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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054364 | 54,364 | Ca3427-like, PBP 2 | Ca3427-like_PBP2 | Domain | 2,602 | false | false | This entry represents domain II of CA3427 from Candida albicans ( ), which consists of a 5 stranded β-sheet [ ]. Members of this group are found in fungi and bacteria. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22384"
] | [
"PBP2_Ca3427_like"
] | [
2602
] | 1 | [] | [] | [] | 0 | [
"2x7p",
"2x7q"
] | 2 | [
"PUB00066137"
] | [
"21494601"
] | [
"The conserved Candida albicans CA3427 gene product defines a new family of proteins exhibiting the generic periplasmic binding protein structural fold."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
907,
1690,
5
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Ca3427-like, PBP 2 | Ca3427-like, PBP 2 | Ca3427-like_PBP2 | 2 |
IPR054365 | 54,365 | Lreu_0056-like | Lreu_0056-like | Domain | 268 | false | false | This entry represents a domain found in a family of uncharacterised Lactobacillus proteins. The structure of a family member, a hypothetical protein Lreu_0056 from Lactobacillus reuteri ( ), adopts an α+β structure in order α(2)-β(5)-α(2) consisting of a five-stranded antiparallel β-sheet with helices packed on one sid... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF22125",
"cd15778"
] | [
"Lreu_0056_like",
"Lreu_0056_like"
] | [
268,
187
] | 2 | [] | [] | [] | 0 | [
"2mqd"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
268
] | 1 | [] | [] | 0 | true | Domain | Lreu_0056-like | Lreu_0056-like | Lreu_0056-like | 5 |
IPR054366 | 54,366 | RepB/MobA-like, C-terminal domain | RepB/MobA-like_C | Domain | 238 | false | false | This entry represents a domain found at the C-terminal of DNA primase from Acidithiobacillus ferrooxidans (RepB), Mobilization protein A from Escherichia coli (MobA) and similar sequences mainly found in proteobacteria. This domain adopts a helical configuration [ ]. RepB is a DNA-primase produced by P4-like phages. It... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22448"
] | [
"RepB_primase_C"
] | [
238
] | 1 | [] | [] | [] | 0 | [
"3h20"
] | 1 | [
"PUB00052236",
"PUB00089696",
"PUB00154402"
] | [
"19416864",
"8955311",
"1738602"
] | [
"Structure and function of primase RepB' encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode.",
"The primase of broad-host-range plasmid R1162 is active in conjugal transfer.",
"In vitro cleavage of double- and single-stranded DNA by plasmid RSF1010-encoded mobilizatio... | [
2009,
1996,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Gigaspora margarita",
"Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2)",
"unclassified sequences"
] | [
231,
1,
1,
5
] | 4 | [] | [] | 0 | true | Domain | RepB/MobA-like, C-terminal domain | RepB/MobA-like, C-terminal domain | RepB/MobA-like_C | 4 |
IPR054367 | 54,367 | Oxo-glucose-6-phosphate:glutamate aminotransferase, N-terminal domain | NtdA_N | Domain | 78 | false | false | This entry represents the N-terminal domain of 3-oxo-glucose-6-phosphate:glutamate aminotransferase from Bacillus subtilis (NtdA), which is not found in other aminotransferases and consists of two-stranded parallel β-sheet flanked by two α-helices [ ]. This domain may be involved in protein-protein interactions. NtdA i... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22127"
] | [
"NtdA_N"
] | [
78
] | 1 | [] | [] | [] | 0 | [
"4k2b",
"4k2i",
"4k2m",
"7kz3",
"7kz5",
"7kz6",
"7kzd"
] | 7 | [
"PUB00154124",
"PUB00154444",
"PUB00154445"
] | [
"24097983",
"14612444",
"23586652"
] | [
"The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.",
"RNA polymerase mutation activates the production of a dormant antibiotic 3,3'-neotrehalosadiamine via an autoinduction mechanism in Bacillus subtil... | [
2013,
2004,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
78
] | 1 | [] | [] | 0 | true | Domain | Oxo-glucose-6-phosphate:glutamate aminotransferase, N-terminal domain | Oxo-glucose-6-phosphate:glutamate aminotransferase, N-terminal domain | NtdA_N | 1 |
IPR054368 | 54,368 | Alp7A-like, C-terminal domain | Alp7A-like_C | Domain | 699 | false | false | Bacterial Actin-Like Proteins (ALPs) participate in many biologically, clinically and commercially important processes, including segregation of low-copy plasmids. Alp7A is a bacterial actin that functions in plasmid segregation. It is composed of two domains both structurally similar to domains of actin-like ATPases (... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22128"
] | [
"Alp7A_like_C"
] | [
699
] | 1 | [] | [] | [] | 0 | [
"5ec0"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Opisthokonta"
] | [
694,
3,
2
] | 3 | [] | [] | 0 | true | Domain | Alp7A-like, C-terminal domain | Alp7A-like, C-terminal domain | Alp7A-like_C | 4 |
IPR054369 | 54,369 | CRISPR-associated endonuclease Cas9, wedge domain | Cas9_WED | Domain | 107 | false | false | In the type II CRISPR-Cas system, the Cas9 effector nuclease associates with dual guide RNAs (crRNA and trans-activating crRNA (tracrRNA)) and cleaves double-stranded DNA targets complementary to the crRNA guide. Cas9 is composed of multiple domains. This entry represents the so-called wedge (WED) domain that is found ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22129"
] | [
"CjCas9_WED-like"
] | [
107
] | 1 | [] | [] | [] | 0 | [
"5x2g",
"5x2h"
] | 2 | [
"PUB00091160"
] | [
"28306506"
] | [
"Crystal Structure of the Minimal Cas9 from Campylobacter jejuni Reveals the Molecular Diversity in the CRISPR-Cas9 Systems."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Campylobacterales"
] | [
107
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease Cas9, wedge domain | CRISPR-associated endonuclease Cas9, wedge domain | Cas9_WED | 5 |
IPR054370 | 54,370 | T4SS protein CagL-like | CagL-like | Family | 618 | false | false | This family includes CagL from Helicobacter pylori ( ), a type IV secretion system (T4SS) pilus protein that interacts with several integrins through an helical RGD motif. It shows an all-α structure that undergoes specific conformational changes depending on pH variations. These changes also affect the exposure of the... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22450"
] | [
"CagL"
] | [
618
] | 1 | [] | [] | [] | 0 | [
"3zci",
"3zcj",
"4cii",
"4x5u",
"4yvm"
] | 5 | [
"PUB00153843",
"PUB00153844",
"PUB00153845",
"PUB00153846"
] | [
"24076404",
"24816107",
"25837254",
"25839651"
] | [
"A helical RGD motif promoting cell adhesion: crystal structures of the Helicobacter pylori type IV secretion system pilus protein CagL.",
"Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL.",
"Integrin engagement by the helical RGD moti... | [
2013,
2014,
2015,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Helicobacter pylori"
] | [
618
] | 1 | [] | [] | 0 | true | Family | T4SS protein CagL-like | T4SS protein CagL-like | CagL-like | 3 |
IPR054371 | 54,371 | Exosome RNA binding protein RRP4, N-terminal domain | RRP4_N | Domain | 386 | false | false | This domain is found N-terminal in exosome RNA binding protein RRP4 and related proteins from archaea [ , , , , ]. RRP4 is a part of the exosome regulatory substrate recognition platform. This domain is structurally similar to ribosomal L27 protein. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22625"
] | [
"ECR1_N_2"
] | [
386
] | 1 | [] | [] | [] | 0 | [
"2ba0",
"2je6",
"2jea",
"2jeb",
"3l7z",
"4ba1",
"4ba2"
] | 7 | [
"PUB00035570",
"PUB00035572",
"PUB00055172",
"PUB00065825",
"PUB00152001"
] | [
"16285927",
"17380186",
"20090900",
"23376952",
"25043052"
] | [
"Structural framework for the mechanism of archaeal exosomes in RNA processing.",
"RNA channelling by the archaeal exosome.",
"Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.",
"Crystal structure of an RNA-bound 11-subunit eukaryotic exosom... | [
2005,
2007,
2010,
2013,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Spironucleus salmonicida",
"ecological metagenomes"
] | [
373,
1,
12
] | 3 | [] | [] | 0 | true | Domain | Exosome RNA binding protein RRP4, N-terminal domain | Exosome RNA binding protein RRP4, N-terminal domain | RRP4_N | 7 |
IPR054372 | 54,372 | Gp38-like | Gp38-like | Family | 227 | false | false | This entry represents a family of proteins from tailed bacteriophages, including the gene product 38 (Gp38) from Lactococcus phage, a short protein consisting of 71 amino acids. It is also known as the AbiQ resistance protein due to its involvement in escaping bacterial killing mediated by the AbiQ protein. Gp38 is exp... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22130"
] | [
"Phage_gp38"
] | [
227
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154446"
] | [
"23813728"
] | [
"Effect of the abortive infection mechanism and type III toxin/antitoxin system AbiQ on the lytic cycle of Lactococcus lactis phages."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes"
] | [
6,
221
] | 2 | [] | [] | 0 | true | Family | Gp38-like | Gp38-like | Gp38-like | 4 |
IPR054373 | 54,373 | CRISPR-associated endonuclease Cas9, PI domain, C-terminal, campylobacterales | Cas9_PI_C_campylobact | Domain | 118 | false | false | In the type II CRISPR-Cas system, the Cas9 effector nuclease associates with dual guide RNAs (crRNA and trans-activating crRNA (tracrRNA)) and cleaves double-stranded DNA targets complementary to the crRNA guide. Cas9 is composed of multiple domains. This entry represents the C-terminal lobe of the so-called PAM-intera... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22131"
] | [
"CjCas9_PI_CTD"
] | [
118
] | 1 | [] | [] | [] | 0 | [
"5x2g",
"5x2h"
] | 2 | [
"PUB00091160"
] | [
"28306506"
] | [
"Crystal Structure of the Minimal Cas9 from Campylobacter jejuni Reveals the Molecular Diversity in the CRISPR-Cas9 Systems."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Campylobacterales"
] | [
118
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease Cas9, PI domain, C-terminal, campylobacterales | CRISPR-associated endonuclease Cas9, PI domain, C-terminal, campylobacterales | Cas9_PI_C_campylobact | 2 |
IPR054374 | 54,374 | AF1548-like, C-terminal | AF1548-like_C | Domain | 269 | false | false | This domain is found at the C-terminal of the uncharacterised protein AF_1548 from Archaeoglobus fulgidus and similar prokaryotic proteins. This domain is often found associated with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22357"
] | [
"AF1548-like_C"
] | [
269
] | 1 | [] | [] | [] | 0 | [
"1y88"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
29,
235,
5
] | 3 | [] | [] | 0 | true | Domain | AF1548-like, C-terminal | AF1548-like, C-terminal | AF1548-like_C | 9 |
IPR054375 | 54,375 | MrkH-like, YcgR-like domain | MrkH_YcgR-like_dom | Domain | 144 | false | false | This entry represents the YcgR-like domain found at the N-terminal of MrkH ( ) from Klebsiella pneumoniae and similar sequences [ ]. Some members included in this contain a PilZ domain ( ) at the C-terminal. MrkH is a c-di-GMP-related transcriptional regulator that affects type 3 fimbrial expression in response to cell... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22363"
] | [
"MrkH_YcgR_like"
] | [
144
] | 1 | [] | [] | [] | 0 | [
"5ejl",
"5kec",
"5ked",
"5kgo"
] | 4 | [
"PUB00154080"
] | [
"27650952"
] | [
"The PilZ domain of MrkH represents a novel DNA binding motif."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales",
"Thelohanellus kitauei"
] | [
143,
1
] | 2 | [] | [] | 0 | true | Domain | MrkH-like, YcgR-like domain | MrkH-like, YcgR-like domain | MrkH_YcgR-like_dom | 7 |
IPR054376 | 54,376 | CdsD, periplasmic PD2 domain | CdsD_PD2 | Domain | 48 | false | false | This domain is found in CdsD from Chlamydia trachomatis ( ) and similar sequences from Chlamydia. CdsD is a structural contact-dependent secretion (Cds) protein that form part of the basal body of the type III secretion system (T3SS) injectisome of the bacteria. The periplasmic part of this protein contains at least 3 ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22598"
] | [
"CdsD_PD2"
] | [
48
] | 1 | [] | [] | [] | 0 | [
"4qo6",
"4qq0"
] | 2 | [
"PUB00076172",
"PUB00153859"
] | [
"23908767",
"26914207"
] | [
"In situ structural analysis of the Yersinia enterocolitica injectisome.",
"The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis."
