
2012,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5763
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
32,
3,
14,
11,
16
] | 5 | true | Domain | FAM13A-like domain | FAM13A-like domain | FAM13A_dom | 1 |
IPR059030 | 59,030 | Epg5-like, central TPR repeats | TPR_Epg5_mid | Domain | 1,912 | false | false | This is a region of tetratricopeptide (TPR)-like repeats found in Ectopic P granules protein 5 homolog from Drosophila melanogaster (Epg5) and similar proteins mainly from animals. Epg5 plays a role in late steps of autophagy [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26103"
] | [
"TPR_Epg5"
] | [
1912
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00070599",
"PUB00070607",
"PUB00161491",
"PUB00161492",
"PUB00161493",
"PUB00161494",
"PUB00161495"
] | [
"20550938",
"23222957",
"26917586",
"22451698",
"24374177",
"25124690",
"29130391"
] | [
"C. elegans screen identifies autophagy genes specific to multicellular organisms.",
"Recessive mutations in EPG5 cause Vici syndrome, a multisystem disorder with defective autophagy.",
"EPG5-related Vici syndrome: a paradigm of neurodevelopmental disorders with defective autophagy.",
"Autophagy genes functio... | [
2010,
2013,
2016,
2012,
2014,
2014,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1912
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3,
7,
1,
3
] | 6 | true | Domain | Epg5-like, central TPR repeats | Epg5-like, central TPR repeats | TPR_Epg5_mid | 4 |
IPR059031 | 59,031 | STAC3-related SH3 domain | SH3_20 | Domain | 783 | false | false | This SH3-like domain is found in uncharacterised proteins mainly from Metazoa. It has a detectable similarity to the SH3 domain of STAC3 and is usually found in tandem with another SH3-like domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26085"
] | [
"SH3_20"
] | [
783
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
783
] | 1 | [
"Caenorhabditis elegans",
"Drosophila melanogaster"
] | [
5,
8
] | 2 | true | Domain | STAC3-related SH3 domain | STAC3-related SH3 domain | SH3_20 | 7 |
IPR059033 | 59,033 | ATP-dependent DNA repair protein/ubiquitin-protein ligase E3 IRC20, alpha-helical domain | IRC20_dom | Domain | 1,603 | false | false | This predicted domain is found in a group of uncharacterised fungal proteins, including yeast ATP-dependent DNA repair protein/ubiquitin-protein ligase E3 IRC20, which directs homologous recombination (HR)-mediated double-strand break (DSB) repair towards the synthesis dependent strand annealing (SDSA) pathway [ ], pro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26021"
] | [
"Ferritin_C144_05"
] | [
1603
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-SCE-8866654",
"R-SPO-8866654"
] | [
"REACTOME:R-SCE-8866654",
"REACTOME:R-SPO-8866654"
] | 2 | [] | 0 | [
"PUB00163355"
] | [
"33202365"
] | [
"The ATPase Irc20 facilitates Rad51 chromatin enrichment during homologous recombination in yeast Saccharomyces cerevisiae."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1603
] | 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,
1,
1
] | 3 | true | Domain | ATP-dependent DNA repair protein/ubiquitin-protein ligase E3 IRC20, alpha-helical domain | ATP-dependent DNA repair protein/ubiquitin-protein ligase E3 IRC20, alpha-helical domain | IRC20_dom | 3 |
IPR059034 | 59,034 | AEBP2-like, C-terminal SH3 domain | SH3_AEBP2_C | Domain | 1,885 | false | false | This domain is found at the C-terminal end of human Zinc finger protein AEBP2 and similar sequences mainly found in animals, including Zinc finger protein jing. This domain shows a mainly β configuration. AEBP2 acts as an accessory subunit for the core Polycomb repressive complex 2, which mediates histone H3K27 trimeth... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26014"
] | [
"SH3_AEBP2_C"
] | [
1885
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-212300",
"R-BTA-3214841",
"R-DME-212300",
"R-DRE-212300",
"R-HSA-212300",
"R-HSA-3214841",
"R-MMU-212300",
"R-MMU-3214841"
] | [
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-3214841",
"REACTOME:R-DME-212300",
"REACTOME:R-DRE-212300",
"REACTOME:R-HSA-212300",
"REACTOME:R-HSA-3214841",
"REACTOME:R-MMU-212300",
"REACTOME:R-MMU-3214841"
] | 8 | [
"5wai",
"6c23",
"6c24",
"6wkr",
"7kso",
"8eqv",
"8fyh",
"8t9g",
"8tas",
"8tb9",
"8vmi",
"8vml",
"8vnv",
"8vnz",
"9c8u",
"9dch"
] | 16 | [
"PUB00102932",
"PUB00107040",
"PUB00145421",
"PUB00145423",
"PUB00161464",
"PUB00161465",
"PUB00161466",
"PUB00161467",
"PUB00161468",
"PUB00161469",
"PUB00161690",
"PUB00161691",
"PUB00161692"
] | [
"31959557",
"15225548",
"29348366",
"29499137",
"11152631",
"12015288",
"12111212",
"37733873",
"39774834",
"39231985",
"16510782",
"16648585",
"18036784"
] | [
"A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island Chromatin.",
"SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex.",
"Structures of human PRC2 with its cofactors AEBP2 and JARID2.",
"Unique Structural Platforms of Suz12 Dicta... | [
2020,
2004,
2018,
2018,
2001,
2002,
2002,
2023,
2025,
2024,
2006,
2006,
2008
] | 13 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
1885
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
7,
4,
6
