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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR058746 | 58,746 | Topors, zinc finger, RING-type | Znf_RING-type_Topors | Domain | 2,951 | false | false | This entry represents the zinc finger RING-type domain in human E3 ubiquitin-protein ligase Topors and related proteins mainly found in animals and plants. Topors, also known as topoisomerase I-binding RING finger protein, tumour suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously ex... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd16574"
] | [
"RING-HC_Topors"
] | [
2951
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.27",
"PWY-7511",
"R-HSA-3899300",
"R-HSA-4085377",
"R-HSA-4755510",
"R-MMU-3899300",
"R-MMU-4085377",
"R-MMU-4755510"
] | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-HSA-3899300",
"REACTOME:R-HSA-4085377",
"REACTOME:R-HSA-4755510",
"REACTOME:R-MMU-3899300",
"REACTOME:R-MMU-4085377",
"REACTOME:R-MMU-4755510"
] | 8 | [] | 0 | [
"PUB00107792",
"PUB00135439",
"PUB00135440",
"PUB00135441",
"PUB00135442",
"PUB00135443",
"PUB00135444",
"PUB00135445",
"PUB00135446",
"PUB00135447",
"PUB00135448",
"PUB00135449",
"PUB00135450",
"PUB00135451",
"PUB00135452",
"PUB00135453",
"PUB00135454",
"PUB00135455",
"PUB001354... | [
"14871887",
"10352183",
"11278651",
"10415337",
"12083797",
"24529480",
"18077445",
"22972498",
"17976381",
"16122737",
"22912899",
"21159800",
"20429939",
"19821153",
"19473992",
"19053840",
"17803295",
"15735665",
"15703819",
"15247280",
"15107820",
"14516784",
"1184224... | [
"Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein.",
"Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein.",
"Cloning and characterization of LUN, a novel rin... | [
2004,
1999,
2001,
1999,
2002,
2014,
2008,
2012,
2007,
2005,
2012,
2011,
2010,
2010,
2009,
2008,
2007,
2005,
2005,
2004,
2004,
2003,
2002,
2005,
2010
] | 25 | [
"IPR001841"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2951
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
11,
2,
2,
2,
2,
9,
2,
12
] | 8 | true | Domain | Topors, zinc finger, RING-type | Topors, zinc finger, RING-type | Znf_RING-type_Topors | 8 |
IPR058747 | 58,747 | ATPase PglY, C-terminal domain | PglY_C | Domain | 624 | false | false | This entry represents the C-terminal domain of ATPase PglY and similar bacterial proteins. PglY is predicted to be composed of a bundle of α-helices. The ATPase PglY is part of a type 2 BREX system, which provides immunity against bacteriophage infections. It was previously known as the phage growth limitation (Pgl) sy... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26382"
] | [
"BREX_PglY_6th"
] | [
624
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105105",
"PUB00151239",
"PUB00161155"
] | [
"25592393",
"11972785",
"7642495"
] | [
"The phage growth limitation system in Streptomyces coelicolor A(3)2 is a toxin/antitoxin system, comprising enzymes with DNA methyltransferase, protein kinase and ATPase activity.",
"Genetics of the phage growth limitation (Pgl) system of Streptomyces coelicolor A3(2).",
"Two genes involved in the phase-variab... | [
2015,
2002,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
616,
8
] | 2 | [] | [] | 0 | true | Domain | ATPase PglY, C-terminal domain | ATPase PglY, C-terminal domain | PglY_C | 1 |
IPR058748 | 58,748 | ATPase PglY, 5th domain | PglY_5th | Domain | 622 | false | false | This entry represents the 5th domain in ATPase PglY and similar bacterial proteins. The ATPase PglY is part of a type 2 BREX system, which provides immunity against bacteriophage infections. It was previously known as the phage growth limitation (Pgl) system and offers protection against bacteriophage phiC31. The syste... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26381"
] | [
"BREX_PglY_5th"
] | [
622
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105105",
"PUB00151239",
"PUB00161155"
] | [
"25592393",
"11972785",
"7642495"
] | [
"The phage growth limitation system in Streptomyces coelicolor A(3)2 is a toxin/antitoxin system, comprising enzymes with DNA methyltransferase, protein kinase and ATPase activity.",
"Genetics of the phage growth limitation (Pgl) system of Streptomyces coelicolor A3(2).",
"Two genes involved in the phase-variab... | [
2015,
2002,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
614,
8
] | 2 | [] | [] | 0 | true | Domain | ATPase PglY, 5th domain | ATPase PglY, 5th domain | PglY_5th | 1 |
IPR058749 | 58,749 | Homing endonuclease-like | Homing_endonuclease-like | Family | 205 | false | false | This entry represents a family of archaeal proteins that show strong structural similarity to homing endonucleases. This entry also includes putative Cobalamin biosynthesis proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26411"
] | [
"LAGLIDADG_4"
] | [
205
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales"
] | [
3,
202
] | 2 | [] | [] | 0 | true | Family | Homing endonuclease-like | Homing endonuclease-like | Homing_endonuclease-like | 4 |
IPR058750 | 58,750 | Epg5-like, TPR | TPR_Epg5 | Domain | 1,988 | false | false | This is a region of tetratricopeptide (TPR)-like repeats found in Ectopic P granules protein 5 homolog from Drosophila melanogaster (Epg5) and similar proteins mainly from animals. Epg5 plays a role in late steps of autophagy [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26573"
] | [
"TPR_Epg5_2"
] | [
1988
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00070599",
"PUB00070607",
"PUB00161491",
"PUB00161492",
"PUB00161493",
"PUB00161494",
"PUB00161495"
] | [
"20550938",
"23222957",
"26917586",
"22451698",
"24374177",
"25124690",
"29130391"
] | [
"C. elegans screen identifies autophagy genes specific to multicellular organisms.",
"Recessive mutations in EPG5 cause Vici syndrome, a multisystem disorder with defective autophagy.",
"EPG5-related Vici syndrome: a paradigm of neurodevelopmental disorders with defective autophagy.",
"Autophagy genes functio... | [
2010,
2013,
2016,
2012,
2014,
2014,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1988
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
2,
8,
1,
4
] | 6 | true | Domain | Epg5-like, TPR | Epg5-like, TPR | TPR_Epg5 | 6 |
IPR058752 | 58,752 | RDRP, C-terminal head domain | RDRP_C_head | Domain | 6,018 | false | false | This domain is found C-terminal in eukaryotic RDRP proteins. This domain folds into an array of α-helices, and it is known as the head [ ]. The head domain was proposed to interact with incoming template RNA, helping guide the RNA to the active site. RNA dependent RNA polymerases (RDRP) enzymes (RDRP; ) are involved in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26253"
] | [
"RdRP_head"
] | [
6018
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"7eu0",
"7eu1",
"7roz",
"7rqs",
"7w82",
"7w84",
"7w88",
"8xmb",
"8xmc",
"8xmd",
"8xme"
] | 11 | [
"PUB00016353",
"PUB00035781",
"PUB00155792"
] | [
"12553882",
"16691418",
"34903670"
] | [
"Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases.",
"On the origin and functions of RNA-mediated silencing: from protists to man.",
"Structure and RNA template requirements of <i>Arabidopsis</i... | [
2003,
2006,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Eukaryota",
"bioreactor metagenome"
] | [
3,
6014,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
39,
5,
1,
13,
1,
35
] | 6 | true | Domain | RDRP, C-terminal head domain | RDRP, C-terminal head domain | RDRP_C_head | 7 |
IPR058754 | 58,754 | Otogelin-like, N-terminal domain | OTOGL-like_N | Domain | 1,203 | false | false | This entry represents the N-terminal domain in Otogelin-like proteins in proteins from vertebrates. This domain is approximately 30 amino acids long and contains conserved cysteine residues that stabilise β-sheets, forming an EGF-like fold. Otogelin is a structurally complex glycoprotein with specialised roles in the i... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25961"
] | [
"OTOGL_N"
] | [
1203
] | 1 | [
"REACTOME"
] | [
"R-HSA-9662361"
] | [
"REACTOME:R-HSA-9662361"
] | 1 | [] | 0 | [
"PUB00101009",
"PUB00161232",
"PUB00161486"
] | [
"31776257",
"9405633",
"17911254"
] | [
"Otogelin, otogelin-like, and stereocilin form links connecting outer hair cell stereocilia to each other and the tectorial membrane.",
"Otogelin: a glycoprotein specific to the acellular membranes of the inner ear.",
"Gel-forming mucins appeared early in metazoan evolution."