] | [
2013,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
47,
1
] | 2 | [] | [] | 0 | true | Domain | CdsD, periplasmic PD2 domain | CdsD, periplasmic PD2 domain | CdsD_PD2 | 9 |
IPR054377 | 54,377 | tRNA(Ile)-lysidine synthase-like, C-terminal domain | TilS-like_C | Domain | 10 | false | false | This entry represents the C-terminal domain of tRNA(Ile)-lysidine synthase from Aquifex aeolicus (TilS) and similar bacterial sequences. TilS ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner [ ]. It is probably implic... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22132"
] | [
"TilS-like"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"1wy5",
"2e21",
"2e89"
] | 3 | [
"PUB00034489"
] | [
"15894617"
] | [
"Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | tRNA(Ile)-lysidine synthase-like, C-terminal domain | tRNA(Ile)-lysidine synthase-like, C-terminal domain | TilS-like_C | 7 |
IPR054378 | 54,378 | Type VI lipoprotein IgE-like, C-terminal domain | IgE-like_C | Domain | 110 | false | false | This entry represents the C-terminal domain of the intracellular growth locus E (IglE) protein from Francisella tularensis subsp. novicida [ ]. The lipoprotein IglE has been identified as a virulence factor that functions as a regulator of the Type IV system-mediated secretion [ ]. This domain is predicted to show a ma... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22361"
] | [
"IglE_N"
] | [
110
] | 1 | [] | [] | [] | 0 | [
"5amt",
"5amu"
] | 2 | [
"PUB00106260",
"PUB00154022"
] | [
"27830989",
"21139203"
] | [
"A mutagenesis-based approach identifies amino acids in the N-terminal part of Francisella tularensis IglE that critically control Type VI system-mediated secretion.",
"Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of intracellular growth locus E (IglE) protein from... | [
2017,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
110
] | 1 | [] | [] | 0 | true | Domain | Type VI lipoprotein IgE-like, C-terminal domain | Type VI lipoprotein IgE-like, C-terminal domain | IgE-like_C | 9 |
IPR054379 | 54,379 | Non-toxic nonhaemagglutinin, helical domain | NTNH_H | Domain | 117 | false | false | This entry represents an elongated helical domain present in Clostridium neurotoxins, including non-toxic nonhaemagglutinin (NTNH). The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin (BoNT) [ , , ]. Bacteria of the Clostridium genus produce protein neurotoxin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22133"
] | [
"Toxin_BN_H"
] | [
117
] | 1 | [] | [] | [] | 0 | [
"3v0a",
"3v0b",
"3vuo",
"4zkt",
"8byp",
"8qft",
"9arj",
"9ark",
"9arl",
"9ea9",
"9qc7",
"9qc8",
"9qcm",
"9qco"
] | 14 | [
"PUB00020995",
"PUB00020996",
"PUB00062647",
"PUB00105422",
"PUB00154288",
"PUB00154289"
] | [
"11233171",
"11595633",
"22363010",
"25592073",
"22828508",
"26639353"
] | [
"Characterization of nicking of the nontoxic-nonhemagglutinin components of Clostridium botulinum types C and D progenitor toxin.",
"Clostridium botulinum and its neurotoxins: a metabolic and cellular perspective.",
"Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.",
"Two-component systems... | [
2000,
2001,
2012,
2015,
2012,
2015
] | 6 | [] | [] | 0 | 0 | null | [
"Clostridia",
"unclassified Caudoviricetes"
] | [
113,
4
] | 2 | [] | [] | 0 | true | Domain | Non-toxic nonhaemagglutinin, helical domain | Non-toxic nonhaemagglutinin, helical domain | NTNH_H | 1 |
IPR054380 | 54,380 | BA_2335-like | BA_2335-like | Family | 134 | false | false | This protein family includes the uncharacterised protein BA_2335 from Bacillus anthracis and similar sequences from Bacilli. It adopts a β-sandwich configuration. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22372"
] | [
"BA_2335-like"
] | [
134
] | 1 | [] | [] | [] | 0 | [
"4h4n"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
134
] | 1 | [] | [] | 0 | true | Family | BA_2335-like | BA_2335-like | BA_2335-like | 7 |
IPR054381 | 54,381 | CydS-like | CydS | Family | 209 | false | false | This entry represents the CydS subunit of the cytochrome bd oxidase [ ]. This protein is very short and forms a single α-helix that is part of the complex [ ]. Members of this family are found in Bacillales. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22282"
] | [
"CydS"
] | [
209
] | 1 | [] | [] | [] | 0 | [
"5doq",
"5ir6"
] | 2 | [
"PUB00153898"
] | [
"27126043"
] | [
"Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
209
] | 1 | [] | [] | 0 | true | Family | CydS-like | CydS-like | CydS | 7 |
IPR054382 | 54,382 | Winged helix domain, alphaproteobacteria | wHTH_alphaproteobact | Domain | 207 | false | false | This entry represents a winged helix-turn-helix (wHTH) domain mainly found in alphaproteobacteria that is likely to be involved in DNA-binding. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22324"
] | [
"HTH_91"
] | [
207
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"marine sediment metagenome"
] | [
206,
1
] | 2 | [] | [] | 0 | true | Domain | Winged helix domain, alphaproteobacteria | Winged helix domain, alphaproteobacteria | wHTH_alphaproteobact | 3 |
IPR054383 | 54,383 | PspA associated protein B-like | PspAB-like | Family | 1,757 | false | false | This entry represents a family of poorly characterised prokaryotic proteins, including PspA associated protein B, a component of the Psp system. It occurs in an operon with a membrane-associated metallopeptidase. In addition, these two genes occur in operon with the PspA-PspAA dyad [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22742"
] | [
"PspAB"
] | [
1757
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00158885"
] | [
"38809013"
] | [
"The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
390,
1343,
24
] | 3 | [] | [] | 0 | true | Family | PspA associated protein B-like | PspA associated protein B-like | PspAB-like | 2 |
IPR054384 | 54,384 | SecDF, P1 head subdomain | SecDF_P1_head | Domain | 27,000 | false | false | This entry represents the head subdomain from P1 domain from SecDF proteins, which constitutes a critical element for proton transport [ , , ]. P1 domain binds an unfolded protein, and undergoes functionally important conformational changes. SecDF functions as a membrane-integrated chaperone that mediates ATP-independe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22599"
] | [
"SecDF_P1_head"
] | [
27000
] | 1 | [
"REACTOME"
] | [
"R-HSA-1222387"
] | [
"REACTOME:R-HSA-1222387"
] | 1 | [
"3aqo",
"3aqp",
"5mg3",
"5xam",
"5xan",
"5xap",
"5yhf"
] | 7 | [
"PUB00059727",
"PUB00102157",
"PUB00152004"
] | [
"21562494",
"27924919",
"28467902"
] | [
"Structure and function of a membrane component SecDF that enhances protein export.",
"A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.",
"Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF."
] | [
2011,
2016,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Siphoviridae sp. ctJ0s2",
"unclassified sequences"
] | [
26264,
67,
84,
1,
584
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | SecDF, P1 head subdomain | SecDF, P1 head subdomain | SecDF_P1_head | 3 |
IPR054385 | 54,385 | Anti-restriction endonuclease | Arn | Family | 116 | false | false | This entry represents Anti-restriction endonuclease from Enterobacteria phage T4 () proteins and similar sequences from tailed bacteriophages. Arn plays a role in the inhibition of the host restriction-modification system. Arn was identified as an inhibitor of the restriction enzyme McrBC. Its structure consists of a t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22134"
] | [
"DM_Arn"
] | [
116
] | 1 | [] | [] | [] | 0 | [
"3wx4"
] | 1 | [
"PUB00153909"
] | [
"25118281"
] | [
"The T4 phage DNA mimic protein Arn inhibits the DNA binding activity of the bacterial histone-like protein H-NS."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
116
] | 1 | [] | [] | 0 | true | Family | Anti-restriction endonuclease | Anti-restriction endonuclease | Arn | 3 |
IPR054386 | 54,386 | RIM, zinc finger | RIM_Znf | Domain | 6,907 | false | false | This entry represents the zinc finger domain of Regulating synaptic membrane exocytosis protein 1/2 (RIM1/2) and related proteins. This domain alone is responsible for the interaction with Munc13-1 by engaging with the Munc13-1 C2A domain [ ]. Structurally, this domain is similar to FIVE zinc fingers. RIM proteins are ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22601"
] | [
"RIM2a_ZnF"
] | [
6907
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-210500",
"R-CEL-212676",
"R-CEL-264642",
"R-CEL-888590",
"R-HSA-181429",
"R-HSA-181430",
"R-HSA-210500",
"R-HSA-212676",
"R-HSA-264642",
"R-HSA-888590",
"R-MMU-181429",
"R-MMU-181430",
"R-MMU-210500",
"R-MMU-212676",
"R-MMU-264642",
"R-MMU-888... | [
"REACTOME:R-CEL-181429",
"REACTOME:R-CEL-181430",
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-264642",
"REACTOME:R-CEL-888590",
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-181430",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-212676",
"REACTOME:R-HSA-264642",
"REACTOME:R-HSA-888... | 24 | [
"2a20",
"2cjs"
] | 2 | [
"PUB00039109",
"PUB00073382",
"PUB00073383",
"PUB00073386",
"PUB00073738"
] | [
"16052212",
"20370319",
"25343783",
"21262468",
"17124501"
] | [
"A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?",
"RIM proteins and their role in synapse function.",
"RIM1 and RIM2 redundantly determine Ca2+ channel density and readily-releasable pool size at a large hindbrain synapse.",
"RIM determines Ca²+ channel density and vesicle docking at the pr... | [
2005,
2010,
2014,
2011,
2006
] | 5 | [
"IPR017455"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
6907
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
139,
14,
16,
16,
29
] | 6 | true | Domain | RIM, zinc finger | RIM, zinc finger | RIM_Znf | 6 |
IPR054387 | 54,387 | Argonaute, N-terminal domain, bacteria | Ago_N_bact | Domain | 8 | false | false | This domain is found at the N-terminal bacterial Argonaute (Ago) [ , ]. Ago binds small RNA or DNA guides, which provide base-pairing specificity for the recognition and cleavage of complementary nucleic acid targets. Bacterial Ago uses 5'-hydroxylated guide RNAs to recognise and cleave single-stranded target sequences... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22136"
] | [
"MpAgo_N-like"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"5i4a",
"5ux0"
] | 2 | [
"PUB00153794",
"PUB00153795"
] | [
"27035975",
"28520746"
] | [
"A bacterial Argonaute with noncanonical guide RNA specificity.",
"DNA recognition by an RNA-guided bacterial Argonaute."