] | 5 | true | Domain | AEBP2-like, C-terminal SH3 domain | AEBP2-like, C-terminal SH3 domain | SH3_AEBP2_C | 2 |
IPR059035 | 59,035 | Fibronectin type I domain, arthropods | Fn1_3 | Domain | 433 | false | false | This entry represents a fibronectin type I domain found in a variety of arthropods proteins that contain domains. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25868"
] | [
"Fn1_3"
] | [
433
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mandibulata"
] | [
433
] | 1 | [
"Drosophila melanogaster"
] | [
9
] | 1 | true | Domain | Fibronectin type I domain, arthropods | Fibronectin type I domain, arthropods | Fn1_3 | 8 |
IPR059036 | 59,036 | RUFY4-like domain | RUFY4_dom | Domain | 571 | false | false | This domain is found in human RUN and FYVE domain-containing protein 4 (RUFY4) and similar animal proteins. RUFY4 positively regulates macroautophagy in primary dendritic cells. This domain is predicted to adopt an α configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25366"
] | [
"RUFY4"
] | [
571
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
571
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
1
] | 3 | true | Domain | RUFY4-like domain | RUFY4-like domain | RUFY4_dom | 6 |
IPR059037 | 59,037 | Domain of unknown function (DUF7881), N-terminal domain | DUF7881_N | Domain | 41 | false | false | This entry represents the N-terminal domain of unknown function found in Trypanosoma proteins. According to structure predictions it could adopt a DNA clamp fold. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25365"
] | [
"DUF7881_N"
] | [
41
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00101311"
] | [
"12888511"
] | [
"Evolutionary clues to DNA polymerase III beta clamp structural mechanisms."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Trypanosomatidae"
] | [
41
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF7881), N-terminal domain | Domain of unknown function (DUF7881), N-terminal domain | DUF7881_N | 8 |
IPR059038 | 59,038 | Domain of unknown function (DUF7881), C-terminal domain | DUF7881_C | Domain | 41 | false | false | This entry represents the C-terminal domain of unknown function found in Trypanosoma proteins. According to structure predictions it could adopt a DNA clamp fold. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25363"
] | [
"DUF7881_C"
] | [
41
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00101311"
] | [
"12888511"
] | [
"Evolutionary clues to DNA polymerase III beta clamp structural mechanisms."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Trypanosomatidae"
] | [
41
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function (DUF7881), C-terminal domain | Domain of unknown function (DUF7881), C-terminal domain | DUF7881_C | 8 |
IPR059039 | 59,039 | ZNF380, coiled-coil | ZNF380_CC | Domain | 1,827 | false | false | This entry represents a coiled-coil region found at the C-terminal end of ZNF830. Zinc finger protein 830 (ZNF830; also known as coiled-coil domain-containing protein 16 or CCDC16) contains a C2H2-type zinc finger and a coiled-coil region . It is a component of the XAB2 complex, which binds RNA [ ], and a component of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23406"
] | [
"ZNF380_CC"
] | [
1827
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6781823",
"R-HSA-6781827",
"R-HSA-6782135",
"R-HSA-6782210",
"R-HSA-72163",
"R-MMU-6781823",
"R-MMU-6782135",
"R-MMU-6782210",
"R-MMU-72163",
"R-RNO-6781823",
"R-RNO-6782135",
"R-RNO-6782210",
"R-RNO-72163",
"R-XTR-6781823",
"R-XTR-6782135",
"R-XTR-6782210",
"R-XTR-72163"
] | [
"REACTOME:R-HSA-6781823",
"REACTOME:R-HSA-6781827",
"REACTOME:R-HSA-6782135",
"REACTOME:R-HSA-6782210",
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-6781823",
"REACTOME:R-MMU-6782135",
"REACTOME:R-MMU-6782210",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-6781823",
"REACTOME:R-RNO-6782135",
"REACTOME:R-... | 17 | [] | 0 | [
"PUB00090460",
"PUB00090461"
] | [
"17981804",
"25599396"
] | [
"Isolation of XAB2 complex involved in pre-mRNA splicing, transcription, and transcription-coupled repair.",
"The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes."
] | [
2008,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1827
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
1,
2,
2,
3,
2,
2,
2
] | 7 | true | Domain | ZNF380, coiled-coil | ZNF380, coiled-coil | ZNF380_CC | 9 |
IPR059040 | 59,040 | CyaD-like, alpha-helical hairpin domain | HH_CyaD-like | Domain | 1,001 | false | false | This domain is found in the Protein CyaD from Bordetella pertussis and related proteins from proteobacteria, including Hemolysin secretion protein D from Escherichia coli (HlyD). CyaD is necessary for transport of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin), a bifunctional protein with both adenylate ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25988"
] | [
"HH_CyaD"
] | [
1001
] | 1 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"5c21",
"5c22",
"8dck"
] | 3 | [
"PUB00068111",
"PUB00078037"
] | [
"2905265",
"26833388"
] | [
"Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis.",
"Crystal Structure of a Soluble Fragment of the Membrane Fusion Protein HlyD in a Type I Secretion System of Gram-Negative Bacteria."