] | [
2019,
1997,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1203
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
2,
3
] | 4 | true | Domain | Otogelin-like, N-terminal domain | Otogelin-like, N-terminal domain | OTOGL-like_N | 1 |
IPR058755 | 58,755 | Otogelin-like, Fn1-VW hybrid domain | Fn1-VW_OTOGL | Domain | 1,337 | false | false | This entry represents a Fn1-VW hybrid domain in Otogelin proteins from vertebrates. The Fn1-VW hybrid domain combines the VW β-sandwich with an Fn1-like subdomain (antiparallel β-sheets linked by loops). Otogelin is a structurally complex glycoprotein with specialised roles in the inner ear membranes. While it shares s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25960"
] | [
"Fn1-VW_OTOGL"
] | [
1337
] | 1 | [
"REACTOME"
] | [
"R-HSA-9662361"
] | [
"REACTOME:R-HSA-9662361"
] | 1 | [] | 0 | [
"PUB00101009",
"PUB00161232",
"PUB00161486"
] | [
"31776257",
"9405633",
"17911254"
] | [
"Otogelin, otogelin-like, and stereocilin form links connecting outer hair cell stereocilia to each other and the tectorial membrane.",
"Otogelin: a glycoprotein specific to the acellular membranes of the inner ear.",
"Gel-forming mucins appeared early in metazoan evolution."
] | [
2019,
1997,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1337
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
3,
6
] | 4 | true | Domain | Otogelin-like, Fn1-VW hybrid domain | Otogelin-like, Fn1-VW hybrid domain | Fn1-VW_OTOGL | 5 |
IPR058756 | 58,756 | Liposome tubulation protein MamY, C-terminal domain | MamY_C | Domain | 10 | false | false | This entry represents the C-terminal α-helical domain of Liposome tubulation protein MamY and similar proteins from rhodospirillales. The magnetosome MamY family is involved in the formation of mature magnetosomes by causing tubulation when interacting with magnetosome-derived liposomes. It binds preferentially to card... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26389"
] | [
"MamY_C"
] | [
10
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106122",
"PUB00106123",
"PUB00161334",
"PUB00161647"
] | [
"20345667",
"30039923",
"30367002",
"31358981"
] | [
"Identification and functional characterization of liposome tubulation protein from magnetotactic bacteria.",
"Enhanced Tubulation of Liposome Containing Cardiolipin by MamY Protein from Magnetotactic Bacteria.",
"Work Patterns of MamXY Proteins during Magnetosome Formation in <i>Magnetospirillum gryphiswaldens... | [
2010,
2018,
2019,
2019
] | 4 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | Liposome tubulation protein MamY, C-terminal domain | Liposome tubulation protein MamY, C-terminal domain | MamY_C | 5 |
IPR058757 | 58,757 | UFSP2, N-terminal MPN-like domain | UFSP2_MPN_N | Domain | 299 | false | false | This entry represents the N-terminal domain in UFSP2 (Probable Ufm1-specific protease 2) and similar proteins found in insects. UFM1-specific isopeptidase 1 and 2 (UFSP1 and UFSP2) are cysteine peptidases essential for both the processing and activation of ubiquitin-fold modifier 1 (Ufm1, ) and for releasing Ufm1 from ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26560"
] | [
"UFSP2_MPN_insect"
] | [
299
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034739",
"PUB00034740",
"PUB00151643",
"PUB00154319",
"PUB00154320"
] | [
"17182609",
"15071506",
"21228277",
"27240952",
"29251776"
] | [
"Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2.",
"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier.",
"Structure of ubiquitin-fold modifier 1-specific protease UfSP2.",
"The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition a... | [
2007,
2004,
2011,
2016,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Pancrustacea"
] | [
299
] | 1 | [
"Drosophila melanogaster"
] | [
1
] | 1 | true | Domain | UFSP2, N-terminal MPN-like domain | UFSP2, N-terminal MPN-like domain | UFSP2_MPN_N | 1 |
IPR058758 | 58,758 | E3 ubiquitin-protein ligase RNF216, UBA domain | UBA_RNF216 | Domain | 1,930 | false | false | This is the predicted UBA domain found in RNF216 and similar animal and fungal sequences. E3 ubiquitin-protein ligase RNF216, also known as Triad domain-containing protein 3 (Triad3A), is a RBR-type E3 ubiquitin-protein ligase that interacts with several components of Toll-like receptor (TLR) signalling and promotes th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26112"
] | [
"UBA_RNF216"
] | [
1930
] | 1 | [
"REACTOME"
] | [
"R-HSA-936440"
] | [
"REACTOME:R-HSA-936440"
] | 1 | [] | 0 | [
"PUB00103513",
"PUB00103514",
"PUB00103515",
"PUB00103516",
"PUB00103517",
"PUB00103518",
"PUB00103519",
"PUB00103520",
"PUB00103521",
"PUB00103522",
"PUB00161507",
"PUB00161508",
"PUB00161509",
"PUB00161510"
] | [
"23656588",
"15107846",
"25841028",
"16968706",
"15367624",
"11854271",
"19893624",
"25484083",
"21270397",
"24945773",
"34998453",
"30649198",
"33724554",
"37439148"
] | [
"Ataxia, dementia, and hypogonadotropism caused by disordered ubiquitination.",
"Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors.",
"RNF216 mutations as a novel cause of autosomal recessive Huntington-like disorder.",
"Triad3A regulates ubiquitination and proteasomal degradation of RIP1... | [
2013,
2004,
2015,
2006,
2004,
2002,
2009,
2014,
2011,
2014,
2022,
2019,
2021,
2023
] | 14 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1930
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus"
] | [
1,
5,
1,
1,
4
] | 5 | true | Domain | E3 ubiquitin-protein ligase RNF216, UBA domain | E3 ubiquitin-protein ligase RNF216, UBA domain | UBA_RNF216 | 4 |
IPR058759 | 58,759 | Pilin, mycobacteria | Pilin_mycobact | Family | 276 | false | false | The mycobacterial pilin family comprises structural subunits of pili, which are thin, flexible, coiled-coil, aggregative fibres. These pili play a crucial role in mediating adhesion to the extracellular matrix, facilitating direct interaction with the host epithelium during infection, particularly in the lungs or other... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26380"
] | [
"Pilin_Mycobact"
] | [
276
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161414"
] | [
"17360408"
] | [
"Mycobacterium tuberculosis produces pili during human infection."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Mycobacteriales"
] | [
276
] | 1 | [] | [] | 0 | true | Family | Pilin, mycobacteria | Pilin, mycobacteria | Pilin_mycobact | 8 |
IPR058760 | 58,760 | RESC11-like | RESC11-like | Family | 55 | false | false | This entry represents the RNA-editing substrate-binding complex 11 protein (RESC11) from Trypanosoma brucei, a component of RESC which together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs [ ]. RESC stabilises gRNAs a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26230"
] | [
"RESC11"
] | [
55
] | 1 | [] | [] | [] | 0 | [
"8fni",
"8fnk"
] | 2 | [
"PUB00160174"
] | [
"37410820"
] | [
"Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
55
] | 1 | [] | [] | 0 | true | Family | RESC11-like | RESC11-like | RESC11-like | 5 |
IPR058762 | 58,762 | Collectin-12 domain | COLEC12_dom | Domain | 1,200 | false | false | This domain is found in human Collectin-12 (COLEC12) and similar sequences from vertebrates. This domain, which is often found associated with and , is predicted to adopt an α-helical configuration. COLEC12 is a Scavenger receptor that displays several functions associated with host defence. It promotes binding and pha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26004"
] | [
"COLEC12"
] | [
1200
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-198933",
"R-BTA-3000480",
"R-HSA-198933",
"R-HSA-3000480"
] | [
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-3000480",
"REACTOME:R-HSA-198933",
"REACTOME:R-HSA-3000480"
] | 4 | [] | 0 | [
"PUB00161181",
"PUB00161182",
"PUB00161183",
"PUB00161184",
"PUB00161185",
"PUB00161186"
] | [
"11162630",
"11564734",
"12761161",
"15845541",
"16868960",
"11718900"
] | [
"Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family.",
"The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells.",
"SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antige... | [
2001,
2001,
2003,
2005,
2006,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1200
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
2,
4
] | 4 | true | Domain | Collectin-12 domain | Collectin-12 domain | COLEC12_dom | 2 |