] | [
2016,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Thermotogae"
] | [
8
] | 1 | [] | [] | 0 | true | Domain | Argonaute, N-terminal domain, bacteria | Argonaute, N-terminal domain, bacteria | Ago_N_bact | 3 |
IPR054388 | 54,388 | T6SS, Phospholipase effector Tle1-like, C-terminal domain | Tle1-like_C | Domain | 451 | false | false | This entry represents a domain found in the type VI secretion system (T6SS) Phospholipase effector Tle1 from Pseudomonas aeruginosa ( ) and similar proteins from proteobacteria. Tle1, which hydrolyse membrane phospholipids, is organised into two distinct parts, the phospholipase catalytic module ( ) and the putative me... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22137"
] | [
"T6SS_Tle1-like_C"
] | [
451
] | 1 | [] | [] | [] | 0 | [
"4o5p"
] | 1 | [
"PUB00154252"
] | [
"25084336"
] | [
"Structure of the type VI secretion phospholipase effector Tle1 provides insight into its hydrolysis and membrane targeting."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"Tilletia indica"
] | [
450,
1
] | 2 | [] | [] | 0 | true | Domain | T6SS, Phospholipase effector Tle1-like, C-terminal domain | T6SS, Phospholipase effector Tle1-like, C-terminal domain | Tle1-like_C | 9 |
IPR054390 | 54,390 | Argonaute, N-terminal domain, archaea | Ago_N_arc | Domain | 2 | false | false | Argonaute (Ago) proteins are found in all three domains of life. They share a common molecular architecture, with the C-terminal lobe consisting of the middle (Mid) and PIWI (P element wimpy testis) domains and the N-terminal lobe containing the N-terminal and PIWI-Argonaute-Zwille (PAZ) domains. Archaeal argonaute pro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22138"
] | [
"MjAgo_N-like"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"5g5s",
"5g5t"
] | 2 | [
"PUB00153796"
] | [
"28319084"
] | [
"Structural and mechanistic insights into an archaeal DNA-guided Argonaute protein."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Methanocaldococcus"
] | [
2
] | 1 | [] | [] | 0 | true | Domain | Argonaute, N-terminal domain, archaea | Argonaute, N-terminal domain, archaea | Ago_N_arc | 7 |
IPR054391 | 54,391 | DNA repair helicase XPD, arch domain | XPD_arch | Domain | 14 | false | false | This domain is found in DNA repair helicase XPD from Sulfurisphaera tokodaii ( ) and similar archaeal proteins. XPD, which functions as a 5'-3' DNA helicase, shows three major domains. This entry represents the central domain, called arch domain, which folds into a mixed α/β topology with a four-stranded antiparallel β... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22139"
] | [
"XPD_arch"
] | [
14
] | 1 | [] | [] | [] | 0 | [
"2vl7"
] | 1 | [
"PUB00049787"
] | [
"18510925"
] | [
"Structure of the DNA repair helicase XPD."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
14
] | 1 | [] | [] | 0 | true | Domain | DNA repair helicase XPD, arch domain | DNA repair helicase XPD, arch domain | XPD_arch | 9 |
IPR054392 | 54,392 | VipD-like, C-terminal domain | VipD-like_C | Domain | 13 | false | false | This domain is found in VipD from Legionella pneumophila (effector vacuolar protein sorting inhibitor protein D, ), which localises to early endosomal membranes and alters their lipid and protein composition. This process protects the pathogen from endosomal fusion. VipD adopts a two-domain fold, with a N-terminal doma... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22140"
] | [
"VipD-like_C"
] | [
13
] | 1 | [] | [] | [] | 0 | [
"4akf",
"4kyi"
] | 2 | [
"PUB00063981",
"PUB00154325"
] | [
"23271971",
"25114243"
] | [
"VipD of Legionella pneumophila targets activated Rab5 and Rab22 to interfere with endosomal trafficking in macrophages.",
"Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5."
] | [
2012,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Legionella"
] | [
13
] | 1 | [] | [] | 0 | true | Domain | VipD-like, C-terminal domain | VipD-like, C-terminal domain | VipD-like_C | 7 |
IPR054393 | 54,393 | Thiaminase-1, insert domain | Thiaminase-1_dom | Domain | 104 | false | false | This domain is found in Thiaminase-1 from Paenibacillus thiaminolyticus and similar bacterial sequences. This enzyme degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles. This entry represents one of its two α/β-type domains, which is inserted into the other ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22141"
] | [
"Thiaminase-1_dom"
] | [
104
] | 1 | [] | [] | [] | 0 | [
"2thi",
"3thi",
"4kys",
"4thi"
] | 4 | [
"PUB00032916",
"PUB00154279"
] | [
"9843405",
"24079939"
] | [
"Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 A resolution.",
"Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture ."
] | [
1998,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Ancylostoma ceylanicum",
"Bacteria"
] | [
1,
103
] | 2 | [] | [] | 0 | true | Domain | Thiaminase-1, insert domain | Thiaminase-1, insert domain | Thiaminase-1_dom | 4 |
IPR054395 | 54,395 | Capsid protein, C-terminal domain, fungal virus | P2_C_fungal_virus | Domain | 9 | false | false | This domain is found at the C-terminal end of Capsid protein from Penicillium chrysogenum virus (P2), which self-assembles to form an icosahedral capsid with a T=1 symmetry. It is organised into two domains with similar α-β topology ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22144"
] | [
"Fungal_virus_P2_C"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"3j3i"
] | 1 | [
"PUB00151866"
] | [
"24821769"
] | [
"Cryo-EM near-atomic structure of a dsRNA fungal virus shows ancient structural motifs preserved in the dsRNA viral lineage."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Chrysoviridae",
"viral metagenome"
] | [
8,
1
] | 2 | [] | [] | 0 | true | Domain | Capsid protein, C-terminal domain, fungal virus | Capsid protein, C-terminal domain, fungal virus | P2_C_fungal_virus | 4 |
IPR054396 | 54,396 | GtfA, extended beta-sheet meander domain | GtfA_EBD | Domain | 767 | false | false | This entry represents the extended β-sheet meander domain (EBD) of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit [ , ] and similar proteins mainly from firmicutes. GtfA is the core enzyme of the OGT complex, which also includes the co-activator GtfB, to glycosylate the serine-rich repeat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22145"
] | [
"GtfA_EBD"
] | [
767
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.4.1.-",
"PWY-1901",
"PWY-1961",
"PWY-1981",
"PWY-2021",
"PWY-2881",
"PWY-2901",
"PWY-2902",
"PWY-4421",
"PWY-4801",
"PWY-5094",
"PWY-5105",
"PWY-5129",
"PWY-5139",
"PWY-5160",
"PWY-5161",
"PWY-5268",
"PWY-5284",
"PWY-5286",
"PWY-5310",
"PWY-5312",
"PWY-5313",
"PWY-5317... | [
"EC:2.4.1.-",
"METACYC:PWY-1901",
"METACYC:PWY-1961",
"METACYC:PWY-1981",
"METACYC:PWY-2021",
"METACYC:PWY-2881",
"METACYC:PWY-2901",
"METACYC:PWY-2902",
"METACYC:PWY-4421",
"METACYC:PWY-4801",
"METACYC:PWY-5094",
"METACYC:PWY-5105",
"METACYC:PWY-5129",
"METACYC:PWY-5139",
"METACYC:PWY-5... | 200 | [
"4pqg",
"5e9t",
"5e9u"
] | 3 | [
"PUB00153993",
"PUB00153994"
] | [
"26884191",
"24936067"
] | [
"Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein.",
"Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins."
] | [
2016,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillati",
"human gut metagenome"
] | [
765,
2
] | 2 | [] | [] | 0 | true | Domain | GtfA, extended beta-sheet meander domain | GtfA, extended beta-sheet meander domain | GtfA_EBD | 7 |
IPR054397 | 54,397 | LicP, N-terminal prodomain | LicP_N_prodom | Domain | 3 | false | false | LicP is a class II LanP protease that is involved in the biosynthesis of the lantibiotic lichenicidin. This enzyme is an extracellularly located serine protease expressed by some strains of Bacillus licheniformis and undergoes a self-cleavage maturation resulting in two fragments, the N-terminal prodomain (this entry) ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22146"
] | [
"LicP_NPro"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"4zoq"
] | 1 | [
"PUB00154035"
] | [
"30090246"
] | [
"Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
3
] | 1 | [] | [] | 0 | true | Domain | LicP, N-terminal prodomain | LicP, N-terminal prodomain | LicP_N_prodom | 2 |
IPR054398 | 54,398 | AcrIC5-like domain | AcrIC5-like_dom | Domain | 43 | false | false | This entry represents a domain that covers the whole length of AcrIC5 and is found at the C-terminal end of other proteins from tailed bacteriophages and bacterial prophages. AcrIC5 is one of the earliest discovered AcrIC proteins that inhibit type I-C CRISPR-Cas systems. AcrIC5 adopts an α/β structure consisting of a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22147"
] | [
"AcrIC5"
] | [
43
] | 1 | [] | [] | [] | 0 | [
"7yhr"
] | 1 | [
"PUB00153792"
] | [
"35952606"
] | [
"High-resolution crystal structure of the anti-CRISPR protein AcrIC5."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
37,
6
] | 2 | [] | [] | 0 | true | Domain | AcrIC5-like domain | AcrIC5-like domain | AcrIC5-like_dom | 9 |
IPR054399 | 54,399 | Fervidolysin-like, N-terminal prodomain | Fervidolysin-like_N_prodom | Domain | 3,156 | false | false | This entry represents the N-terminal prodomain of Fervidolysin from Fervidobacterium pennivorans, an extracellular subtilisin-like serine protease able to degrade keratin into peptides [ , ]. This domain folds into a globular α/β structure consisting of four-stranded antiparallel β-sheet and two α-helices packed on one... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22148"
] | [
"Fervidolysin_NPro-like"
] | [
3156
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.21.-",
"PWY-7884"
] | [
"EC:3.4.21.-",
"METACYC:PWY-7884"
] | 2 | [
"1r6v",
"1spb"
] | 2 | [
"PUB00030557",
"PUB00154434"
] | [
"14687574",
"16535379"
] | [
"Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin.",
"Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales."
] | [
2004,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
107,
2939,
28,
82
] | 4 | [] | [] | 0 | true | Domain | Fervidolysin-like, N-terminal prodomain | Fervidolysin-like, N-terminal prodomain | Fervidolysin-like_N_prodom | 7 |
IPR054400 | 54,400 | Fervidolysin, second beta-sandwich domain | Fervidolysin_SD2 | Domain | 30 | false | false | This entry represents the C-terminal second β-sandwich domain (SD2) present in Fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme that allows this bacterium to grow on native feathers [ ] and similar sequences mainly found in Thermotogales. This domain shows a pair of four-stranded β-sheets [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22349"
] | [
"Fervidolysin_SD2"
] | [
30
] | 1 | [] | [] | [] | 0 | [
"1r6v"
] | 1 | [
"PUB00030557",
"PUB00154434"
] | [
"14687574",
"16535379"
] | [
"Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin.",
"Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales."
] | [
2004,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Thermotogae"
] | [
30
] | 1 | [] | [] | 0 | true | Domain | Fervidolysin, second beta-sandwich domain | Fervidolysin, second beta-sandwich domain | Fervidolysin_SD2 | 8 |
IPR054401 | 54,401 | Type IV pilin Tt1219-like, C-terminal | Tt1219-like_C | Domain | 10 | false | false | This entry is found at the C-terminal of the type IV pilin Tt1219 from Thermus thermophilus ( ) and similar sequences. This protein is likely involved in the formation of polymers that extend from the surface of the bacterial cell and could mediate a wide variety of functions such as adhesion, motility and natural comp... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22149"
] | [
"Tt1219-like"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"5g23",
"5g24"
] | 2 | [
"PUB00154303"
] | [
"27612581"
] | [
"Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Thermus"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | Type IV pilin Tt1219-like, C-terminal | Type IV pilin Tt1219-like, C-terminal | Tt1219-like_C | 8 |
IPR054402 | 54,402 | Type IV pilin Tt1218-like domain | Tt1218-like_dom | Domain | 1,642 | false | false | This entry represents a domain found in Tt1218 from Thermus thermophilus ( ) and similar sequences from proteobacteria. Tt1218 is a type IV pilin likely involved in the formation of polymers that extend from the surface of the bacterial cell and could mediate a wide variety of functions such as adhesion, motility and n... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22150"
] | [
"Tt1218-like"
] | [
1642
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154303"
] | [
"27612581"
] | [
"Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1614,
2,
26
] | 3 | [] | [] | 0 | true | Domain | Type IV pilin Tt1218-like domain | Type IV pilin Tt1218-like domain | Tt1218-like_dom | 7 |
IPR054403 | 54,403 | RNA-dependent RNA polymerase, palm domain, ribovirus | RdRp_palm_ribovirus | Domain | 76 | false | false | This entry represents predicted palm domain of RdRp from viruses. The replicase has a non-canonical arrangement in the palm sub-domain of the RNA-dependent RNA polymerase (RdRP), with a sequence permutation where the active site is anchored that is also found in Birnaviridae [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22152"
] | [
"Permu_RdRp_palm"
] | [
76
] | 1 | [] | [] | [] | 0 | [
"4xha",
"4xhi",
"5cx6",
"5cyr",
"7om2",
"7om6",
"7om7",
"7om9",
"7oma"
] | 9 | [
"PUB00154157",
"PUB00154158"
] | [
"26625123",
"34203380"
] | [
"The Structure of the RNA-Dependent RNA Polymerase of a Permutotetravirus Suggests a Link between Primer-Dependent and Primer-Independent Polymerases.",
"Snapshots of a Non-Canonical RdRP in Action."