] | [
1988,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
996,
2,
3
] | 3 | [] | [] | 0 | true | Domain | CyaD-like, alpha-helical hairpin domain | CyaD-like, alpha-helical hairpin domain | HH_CyaD-like | 1 |
IPR059041 | 59,041 | Deleted in lung and esophageal cancer protein 1, Ig-like domain | Ig_DLEC1_1 | Domain | 1,428 | false | false | This domain is found in the human DLEC1 and other animal proteins. It is predicted to fold into a β-sandwich with an Ig-like topology. It shares significant sequence similarity with Ig-like domains found in Cep192 and hydin. This domain is not present in rat homologues. Deleted in lung and esophageal cancer (DLEC1) is ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23277"
] | [
"Ig_Dlec1_1"
] | [
1428
] | 1 | [] | [] | [] | 0 | [
"7n6g",
"7sqc",
"9ijj"
] | 3 | [
"PUB00078381",
"PUB00078382",
"PUB00078641",
"PUB00078642",
"PUB00078643",
"PUB00155671"
] | [
"25648635",
"25746324",
"21443130",
"20630829",
"19156137",
"33144677"
] | [
"DLEC1, a 3p tumor suppressor, represses NF-κB signaling and is methylated in prostate cancer.",
"DLEC1 is not silenced solely by promoter methylation in head and neck squamous cell carcinoma.",
"Epigenetic inactivation of deleted in lung and esophageal cancer 1 gene by promoter methylation in gastric and color... | [
2015,
2015,
2010,
2010,
2009,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1428
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
5,
5,
6
] | 4 | true | Domain | Deleted in lung and esophageal cancer protein 1, Ig-like domain | Deleted in lung and esophageal cancer protein 1, Ig-like domain | Ig_DLEC1_1 | 7 |
IPR059042 | 59,042 | ZNF598, C2H2 zinc finger domain | Znf_C2H2_ZNF598 | Domain | 962 | false | false | This C2H2 zinc finger domain is found in human E3 ubiquitin-protein ligase ZNF598 and other animal proteins. ZNF598 plays a key role in the ribosome quality control (RQC), a pathway that takes place when the ribosome has stalled during translation, leading to degradation of nascent peptide chains. ZNF598 is activated w... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23208"
] | [
"zf_C2H2_ZNF598"
] | [
962
] | 1 | [
"EC",
"METACYC"
] | [
"2.3.2.27",
"PWY-7511"
] | [
"EC:2.3.2.27",
"METACYC:PWY-7511"
] | 2 | [] | 0 | [
"PUB00092042",
"PUB00092043",
"PUB00155780"
] | [
"28065601",
"22751931",
"29719242"
] | [
"Initiation of Quality Control during Poly(A) Translation Requires Site-Specific Ribosome Ubiquitination.",
"A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian development.",
"ZNF598 Plays Distinct Roles in Interferon-Stimulated Gene Expression and Poxvirus Protein Synthesis."
] | [
2017,
2012,
2018
] | 3 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Metazoa"
] | [
962
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
1,
4
] | 4 | true | Domain | ZNF598, C2H2 zinc finger domain | ZNF598, C2H2 zinc finger domain | Znf_C2H2_ZNF598 | 7 |
IPR059043 | 59,043 | M02D8_5-like, fourth CUB domain | CUB_M02D8_5_4th | Domain | 34 | false | false | This entry represents the fourth occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23063"
] | [
"CUB_M02D8_5_4th"
] | [
34
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Rhabditida"
] | [
34
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, fourth CUB domain | M02D8_5-like, fourth CUB domain | CUB_M02D8_5_4th | 6 |
IPR059044 | 59,044 | Transmembrane 6 superfamily member 1/2, transmembrane domain | TM_Tm6sf1/2 | Domain | 2,341 | false | false | This domain is found at the N-terminal end of Transmembrane 6 superfamily member 1/2 (Tm6sf1/2) from mouse and similar proteins mainly found in vertebrates. Tm6sf1 may function as sterol isomerase [ , ]. Tm6sf2 is a regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26083"
] | [
"TM_Tm6sf2"
] | [
2341
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00077739",
"PUB00102136",
"PUB00102144",
"PUB00102145",
"PUB00102147",
"PUB00102149"
] | [
"25566323",
"24633158",
"25422095",
"24531328",
"28027591",
"24927523"
] | [
"TM6SF2 and MAC30, new enzyme homologs in sterol metabolism and common metabolic disease.",
"Systematic evaluation of coding variation identifies a candidate causal variant in TM6SF2 influencing total cholesterol and myocardial infarction risk.",
"Transmembrane 6 superfamily 1 (Tm6sf1) is a novel lysosomal tran... | [
2014,
2014,
2015,
2014,
2017,
2014
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2341
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
9,
8,
7
] | 4 | true | Domain | Transmembrane 6 superfamily member 1/2, transmembrane domain | Transmembrane 6 superfamily member 1/2, transmembrane domain | TM_Tm6sf1/2 | 7 |
IPR059045 | 59,045 | M02D8_5-like, first CUB domain | CUB_M02D8_5_1st | Domain | 29 | false | false | This entry represents the first occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23060"
] | [
"CUB_M02D8_5_1st"
] | [
29
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Rhabditomorpha"
] | [
29
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, first CUB domain | M02D8_5-like, first CUB domain | CUB_M02D8_5_1st | 7 |
IPR059046 | 59,046 | M02D8_5-like, second CUB domain | CUB_M02D8_5_2nd | Domain | 73 | false | false | This entry represents the second occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23061"
] | [
"CUB_M02D8_5_2nd"
] | [
73
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
73
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, second CUB domain | M02D8_5-like, second CUB domain | CUB_M02D8_5_2nd | 1 |
IPR059047 | 59,047 | M02D8_5-like, third CUB domain | CUB_M02D8_5_3rd | Domain | 75 | false | false | This entry represents the third occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23062"
] | [
"CUB_M02D8_5_3rd"
] | [
75
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
75
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, third CUB domain | M02D8_5-like, third CUB domain | CUB_M02D8_5_3rd | 7 |