IPR058763 | 58,763 | RDR1/2-like, RRM domain | RRM_RDR1/2-like | Domain | 1,715 | false | false | This RRM domain is found N-terminal in the RNA-dependent RNA polymerase 1 and 2 (RDR1, RDR2) from Arabidopsis thaliana and related plant proteins. RDR1/2 are involved in the production of small interfering RNAs (siRNAs). RDR1 is involved in antiviral silencing, amplifying silencing signals during viral infections [ , ]... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26250"
] | [
"RRM_RdRP1_2"
] | [
1715
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"7eu0",
"7eu1",
"7roz",
"7rqs",
"7w84",
"7w88",
"8xmb",
"8xmc",
"8xmd",
"8xme"
] | 10 | [
"PUB00148894",
"PUB00148896",
"PUB00155792",
"PUB00155793"
] | [
"19308254",
"19966292",
"34903670",
"23142082"
] | [
"Small RNA deep sequencing reveals role for Arabidopsis thaliana RNA-dependent RNA polymerases in viral siRNA biogenesis.",
"RNAi-mediated viral immunity requires amplification of virus-derived siRNAs in Arabidopsis thaliana.",
"Structure and RNA template requirements of <i>Arabidopsis</i> RNA-DEPENDENT RNA POL... | [
2009,
2010,
2021,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1715
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
3,
8
] | 3 | true | Domain | RDR1/2-like, RRM domain | RDR1/2-like, RRM domain | RRM_RDR1/2-like | 1 |
IPR058764 | 58,764 | NPHP4, SK-like domain | NPHP4_SK | Domain | 935 | false | false | This entry represents a small-conductance potassium channel (SK) like domain in human Nephrocystin-4 (NPHP4) and related eukaryotic proteins. NPHP4 is involved in the organisation of apical junctions and the subapical actin network in multiciliated epithelial cells. It plays a crucial role in building functional cilia ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26173"
] | [
"NPHP4_SK"
] | [
935
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2028269",
"R-HSA-5620912",
"R-MMU-2028269",
"R-MMU-5620912"
] | [
"REACTOME:R-HSA-2028269",
"REACTOME:R-HSA-5620912",
"REACTOME:R-MMU-2028269",
"REACTOME:R-MMU-5620912"
] | 4 | [] | 0 | [
"PUB00070859",
"PUB00074744",
"PUB00129248"
] | [
"15661758",
"16339905",
"21357692"
] | [
"Characterization of the nephrocystin/nephrocystin-4 complex and subcellular localization of nephrocystin-4 to primary cilia and centrosomes.",
"Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations.",
"Nephrocystin-4 regulates Pyk2-induced... | [
2005,
2005,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
935
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
2,
3,
4
] | 4 | true | Domain | NPHP4, SK-like domain | NPHP4, SK-like domain | NPHP4_SK | 8 |
IPR058765 | 58,765 | NPHP4, C2-like domain | NPHP4_C2-like | Domain | 1,485 | false | false | This entry represents the third C2 domain in human Nephrocystin-4 (NPHP4) and related eukaryotic proteins. C2 domains have not been reviously identified in NPHP4. However, RPGRIP1 C2 domain interacts with NPH4 which could hint a C2 homology region in NPH4 [ ]. NPHP4 is involved in the organisation of apical junctions a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26186"
] | [
"NPHP4_C2_3rd"
] | [
1485
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2028269",
"R-HSA-5620912",
"R-MMU-2028269",
"R-MMU-5620912"
] | [
"REACTOME:R-HSA-2028269",
"REACTOME:R-HSA-5620912",
"REACTOME:R-MMU-2028269",
"REACTOME:R-MMU-5620912"
] | 4 | [] | 0 | [
"PUB00070859",
"PUB00074744",
"PUB00129248"
] | [
"15661758",
"16339905",
"21357692"
] | [
"Characterization of the nephrocystin/nephrocystin-4 complex and subcellular localization of nephrocystin-4 to primary cilia and centrosomes.",
"Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations.",
"Nephrocystin-4 regulates Pyk2-induced... | [
2005,
2005,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1485
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
8,
4,
3,
3
] | 5 | true | Domain | NPHP4, C2-like domain | NPHP4, C2-like domain | NPHP4_C2-like | 7 |
IPR058766 | 58,766 | XRCC3/RAD51 homolog 2, helix-hairpin-helix domain | HHH_XRCC3_RAD51B | Domain | 2,544 | false | false | This domain is found at the N-terminal end of human DNA repair protein XRCC3 and RAD51 homolog 2 (RAD51B) and similar proteins from animals and plants. This domain is predicted to adopt a helix-hairpin-helix (HHH) fold. XRCC3 is involved in the homologous recombination repair pathway of double-stranded DNA, thought to ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26169"
] | [
"HHH_XRCC3_RpoA"
] | [
2544
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"R-HSA-5693579",
"R-HSA-5693616",
"R-HSA-9701192",
"R-HSA-9704331",
"R-HSA-9704646",
"R-HSA-9709603",
"R-HSA-983231",
"R-MMU-5685942",
"R-MMU-5693568",
"R-MMU-5693579",
"R-MMU-5693616",
"R-MMU-983231"
] | [
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693579",
"REACTOME:R-HSA-5693616",
"REACTOME:R-HSA-9701192",
"REACTOME:R-HSA-9704331",
"REACTOME:R-HSA-9704646",
"REACTOME:R-HSA-9709603",
"REACTOME:R-HSA-983231",
"REACTOME:R-MMU-5685942",
"REACTOME... | 15 | [
"8faz",
"8gbj",
"8gja",
"8ouy",
"8ouz",
"9svy",
"9sw0"
] | 7 | [
"PUB00073165",
"PUB00073166",
"PUB00073168",
"PUB00102685",
"PUB00161265",
"PUB00161266",
"PUB00161267"
] | [
"11751635",
"23149936",
"12441335",
"23108668",
"20413593",
"11751636",
"11842113"
] | [
"Identification and purification of two distinct complexes containing the five RAD51 paralogs.",
"Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway.",
"Holliday junction binding activity of the human Rad51B protein.",
"The RAD51 paralog... | [
2001,
2013,
2003,
2013,
2010,
2001,
2002
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Sphingobacterium"
] | [
2541,
3
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
3,
5,
13,
3,
2,
9,
6
] | 7 | true | Domain | XRCC3/RAD51 homolog 2, helix-hairpin-helix domain | XRCC3/RAD51 homolog 2, helix-hairpin-helix domain | HHH_XRCC3_RAD51B | 3 |
IPR058767 | 58,767 | MCM8, N-terminal domain | MCM8_N | Domain | 1,555 | false | false | This domain is found N-terminal in the DNA helicase MCM8 and related proteins. Minichromosome maintenance 8 (MCM8) is a member of the minichromosome maintenance family, which possesses helicase and ATPase activity. It interacts with MCM9 and participates in homologous recombination repair [ ] and (HR) repair pathway. M... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26065"
] | [
"MCM8_N"
] | [
1555
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.6.2.4",
"R-BTA-176187",
"R-BTA-68689",
"R-BTA-68949",
"R-BTA-68962",
"R-DME-176187",
"R-DME-68689",
"R-DME-68949",
"R-DME-68962",
"R-GGA-176187",
"R-GGA-68689",
"R-GGA-68949",
"R-GGA-68962",
"R-HSA-113507",
"R-HSA-176187",
"R-HSA-176974",
"R-HSA-68689",
"R-HSA-68949",
"R-HSA-6... | [
"EC:5.6.2.4",
"REACTOME:R-BTA-176187",
"REACTOME:R-BTA-68689",
"REACTOME:R-BTA-68949",
"REACTOME:R-BTA-68962",
"REACTOME:R-DME-176187",
"REACTOME:R-DME-68689",
"REACTOME:R-DME-68949",
"REACTOME:R-DME-68962",
"REACTOME:R-GGA-176187",
"REACTOME:R-GGA-68689",
"REACTOME:R-GGA-68949",
"REACTOME:R... | 30 | [
"7dp3",
"7w7p",
"7wi7",
"7yox",
"8s91",
"8s92",
"8s94"
] | 7 | [
"PUB00141337",
"PUB00161335"
] | [
"23401855",
"34043945"
] | [
"The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to facilitate homologous recombination.",
"Structural study of the N-terminal domain of human MCM8/9 complex."
] | [
2013,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1555
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
3,
1,
2
] | 5 | true | Domain | MCM8, N-terminal domain | MCM8, N-terminal domain | MCM8_N | 6 |
IPR058768 | 58,768 | MCM9, N-terminal domain | MCM9_N | Domain | 1,874 | false | false | This domain is found N-terminal in the DNA helicase MCM9 and related proteins. MCM9 is a component of MCM8/MCM9 complex which is involved in homologous recombination repair pathway. Its dysfunction can cause genome instability. MCM8/MCM9 complex forms a 3:3 hetero-hexamer in an alternating pattern [ ]. The MCM8/MCM9 co... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26066"
] | [
"MCM9_N"
] | [
1874
] | 1 | [
"EC"
] | [
"5.6.2.4"
] | [
"EC:5.6.2.4"
] | 1 | [
"7dpd",
"7w7p",
"7wi7",
"7yox",
"8s91",
"8s92",
"8s94"
] | 7 | [
"PUB00141337",
"PUB00161335"
] | [
"23401855",
"34043945"
] | [
"The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to facilitate homologous recombination.",
"Structural study of the N-terminal domain of human MCM8/9 complex."