] | [
2015,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Neoptera",
"Viruses"
] | [
11,
65
] | 2 | [] | [] | 0 | true | Domain | RNA-dependent RNA polymerase, palm domain, ribovirus | RNA-dependent RNA polymerase, palm domain, ribovirus | RdRp_palm_ribovirus | 9 |
IPR054405 | 54,405 | Elongation factor SelB, second winged-helix domain | SelB_WH2 | Domain | 3 | false | false | This domain is found in Elongation factor SelB from Aquifex aeolicus ( ) and similar prokaryotic proteins. SelB is a selenocysteine(Sec)-specific elongation factor that brings the selenocysteinyl-tRNA(Sec) to the ribosome. It consists of three EF-Tu-like domains (D1-3, where is the first one), followed by four winged-h... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22154"
] | [
"SelB_WH2"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"4zu9"
] | 1 | [
"PUB00151844"
] | [
"26304550"
] | [
"Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Aquificaceae"
] | [
3
] | 1 | [] | [] | 0 | true | Domain | Elongation factor SelB, second winged-helix domain | Elongation factor SelB, second winged-helix domain | SelB_WH2 | 9 |
IPR054406 | 54,406 | Mre11, accessory DNA binding capping domain | Mre11_acc_DNA_cap | Domain | 5 | false | false | This entry represents the accessory DNA binding capping domain found in Thermotoga maritima Mre11. Mre11, together with Rad50, form the MR protein complex involved in DNA double-strand break repair [ , ]. This domain forms the nuclease module with the phosphodiesterase domain at the N-terminal [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22155"
] | [
"Mre11_acc_DNA_cap"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"2q8u",
"3qg5",
"3thn",
"3tho",
"4nzv",
"4o24",
"4o43",
"4o4k",
"4o5g",
"6asc",
"6x1y",
"6x1z"
] | 12 | [
"PUB00055796",
"PUB00057008",
"PUB00091856",
"PUB00154076",
"PUB00154077"
] | [
"21458667",
"21937514",
"24316220",
"20122942",
"33115610"
] | [
"The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair.",
"ATP driven structural changes of the bacterial Mre11:Rad50 catalytic head complex.",
"DNA double-strand break repair pathway choice is directed by distinct MRE11 nuclease activities.",
"Crystal structure of... | [
2011,
2011,
2014,
2010,
2021
] | 5 | [] | [] | 0 | 0 | null | [
"Thermotoga"
] | [
5
] | 1 | [] | [] | 0 | true | Domain | Mre11, accessory DNA binding capping domain | Mre11, accessory DNA binding capping domain | Mre11_acc_DNA_cap | 5 |
IPR054407 | 54,407 | Thiaminase I-like, N-terminal domain | Thiaminase_I-like_N | Domain | 6 | false | false | This entry represents a domain found at the the N-terminal end of Thiaminase I from the amoeba Naegleria gruberi ( ) and similar sequences from lower eukaryotes. This enzyme catalyse the elimination of the thiazole ring moiety from thiamin through substitution of the methylene group. This domain has thiaminase I activi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22156"
] | [
"Thiaminase_I-like_N"
] | [
6
] | 1 | [] | [] | [] | 0 | [
"4hcw",
"4hcy"
] | 2 | [
"PUB00154280"
] | [
"24351929"
] | [
"Structure of a eukaryotic thiaminase I."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Naegleria"
] | [
6
] | 1 | [] | [] | 0 | true | Domain | Thiaminase I-like, N-terminal domain | Thiaminase I-like, N-terminal domain | Thiaminase_I-like_N | 1 |
IPR054409 | 54,409 | Amylopullulanase, X25 domain | X25_BaPul-like | Domain | 1,348 | false | false | X25 is a domain inserted in X45 domain of Bacillus acidopullulyticus pullulanase. This type of insertion is common in proteins containing X45-X25 pair. X25 domain itself is also found in tandem copies, such as in the highly modular amylopullulanase from Geobacillus stearothermophilus [ ]. It is likely that this domain ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22058"
] | [
"X25_BaPul_like"
] | [
1348
] | 1 | [
"EC",
"EC"
] | [
"3.2.1.1",
"3.2.1.41"
] | [
"EC:3.2.1.1",
"EC:3.2.1.41"
] | 2 | [
"2wan"
] | 1 | [
"PUB00080513"
] | [
"19382205"
] | [
"Structure of a pullulanase from Bacillus acidopullulyticus."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1319,
22,
7
] | 3 | [] | [] | 0 | true | Domain | Amylopullulanase, X25 domain | Amylopullulanase, X25 domain | X25_BaPul-like | 4 |
IPR054410 | 54,410 | ORF239-like | ORF239-like | Family | 4 | false | false | This entry represents a family of viral proteins, including ORF239 from Pyrobaculum Spherical Virus ( ), which shows an all-α configuration [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22056"
] | [
"ORF239-like"
] | [
4
] | 1 | [] | [] | [] | 0 | [
"2x3m"
] | 1 | [
"PUB00054436"
] | [
"20419351"
] | [
"The Scottish Structural Proteomics Facility: targets, methods and outputs."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Alphaglobulovirus"
] | [
4
] | 1 | [] | [] | 0 | true | Family | ORF239-like | ORF239-like | ORF239-like | 7 |
IPR054411 | 54,411 | BVU_2266-like | BVU_2266-like | Family | 28 | false | false | This family represents BVU_2266 from Phocaeicola vulgatus ( ) and similar sequences from bacteroidetes. Members of this family show 16-stranded β-barrels resembling outer membrane porins. The interior of the barrels is mostly occupied by an insert with a partially helical structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22054"
] | [
"BVU_2266-like"
] | [
28
] | 1 | [] | [] | [] | 0 | [
"3tzg"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
28
] | 1 | [] | [] | 0 | true | Family | BVU_2266-like | BVU_2266-like | BVU_2266-like | 3 |
IPR054412 | 54,412 | GndA domain | GndA_dom | Domain | 2 | false | false | This domain covers the whole protein sequence in GndA from Escherichia coli, a small open reading frame (smORF)-encoded heat shock protein contained entirely within the 6-phosphogluconate dehydrogenase Gnd ( ) that is predicted to form a transmembrane helix [ ]. It is also found in combination with other domains in oth... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22051"
] | [
"GndA"
] | [
2
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153985"
] | [
"29039649"
] | [
"Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Escherichia coli"
] | [
2
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | GndA domain | GndA domain | GndA_dom | 8 |
IPR054413 | 54,413 | LSO1/LSO2 | LSO1/2 | Domain | 1,780 | false | false | This entry includes Protein LSO1 and LSO2 from Saccharomyces cerevisiae and similar sequences mainly found in fungi. LSO1 is likely to play a role in iron homeostasis. Its paralogue LSO2, which is constitutively expressed, is a ribosome-associated protein required for translational recovery after starvation from statio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22048"
] | [
"LSO1_2-like"
] | [
1780
] | 1 | [] | [] | [] | 0 | [
"6z6j",
"6z6k",
"6zu5",
"8t3a"
] | 4 | [
"PUB00154049",
"PUB00154050"
] | [
"26450372",
"30208026"
] | [
"The late-annotated small ORF LSO1 is a target gene of the iron regulon of Saccharomyces cerevisiae.",
"Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast."
] | [
2015,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1780
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
1
] | 3 | true | Domain | LSO1/LSO2 | LSO1/LSO2 | LSO1/2 | 8 |
IPR054414 | 54,414 | Coiled-coil domain-containing protein 124/Oxs1, C-terminal | Ccdc124/Oxs1_C | Domain | 4,382 | false | false | This entry represents the C-terminal domain found in Coiled-coil domain-containing protein 124 (Ccdc124) from animals and Oxs1 from fission yeasts. Oxs1 (oxidative stress transcription corepressor Oxs1) and Pap1 form a complex to regulate transcription when cells are exposed to diamide or Cd which causes disulfide stre... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06244"
] | [
"Ccdc124"
] | [
4382
] | 1 | [] | [] | [] | 0 | [
"6z6l",
"6zm7",
"6zme",
"8k2c",
"8xsy"
] | 5 | [
"PUB00073830",
"PUB00091062"
] | [
"23894443",
"27664222"
] | [
"Coiled-coil domain containing protein 124 is a novel centrosome and midbody protein that interacts with the Ras-guanine nucleotide exchange factor 1B and is involved in cytokinesis.",
"A Pap1-Oxs1 signaling pathway for disulfide stress in Schizosaccharomyces pombe."