IPR059048 | 59,048 | M02D8_5-like, fifth CUB domain | CUB_M02D8_5_5th | Domain | 56 | false | false | This entry represents the fifth occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23064"
] | [
"CUB_M02D8_5_5th"
] | [
56
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
56
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, fifth CUB domain | M02D8_5-like, fifth CUB domain | CUB_M02D8_5_5th | 5 |
IPR059049 | 59,049 | TSEN34, N-terminal domain | TSEN34_N | Domain | 2,883 | false | false | This domain is found at the N-terminal end of human tRNA-splicing endonuclease subunit Sen34 (TSEN34). This domain shows an α-β configuration and is often found associated with . TSEN34 constitutes one of the two catalytic subunits of the tRNA-splicing endonuclease complex, a complex responsible for identification and ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26577"
] | [
"TSEN34_N"
] | [
2883
] | 1 | [
"EC",
"METACYC",
"METACYC",
"REACTOME"
] | [
"4.6.1.16",
"PWY-6689",
"PWY-7803",
"R-HSA-6784531"
] | [
"EC:4.6.1.16",
"METACYC:PWY-6689",
"METACYC:PWY-7803",
"REACTOME:R-HSA-6784531"
] | 4 | [
"7uxa",
"7zrz",
"8hmy",
"8hmz",
"8iss"
] | 5 | [
"PUB00044697",
"PUB00161496",
"PUB00161497",
"PUB00161498"
] | [
"15109492",
"37231153",
"37028420",
"37770519"
] | [
"Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation.",
"Structural basis for pre-tRNA recognition and processing by the human tRNA splicing endonuclease complex.",
"Structural basis of pre-tRNA intron removal by human tRNA splicing endonuclease.",
... | [
2004,
2023,
2023,
2023
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2883
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
4,
8,
8,
1,
3,
1,
1
] | 8 | true | Domain | TSEN34, N-terminal domain | TSEN34, N-terminal domain | TSEN34_N | 5 |
IPR059050 | 59,050 | Rv3660c-like, CheY-like N-terminal domain | Rv3660c_N | Domain | 3,176 | false | false | This domain is found at the N-terminal end of the uncharacterised protein Rv3660c. This domain is predicted to adopt a CheY-like response regulator fold. Rv3660c from Mycobacterium tuberculosis (Septum site determining protein, Ssd) plays a role in septum formation [ , ]. Members of this protein family belong to the Mi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26563"
] | [
"Rv3660c_N"
] | [
3176
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053710",
"PUB00059195",
"PUB00135927"
] | [
"12370432",
"16735741",
"21504606"
] | [
"Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins.",
"Identification of cell cycle regulators in Mycobacterium tuberculosis by inhibition of septum formation and global transcriptional analysis.",
"Mycobacterium tuberculosis septum site determinin... | [
2002,
2006,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Pleodorina starrii",
"metagenomes"
] | [
3153,
1,
22
] | 3 | [] | [] | 0 | true | Domain | Rv3660c-like, CheY-like N-terminal domain | Rv3660c-like, CheY-like N-terminal domain | Rv3660c_N | 5 |
IPR059051 | 59,051 | MTH_967-like, PD-(D/E)XK domain | MTH_967_PDDEXK | Domain | 792 | false | false | This entry represents a PD-(D/E)XK endonuclease domain found in MTH_967 from Methanothermobacter thermautotrophicus and similar proteins. These domains are most similar from a structural point of view to archaeal holliday junction resolvase proteins. These proteins contains an N and C-terminal PD-(D/E)XK domain that in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26553"
] | [
"PDDEXK_19"
] | [
792
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
772,
20
] | 2 | [] | [] | 0 | true | Domain | MTH_967-like, PD-(D/E)XK domain | MTH_967-like, PD-(D/E)XK domain | MTH_967_PDDEXK | 5 |
IPR059052 | 59,052 | YbhG-like, alpha-helical hairpin domain | HH_YbhG-like | Domain | 7,569 | false | false | This domain is found in the membrane protein YbhG from Escherichia coli and related uncharacterised proteins from bacteria that are members of the UPF0194 family. This domain is usually found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25881"
] | [
"HH_YBHG"
] | [
7569
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
7469,
14,
86
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | YbhG-like, alpha-helical hairpin domain | YbhG-like, alpha-helical hairpin domain | HH_YbhG-like | 8 |
IPR059054 | 59,054 | Inh, N-terminal domain | Inh_N | Domain | 385 | false | false | This entry represents the N-terminal domain of Inh protein. This N-terminal domain is predicted to be composed of a three α helix bundle. Bacteriophage T4 inhibitor (Inh) protein functions as an inhibitor of the prohead protease gp21. The inh gene is located upstream of the hoc gene in the T4 genome. The protein is app... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26097"
] | [
"Phage_Inh_N"
] | [
385
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161406"
] | [
"2377482"
] | [
"The nucleotide sequence of the region of bacteriophage T4 inh(lip)-hoc genes."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"Viruses",
"viral metagenome"
] | [
2,
382,
1
] | 3 | [] | [] | 0 | true | Domain | Inh, N-terminal domain | Inh, N-terminal domain | Inh_N | 5 |
IPR059055 | 59,055 | Inh, C-terminal domain | Inh_C | Domain | 324 | false | false | This entry represents the C-terminal domain of Inh protein. This C-terminal domain is predicted to be composed of a three stranded β sheet with three α helices packed on one side. Bacteriophage T4 inhibitor (Inh) protein functions as an inhibitor of the prohead protease gp21. The inh gene is located upstream of the hoc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26098"
] | [
"Phage_Inh_C"
] | [
324
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161406"
] | [
"2377482"
] | [
"The nucleotide sequence of the region of bacteriophage T4 inh(lip)-hoc genes."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Flagellimonas marina",
"Viruses"
] | [
1,
323
] | 2 | [] | [] | 0 | true | Domain | Inh, C-terminal domain | Inh, C-terminal domain | Inh_C | 1 |