] | [
2013,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1874
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
3,
13,
2,
2,
3,
2
] | 7 | true | Domain | MCM9, N-terminal domain | MCM9, N-terminal domain | MCM9_N | 7 |
IPR058769 | 58,769 | MCMDC2, N-terminal domain | MCMDC2_N | Domain | 1,049 | false | false | This domain is found N-terminal in the Minichromosome maintenance domain-containing protein 2 (MCMDC2) and related proteins. This domain is related to the N-terminal domain of MCM proteins and is predicted to adopt similar structure. MCMDC2 is essential for invasion of homologous sequences by RAD51- and DMC1-coated sin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26063"
] | [
"MCMDC2_N"
] | [
1049
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161336",
"PUB00161337"
] | [
"27986806",
"27760146"
] | [
"Repair of Meiotic DNA Breaks and Homolog Pairing in Mouse Meiosis Requires a Minichromosome Maintenance (MCM) Paralog.",
"Alignment of Homologous Chromosomes and Effective Repair of Programmed DNA Double-Strand Breaks during Mouse Meiosis Require the Minichromosome Maintenance Domain Containing 2 (MCMDC2) Protei... | [
2017,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mycoplasmopsis bovigenitalium"
] | [
1048,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
4,
6
] | 4 | true | Domain | MCMDC2, N-terminal domain | MCMDC2, N-terminal domain | MCMDC2_N | 2 |
IPR058770 | 58,770 | ABCF3, PWI-like helical bundle domain | PWI_ABCF3 | Domain | 2,360 | false | false | This domain is found in the human ATP-binding cassette sub-family F member 3 (ABCF3) and related proteins. ABCF3 enhances OAS1B-mediated flavivirus resistance by localising to the virus-remodelled endoplasmic reticulum and reducing viral RNA synthesis [ , ]. In humans, ABCF3 promotes cell proliferation through interact... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26051"
] | [
"PWI_ABCF3"
] | [
2360
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161427",
"PUB00161428"
] | [
"22623793",
"31413116"
] | [
"Identification of novel host cell binding partners of Oas1b, the protein conferring resistance to flavivirus-induced disease in mice.",
"Biochemical characterization of the mouse ABCF3 protein, a partner of the flavivirus-resistance protein OAS1B."
] | [
2012,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2360
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
1,
1,
5,
3,
3,
4,
4
] | 9 | true | Domain | ABCF3, PWI-like helical bundle domain | ABCF3, PWI-like helical bundle domain | PWI_ABCF3 | 8 |
IPR058771 | 58,771 | CCDC43, PWI-like domain | PWI_CCDC43 | Domain | 1,395 | false | false | This domain is found in the human Coiled-Coil Domain-Containing protein 43 (CCDC43) and related proteins. The domain represented by this entry has a detectable similarity to known PWI domains and is predicted to adopt similar structure. CCDC43 is associated with cancer progression, particularly in gastric cancer and he... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26091"
] | [
"PWI_CCDC43"
] | [
1395
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161429"
] | [
"32278016"
] | [
"The CCDC43-ADRM1 axis regulated by YY1, promotes proliferation and metastasis of gastric cancer."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1395
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
3,
1,
3
] | 5 | true | Domain | CCDC43, PWI-like domain | CCDC43, PWI-like domain | PWI_CCDC43 | 2 |
IPR058772 | 58,772 | ADGRG2, N-terminal domain | ADGRG2_N | Domain | 993 | false | false | This domain is found in the homologues of ADGRG2 (adhesion G protein-coupled receptor G2). The domain represented by this entry precedes the GAIN and the transmembrane domains. It is predicted to adopt a globular α/β structure consisting of four-stranded antiparallel β-sheet packed on one side with two α-helices resemb... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26152"
] | [
"ADGRG2_N"
] | [
993
] | 1 | [] | [] | [] | 0 | [
"7wui",
"7xke",
"7yp7",
"8ykd"
] | 4 | [
"PUB00137747",
"PUB00161115",
"PUB00161116",
"PUB00161242",
"PUB00161660",
"PUB00161661",
"PUB00161662"
] | [
"24227709",
"15367682",
"29393851",
"35982227",
"33303626",
"34234254",
"39884271"
] | [
"Gpr126 functions in Schwann cells to control differentiation and myelination via G-protein activation.",
"Targeted deletion of the epididymal receptor HE6 results in fluid dysregulation and male infertility.",
"Gq activity- and β-arrestin-1 scaffolding-mediated ADGRG2/CFTR coupling are required for male fertil... | [
2013,
2004,
2018,
2022,
2021,
2021,
2025
] | 7 | [] | [] | 0 | 0 | null | [
"Tetrapoda"
] | [
993
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
6,
11
] | 3 | true | Domain | ADGRG2, N-terminal domain | ADGRG2, N-terminal domain | ADGRG2_N | 9 |
IPR058773 | 58,773 | Endo-beta-1,2-glucanase SGL | SGL_GH162 | Domain | 400 | false | false | This entry represents the endo-beta-1,2-glucanase (SGL) from Talaromyces funiculosus, a soil fungus, and related proteins. TfSGL specifically hydrolyses linear and cyclic beta-1,2-glucans to sophorose (Glc-beta-1,2-Glc) as a main product [ ]. TfSGL is an inverting enzyme and belongs to GH162 family. This enzyme adopts ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26157"
] | [
"SGL_GH162"
] | [
400
] | 1 | [] | [] | [] | 0 | [
"6imu",
"6imv",
"6imw"
] | 3 | [
"PUB00158834"
] | [
"30926603"
] | [
"Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Candidatus Abzuiibacterium crystallinum",
"Eukaryota"
] | [
1,
399
] | 2 | [] | [] | 0 | true | Domain | Endo-beta-1,2-glucanase SGL | Endo-beta-1,2-glucanase SGL | SGL_GH162 | 1 |
IPR058774 | 58,774 | RNA-editing substrate-binding complex 7 protein | RESC7 | Domain | 70 | false | false | This domain is found in the RNA-editing substrate-binding complex 7 protein (RESC7) from Trypanosoma brucei, a component of RESC which together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs [ ]. RESC stabilises gRNAs a... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF26165",
"cd23679"
] | [
"RESC7",
"RESC7"
] | [
70,
64
] | 2 | [] | [] | [] | 0 | [
"8fnc",
"8fnf",
"8fni",
"8fnk"
] | 4 | [
"PUB00157634",
"PUB00157638",
"PUB00157639",
"PUB00158232",
"PUB00158233",
"PUB00160174"
] | [
"32191849",
"30213880",
"33677542",
"26447184",
"25225332",
"37410820"
] | [
"Lexis and Grammar of Mitochondrial RNA Processing in Trypanosomes.",
"Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes.",
"Trypanosome RNAEditing Substrate Binding Complex integrity and function depends on the upstream action of RESC10.",
"Integrity of the core mit... | [
2020,
2018,
2021,
2015,
2014,
2023
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
70
] | 1 | [] | [] | 0 | true | Domain | RNA-editing substrate-binding complex 7 protein | RNA-editing substrate-binding complex 7 protein | RESC7 | 5 |
IPR058775 | 58,775 | DUF8054, central domain | DUF8054_M | Domain | 697 | false | false | This entry represents the central α+β domain found in a group of uncharacterised proteins from halobacteria. The function of these proteins is unknown. This domain is associated with and . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26238"
] | [
"DUF8054_M"
] | [
697
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
697
] | 1 | [] | [] | 0 | true | Domain | DUF8054, central domain | DUF8054, central domain | DUF8054_M | 6 |
IPR058776 | 58,776 | Potassium/proton antiporter subunit KhtT-like, N-terminal domain | KhtT-like_N | Domain | 4,562 | false | false | This domain is found at the N-terminal end of KhtT from Bacillus subtilis and similar proteins from prokaryotes. This domain adopts an unusual fold, comprised of a twisted five antiparallel β-sheet followed by an α-helix [ ]. KhtT is required for activity of the potassium/proton antiporter KhtU. It is involved in prote... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25991"
] | [
"KhtT_N"
] | [
4562
] | 1 | [] | [] | [] | 0 | [
"7agv",
"7agw",
"7agy",
"7ahm",
"7aht"
] | 5 | [
"PUB00044836",
"PUB00060345",
"PUB00086658",
"PUB00161311",
"PUB00161312"
] | [
"17679694",
"14987767",
"24330391",
"33790011",
"12923086"
] | [
"Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity.",
"Modulation of the K+ efflux activity of Bacillus subtilis YhaU by YhaT and the C-terminal region of YhaS.",
"Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent a... | [
2007,
2004,
2014,
2021,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"freshwater metagenome"
] | [
4237,
3,
316,
6
] | 4 | [] | [] | 0 | true | Domain | Potassium/proton antiporter subunit KhtT-like, N-terminal domain | Potassium/proton antiporter subunit KhtT-like, N-terminal domain | KhtT-like_N | 1 |
IPR058777 | 58,777 | TXNDC11, thioredoxin-like domain | TXNDC11_thioredoxin | Domain | 1,110 | false | false | This domain is found in the human Thioredoxin domain-containing protein 11 (TXNDC11) and related proteins from vertebrates. TXNDC11 is overexpressed in glioma and its high expression levels are usually associated with a poor clinical prognosis [ ]. TXNDC11 acts as a redox regulator involved in protein folding of thyroi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26234"
] | [
"TXNDC11_2nd"
] | [
1110
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00116576",
"PUB00161500"
] | [
"15561711",
"35116356"
] | [
"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein.",
"High expression of <i>TXNDC11</i> indicated unfavorable prognosis of glioma."