] | [
2013,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"viral metagenome"
] | [
4381,
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",
"Schizosaccharomyces pombe (stra... | [
5,
2,
1,
1,
1,
1,
2,
5,
2,
1,
3
] | 11 | true | Domain | Coiled-coil domain-containing protein 124/Oxs1, C-terminal | Coiled-coil domain-containing protein 124/Oxs1, C-terminal | Ccdc124/Oxs1_C | 9 |
IPR054415 | 54,415 | Sporulation protein 24 | SPO24 | Family | 83 | false | false | This family includes Sporulation protein 24 from Saccharomyces cerevisiae (SPO24) and similar sequences from yeast. SPO24 is a 67-amino-acid protein required for efficient sporulation [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22044"
] | [
"SPO24"
] | [
83
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154242"
] | [
"25127041"
] | [
"SPO24 is a transcriptionally dynamic, small ORF-encoding locus required for efficient sporulation in Saccharomyces cerevisiae."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
83
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Sporulation protein 24 | Sporulation protein 24 | SPO24 | 8 |
IPR054416 | 54,416 | Glutathione S-transferase UstS-like , C-terminal domain | GST_UstS-like_C | Domain | 6,410 | false | false | This domain is found at the C-terminal end of a group of Glutathione transferases (GST) mainly found in fungi and bacteria, including Glutathione S-transferase-like protein ustS from Aspergillus flavus, Beta-etherase from Sphingobium sp. (LigE) and from Phanerodontia chrysosporium (GTE1). UstS is part of the gene clust... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22041"
] | [
"GST_C_7"
] | [
6410
] | 1 | [] | [] | [] | 0 | [
"4f03",
"4g19",
"4lmv",
"4lmw",
"4yam",
"4yan",
"6j3e",
"6j3f",
"6j3g",
"6j3h",
"7yoc",
"7yp0",
"8k2o",
"8k2p"
] | 14 | [
"PUB00082329",
"PUB00082330",
"PUB00082331",
"PUB00153616",
"PUB00153989",
"PUB00153990",
"PUB00153991",
"PUB00153992"
] | [
"27166860",
"26703898",
"24841822",
"26637355",
"28104507",
"30683313",
"30928378",
"23007392"
] | [
"Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post-translationally Modified Peptide Ustiloxin B in Filamentous Fungi.",
"Class of cyclic ribosomal peptide synthetic genes in filamentous fungi.",
"Characterization of the biosynthetic gene cluster for the ribosomally synthesized cyclic pe... | [
2016,
2016,
2014,
2016,
2017,
2019,
2019,
2012
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1156,
5243,
11
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Zea mays"
] | [
1,
1
] | 2 | true | Domain | Glutathione S-transferase UstS-like , C-terminal domain | Glutathione S-transferase UstS-like , C-terminal domain | GST_UstS-like_C | 1 |
IPR054417 | 54,417 | Secreted glycosylated protein U9-ORF | U9-ORF | Family | 14 | false | false | This family represents the secreted glycosylated protein U9-ORF from Mus musculus and similar sequences from vertebrates. U9-ORF is a 118-residues protein encoded by U90926, a long non-coding RNAs (lncRNAs) that has been associated with the proliferation of herpes simplex virus 1 (HSV-1) in retinal photoreceptor cells ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22040"
] | [
"U9-ORF"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154315",
"PUB00154316",
"PUB00154317"
] | [
"33173149",
"34108530",
"36705532"
] | [
"Long noncoding RNA U90926 is crucial for herpes simplex virus type 1 proliferation in murine retinal photoreceptor cells.",
"Human U90926 orthologous long non-coding RNA as a novel biomarker for visual prognosis in herpes simplex virus type-1 induced acute retinal necrosis.",
"Long Noncoding RNA U90926 Is Indu... | [
2020,
2021,
2023
] | 3 | [] | [] | 0 | 0 | null | [
"Boreoeutheria"
] | [
14
] | 1 | [
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2
] | 2 | true | Family | Secreted glycosylated protein U9-ORF | Secreted glycosylated protein U9-ORF | U9-ORF | 4 |
IPR054418 | 54,418 | Aminodeoxyfutalosine deaminase/Imidazolonepropionase-like, composite domain, N-terminal | MQNX/HUTI_composite_N | Domain | 4,377 | false | false | This entry represents the N-terminal segment of the composite domain usually found in metal-dependent hydrolases, including Imidazolonepropionase from Paracoccus denitrificans (HUTI) and Aminodeoxyfutalosine deaminase from Deinococcus radiodurans (MQNX). HUTI catalyses the hydrolytic cleavage of the carbon-nitrogen bon... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22039"
] | [
"HUTI_composite_bact"
] | [
4377
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.5.2.7",
"PWY-5028",
"PWY-5030"
] | [
"EC:3.5.2.7",
"METACYC:PWY-5028",
"METACYC:PWY-5030"
] | 3 | [
"2imr"
] | 1 | [
"PUB00154432"
] | [
"23972005"
] | [
"Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
340,
3858,
134,
45
] | 4 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
8
] | 2 | true | Domain | Aminodeoxyfutalosine deaminase/Imidazolonepropionase-like, composite domain, N-terminal | Aminodeoxyfutalosine deaminase/Imidazolonepropionase-like, composite domain, N-terminal | MQNX/HUTI_composite_N | 4 |
IPR054419 | 54,419 | NSF, AAA+ ATPase lid domain | NSF_ATPase_lid | Domain | 2,856 | false | false | This entry represents the ATPase lid domain of the second AAA+ ATP-binding domain (also known as D2) of animal NSF proteins [ ], which is found at the C terminus. NFS proteins are responsible for essential membrane fusion events. They play the role of a chaperone by activating the SNAP receptor proteins (SNAREs) so tha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21964"
] | [
"NSF_ATPase_lid"
] | [
2856
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.6",
"R-CEL-204005",
"R-CEL-6807878",
"R-CEL-6811434",
"R-CEL-6811438",
"R-CEL-6811440",
"R-DME-204005",
"R-DME-416993",
"R-DME-6807878",
"R-DME-6811434",
"R-DME-6811438",
"R-DME-6811440",
"R-HSA-204005",
"R-HSA-416993",
"R-HSA-6807878",
"R-HSA-6811434",
"R-HSA-6811438",
"R-H... | [
"EC:3.6.4.6",
"REACTOME:R-CEL-204005",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-CEL-6811438",
"REACTOME:R-CEL-6811440",
"REACTOME:R-DME-204005",
"REACTOME:R-DME-416993",
"REACTOME:R-DME-6807878",
"REACTOME:R-DME-6811434",
"REACTOME:R-DME-6811438",
"REACTOME:R-DME-6811440... | 30 | [
"1d2n",
"1nsf",
"3j94",
"3j95",
"3j96",
"3j97",
"3j98",
"3j99",
"6ip2",
"6mdm",
"6mdn",
"6mdo",
"6mdp",
"9nv9",
"9nvd",
"9ojr",
"9oju",
"9ojz",
"9ok5",
"9okc",
"9olj",
"9olo",
"9omq",
"9paf",
"9pag",
"9pb9",
"9pba",
"9pbf",
"9pbv",
"9pc3",
"9pcx",
"9pcz"... | 40 | [
"PUB00022273",
"PUB00028321",
"PUB00154121",
"PUB00154122",
"PUB00154123"
] | [
"9731775",
"9727495",
"25581794",
"30989110",
"30198481"
] | [
"Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.",
"Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.",
"Mechanistic insights into the recycling machine of the SNARE complex.",
"Mechanistic insights into ... | [
1998,
1998,
2015,
2019,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Lymphocystivirus"
] | [
2852,
4
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
6,
5,
19,
1,
5
] | 6 | true | Domain | NSF, AAA+ ATPase lid domain | NSF, AAA+ ATPase lid domain | NSF_ATPase_lid | 4 |
IPR054420 | 54,420 | RAE1/2 domain I, C-terminal region | RAE1_2_domI_C | Domain | 1,448 | false | false | This entry represents the C-terminal region of domain I from Rab escort proteins 1/2 (RAE1/2, also known as Rab proteins geranylgeranyltransferase component A 1/2) which are the substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex [ , ]. These proteins bind unprenylated Rab proteins and prese... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22603"
] | [
"RAE1_2_domI_C"
] | [
1448
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6803205",
"R-HSA-8873719",
"R-HSA-8876198",
"R-MMU-6803205",
"R-MMU-8873719",
"R-MMU-8876198",
"R-RNO-6803205",
"R-RNO-8873719",
"R-RNO-8876198"
] | [
"REACTOME:R-HSA-6803205",
"REACTOME:R-HSA-8873719",
"REACTOME:R-HSA-8876198",
"REACTOME:R-MMU-6803205",
"REACTOME:R-MMU-8873719",
"REACTOME:R-MMU-8876198",
"REACTOME:R-RNO-6803205",
"REACTOME:R-RNO-8873719",
"REACTOME:R-RNO-8876198"
] | 9 | [
"1ltx",
"1vg0",
"1vg9"
] | 3 | [
"PUB00027139",
"PUB00032083"
] | [
"12620235",
"15186776"
] | [
"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase.",
"Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease."
] | [
2003,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1448
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
6,
13
] | 4 | true | Domain | RAE1/2 domain I, C-terminal region | RAE1/2 domain I, C-terminal region | RAE1_2_domI_C | 5 |
IPR054421 | 54,421 | McpB, second HAMP domain | McpB_HAMP_2nd | Domain | 304 | false | false | This entry represents the second HAMP domain found in Methyl-accepting chemotaxis protein McpB from Pseudomonas aeruginosa and similar sequences from proteobacteria. McpB, also known as Aerotaxis transducer Aer2, is a chemoreceptor that plays a critical role in the virulence and pathogenesis of the bacteria. This domai... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21927"
] | [
"McpB_HAMP_2"
] | [
304
] | 1 | [] | [] | [] | 0 | [
"3lnr",
"4i3m",
"4i44"
] | 3 | [
"PUB00058629",
"PUB00065072"
] | [
"20399181",
"23424282"
] | [
"Structure of concatenated HAMP domains provides a mechanism for signal transduction.",
"HAMP Domain Conformers That Propagate Opposite Signals in Bacterial Chemoreceptors."
] | [
2010,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanolobus",
"mine drainage metagenome"
] | [
301,
2,
1
] | 3 | [] | [] | 0 | true | Domain | McpB, second HAMP domain | McpB, second HAMP domain | McpB_HAMP_2nd | 9 |
IPR054423 | 54,423 | Replitron, C-terminal domain | Replitron_C | Domain | 22 | false | false | This entry represents a presumed domain found adjacent to the HUH endonuclease domain ( ) of the eukaryotic transposase encoded by Replitron, a fourth independent group of DNA transposons encoding HUH endonuclease that are found in genomes of green algae and plants, diverse stramenopiles including brown seaweeds and li... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21860"
] | [
"Replitron_C"
] | [
22
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154199"
] | [
"36688326"
] | [
"Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
22
] | 1 | [] | [] | 0 | true | Domain | Replitron, C-terminal domain | Replitron, C-terminal domain | Replitron_C | 7 |
IPR054424 | 54,424 | Replitron, HUH endonuclease domain | Replitron_HUH | Domain | 222 | false | false | This entry represents the Rep HUH endonuclease domain of the eukaryotic transposase encoded by replitrons, a fourth independent group of DNA transposons found in genomes of green algae and plants, diverse stramenopiles including brown seaweeds and likely also cryptophytes and haptophytes, which suggests an ancient orig... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF21859"
] | [
"Replitron_HUH"
] | [
222
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153358",
"PUB00154431"
] | [
"34403695",
"37307447"
] | [
"The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.",
"Replitrons: A major group of eukaryotic transposons encoding HUH endonuclease."
] | [
2021,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
222
] | 1 | [] | [] | 0 | true | Domain | Replitron, HUH endonuclease domain | Replitron, HUH endonuclease domain | Replitron_HUH | 6 |
IPR054425 | 54,425 | Cdc6/ORC1-like, ATPase lid domain | Cdc6_ORC1-like_ATPase_lid | Domain | 5,673 | false | false | This entry represents the AAA+ ATPase lid domain of eukaryotic Cdc6/ORC proteins and its homologues from archaea [ , , , , ]. Cdc6 is involved in the initiation of DNA replication. It also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22606"
] | [
"Cdc6-ORC-like_ATPase_lid"
] | [
5673
] | 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-HSA-1362277",
"R-HSA-176187",
"R-HSA-68689",
"R-HSA-68867",
"R-HSA-68949",
"R-HSA-68962",
"R-HSA-69017",
"R-HSA-69205",
"R-MMU-176187",
"R-MMU-68689",
"R-MMU-68949",
"R-MMU-68962",
"R-MMU-69017",
"R-PFA-68616",
"R-PFA-68949",
"R-SCE-176187",
"R-SCE-68689",
"R-SCE-68962",
"R-SC... | [
"REACTOME:R-HSA-1362277",
"REACTOME:R-HSA-176187",
"REACTOME:R-HSA-68689",
"REACTOME:R-HSA-68867",
"REACTOME:R-HSA-68949",
"REACTOME:R-HSA-68962",
"REACTOME:R-HSA-69017",
"REACTOME:R-HSA-69205",
"REACTOME:R-MMU-176187",
"REACTOME:R-MMU-68689",
"REACTOME:R-MMU-68949",
"REACTOME:R-MMU-68962",
... | 24 | [
"1w5s",
"1w5t",
"5v8f",
"6wgc",
"6wgg",
"6wgi",
"7jgr",
"7jgs",
"7jk2",
"7jk3",
"7jk4",
"7mca",
"7tjh",
"7tji",
"7tjj",
"7tjk",
"8rwv",
"8s0e",
"9bcx"
] | 19 | [
"PUB00013199",
"PUB00032187",
"PUB00048937",
"PUB00049536",
"PUB00091300"
] | [
"11030343",
"15465044",
"17761879",
"17761880",
"25762138"
] | [
"Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.",
"Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix.",
"Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.",
"Structural basis of DNA r... | [
2000,
2004,
2007,
2007,
2015
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Thermoprotei"
] | [
5669,
4
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
10,
1,
1,
9,
2,
3,
2,
2,
2,
1,
1,
8
] | 12 | true | Domain | Cdc6/ORC1-like, ATPase lid domain | Cdc6/ORC1-like, ATPase lid domain | Cdc6_ORC1-like_ATPase_lid | 4 |
IPR054426 | 54,426 | TOTE conflict systems, S1/CSD-like domain 1 | S1CSD-TOTE-1 | Domain | 125 | false | false | This entry represents a presumed ribonucleoprotein complex-forming domain of the TOTE systems, potentially binding ssRNAs derived from hybrid duplexes bound by the systems. It is typically found in a two-domain tandem repeat arrangement, this is the first domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22708"
] | [
"S1CSD-TOTE-1"
] | [
125
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
122,
3
] | 2 | [] | [] | 0 | true | Domain | TOTE conflict systems, S1/CSD-like domain 1 | TOTE conflict systems, S1/CSD-like domain 1 | S1CSD-TOTE-1 | 9 |