IPR059056 | 59,056 | M02D8_5-like, seventh CUB domain | CUB_M02D8_5_7th | Domain | 32 | false | false | This entry represents the seventh occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . Th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23068"
] | [
"CUB_M02D8_5_7th"
] | [
32
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Rhabditomorpha"
] | [
32
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, seventh CUB domain | M02D8_5-like, seventh CUB domain | CUB_M02D8_5_7th | 1 |
IPR059057 | 59,057 | M02D8_5-like, sixth CUB domain | CUB_M02D8_5_6th | Domain | 30 | false | false | This entry represents the sixth occurrence of the CUB domain in a family of uncharacterised proteins present in nematodes. These uncharacterised nematode proteins contain multiple consecutive repeats of the CUB domain, represented by distinct entries: first , second , third , fourth , fifth , sixth , and seventh . The ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23059"
] | [
"CUB_M02D8_5_6th"
] | [
30
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00155592"
] | [
"21954942"
] | [
"Structure and properties of the Ca(2+)-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Rhabditomorpha"
] | [
30
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | M02D8_5-like, sixth CUB domain | M02D8_5-like, sixth CUB domain | CUB_M02D8_5_6th | 5 |
IPR059058 | 59,058 | Zinc finger protein 462, C2H2 zinc finger | Znf-C2H2_ZNF462 | Domain | 1,388 | false | false | This domain is found in the human Zinc finger protein 462 and related proteins. This protein is involved in transcription by regulating chromatin structure and organisation [ , ]. ZNF462 is a multidomain proteins that contains a number of classical C2H2 zinc fingers. This entry represents one of them. Zinc finger (Znf)... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23075"
] | [
"zf-C2H2_ZNF462_11"
] | [
1388
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00155929",
"PUB00155930"
] | [
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"20219459",
"21570965"
] | [
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptides for the regulation of gene expression.",
"Zinc finger proteins: new ... | [
2002,
2007,
2005,
2005,
1999,
2001,
2010,
2011
] | 8 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
1388
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
3,
2
] | 4 | true | Domain | Zinc finger protein 462, C2H2 zinc finger | Zinc finger protein 462, C2H2 zinc finger | Znf-C2H2_ZNF462 | 6 |
IPR059059 | 59,059 | Zinc finger protein 462-like, seventh C2H2 zinc finger | Znf-C2H2_7th_ZNF462 | Domain | 1,541 | false | false | This domain is found in the human Zinc finger protein 462 and related proteins. This protein is involved in transcription by regulating chromatin structure and organisation [ , ]. ZNF462 is a multidomain protein that contains a number of classical C2H2 zinc fingers. This entry represents one of them. This domain is als... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23225"
] | [
"zf-C2H2_7th_ZNF462"
] | [
1541
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-DME-8936459",
"R-DME-983231"
] | [
"REACTOME:R-DME-8936459",
"REACTOME:R-DME-983231"
] | 2 | [] | 0 | [
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00155929",
"PUB00155930",
"PUB00161694",
"PUB00161695"
] | [
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"20219459",
"21570965",
"9367989",
"9367990"
] | [
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptides for the regulation of gene expression.",
"Zinc finger proteins: new ... | [
2002,
2007,
2005,
2005,
1999,
2001,
2010,
2011,
1997,
1997
] | 10 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Pseudonocardiaceae",
"viral metagenome"
] | [
1535,
5,
1
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
5,
5,
3,
3
] | 5 | true | Domain | Zinc finger protein 462-like, seventh C2H2 zinc finger | Zinc finger protein 462-like, seventh C2H2 zinc finger | Znf-C2H2_7th_ZNF462 | 9 |
IPR059060 | 59,060 | Niban 1/2/3 domain | Niban_1/2/3_dom | Domain | 3,463 | false | false | This domain is found towards the C-terminal end of human Protein Niban 2 and similar animal proteins, including Niban 1 and 3. Niban2 may play a role in apoptosis suppression and promote melanoma cell invasion in vitro [ , ]. This entry represents the C-terminal region of the helix bundle domain, which shows a distorte... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26086"
] | [
"Niban2"
] | [
3463
] | 1 | [] | [] | [] | 0 | [
"7ctp"
] | 1 | [
"PUB00059989",
"PUB00059995",
"PUB00158513",
"PUB00161371",
"PUB00161372"
] | [
"17588536",
"21148485",
"33142954",
"19362540",
"25342806"
] | [
"The endoplasmic reticulum stress-inducible protein Niban regulates eIF2alpha and S6K1/4E-BP1 phosphorylation.",
"FAM129B/MINERVA, a novel adherens junction-associated protein, suppresses apoptosis in HeLa cells.",
"Structural Insight on Functional Regulation of Human MINERVA Protein.",
"Functional proteomics... | [
2007,
2011,
2020,
2009,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3463
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
13,
7,
8
] | 4 | true | Domain | Niban 1/2/3 domain | Niban 1/2/3 domain | Niban_1/2/3_dom | 7 |
IPR059061 | 59,061 | Gins15, N-terminal domain | Gins15_N | Domain | 47 | false | false | This entry represents the N-terminal (A domain) in Gins15 ( ) from archaea. This domain consists primarily of α-helical structures and corresponds to the A domain in the circularly permuted AB domain arrangement of Gins15 [ ]. While the N-terminal domain does not directly interact with Cdc45, it plays an important stru... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25864"
] | [
"Gins15_N"
] | [
47
] | 1 | [] | [] | [] | 0 | [
"9moj"
] | 1 | [
"PUB00083145",
"PUB00088351"
] | [
"27821767",
"21527023"
] | [
"Archaeal orthologs of Cdc45 and GINS form a stable complex that stimulates the helicase activity of MCM.",
"Architectures of archaeal GINS complexes, essential DNA replication initiation factors."