] | [
2005,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
1110
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
6,
5
] | 4 | true | Domain | TXNDC11, thioredoxin-like domain | TXNDC11, thioredoxin-like domain | TXNDC11_thioredoxin | 3 |
IPR058778 | 58,778 | FAR1-related sequence 11-like, HTH-like domain | HTH_FAR1-11-like | Domain | 1,800 | false | false | This entry represents an uncharacterised domain in FAR1-related sequence 11 proteins from plants. This domain contains a helix-turn-helix structure. This domain is also found in the putative protein FAR1-related sequence 10 from Arabidopsis thaliana. FAR1 proteins are involved in the regulation of light-mediated develo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26175"
] | [
"HTH_FAR1"
] | [
1800
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044720",
"PUB00161280",
"PUB00161281"
] | [
"18715961",
"37384577",
"29930561"
] | [
"Discrete and essential roles of the multiple domains of Arabidopsis FHY3 in mediating phytochrome A signal transduction.",
"Emerging Roles of FHY3 and FAR1 as System Integrators in Plant Development.",
"FAR1-RELATED SEQUENCE (FRS) and FRS-RELATED FACTOR (FRF) Family Proteins in <i>Arabidopsis</i> Growth and De... | [
2008,
2023,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1800
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica"
] | [
11,
4
] | 2 | true | Domain | FAR1-related sequence 11-like, HTH-like domain | FAR1-related sequence 11-like, HTH-like domain | HTH_FAR1-11-like | 9 |
IPR058779 | 58,779 | NUP210, Ig-like domain 13 | Ig_NUP210_13th | Domain | 2,443 | false | false | This domain is found in Nuclear pore membrane glycoprotein 210 (NUP210) and its homologues. The domain represented by this entry is one of these constituent Ig-like domains and has a significant structural similarity to cadherin domains. NUP210 is essential for nuclear pore assembly and fusion, nuclear pore spacing, as... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26181"
] | [
"Ig_NUP210_13th"
] | [
2443
] | 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-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-DME-170822",
"R-DME-3108214",
"R-DME-3301854",
"R-DME-4085377",
"R-DME-4551638",
"R-DME-4615885",
"R-DME-5578749",
"R-HSA-1169408",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-HSA-165054",
"R-... | [
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3301854",
"REACTOME:R-DME-4085377",
"REACTOME:R-DME-4551638",
"REACTOME:R-DME-4615885",
"REACTOME:R-DME-5578749",
"REACTOME:R-H... | 69 | [
"7r5j",
"7r5k",
"9hcj"
] | 3 | [
"PUB00154131",
"PUB00161295"
] | [
"35679397",
"2738089"
] | [
"AI-based structure prediction empowers integrative structural analysis of human nuclear pores.",
"Primary structure analysis of an integral membrane glycoprotein of the nuclear pore."
] | [
2022,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2443
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
4,
5,
7
] | 6 | true | Domain | NUP210, Ig-like domain 13 | NUP210, Ig-like domain 13 | Ig_NUP210_13th | 3 |
IPR058780 | 58,780 | YhfM-like domain | YhfM-like_dom | Domain | 1,359 | false | false | This entry represents a domain that cover most of the length of the Bacillus subtilis uncharacterised YhfM protein and similar sequences from bacilalles. In some sequences, this domain is found associated with | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26353"
] | [
"YhfM"
] | [
1359
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Rhizophagus irregularis",
"metagenomes"
] | [
1356,
1,
2
] | 3 | [] | [] | 0 | true | Domain | YhfM-like domain | YhfM-like domain | YhfM-like_dom | 2 |
IPR058781 | 58,781 | AprE-like, long alpha-helical hairpin | HH_AprE-like | Domain | 13,725 | false | false | This domain is found in Alkaline protease secretion protein AprE from Pseudomonas aeruginosa and related proteins including Type I secretion system membrane fusion protein PrsE, Exopolysaccharide production protein ExoF and Proteases secretion protein PrtE. AprE is involved in the secretion of alkaline protease [ ]. Pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25994"
] | [
"HH_AprE"
] | [
13725
] | 1 | [] | [] | [] | 0 | [
"5nen"
] | 1 | [
"PUB00001184",
"PUB00001820",
"PUB00161136",
"PUB00161649"
] | [
"2184029",
"1427098",
"11902715",
"8439670"
] | [
"Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin.",
"Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways.",
"The Rhizo... | [
1990,
1992,
1997,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nitrosopumilus salarius BD31",
"Eukaryota",
"unclassified sequences"
] | [
13605,
1,
35,
84
] | 4 | [] | [] | 0 | true | Domain | AprE-like, long alpha-helical hairpin | AprE-like, long alpha-helical hairpin | HH_AprE-like | 7 |
IPR058782 | 58,782 | GIY-YIG domain | GIY_YIG_3 | Domain | 305 | false | false | This entry represents a domain from a family of uncharacterised proteins found predominantly in halophilic archaea, specifically within the Halobacteria class. The proteins containing this domain are typically around 230 to 240 amino acids in length. The domain is highly conserved across various species within the Sten... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26468"
] | [
"GIY_YIG_3"
] | [
305
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
133,
153,
19
] | 3 | [] | [] | 0 | true | Domain | GIY-YIG domain | GIY-YIG domain | GIY_YIG_3 | 8 |
IPR058783 | 58,783 | IREH1/IRE-like, N-terminal domain | IREH1/IRE-like_N | Domain | 2,184 | false | false | This domain is found towards the N-terminal end of Probable serine/threonine protein kinase IREH1 and IRE from Arabidopsis thaliana and similar plant sequences. IREH1 may be involved in root hair elongation. IRE modulates root tip growth and may play a common role in the tip growth of plant cells [ ]. This domain is pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26031"
] | [
"IREH1"
] | [
2184
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [] | 0 | [
"PUB00161309"
] | [
"12000677"
] | [
"The IRE gene encodes a protein kinase homologue and modulates root hair growth in Arabidopsis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2184
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
17,
10,
30
] | 3 | true | Domain | IREH1/IRE-like, N-terminal domain | IREH1/IRE-like, N-terminal domain | IREH1/IRE-like_N | 9 |
IPR058785 | 58,785 | FCP1, barrel-sandwich hybrid domain | BSH_FCP1 | Domain | 849 | false | false | This domain is found in the human RNA polymerase II subunit A C-terminal domain phosphatase, also known as Fcp1, and related animal proteins. This barrel-sandwich hybrid domain is found at the N-terminal end of Fcp1. This domain contains a large insertion that is likely disordered. Fcp1 catalyses the dephosphorylation ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26077"
] | [
"BSH_Fcp1"
] | [
849
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-112382",
"R-HSA-113418",
"R-HSA-167152",
"R-HSA-167158",
"R-HSA-167200",
"R-HSA-167238",
"R-HSA-167242",
"R-HSA-167243",
"R-HSA-167246",
"R-HSA-167287",
"R-HSA-167290",
"R-HSA-674695",
"R-HSA-6796648",
"R-HSA-75955",
"R-MMU-112382",
"R-MMU-113418",
"R-MMU-674695",
"R-MMU-679... | [
"REACTOME:R-HSA-112382",
"REACTOME:R-HSA-113418",
"REACTOME:R-HSA-167152",
"REACTOME:R-HSA-167158",
"REACTOME:R-HSA-167200",
"REACTOME:R-HSA-167238",
"REACTOME:R-HSA-167242",
"REACTOME:R-HSA-167243",
"REACTOME:R-HSA-167246",
"REACTOME:R-HSA-167287",
"REACTOME:R-HSA-167290",
"REACTOME:R-HSA-674... | 19 | [] | 0 | [
"PUB00090490",
"PUB00142978"
] | [
"12721286",
"22692537"
] | [
"A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.",
"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
] | [
2003,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Selenobaculum gibii"
] | [
848,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
2,
3
] | 4 | true | Domain | FCP1, barrel-sandwich hybrid domain | FCP1, barrel-sandwich hybrid domain | BSH_FCP1 | 4 |
IPR058786 | 58,786 | LcnD/ComB-like, barrel-sandwich hybrid domain | BSH_LcnD/ComB | Domain | 728 | false | false | This domain is found in the Lactococcin A secretion protein LcnD from Lactococcus lactis and related proteins, including Transport protein ComB and Mesentericin Y105 secretion protein MesE. LcnD is a protein involved in the secretion system of lactococcin A. As a part of this system it interacts with LcnC [ ]. ComB bel... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25935"
] | [
"BSH_LcnD"
] | [
728
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00087451",
"PUB00161880"
] | [
"11731132",
"7883181"
] | [
"Proteins of the lactococcin A secretion system: lcnD encodes two in-frame proteins.",
"Competence for genetic transformation in Streptococcus pneumoniae: organization of a regulatory locus with homology to two lactococcin A secretion genes."