IPR054427 | 54,427 | TOTE conflict systems, S1/CSD-like domain 2 | S1CSD-TOTE-2 | Domain | 225 | false | false | This entry represents a presumed ribonucleoprotein complex-forming domain of the TOTE ((TPR, OB, TBP, Effector) conflict systems, potentially binding ssRNAs derived from hybrid duplexes bound by the systems. It is typically found in a two-domain tandem repeat arrangement, this is the second domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22707"
] | [
"S1CSD-TOTE-2"
] | [
225
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Neophaeococcomyces mojaviensis",
"metagenomes"
] | [
221,
1,
3
] | 3 | [] | [] | 0 | true | Domain | TOTE conflict systems, S1/CSD-like domain 2 | TOTE conflict systems, S1/CSD-like domain 2 | S1CSD-TOTE-2 | 5 |
IPR054428 | 54,428 | TMADH/DMDH/HD, second alpha/beta domain | TMADH/DMDH/HD_second_a-b | Domain | 517 | false | false | This domain is found in a group of diverse dehydrogenases from the old yellow enzyme (OYE) superfamily, such as histamine dehydrogenase (HD) from Nocardioides simplex, dimethylamine dehydrogenases (DMDH), trimethylamine dehydrogenase (TMADH) from Methylophilus methylotrophus (sp. W(3)A(1)) [ , , , , ], in which it has ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22620"
] | [
"OYE-like_second_a-b"
] | [
517
] | 1 | [] | [] | [] | 0 | [
"1djn",
"1djq",
"1o94",
"1o95",
"2tmd",
"3k30",
"6de6",
"6l6j"
] | 8 | [
"PUB00024213",
"PUB00033232",
"PUB00086778",
"PUB00086783",
"PUB00154141",
"PUB00154142",
"PUB00154405"
] | [
"10869173",
"12567183",
"3771568",
"15311941",
"20538584",
"31061390",
"32830294"
] | [
"Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)).",
"Extensive conformational sampling in a ternary electron transfer complex.",
"Three-dimensional structure of the iron-sulfur flavoprotein tr... | [
2000,
2003,
1986,
2004,
2010,
2019,
2020
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Marsarchaeota group 1",
"Geodia barretti",
"ecological metagenomes"
] | [
494,
2,
2,
19
] | 4 | [] | [] | 0 | true | Domain | TMADH/DMDH/HD, second alpha/beta domain | TMADH/DMDH/HD, second alpha/beta domain | TMADH/DMDH/HD_second_a-b | 6 |
IPR054429 | 54,429 | Muscleblind-like, CCCH zinc finger | Znf-CCCH_Muscleblind-like | Domain | 10,512 | false | false | This is the CCCH-type zinc finger domain found in muscleblind (MBL) from Drosophila and its homologues. MBL is required for terminal differentiation of photoreceptor cells and it is vital for embryonic development [ ]. Mammalian MBL-like proteins (MBL1-4) mediate pre-mRNA alternative splicing regulation [ , ]. They act... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22628"
] | [
"zf-CCCH_10"
] | [
10512
] | 1 | [] | [] | [] | 0 | [
"2e5s",
"2rpp",
"3d2n",
"3d2q",
"3d2s",
"5u6h",
"5u6l",
"5u9b"
] | 8 | [
"PUB00047341",
"PUB00051219",
"PUB00091371",
"PUB00153406",
"PUB00154336",
"PUB00154408",
"PUB00154409"
] | [
"19177353",
"19043415",
"22407013",
"31283468",
"28718627",
"37548402",
"9334280"
] | [
"Solution structure of the RNA binding domain in the human muscleblind-like protein 2.",
"Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1.",
"Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA.",
"Identificatio... | [
2009,
2008,
2012,
2019,
2017,
2023,
1997
] | 7 | [
"IPR000571"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"invertebrate metagenome"
] | [
10511,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
7,
76,
25,
26,
24,
1,
29,
43
] | 8 | true | Domain | Muscleblind-like, CCCH zinc finger | Muscleblind-like, CCCH zinc finger | Znf-CCCH_Muscleblind-like | 3 |
IPR054430 | 54,430 | Baseplate wedge protein gp10, domain 3 | Gp10_D3 | Domain | 319 | false | false | This domain is found in the central region of Baseplate wedge protein gp10 and related viral proteins. This domain folds into a β-sandwich. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22670"
] | [
"Gp10_D3"
] | [
319
] | 1 | [] | [] | [] | 0 | [
"2fl8",
"2fl9",
"5hx2",
"5iv5",
"5iv7",
"9f4a",
"9f4b"
] | 7 | [
"PUB00040707",
"PUB00151773"
] | [
"16554069",
"26929357"
] | [
"Evolution of bacteriophage tails: Structure of T4 gene product 10.",
"Role of bacteriophage T4 baseplate in regulating assembly and infection."
] | [
2006,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Flagellimonas marina",
"Viruses"
] | [
1,
318
] | 2 | [] | [] | 0 | true | Domain | Baseplate wedge protein gp10, domain 3 | Baseplate wedge protein gp10, domain 3 | Gp10_D3 | 8 |
IPR054433 | 54,433 | RNA-dependent RNA polymerase, thumb domain, ribovirus | RdRp_thumb_ribovirus | Domain | 71 | false | false | This helical bundle domain, known as the thumb domain, is found in the RNA-dependent RNA polymerase (RdRp) of viruses ( ), C-terminal to the palm domain ( ). This domain is larger than the thumb domains of other viral ssRNA RdRPs [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22260"
] | [
"Permu_RdRp_thumb"
] | [
71
] | 1 | [] | [] | [] | 0 | [
"4xha",
"4xhi",
"5cx6",
"5cyr",
"7om2",
"7om6",
"7om7",
"7om9",
"7oma"
] | 9 | [
"PUB00154157",
"PUB00154158"
] | [
"26625123",
"34203380"
] | [
"The Structure of the RNA-Dependent RNA Polymerase of a Permutotetravirus Suggests a Link between Primer-Dependent and Primer-Independent Polymerases.",
"Snapshots of a Non-Canonical RdRP in Action."
] | [
2015,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Neoptera",
"Viruses"
] | [
9,
62
] | 2 | [] | [] | 0 | true | Domain | RNA-dependent RNA polymerase, thumb domain, ribovirus | RNA-dependent RNA polymerase, thumb domain, ribovirus | RdRp_thumb_ribovirus | 5 |
IPR054434 | 54,434 | Argonaute, middle domain, bacteria | Ago_MID_bact | Domain | 8 | false | false | This entry represents the middle domain of bacterial argonaute (Ago) [ , ]. Ago binds small RNA or DNA guides, which provide base-pairing specificity for the recognition and cleavage of complementary nucleic acid targets. Bacterial Ago adopts a bilobed structure; an N-terminal and a PAZ domain constitute one lobe, the ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22362"
] | [
"Ago_MID_bact"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"5i4a",
"5ux0"
] | 2 | [
"PUB00153794",
"PUB00153795"
] | [
"27035975",
"28520746"
] | [
"A bacterial Argonaute with noncanonical guide RNA specificity.",
"DNA recognition by an RNA-guided bacterial Argonaute."
] | [
2016,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Thermotogae"
] | [
8
] | 1 | [] | [] | 0 | true | Domain | Argonaute, middle domain, bacteria | Argonaute, middle domain, bacteria | Ago_MID_bact | 9 |
IPR054436 | 54,436 | Argonaute, PAZ domain, methanocaldococcus | Ago_PAZ_methanocaldococcus | Domain | 2 | false | false | This entry represents the PAZ domain of Protein argonaute from Methanocaldococcus jannaschii (Ago, [ ]) and similar sequences. Ago is a DNA-guided ssDNA endonuclease that may play a role in defence against invading genetic elements that uses short ssDNA sequences as guides (gDNA) to bind complementary target strands re... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22333"
] | [
"Ago_PAZ_arc"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"5g5s",
"5g5t"
] | 2 | [
"PUB00153796",
"PUB00153797"
] | [
"28319084",
"28319081"
] | [
"Structural and mechanistic insights into an archaeal DNA-guided Argonaute protein.",
"Guide-independent DNA cleavage by archaeal Argonaute from Methanocaldococcus jannaschii."
] | [
2017,
2017
] | 2 | [
"IPR003100"
] | [] | 1 | 0 | 1 | [
"Methanocaldococcus"
] | [
2
] | 1 | [] | [] | 0 | true | Domain | Argonaute, PAZ domain, methanocaldococcus | Argonaute, PAZ domain, methanocaldococcus | Ago_PAZ_methanocaldococcus | 7 |
IPR054437 | 54,437 | PspA-associated domain | PspA-assoc_dom | Domain | 1,692 | false | false | This entry represents a trihelical domain (α+β) with highly conserved R and D, which occurs as a two-gene cluster with PspA in prokariotic sequences. This domain covers the whole length of the protein in most sequences, but is occasionally found fused to an N-terminal PspA in actinobacteria and chloroflexi [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22743"
] | [
"PspAA"
] | [
1692
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00158885"
] | [
"38809013"
] | [
"The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"metagenomes"
] | [
79,
1596,
2,
15
] | 4 | [] | [] | 0 | true | Domain | PspA-associated domain | PspA-associated domain | PspA-assoc_dom | 5 |
IPR054438 | 54,438 | Structural cement protein E217 gp24/Pam3 gp6 | Struct_cement_gp24/gp6 | Family | 1,246 | false | false | E217 is a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa [ ]. Gp24 is a trimeric structural protein and component of the E217 icosahedral head. Gp24 adopts a beta-tulip fold similar to the gp87 protein found in the thermophilic phage P74-26. Each gp24 s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22758"
] | [
"Phage_cement"
] | [
1246
] | 1 | [] | [] | [] | 0 | [
"8frs",
"8hdt",
"9b40",
"9kmg",
"9kmh",
"9kzj"
] | 6 | [
"PUB00153918",
"PUB00154413"
] | [
"37422479",
"36656854"
] | [
"High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217.",
"Fine structure and assembly pattern of a minimal myophage Pam3."
] | [
2023,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanosarcinales",
"Opisthokonta",
"Viruses",
"metagenomes"
] | [
701,
2,
4,
523,
16
] | 5 | [] | [] | 0 | true | Family | Structural cement protein E217 gp24/Pam3 gp6 | Structural cement protein E217 gp24/Pam3 gp6 | Struct_cement_gp24/gp6 | 7 |
IPR054440 | 54,440 | Tail fiber protein gp32-like | Gp32-like | Family | 770 | false | false | This entry represents a family of proteins from tailed bacteriophages and bacterial prophages, including Gp32 from E217, a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Stacked hexamers of the tail tube protein gp32 form the central tube of the E217 t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22764"
] | [
"E217_Gp32"
] | [
770
] | 1 | [] | [] | [] | 0 | [
"8env",
"8eon",
"8fuv",
"9b42",
"9b45"
] | 5 | [
"PUB00153918"
] | [
"37422479"
] | [
"High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Linnemannia gamsii",
"Viruses",
"metagenomes"
] | [
466,
2,
300,
2
] | 4 | [] | [] | 0 | true | Family | Tail fiber protein gp32-like | Tail fiber protein gp32-like | Gp32-like | 8 |
IPR054441 | 54,441 | Collar protein gp28-like | Gp28-like | Family | 250 | false | false | This entry represents a family of proteins from tailed bacteriophages and proteobacterial prophages, including Gp28 from E217, a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. The collar protein gp28 is located at the neck of the E217 virion. Gp28 cons... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22755"
] | [
"E217_gp28"
] | [
250
] | 1 | [] | [] | [] | 0 | [
"8fvh",
"9b42"
] | 2 | [
"PUB00153918"
] | [
"37422479"
] | [
"High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Linnemannia gamsii",
"Viruses",
"plant metagenome"
] | [
117,
2,
130,
1
] | 4 | [] | [] | 0 | true | Family | Collar protein gp28-like | Collar protein gp28-like | Gp28-like | 6 |
IPR054442 | 54,442 | E217 Baseplate component gp38-like | E217_Gp38-like | Family | 243 | false | false | This entry represents a family of proteins from tailed bacteriophages, including Gp38 from E217, a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Gp38 is a baseplate cap component that forms a heterodimeric complex with Gp37. These proteins adopt a sim... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22760"
] | [
"Gp38_E217"
] | [
243
] | 1 | [] | [] | [] | 0 | [
"8eon",
"9b45"
] | 2 | [
"PUB00153918"
] | [
"37422479"
] | [
"High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Komagataeibacter melomenusus",
"Viruses"
] | [
1,
242
] | 2 | [] | [] | 0 | true | Family | E217 Baseplate component gp38-like | E217 Baseplate component gp38-like | E217_Gp38-like | 6 |
IPR054443 | 54,443 | Glycan binding protein Y3-like domain | Y3-like_dom | Domain | 379 | false | false | This entry represents the domain present in the glycan-binding protein Y3 from Coprinus comatus ( ) and related proteins from fungi. The structure of this domain consists of an α-β-α sandwich motif, which includes three α-helices and a five-stranded β-sheet. This domain is characterised by the presence of four intramol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22803"
] | [
"GBD_Y3"
] | [
379
] | 1 | [] | [] | [] | 0 | [
"5v6i",
"5v6j"
] | 2 | [
"PUB00153962"
] | [
"28784797"
] | [
"Cytotoxic protein from the mushroom <i>Coprinus comatus</i> possesses a unique mode for glycan binding and specificity."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Dikarya"
] | [
379
] | 1 | [] | [] | 0 | true | Domain | Glycan binding protein Y3-like domain | Glycan binding protein Y3-like domain | Y3-like_dom | 7 |
IPR054444 | 54,444 | YoaL-like | YoaL-like | Family | 228 | false | false | This protein family includes YoaL from Escherichia coli, the product of a small open reading frame (smORF), which may serve a regulatory role in the expression of its downstream gene [ ]. Members of this group are specific to Enterobacterales. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22867"
] | [
"YoaL"
] | [
228
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105763"
] | [
"30837344"
] | [
"Identifying Small Proteins by Ribosome Profiling with Stalled Initiation Complexes."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacteriaceae",
"human gut metagenome"
] | [
227,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | YoaL-like | YoaL-like | YoaL-like | 4 |
IPR054445 | 54,445 | T3SS, peptide-binding chaperone domain | T3SS_chaperone_dom | Domain | 100 | false | false | This domain is observed in proteins from bacterial host systems predicted to counter viral ribosylating toxins. They are predicted to function as peptide-binding chaperone domains that target proteins modified by ADPr and potentially misfolded as a consequence [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22553"
] | [
"TY-Chap2"
] | [
100
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153825",
"PUB00154313"
] | [
"36146784",
"36968432"
] | [
"Apprehending the NAD<sup>+</sup>-ADPr-Dependent Systems in the Virus World.",
"A library of sensitive position-specific scoring matrices for high-throughput identification of nuclear pore complex subunits."