] | [
2016,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
47
] | 1 | [] | [] | 0 | true | Domain | Gins15, N-terminal domain | Gins15, N-terminal domain | Gins15_N | 2 |
IPR059062 | 59,062 | Gins15, C-terminal domain | Gins15_C | Domain | 53 | false | false | This entry represents the C-terminal (B domain) in Gins15 ( ) from archaea. This domain is predominantly composed of β-strands and corresponds to the B domain in the AB domain arrangement of Gins15 [ ]. The C-terminal B domain is both necessary and sufficient for interaction with Cdc45, forming a key interface in the C... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25865"
] | [
"Gins15_C"
] | [
53
] | 1 | [] | [] | [] | 0 | [
"9moj"
] | 1 | [
"PUB00083145",
"PUB00088351"
] | [
"27821767",
"21527023"
] | [
"Archaeal orthologs of Cdc45 and GINS form a stable complex that stimulates the helicase activity of MCM.",
"Architectures of archaeal GINS complexes, essential DNA replication initiation factors."
] | [
2016,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoprotei"
] | [
53
] | 1 | [] | [] | 0 | true | Domain | Gins15, C-terminal domain | Gins15, C-terminal domain | Gins15_C | 9 |
IPR059063 | 59,063 | Sliding clamp-binding bacterial toxin SocB | SocB | Family | 84 | false | false | This entry represents the SocB toxin found in a toxin-antitoxin system in bacteria. SocB is a protein toxin that inhibits DNA replication by binding to the β sliding clamp DnaN through a conserved clamp-binding motif. When SocB accumulates, it competes with DNA polymerase III for binding to DnaN, leading to replication... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF047746",
"PF26318"
] | [
"SocB_toxin",
"SocB"
] | [
65,
84
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100160",
"PUB00159666"
] | [
"24239291",
"34841338"
] | [
"A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.",
"Bacterial toxin-antitoxin modules: classification, functions, and association with persistence."
] | [
2013,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenome"
] | [
83,
1
] | 2 | [] | [] | 0 | true | Family | Sliding clamp-binding bacterial toxin SocB | Sliding clamp-binding bacterial toxin SocB | SocB | 7 |
IPR059064 | 59,064 | TYRAAT2-like, C-terminal domain | TYRAAT2_C | Domain | 1,914 | false | false | This domain is found at the C-terminal of Arogenate dehydrogenase 2 (TYRAAT2) and in two copies in Arogenate dehydrogenase 1 (TYRAAT1), both chloroplastic from Arabidopsis thaliana, as well as in similar plant proteins. This region is predicted to adopt an α helical structure. TYRAAT1, which is involved in the biosynth... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26213"
] | [
"TYRAAT1_C"
] | [
1914
] | 1 | [] | [] | [] | 0 | [
"5t95",
"5t9e",
"5t9f",
"5whx"
] | 4 | [
"PUB00011044"
] | [
"12354106"
] | [
"Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
101,
1797,
16
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
6,
16
] | 3 | true | Domain | TYRAAT2-like, C-terminal domain | TYRAAT2-like, C-terminal domain | TYRAAT2_C | 6 |
IPR059065 | 59,065 | Tag1-like, fourth Ig-like domain | Ig_Tag1-like_4th | Domain | 1,016 | false | false | This entry describes the fourth Ig-like domain in putative Tag1 and related fungal proteins. The proteins represented by this entry have more than three Ig-like domains. This domain shows homology to LEA-2 domains. This domain can be found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26150"
] | [
"LEA-2_4"
] | [
1016
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100166",
"PUB00100170"
] | [
"34347309",
"33536246"
] | [
"TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.",
"Vacuolar protein Tag1 and Atg1-Atg13 regulate autophagy termination during persistent starvation in <i>S. cerevisiae</i>."