] | [
2001,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine metagenome"
] | [
727,
1
] | 2 | [] | [] | 0 | true | Domain | LcnD/ComB-like, barrel-sandwich hybrid domain | LcnD/ComB-like, barrel-sandwich hybrid domain | BSH_LcnD/ComB | 2 |
IPR058787 | 58,787 | D-apionate lactonase, TIM barrel domain | ApnL_M | Domain | 798 | false | false | This entry represents the central TIM barrel domain of ApnL. This domain is likely the catalytic domain and contains the active site of the enzyme. The TIM barrel fold is a common structural motif in many enzymes that catalyse diverse reactions. This domain can also be found C-terminal in uncharacterised proteins or in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25838"
] | [
"Apionate_lact_M"
] | [
798
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091681"
] | [
"29867142"
] | [
"Functional assignment of multiple catabolic pathways for D-apiose."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Effrenium voratum",
"unclassified sequences"
] | [
779,
1,
18
] | 3 | [] | [] | 0 | true | Domain | D-apionate lactonase, TIM barrel domain | D-apionate lactonase, TIM barrel domain | ApnL_M | 9 |
IPR058788 | 58,788 | D-apionate lactonase, N-terminal domain | ApnL_N | Domain | 803 | false | false | This entry represents the N-terminal domain in ApnL proteins. D-apionate lactonase (ApnL) hydrolyses D-apionolactone to D-apionate. The protein is involved in D-apiose catabolism pathways in bacteria. D-apiose is a branched pentose found in the cell walls of higher plants [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25837"
] | [
"Apionate_lact_N"
] | [
803
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091681"
] | [
"29867142"
] | [
"Functional assignment of multiple catabolic pathways for D-apiose."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Effrenium voratum",
"unclassified sequences"
] | [
785,
1,
17
] | 3 | [] | [] | 0 | true | Domain | D-apionate lactonase, N-terminal domain | D-apionate lactonase, N-terminal domain | ApnL_N | 7 |
IPR058789 | 58,789 | D-apionate lactonase, C-terminal domain | ApnL_C | Domain | 650 | false | false | This entry represents the C-terminal immunoglobulin-like domain of ApnL. This domain likely plays a role in protein stability, substrate recognition, or protein-protein interactions. The immunoglobulin-like fold is found in many different proteins with diverse functions. This entry lacks the first strand of the Ig-fold... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25839"
] | [
"Apionate_lact_C"
] | [
650
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091681"
] | [
"29867142"
] | [
"Functional assignment of multiple catabolic pathways for D-apiose."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
618,
25,
7
] | 3 | [] | [] | 0 | true | Domain | D-apionate lactonase, C-terminal domain | D-apionate lactonase, C-terminal domain | ApnL_C | 8 |
IPR058790 | 58,790 | CusB-like, barrel-sandwich hybrid domain | BSH_CusB | Domain | 8,542 | false | false | This domain is found in the Cation efflux system protein CusB and related proteins. CusB is an essential component of the CusCBA tripartite efflux system from Escherichia coli. This protein plays an essential role in bridging the inner membrane efflux pump CusA and the outer membrane channel CusC to mediate resistance ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25919"
] | [
"BSH_CusB"
] | [
8542
] | 1 | [] | [] | [] | 0 | [
"3h94",
"3ne5",
"3ooc",
"3opo",
"3ow7",
"3t51",
"3t53",
"3t56",
"4dnr",
"4dnt",
"4dop"
] | 11 | [
"PUB00055275",
"PUB00058847",
"PUB00099025",
"PUB00159140"
] | [
"21350490",
"19695261",
"9930866",
"27085056"
] | [
"Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.",
"Crystal structure of the membrane fusion protein CusB from Escherichia coli.",
"Molecular basis for resistance to silver cations in Salmonella.",
"SilE is an intrinsically disordered periplasmic \"molecular sponge\" involved in... | [
2011,
2009,
1999,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8365,
21,
156
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | CusB-like, barrel-sandwich hybrid domain | CusB-like, barrel-sandwich hybrid domain | BSH_CusB | 3 |
IPR058791 | 58,791 | CusB-like, three alpha-helical bundle domain | 3HB_CusB | Domain | 5,931 | false | false | This domain is found in the Cation efflux system protein CusB and related proteins. CusB is an essential component of the CusCBA tripartite efflux system from Escherichia coli. This protein plays an essential role in bridging the inner membrane efflux pump CusA and the outer membrane channel CusC to mediate resistance ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25869"
] | [
"3HB_CusB"
] | [
5931
] | 1 | [] | [] | [] | 0 | [
"3h94",
"3ne5",
"3ooc",
"3opo",
"3ow7",
"3t51",
"3t53",
"3t56",
"4dnr",
"4dnt",
"4dop"
] | 11 | [
"PUB00055275",
"PUB00058847",
"PUB00159140"
] | [
"21350490",
"19695261",
"27085056"
] | [
"Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.",
"Crystal structure of the membrane fusion protein CusB from Escherichia coli.",
"SilE is an intrinsically disordered periplasmic \"molecular sponge\" involved in bacterial silver resistance."
] | [
2011,
2009,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5820,
11,
100
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | CusB-like, three alpha-helical bundle domain | CusB-like, three alpha-helical bundle domain | 3HB_CusB | 8 |
IPR058792 | 58,792 | CusB-like, beta-barrel domain | Beta-barrel_RND_2 | Domain | 71,013 | false | false | This domain is found in the periplasmic membrane fusion proteins (MFPs) that are components of the RND tripartite drug efflux pumps. MFPs bridge the outer membrane factor and an inner membrane transporter. One characterised smember is the Cation efflux system protein CusB which is an essential component of the CusCBA t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25954"
] | [
"Beta-barrel_RND_2"
] | [
71013
] | 1 | [] | [] | [] | 0 | [
"3h94",
"3lnn",
"3ne5",
"3ooc",
"3opo",
"3ow7",
"3t51",
"3t53",
"3t56",
"4dnr",
"4dnt",
"4dop",
"4kks",
"4kkt",
"4kku",
"6vej"
] | 16 | [
"PUB00055275",
"PUB00058847"
] | [
"21350490",
"19695261"
] | [
"Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.",
"Crystal structure of the membrane fusion protein CusB from Escherichia coli."
] | [
2011,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ct3z32",
"unclassified sequences"
] | [
70003,
92,
1,
917
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | CusB-like, beta-barrel domain | CusB-like, beta-barrel domain | Beta-barrel_RND_2 | 5 |
IPR058793 | 58,793 | DNA damage response protein D | DDRD | Family | 79 | false | false | This entry represents the DNA damage response protein D (DdrD) protein family, which is one of the most highly induced proteins following radiation exposure or desiccation in Deinococcus species [ ]. DdrD is a DNA binding protein that preferentially binds to single-stranded DNA or duplex DNA with 5' single-stranded ext... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26517"
] | [
"DDRD"
] | [
79
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161203",
"PUB00161204"
] | [
"34052926",
"23840905"
] | [
"Characterization of the DdrD protein from the extremely radioresistant bacterium Deinococcus radiodurans.",
"DdrA, DdrD, and PprA: components of UV and mitomycin C resistance in Deinococcus radiodurans R1."