] | [
2022,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"freshwater metagenome"
] | [
97,
3
] | 2 | [] | [] | 0 | true | Domain | T3SS, peptide-binding chaperone domain | T3SS, peptide-binding chaperone domain | T3SS_chaperone_dom | 6 |
IPR054446 | 54,446 | CIMIP3-like | CIMIP3-like | Family | 397 | false | false | This family represents human CIMIP3 and similar sequences mainly found in vertebrates. CIMIP3 is thought to be a microtubule inner protein (MIP) part of the doublet microtubules (DMTs) in the sperm axoneme [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22581"
] | [
"CIMIP3"
] | [
397
] | 1 | [] | [] | [] | 0 | [
"8otz",
"8snb",
"9fqr"
] | 3 | [
"PUB00151496"
] | [
"37327785"
] | [
"Structural specializations of the sperm tail."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
397
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
4
] | 3 | true | Family | CIMIP3-like | CIMIP3-like | CIMIP3-like | 7 |
IPR054447 | 54,447 | Gateway protein gp29-like | Gp29-like | Family | 228 | false | false | This entry represents a family of proteins from tailed bacteriophages and bacterial prophages, including Gp29 from E217, a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. The gateway protein gp29 is a neck factor of the E217 virion that connects the nec... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22756"
] | [
"E217_gp29"
] | [
228
] | 1 | [] | [] | [] | 0 | [
"8fvh",
"9b42"
] | 2 | [
"PUB00153918"
] | [
"37422479"
] | [
"High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Linnemannia gamsii",
"Viruses",
"plant metagenome"
] | [
102,
1,
123,
2
] | 4 | [] | [] | 0 | true | Family | Gateway protein gp29-like | Gateway protein gp29-like | Gp29-like | 5 |
IPR054448 | 54,448 | Helix-turn-helix domain, putative, ascomycetes | HTH_put_ascomycetes | Domain | 949 | false | false | This entry represents a putative helix-turn-helix domain found C-terminal in a group of uncharacterised proteins from actinomycetes. It may be involved in DNA binding. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22943"
] | [
"HTH_68"
] | [
949
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Paracoccaceae"
] | [
947,
2
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Helix-turn-helix domain, putative, ascomycetes | Helix-turn-helix domain, putative, ascomycetes | HTH_put_ascomycetes | 9 |
IPR054449 | 54,449 | Nonstructural protein, WIV domain | WIV_dom | Domain | 30 | false | false | This domain is found in Nonstructural protein from Lake Sinai virus and similar sequences from arthropod-infecting viruses and lower eukaryotes. It has been named 'Widespread, Intriguing, Versatile' (WIV) domain. This region is likely to play a role in viral infection of arthropods. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22532"
] | [
"WIV_dom"
] | [
30
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Neoptera",
"Viruses"
] | [
17,
13
] | 2 | [] | [] | 0 | true | Domain | Nonstructural protein, WIV domain | Nonstructural protein, WIV domain | WIV_dom | 8 |
IPR054450 | 54,450 | TIL-like domain | TIL-like_dom | Domain | 76 | false | false | This entry represents a small cysteine rich domain that is related to the Trypsin Inhibitor like cysteine rich domain found in . Members of this group are found in nematodes. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22897"
] | [
"TIL_2"
] | [
76
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Ecdysozoa"
] | [
76
] | 1 | [] | [] | 0 | true | Domain | TIL-like domain | TIL-like domain | TIL-like_dom | 4 |
IPR054451 | 54,451 | RhopH3, C-terminal domain | RhopH3_C | Domain | 78 | false | false | This entry represents a domain found towards the C terminus in homologues of High molecular weight rhoptry protein 3 from Plasmodium falciparum (RhopH3) and similar sequences specific to Plasmodium species. RhopH3 is a component of the RhopH complex that is essential for the pathogen erythrocyte invasion and for remode... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22808"
] | [
"RhopH3_C"
] | [
78
] | 1 | [] | [] | [] | 0 | [
"7kiy",
"7mrw"
] | 2 | [
"PUB00154205"
] | [
"33393463"
] | [
"Malaria parasites use a soluble RhopH complex for erythrocyte invasion and an integral form for nutrient uptake."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Plasmodium"
] | [
78
] | 1 | [] | [] | 0 | true | Domain | RhopH3, C-terminal domain | RhopH3, C-terminal domain | RhopH3_C | 1 |
IPR054452 | 54,452 | Minimal SLOG domain | mSLOG_dom | Domain | 91 | false | false | This entry represents a domain predicted to be an active, minimal version of the SLOG domain. It is found N-terminally fused to the DUF4326 domain ( ). It may play a role in base cleavage, potentially forming abasic sites acted on by the DuOB domain ( ) [ ]. Members of this group are found in proteobacteria. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22565"
] | [
"mSLOG"
] | [
91
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153826"
] | [
"36968430"
] | [
"New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"Thelohanellus kitauei",
"hydrothermal vent metagenome"
] | [
89,
1,
1
] | 3 | [] | [] | 0 | true | Domain | Minimal SLOG domain | Minimal SLOG domain | mSLOG_dom | 6 |
IPR054453 | 54,453 | PssL-like | PssL-like | Family | 65 | false | false | This family includes Protein PssL from Escherichia coli, the product of a small open reading frame (smORF), which may serve a regulatory role in expression of downstream gene [ ]. Members of this group are found in Enterobacterales. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22869"
] | [
"PssL"
] | [
65
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105763"
] | [
"30837344"
] | [
"Identifying Small Proteins by Ribosome Profiling with Stalled Initiation Complexes."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
65
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | PssL-like | PssL-like | PssL-like | 8 |
IPR054454 | 54,454 | NGO_1070-like | NGO_1070-like | Family | 44 | false | false | This protein family includes the uncharacterised protein NGO_1070 from Neisseria gonorrhoeae ( ) and similar proteins mainly found in proteobacteria. NGO_1070 adopts a β-barrel fold. Its function is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22300"
] | [
"NGO_1070-like"
] | [
44
] | 1 | [] | [] | [] | 0 | [
"5v77"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
44
] | 1 | [] | [] | 0 | true | Family | NGO_1070-like | NGO_1070-like | NGO_1070-like | 3 |
IPR054455 | 54,455 | TraH, VirB8-like domain | TraH_VirB8-like_dom | Domain | 35 | false | false | This entry represents the VirB8-like domain present in TraH from Enterococcus faecalis ( ) and similar sequences from Bacilli. TraH is part of the type IV secretion system (T4SS) [ ]. This domain shows structural similarity to the VirB8 domain ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22351"
] | [
"TraH_VirB8-like"
] | [
35
] | 1 | [] | [] | [] | 0 | [
"5aiw"
] | 1 | [
"PUB00154297"
] | [
"27103580"
] | [
"VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
35
] | 1 | [] | [] | 0 | true | Domain | TraH, VirB8-like domain | TraH, VirB8-like domain | TraH_VirB8-like_dom | 8 |
IPR054456 | 54,456 | Replication initiation protein, N-terminal | RepD-like_N | Domain | 246 | false | false | This domain is found at the N-terminal end of Replication initiation protein from Staphylococcus aureus (Rep and RepC, D, E, M, N variants of the pT181 family) and similar sequences from Bacilli. Rep proteins, shows similarity with the extended β-sheet in TATA binding protein (TBP) [ ]. Replication of pT181 family plas... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22477"
] | [
"RepD-like_N"
] | [
246
] | 1 | [] | [] | [] | 0 | [
"4cwc",
"4cwe"
] | 2 | [
"PUB00091284"
] | [
"26792891"
] | [
"Structures of replication initiation proteins from staphylococcal antibiotic resistance plasmids reveal protein asymmetry and flexibility are necessary for replication."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halospeciosus flavus",
"Opisthokonta",
"human gut metagenome",
"plasmids"
] | [
238,
1,
3,
1,
3
] | 5 | [] | [] | 0 | true | Domain | Replication initiation protein, N-terminal | Replication initiation protein, N-terminal | RepD-like_N | 5 |
IPR054457 | 54,457 | Phage phiCb5, coat protein | PhiCb5_coat | Family | 256 | false | false | This entry represents a family of proteins from Leviviricetes, including Coat protein from Caulobacter phage phiCb5 ( ), which consists of an N-terminal loop, a five-stranded β-sheet and a C-terminal arm containing two helices [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22387"
] | [
"PhiCb5_coat"
] | [
256
] | 1 | [] | [] | [] | 0 | [
"2w4y",
"2w4z",
"8uej"
] | 3 | [
"PUB00154166",
"PUB00154478"
] | [
"19559027",
"38701202"
] | [
"The structure of bacteriophage phiCb5 reveals a role of the RNA genome and metal ions in particle stability and assembly.",
"Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus."
] | [
2009,
2024
] | 2 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
256
] | 1 | [] | [] | 0 | true | Family | Phage phiCb5, coat protein | Phage phiCb5, coat protein | PhiCb5_coat | 3 |
IPR054458 | 54,458 | Conserved flagellar protein F, immunoglobulin-like domain | FlaF_Ig-like | Domain | 47 | false | false | This domain is found in Conserved flagellar protein F from Sulfolobus acidocaldarius (FlaF, ) and similar archaeal proteins. FlaF is essential for archaellum assembly with an extended N-terminal α-helix connected to a globular domain (this entry). This domain adopts a β-sandwich fold with eight anti-parallel β-strands ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22201"
] | [
"FlaF_Ig-like"
] | [
47
] | 1 | [] | [] | [] | 0 | [
"4p94",
"4zbh",
"5tug",
"6pbk"
] | 4 | [
"PUB00153948",
"PUB00153949"
] | [
"25865246",
"31844299"
] | [
"FlaF Is a β-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein.",
"The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility."