] | [
2022,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1016
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Tag1-like, fourth Ig-like domain | Tag1-like, fourth Ig-like domain | Ig_Tag1-like_4th | 6 |
IPR059067 | 59,067 | ATP-dependent ClpX-like chaperone, zinc ribbon domain | Znf_ribbon_CLPX-like | Domain | 2,283 | false | false | This zinc ribbon domain is found towards the N-terminal of human mitochondrial ATP-dependent clpX-like chaperone (CLPX) and similar proteins in animals. The mitochondrial ATP-dependent clpX-like chaperone (CLPX) functions as an unfoldase. This protein is part of the ClpXP protease complex and is also involved in heme b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26040"
] | [
"Zn_ribbon_CLPX_N"
] | [
2283
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.4.10",
"R-HSA-9837999",
"R-MMU-9837999",
"R-RNO-9837999"
] | [
"EC:3.6.4.10",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-9837999",
"REACTOME:R-RNO-9837999"
] | 4 | [] | 0 | [
"PUB00043206",
"PUB00148681",
"PUB00161557",
"PUB00161558",
"PUB00161559",
"PUB00161560",
"PUB00161561"
] | [
"16963084",
"22841477",
"11923310",
"22710082",
"25957689",
"28874591",
"10347188"
] | [
"Structure of Aart, a designed six-finger zinc finger peptide, bound to DNA.",
"Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX.",
"Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP.",
"Substrate recognition and processing by a Walke... | [
2006,
2012,
2002,
2012,
2015,
2017,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2283
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
4,
5,
6
] | 6 | true | Domain | ATP-dependent ClpX-like chaperone, zinc ribbon domain | ATP-dependent ClpX-like chaperone, zinc ribbon domain | Znf_ribbon_CLPX-like | 3 |
IPR059068 | 59,068 | Prolyl 4-hydroxylase, peptide-substrate-binding domain | TPR_P4H | Domain | 6,877 | false | false | This entry represents the prolyl 4-hydroxylase subunit alpha-1/2/3 peptide substrate binding domain, which is formed by two and a half TPR-like repeats. Prolyl 4-hydroxylase alpha-subunit (P4H) ( ) catalyses the formation of 4-hydroxyproline, a key post-translational modification required for collagen biosynthesis. In ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF23558"
] | [
"TPR_P4H"
] | [
6877
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.11.2",
"PWY-7894",
"R-BTA-1650814",
"R-CEL-1650814",
"R-HSA-1650814",
"R-MMU-1650814",
"R-RNO-1650814"
] | [
"EC:1.14.11.2",
"METACYC:PWY-7894",
"REACTOME:R-BTA-1650814",
"REACTOME:R-CEL-1650814",
"REACTOME:R-HSA-1650814",
"REACTOME:R-MMU-1650814",
"REACTOME:R-RNO-1650814"
] | 7 | [
"1tjc",
"2v5f",
"2yq8",
"4bt8",
"4bt9",
"4bta",
"4btb",
"6evl",
"6evm",
"6evn",
"6evo",
"6evp",
"9hpq",
"9hre",
"9ht8",
"9htd"
] | 16 | [
"PUB00007743",
"PUB00020896",
"PUB00020932",
"PUB00020939",
"PUB00031474",
"PUB00155874",
"PUB00155875"
] | [
"7753822",
"2552442",
"14500733",
"11850189",
"15456751",
"24207127",
"30168208"
] | [
"Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit.",
"Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken emb... | [
1995,
1989,
2003,
2002,
2004,
2013,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Candidatus Scatomorpha pullistercoris",
"Opisthokonta"
] | [
1,
6876
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
57,
11,
8,
9,
16
] | 6 | true | Domain | Prolyl 4-hydroxylase, peptide-substrate-binding domain | Prolyl 4-hydroxylase, peptide-substrate-binding domain | TPR_P4H | 9 |
IPR059069 | 59,069 | Putative Dachshund-homology domain, metazoa | DHD_metazoa | Domain | 98 | false | false | This entry represents an uncharacterised putative Dachshund-homology (DHD) domain that adopts a pseudo Winged helix fold. This domain is found in a range of uncharacterised metazoan proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25867"
] | [
"DHD"
] | [
98
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
98
] | 1 | [] | [] | 0 | true | Domain | Putative Dachshund-homology domain, metazoa | Putative Dachshund-homology domain, metazoa | DHD_metazoa | 6 |
IPR059070 | 59,070 | VPS8-like, TPR-like repeats | TPR_VPS8_2 | Domain | 2,157 | false | false | This region of TPR-like repeats is found towards the C-terminal of Vacuolar protein sorting-associated protein 8 from S. cerevisiae (VPS8) and similar eukaryotic proteins. VPS8 is involved in the retention of proteins to the late-Golgi and plays an integral role in the complex vacuolar protein sorting process. This dom... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25066"
] | [
"TPR_VPS8_2"
] | [
2157
] | 1 | [] | [] | [] | 0 | [
"8qx8"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2157
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
1,
3,
1,
5
] | 4 | true | Domain | VPS8-like, TPR-like repeats | VPS8-like, TPR-like repeats | TPR_VPS8_2 | 8 |
IPR059071 | 59,071 | Vesicle-trafficking protein SEC22a/c, C-terminal domain | SEC22a-c_C | Domain | 1,771 | false | false | This domain is found at the C-terminal end of human SEC22a and SEC22c and similar animals proteins. This domain is found associated to and is predicted to fold into four α helices. This domain is not found in other SEC22 proteins such as SEC22b and Vesicle-associated membrane protein 7. Vesicle-trafficking protein SEC2... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25970"
] | [
"SEC22a_C"
] | [
1771
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-204005",
"R-HSA-204005",
"R-MMU-204005",
"R-RNO-204005"
] | [
"REACTOME:R-BTA-204005",
"REACTOME:R-HSA-204005",
"REACTOME:R-MMU-204005",
"REACTOME:R-RNO-204005"
] | 4 | [] | 0 | [
"PUB00063059",
"PUB00161458"
] | [
"8621431",
"9501016"
] | [
"Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus.",
"Hsec22c: a homolog of yeast Sec22p and mammalian rsec22a and msec22b/ERS-24."