] | [
2021,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Deinococcus"
] | [
79
] | 1 | [] | [] | 0 | true | Family | DNA damage response protein D | DNA damage response protein D | DDRD | 9 |
IPR058794 | 58,794 | LcnD/ComB-like, long helical bundle domain | HB_LcnD/ComB-like | Domain | 849 | false | false | This domain is found in the Lactococcin A secretion protein LcnD from Lactococcus lactis and related proteins. This domain is also found in the Transport protein ComB and Mesentericin Y105 secretion protein MesE. LcnD is a protein involved in the secretion system of lactococcin A. As a part of this system it interacts ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25887"
] | [
"HB_LcnD"
] | [
849
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00087451",
"PUB00161880"
] | [
"11731132",
"7883181"
] | [
"Proteins of the lactococcin A secretion system: lcnD encodes two in-frame proteins.",
"Competence for genetic transformation in Streptococcus pneumoniae: organization of a regulatory locus with homology to two lactococcin A secretion genes."
] | [
2001,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Haloplanus ruber",
"Opisthokonta"
] | [
845,
1,
3
] | 3 | [] | [] | 0 | true | Domain | LcnD/ComB-like, long helical bundle domain | LcnD/ComB-like, long helical bundle domain | HB_LcnD/ComB-like | 7 |
IPR058795 | 58,795 | LcnD/ComB-like, C-terminal domain | LcnD/ComB-like_C | Domain | 940 | false | false | This domain is found in the Lactococcin A secretion protein LcnD from Lactococcus lactis and related proteins, including Transport protein ComB and Mesentericin Y105 secretion protein MesE. The domain represented in this entry folds into a six-stranded closed β-barrel with a greek-key topology which has a structural si... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25940"
] | [
"LcnD_C"
] | [
940
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00087451",
"PUB00161880"
] | [
"11731132",
"7883181"
] | [
"Proteins of the lactococcin A secretion system: lcnD encodes two in-frame proteins.",
"Competence for genetic transformation in Streptococcus pneumoniae: organization of a regulatory locus with homology to two lactococcin A secretion genes."
] | [
2001,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
938,
2
] | 2 | [] | [] | 0 | true | Domain | LcnD/ComB-like, C-terminal domain | LcnD/ComB-like, C-terminal domain | LcnD/ComB-like_C | 1 |
IPR058796 | 58,796 | COP9 signalosome complex subunit 2, C-terminal helix | COPS2_C | Domain | 2,275 | false | false | This short domain is found at the C-terminal end of human COP9 signalosome complex subunit 2 (COPS2) and similar eukaryotic proteins. COPS2 is an essential component of the COP9 signalosome complex, an essential regulator of the ubiquitin conjugation pathway that is involved in phosphorylation of p53/TP53, c-jun/JUN, I... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25983"
] | [
"COPS2_C"
] | [
2275
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5696394",
"R-DME-6781823",
"R-DME-8856825",
"R-DME-8951664",
"R-DME-9013422",
"R-DRE-8856825",
"R-DRE-8951664",
"R-HSA-5696394",
"R-HSA-6781823",
"R-HSA-8856825",
"R-HSA-8951664",
"R-HSA-9013422",
"R-MMU-5696394",
"R-MMU-6781823",
"R-MMU-8856825",
"R-MMU-8951664",
"R-MMU-90134... | [
"REACTOME:R-DME-5696394",
"REACTOME:R-DME-6781823",
"REACTOME:R-DME-8856825",
"REACTOME:R-DME-8951664",
"REACTOME:R-DME-9013422",
"REACTOME:R-DRE-8856825",
"REACTOME:R-DRE-8951664",
"REACTOME:R-HSA-5696394",
"REACTOME:R-HSA-6781823",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8951664",
"REACTOM... | 22 | [
"4d10",
"4d18",
"4wsn",
"6r6h",
"6r7f",
"6r7h",
"6r7i",
"6r7n",
"8h38",
"8h3a",
"8h3f",
"9is6"
] | 12 | [
"PUB00064799",
"PUB00064800",
"PUB00087571",
"PUB00091374",
"PUB00151714",
"PUB00161189",
"PUB00161190",
"PUB00161191",
"PUB00161192",
"PUB00161193",
"PUB00161194",
"PUB00161195"
] | [
"11337587",
"12737805",
"11285227",
"25043011",
"31444342",
"11967155",
"12522100",
"12972599",
"12615944",
"12524175",
"10531038",
"9535219"
] | [
"Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response.",
"The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis.",
"COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system.",
"Crystal struct... | [
2001,
2003,
2001,
2014,
2019,
2002,
2003,
2003,
2003,
2003,
1999,
1998
] | 12 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2275
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
3,
3,
2,
5,
4,
4,
2,
11
] | 8 | true | Domain | COP9 signalosome complex subunit 2, C-terminal helix | COP9 signalosome complex subunit 2, C-terminal helix | COPS2_C | 4 |
IPR058797 | 58,797 | RESC9, N-terminal region | RESC9_N | Domain | 48 | false | false | This domain is found in the RNA-editing substrate-binding complex 9 protein (RESC9) from Trypanosoma brucei, a component of RESC which together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs [ ]. RESC stabilises gRNAs a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26228"
] | [
"RESC9_N"
] | [
48
] | 1 | [] | [] | [] | 0 | [
"8fni",
"8fnk"
] | 2 | [
"PUB00160174"
] | [
"37410820"
] | [
"Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
48
] | 1 | [] | [] | 0 | true | Domain | RESC9, N-terminal region | RESC9, N-terminal region | RESC9_N | 1 |
IPR058798 | 58,798 | RESC9 middle region | RESC9_M | Domain | 46 | false | false | This domain is found in the RNA-editing substrate-binding complex 9 protein (RESC9) from Trypanosoma brucei, a component of RESC which together with RECC forms the editosome that orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs [ ]. RESC stabilises gRNAs a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26229"
] | [
"RESC9_M"
] | [
46
] | 1 | [] | [] | [] | 0 | [
"8fni",
"8fnk"
] | 2 | [
"PUB00160174"
] | [
"37410820"
] | [
"Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Metakinetoplastina"
] | [
46
] | 1 | [] | [] | 0 | true | Domain | RESC9 middle region | RESC9 middle region | RESC9_M | 3 |
IPR058799 | 58,799 | Crocagin biosynthetic protein CgnE/B | CgnE_B | Domain | 385 | false | false | This entry represents Crocagin biosynthetic protein CgnE and its paralogue CgnB from Chondromyces crocatus and related proteins. CgnE and CgnB are both part of a cluster CgnBCDE which is involved in the biosynthesis of tetracyclic crocagin [ ]. Of these four proteins, CgnE and CgnB were identified as unusual peptide-bi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26231"
] | [
"CgnE_B"
] | [
385
] | 1 | [] | [] | [] | 0 | [
"6zsu",
"6zsv"
] | 2 | [
"PUB00161174"
] | [
"36894702"
] | [
"Unusual peptide-binding proteins guide pyrroloindoline alkaloid formation in crocagin biosynthesis."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Durusdinium trenchii"
] | [
382,
3
] | 2 | [] | [] | 0 | true | Domain | Crocagin biosynthetic protein CgnE/B | Crocagin biosynthetic protein CgnE/B | CgnE_B | 3 |
IPR058800 | 58,800 | KKT2/KKT3, zinc finger domain | Znf-KKT2_KKT3 | Domain | 124 | false | false | This domain is found centrally in the Kinetoplastid kinetochore proteins KKT2 and KKT3 and related proteins. It plays a critical role in mediating the centromere localisation of KKT2 and KKT3 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26235"
] | [
"zf-KKT2_KKT3"
] | [
124
] | 1 | [] | [] | [] | 0 | [
"6tlx",
"6tly"
] | 2 | [
"PUB00161552"
] | [
"34081090"
] | [
"Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
124
] | 1 | [] | [] | 0 | true | Domain | KKT2/KKT3, zinc finger domain | KKT2/KKT3, zinc finger domain | Znf-KKT2_KKT3 | 3 |
IPR058801 | 58,801 | PDZD8, N-terminal domain | PDZD8_N | Domain | 1,789 | false | false | This domain is found in the human PDZD8 and related proteins from animals and some fungal species. The domain represented by this entry shares similarity to the so-called TULIPs (Tubular lipid binding proteins) domain fold, which is characteristic of a superfamily of lipid-binding proteins known as Aha1/BPI domain-like... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF26547",
"cd21674"
] | [
"PDZD8_N",
"SMP_PDZD8"
] | [
1787,
1405
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00063300",
"PUB00088665",
"PUB00138656",
"PUB00146950",
"PUB00146951",
"PUB00146952",
"PUB00161396"
] | [
"21834987",
"29097544",
"21549406",
"25771112",
"24554657",
"20573829",
"32686675"
] | [
"Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration.",
"ER-mitochondria tethering by PDZD8 regulates Ca2+ dynamics in mammalian neurons.",
"PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses in... | [
2011,
2017,
2011,
2015,
2014,
2010,
2020
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1789
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
2,
1,
1,
1,
3