] | [
2015,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Litorilinea aerophila",
"Thermoproteati"
] | [
1,
46
] | 2 | [] | [] | 0 | true | Domain | Conserved flagellar protein F, immunoglobulin-like domain | Conserved flagellar protein F, immunoglobulin-like domain | FlaF_Ig-like | 5 |
IPR054459 | 54,459 | Transcriptional cofactor Bfc domain | Bfc_dom | Domain | 79 | false | false | This domain is found in sequences from insects, including the transcriptional cofactor Bfc from Drosophila melanogaster, which adopts a C2-like fold. Bfc is a transcriptional cofactor involved in efferocytosis. Together with Srp mediates expression of the phagocytic receptor crq/croquemort in response to apoptotic cell... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22576"
] | [
"Bfc"
] | [
79
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153832"
] | [
"34860835"
] | [
"bfc, a novel serpent co-factor for the expression of croquemort, regulates efferocytosis in Drosophila melanogaster."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Cyclorrhapha"
] | [
79
] | 1 | [
"Drosophila melanogaster"
] | [
4
] | 1 | true | Domain | Transcriptional cofactor Bfc domain | Transcriptional cofactor Bfc domain | Bfc_dom | 6 |
IPR054460 | 54,460 | DUF5018-related | DUF5018-rel | Domain | 326 | false | false | This domain is found in the putative secreted protein BF4250 from Bacteroides fragilis ( ) and similar bacterial functionally uncharacterised proteins. It adopts a β-sandwich with a greek key topology . This domain seems to be related to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22243"
] | [
"DUF5018-rel"
] | [
326
] | 1 | [] | [] | [] | 0 | [
"3owr",
"3p69"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
322,
4
] | 2 | [] | [] | 0 | true | Domain | DUF5018-related | DUF5018-related | DUF5018-rel | 7 |
IPR054462 | 54,462 | TraI-like, middle domain | TraI_M | Domain | 1,797 | false | false | This entry represents a domain found in the middle region of TraI-like proteins mostly from proteobacteria, including from Methylophaga frappieri. It is found C-terminal to the relaxase domain ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22863"
] | [
"TraI_middle"
] | [
1797
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Tanacetum cinerariifolium",
"metagenomes",
"plasmids"
] | [
1769,
1,
18,
9
] | 4 | [] | [] | 0 | true | Domain | TraI-like, middle domain | TraI-like, middle domain | TraI_M | 8 |
IPR054463 | 54,463 | RxLR effector PexRD54, WY domain | PexRD54_WY | Domain | 1,676 | false | false | This entry represents homologous WY domains of the RxLR effector PexRD54 from Phytophthora infestans and similar proteins from Peronosporales, water moulds that are mainly associated with plant diseases. PexRD54 is an effector that specifically binds host autophagy protein ATG8CL (from the ATG8 family) to stimulate aut... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22748"
] | [
"PexRD54_WY"
] | [
1676
] | 1 | [] | [] | [] | 0 | [
"5gnc",
"5l7s",
"5zc3",
"7xvi",
"7xvk",
"9rdc",
"9ria"
] | 7 | [
"PUB00091265",
"PUB00154161",
"PUB00154162",
"PUB00154163",
"PUB00154475",
"PUB00154476"
] | [
"27458016",
"30926664",
"30077372",
"30703565",
"26765567",
"29932422"
] | [
"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.",
"Structural analysis of <i>Phytophthora</i> suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.",
"Crystal structure of the RxLR effec... | [
2016,
2019,
2018,
2019,
2016,
2018
] | 6 | [] | [] | 0 | 0 | null | [
"Peronosporaceae"
] | [
1676
] | 1 | [] | [] | 0 | true | Domain | RxLR effector PexRD54, WY domain | RxLR effector PexRD54, WY domain | PexRD54_WY | 9 |
IPR054464 | 54,464 | Ubiquitin-like domain, fungal | ULD_fung | Domain | 3,800 | false | false | This entry represents a domain found in a range of fungal proteins. It is predicted to show an ubiquitin like structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22893"
] | [
"ULD_2"
] | [
3800
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3800
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Ubiquitin-like domain, fungal | Ubiquitin-like domain, fungal | ULD_fung | 6 |
IPR054465 | 54,465 | Integrase p58-like, C-terminal domain | Integrase_p58-like_C | Domain | 9,438 | false | false | This domain is found at the C-terminal end of a group of uncharacterised animal proteins that are similar to Integrase p58, the last chain cleaved from the Transposon Ty3-G Gag-Pol polyprotein from Saccharomyces cerevisiae. This domain, which is associated to , is also named SH3 domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22938"
] | [
"Integrase_p58_C"
] | [
9438
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091628",
"PUB00154023"
] | [
"24608367",
"34848735"
] | [
"Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry.",
"Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes."
] | [
2014,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Solemya velum gill symbiont",
"invertebrate metagenome"
] | [
9432,
1,
5
] | 3 | [
"Danio rerio"
] | [
39
] | 1 | true | Domain | Integrase p58-like, C-terminal domain | Integrase p58-like, C-terminal domain | Integrase_p58-like_C | 6 |
IPR054466 | 54,466 | Kinase OspG, kinase domain | OspG_kinase | Domain | 313 | false | false | This entry represents the kinase domain of protein kinase OspG, which is involved in down-regulation of the host innate response induced by invasive bacteria [ , , , , ]. OspG is a an effector kinase that binds host E2 ubiquitin-conjugating enzymes activated with ubiquitin, which enhances its kinase activity, playing a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22303"
] | [
"OspG_kinase"
] | [
313
] | 1 | [] | [] | [] | 0 | [
"4bvu",
"4lrj",
"4lrk",
"4o96",
"4q5e",
"4q5h"
] | 6 | [
"PUB00106325",
"PUB00154137",
"PUB00154138",
"PUB00154139",
"PUB00154140"
] | [
"24373767",
"24446487",
"24856362",
"29420175",
"24712300"
] | [
"NleH defines a new family of bacterial effector kinases.",
"E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis.",
"Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG.",
"CDKL Family Kinases Have Evolved Distinct Structu... | [
2014,
2014,
2014,
2018,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Aspergillus sydowii CBS 593.65",
"Escherichia phage 2B8",
"Pseudomonadota"
] | [
1,
1,
311
] | 3 | [] | [] | 0 | true | Domain | Kinase OspG, kinase domain | Kinase OspG, kinase domain | OspG_kinase | 3 |
IPR054467 | 54,467 | YkoP-like domain | YkoP-like_dom | Domain | 1,187 | false | false | This entry represents a domain that covers the whole length of the sequence in the uncharacterised protein YkoP from Bacillus subtilis, whose structure shows similarity to GNAT family acetyltransferases. This domain is found associated with in some sequences. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22790"
] | [
"YkoP"
] | [
1187
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
1185,
2
] | 2 | [] | [] | 0 | true | Domain | YkoP-like domain | YkoP-like domain | YkoP-like_dom | 4 |
IPR054468 | 54,468 | NrS-1 polymerase-like, HBD domain | NrSPol-like_HBD | Domain | 1,240 | false | false | This entry represents the helix bundle domain (HBD) domain of NrS-1 polymerase (NrSPol) [ ] which together with the N-terminal Prim/Pol domain, is responsible for DNA polymerization and de novo primer synthesis activities. This domain is critical for the primer synthesis activity of NrS-1 polymerase [ ]. Members of thi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22763"
] | [
"NrS1-1_pol-like_HBD"
] | [
1240
] | 1 | [] | [] | [] | 0 | [
"6a9w",
"6jon",
"6jop",
"6joq",
"6k9a",
"6k9b",
"7ola",
"7om0",
"7rr3",
"7rr4"
] | 10 | [
"PUB00151922"
] | [
"32016421"
] | [
"Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Opisthokonta",
"Viruses",
"metagenomes"
] | [
802,
320,
2,
106,
10
] | 5 | [] | [] | 0 | true | Domain | NrS-1 polymerase-like, HBD domain | NrS-1 polymerase-like, HBD domain | NrSPol-like_HBD | 1 |
IPR054469 | 54,469 | Predicted hydrolase, N-terminal domain | Pred_hydrolase_N | Domain | 613 | false | false | This entry represents a domain found at the N-terminal end in an uncharacterised family of proteins mainly found in actinomycetes, including MT2140 from Mycobacterium tuberculosis, a predicted alpha/beta hydrolase that contains at the C-terminal end [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22905"
] | [
"Hydro_N_hd"
] | [
613
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00033394"
] | [
"15688435"
] | [
"Protein domain of unknown function DUF1023 is an alpha/beta hydrolase."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhododendron williamsianum"
] | [
612,
1
] | 2 | [] | [] | 0 | true | Domain | Predicted hydrolase, N-terminal domain | Predicted hydrolase, N-terminal domain | Pred_hydrolase_N | 1 |
IPR054470 | 54,470 | FIMAH domain | FIMAH_dom | Domain | 1,975 | false | false | This entry represents a small α-helical bundle domain found in a group of prokaryotic proteins with a large range of different domain architectures, including Alpha-1,2-mannosidase from Neobacillus novalis ( , [ ]). The proteins containing these domains are extracellular enzymes often involved in cell wall processes. T... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22888"
] | [
"FIMAH"
] | [
1975
] | 1 | [] | [] | [] | 0 | [
"7nsn"
] | 1 | [
"PUB00153947"
] | [
"37071393"
] | [
"Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"marine sediment metagenome"
] | [
13,
1959,
3
] | 3 | [] | [] | 0 | true | Domain | FIMAH domain | FIMAH domain | FIMAH_dom | 9 |
IPR054471 | 54,471 | GPI inositol-deacylase, winged helix domain | GPIID_WHD | Domain | 14,971 | false | false | This winged helix domain (WHD) is found in a number of putative GPI inositol-deacylases from fungi, including Vegetative incompatibility protein HET-E-1. This protein is responsible for vegetative incompatibility through specific interactions with different alleles of the unlinked gene, het-c [ ]. It is also found in A... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22939"
] | [
"WHD_GPIID"
] | [
14971
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153770",
"PUB00153771",
"PUB00154451"
] | [
"28959415",
"34220766",
"7557402"
] | [
"Orange, red, yellow: biosynthesis of azaphilone pigments in <i>Monascus</i> fungi.",
"An Integrated Approach to Determine the Boundaries of the Azaphilone Pigment Biosynthetic Gene Cluster of <i>Monascus ruber</i> M7 Grown on Potato Dextrose Agar.",
"A gene responsible for vegetative incompatibility in the fun... | [
2017,
2021,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
14971
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
3
] | 1 | true | Domain | GPI inositol-deacylase, winged helix domain | GPI inositol-deacylase, winged helix domain | GPIID_WHD | 8 |
IPR054472 | 54,472 | Winged helix domain, variant | WHD | Domain | 2,836 | false | false | This domain is found mainly in uncharacterised bacterial proteins. It is predicted to adopt a globular structure with similarity to MarR family of transcription factors ( ). This domain is found usually in combination with AAA+ ATPase domains ( ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22977"
] | [
"WHD"
] | [
2836
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
71,
2490,
254,
21
] | 4 | [] | [] | 0 | true | Domain | Winged helix domain, variant | Winged helix domain, variant | WHD | 3 |
IPR054473 | 54,473 | Kinesin-like protein KIF2A-like, N-terminal | KIF2A-like_N | Domain | 4,342 | false | false | This domain is found at the N-terminal of human Kinesin-like protein KIF2A and similar animal proteins with a kinesin motor domain ( ). KIF2A, which is required for normal progression through mitosis and for normal brain development, is a plus end-directed microtubule-dependent motor protein with microtubule depolymeri... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22923"
] | [
"KIF2A-like_1st"
] | [
4342
] | 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-DME-6811434",
"R-DME-983189",
"R-HSA-141444",
"R-HSA-2132295",
"R-HSA-2467813",
"R-HSA-2500257",
"R-HSA-5663220",
"R-HSA-6811434",
"R-HSA-68877",
"R-HSA-9648025",
"R-HSA-983189",
"R-MMU-141444",
"R-MMU-2132295",
"R-MMU-2467813",
"R-MMU-2500257",
"R-MMU-5663220",
"R-MMU-6811434",
... | [
"REACTOME:R-DME-6811434",
"REACTOME:R-DME-983189",
"REACTOME:R-HSA-141444",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2500257",
"REACTOME:R-HSA-5663220",
"REACTOME:R-HSA-6811434",
"REACTOME:R-HSA-68877",
"REACTOME:R-HSA-9648025",
"REACTOME:R-HSA-983189",
"REACTOME:R-M... | 29 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4342
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
6,
6,
18,
10,
9
] | 6 | true | Domain | Kinesin-like protein KIF2A-like, N-terminal | Kinesin-like protein KIF2A-like, N-terminal | KIF2A-like_N | 2 |
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