] | [
1996,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
1771
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
10,
5,
7
] | 4 | true | Domain | Vesicle-trafficking protein SEC22a/c, C-terminal domain | Vesicle-trafficking protein SEC22a/c, C-terminal domain | SEC22a-c_C | 8 |
IPR059073 | 59,073 | tRNA (guanine(10)-N(2))-methyltransferase TRMT11, N-terminal domain | TRMT11_N | Domain | 4,871 | false | false | This entry describes the N-terminal THUMP domain in TRMT11 found in eukaryotes. The THUMP domain is primarily involved in recognising and binding RNA substrates, facilitating site-specific modifications [ ]. tRNA (guanine(10)-N(2))-methyltransferase (TRMT11) is a catalytic subunit of an S-adenosyl-L-methionine-dependen... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25904"
] | [
"Tmrp11_N"
] | [
4871
] | 1 | [
"EC",
"METACYC",
"REACTOME"
] | [
"2.1.1.214",
"PWY-6829",
"R-HSA-6782315"
] | [
"EC:2.1.1.214",
"METACYC:PWY-6829",
"REACTOME:R-HSA-6782315"
] | 3 | [] | 0 | [
"PUB00020491"
] | [
"15899842"
] | [
"Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4871
] | 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... | [
4,
1,
2,
1,
6,
4,
1,
2,
10,
1,
1,
3
] | 12 | true | Domain | tRNA (guanine(10)-N(2))-methyltransferase TRMT11, N-terminal domain | tRNA (guanine(10)-N(2))-methyltransferase TRMT11, N-terminal domain | TRMT11_N | 1 |
IPR059074 | 59,074 | Z280C/D-like, C2H2 zinc finger | Znf-C2H2_Z280C_D | Domain | 2,539 | false | false | This C2H2 zinc finger domain is found in several zinc-finger proteins such as Zinc finger protein 280C and 280D as well as protein Pogo transposable element with ZNF domain (POGZ). 280C and 280D are probably involved in transcriptional regulation. POGZ plays a role in mitotic cell cycle progression and is involved in k... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25414"
] | [
"zf-C2H2_Z280C_D"
] | [
2539
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00107331",
"PUB00160208"
] | [
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"20562864",
"26721387"
] | [
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptides for the regulation of gene expression.",
"Zinc finger proteins: new ... | [
2002,
2007,
2005,
2005,
1999,
2001,
2010,
2016
] | 8 | [
"IPR013087"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
2539
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
15,
10,
14,
19
] | 4 | true | Domain | Z280C/D-like, C2H2 zinc finger | Z280C/D-like, C2H2 zinc finger | Znf-C2H2_Z280C_D | 1 |
IPR059076 | 59,076 | Mycoplasma MPN_270/MG131 three-helix transmembrane protein | MPN_270 | Family | 8 | false | false | This entry represents a family of small three-helix transmembrane proteins found in Mycoplasma species. Members contain three predicted transmembrane helices that form a three-helix bundle. In Mycoplasma genitalium, this protein (MG131) has been experimentally demonstrated to be non-essential for growth as determined b... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045746",
"PF25854"
] | [
"MPN270",
"MPN_270"
] | [
5,
8
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Mycoplasma MPN_270/MG131 three-helix transmembrane protein | Mycoplasma MPN_270/MG131 three-helix transmembrane protein | MPN_270 | 4 |
IPR059077 | 59,077 | YopJ | YopJ | Family | 23 | false | false | This entry represents the uncharacterised YopJ protein in bacilli bacteria. The protein is derived from the SPbeta prophage. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26333"
] | [
"YopJ_bacilli"
] | [
23
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Bacillus phage SPbeta"
] | [
22,
1
] | 2 | [] | [] | 0 | true | Family | YopJ | YopJ | YopJ | 1 |
IPR059078 | 59,078 | Nuclear transport factor 2-like domain, nematodes | NTF2-like_nem | Domain | 30 | false | false | This entry represents a domain from a set of uncharacterised proteins in nematodes found in species such as Caenorhabditis elegans. This domain is typically around 110-130 amino acids in length. This domain belongs to the NTF2-like superfamily, characterised by a partial β-barrel structure with α helices enclosing a so... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26531"
] | [
"NTF2_4"
] | [
30
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Caenorhabditis"
] | [
30
] | 1 | [
"Caenorhabditis elegans"
] | [
7
] | 1 | true | Domain | Nuclear transport factor 2-like domain, nematodes | Nuclear transport factor 2-like domain, nematodes | NTF2-like_nem | 2 |
IPR059079 | 59,079 | Disrupted in renal carcinoma protein 1 | DIRC1 | Family | 14 | false | false | This protein family includes human Disrupted in renal carcinoma protein 1 (DIRC1), which has been associated with progression and poor prognosis in gastric cancer [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26134"
] | [
"DIRC1"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161215"
] | [
"30575946"
] | [
"Significant association of DIRC1 overexpression with tumor progression and poor prognosis in gastric cancer."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Boreoeutheria"
] | [
14
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Disrupted in renal carcinoma protein 1 | Disrupted in renal carcinoma protein 1 | DIRC1 | 5 |
IPR059080 | 59,080 | PTC1-like, winged helix-turn-helix domain | WHD_PTC1 | Domain | 3,309 | false | false | This entry represents a winged helix-turn-helix (wHTH) domain found in plant proteins involved in reproductive development, particularly male gametogenesis, meiosis, and tapetal cell development. These proteins generally function as transcription factors regulating key processes in pollen development and meiotic chromo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25874"
] | [
"WHD_plant_repro"
] | [
3309
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00095516",
"PUB00095517",
"PUB00095518",
"PUB00134264",
"PUB00134265",
"PUB00160826",
"PUB00160943",
"PUB00161539",
"PUB00161540",
"PUB00161541"
] | [
"11459834",
"12783800",
"19204280",
"12461128",
"11696184",
"7824655",
"21515697",
"12135930",
"10654613",
"18272967"
] | [
"SWITCH1 (SWI1): a novel protein required for the establishment of sister chromatid cohesion and for bivalent formation at meiosis.",
"The meiotic protein SWI1 is required for axial element formation and recombination initiation in Arabidopsis.",
"Maize AMEIOTIC1 is essential for multiple early meiotic processe... | [
2001,
2003,
2009,
2002,
2001,
1994,
2011,
2002,
2000,
2008
] | 10 | [] | [] | 0 | 0 | null | [
"Viridiplantae"
] | [
3309
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
32,
20,
20
] | 3 | true | Domain | PTC1-like, winged helix-turn-helix domain | PTC1-like, winged helix-turn-helix domain | WHD_PTC1 | 1 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.