] | 6 | true | Domain | PDZD8, N-terminal domain | PDZD8, N-terminal domain | PDZD8_N | 6 |
IPR058802 | 58,802 | MafA-like | MafA-like | Family | 113 | false | false | This entry represents the MafA (meningococcal adhesin family) protein, which functions as a glycolipid-binding adhesin in pathogenic Neisseria species. MafA was originally identified as a 36 kDa adhesin in Neisseria gonorrhoeae that binds to specific glycolipid receptors on host cells, including lactosylceramide, gangl... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26521"
] | [
"MAFA_adhesin"
] | [
113
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161326",
"PUB00161327",
"PUB00161328"
] | [
"2153292",
"31822804",
"33315509"
] | [
"Identification and characterization of a Neisseria gonorrhoeae gene encoding a glycolipid-binding adhesin.",
"Transcriptome analysis of human brain microvascular endothelial cells response to Neisseria meningitidis and its antigen MafA using RNA-seq.",
"The outer-membrane protein MafA of Neisseria meningitidis... | [
1990,
2019,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Darwinula stevensoni"
] | [
110,
3
] | 2 | [] | [] | 0 | true | Family | MafA-like | MafA-like | MafA-like | 1 |
IPR058803 | 58,803 | Kinetoplastid PH-like domain | PH_38 | Domain | 31 | false | false | This entry represents a small family of domains that are found in a group of uncharacterised kinetoplastid proteins. This domain adopts a PH-like domain fold. It is found in proteins that have an N- and C-terminal (this entry) PH-like domains separated by a non-globular linker. This domain is often found in combination... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26289"
] | [
"PH_38"
] | [
31
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Metakinetoplastina"
] | [
31
] | 1 | [] | [] | 0 | true | Domain | Kinetoplastid PH-like domain | Kinetoplastid PH-like domain | PH_38 | 5 |
IPR058804 | 58,804 | SpaO, N-terminal domain | SpaO_N | Domain | 786 | false | false | This entry represents the N-terminal domain of Surface presentation of antigens protein SpaO from Salmonella typhimurium and related proteins. This domain is predicted to structurally resemble the N-terminal domain of FliM ( ). It is followed by two repeats that have similarity to the C-terminal domain of FliM and FliN... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26294"
] | [
"SpaO_N"
] | [
786
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001240",
"PUB00161231"
] | [
"8404849",
"25994170"
] | [
"Cognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri.",
"A common assembly module in injectisome and flagellar type III secretion sorting platforms."
] | [
1993,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
786
] | 1 | [] | [] | 0 | true | Domain | SpaO, N-terminal domain | SpaO, N-terminal domain | SpaO_N | 1 |
IPR058805 | 58,805 | SpaO, FliM/N C-terminal related | SpaO_FliMN_C-like | Domain | 941 | false | false | This entry represents a domain found central in Surface presentation of the antigen protein SpaO from Salmonella typhimurium and related proteins. This domain is homologous to FliM/N C-terminal domain ( ) and has probably originated via a duplication event. SpaO contains two of these domains towards the C-terminal that... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26304"
] | [
"FliMN_C_rel"
] | [
941
] | 1 | [] | [] | [] | 0 | [
"4yx5",
"4yx7",
"4yxa"
] | 3 | [
"PUB00001240",
"PUB00161231"
] | [
"8404849",
"25994170"
] | [
"Cognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri.",
"A common assembly module in injectisome and flagellar type III secretion sorting platforms."
] | [
1993,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
941
] | 1 | [] | [] | 0 | true | Domain | SpaO, FliM/N C-terminal related | SpaO, FliM/N C-terminal related | SpaO_FliMN_C-like | 1 |
IPR058806 | 58,806 | Maml | MamI | Family | 122 | false | false | This protein family includes Magnetosome protein MamI, which is involved in the formation and nucleation of magnetosomes, specialised organelles in certain bacteria that allow them to orient along magnetic fields. Members of this family may play a role in the early stages of magnetosome nucleation and is potentially in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26391"
] | [
"MamI"
] | [
122
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105201",
"PUB00106118",
"PUB00161658"
] | [
"27286560",
"20212111",
"39487238"
] | [
"Genetic and Ultrastructural Analysis Reveals the Key Players and Initial Steps of Bacterial Magnetosome Membrane Biogenesis.",
"Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle.",
"Essential magnetosome proteins MamI and MamL from magneto... | [
2016,
2010,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
113,
9
] | 2 | [] | [] | 0 | true | Family | Maml | Maml | MamI | 8 |
IPR058807 | 58,807 | ScoMcrA-like, N-terminal head domain | ScoMcrA_N | Domain | 1,293 | false | false | This entry represents the N-terminal head domain found in the endonuclease ScoMcrA and related type IV restriction enzymes. This domain exhibits substantial positional variance with respect to the other domains of ScoMcrA [ ]. It folds into an α/β structure composed of three-stranded antiparallel β-sheet and array of α... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26345"
] | [
"ScoMcrA_N"
] | [
1293
] | 1 | [] | [] | [] | 0 | [
"5zmm"
] | 1 | [
"PUB00154747"
] | [
"30409991"
] | [
"Structural basis for the recognition of sulfur in phosphorothioated DNA."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
15,
1267,
11
] | 3 | [] | [] | 0 | true | Domain | ScoMcrA-like, N-terminal head domain | ScoMcrA-like, N-terminal head domain | ScoMcrA_N | 7 |
IPR058808 | 58,808 | ADGRA2/3, GAIN domain | GAIN_ADGRA2/3 | Domain | 3,369 | false | false | This predicted GAIN domain is found in human Adhesion G protein-coupled receptor A2/3 (ADGRA2/3) and similar animal proteins. ADGRA2 is an endothelial receptor which functions together with RECK to enable brain endothelial cells to selectively respond to Wnt7 signals [ , ]. ADGRA3 is an orphan receptor that may have a ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26588"
] | [
"GAIN_ADGRA3"
] | [
3369
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00088750",
"PUB00136018",
"PUB00136019",
"PUB00136022",
"PUB00136023",
"PUB00136025",
"PUB00137731",
"PUB00154885",
"PUB00154886",
"PUB00161236",
"PUB00161237"
] | [
"28803732",
"25558062",
"25373781",
"21421844",
"21282641",
"21071672",
"23821037",
"28289266",
"30026314",
"26051822",
"28288111"
] | [
"Reck and Gpr124 Are Essential Receptor Cofactors for Wnt7a/Wnt7b-Specific Signaling in Mammalian CNS Angiogenesis and Blood-Brain Barrier Regulation.",
"GPR124 functions as a WNT7-specific coactivator of canonical β-catenin signaling.",
"Gpr124 controls CNS angiogenesis and blood-brain barrier integrity by pro... | [
2017,
2015,
2014,
2011,
2011,
2010,
2013,
2017,
2018,
2015,
2017
] | 11 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
3369
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
2,
6,
5,
7
] | 5 | true | Domain | ADGRA2/3, GAIN domain | ADGRA2/3, GAIN domain | GAIN_ADGRA2/3 | 4 |
IPR058809 | 58,809 | DUF8073, central HTH domain | DUF8073_M | Domain | 171 | false | false | This entry represents the central HTH domain found in a family of uncharacterised proteins found in halobacteria. DUF8073 is composed of an N-terminal domain , central domain and C-terminal domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26271"
] | [
"DUF8073_M"
] | [
171
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
171
] | 1 | [] | [] | 0 | true | Domain | DUF8073, central HTH domain | DUF8073, central HTH domain | DUF8073_M | 7 |
IPR058810 | 58,810 | DUF8073, C-terminal domain | DUF8073_C | Domain | 167 | false | false | This entry represents the C-terminal helical domain found in a family of uncharacterised proteins found in halobacteria. DUF8073 is composed of an N-terminal domain , central domain and C-terminal domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26270"
] | [
"DUF8073_C"
] | [
167
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
167
] | 1 | [] | [] | 0 | true | Domain | DUF8073, C-terminal domain | DUF8073, C-terminal domain | DUF8073_C | 2 |
IPR058811 | 58,811 | DUF8073, N-terminal domain | DUF8073_N | Domain | 136 | false | false | This entry represents the N-terminal domain found in a family of uncharacterised proteins found in halobacteria. DUF8073 is composed of an N-terminal domain , central domain and C-terminal domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26272"
] | [
"DUF8073_N"
] | [
136
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
136
] | 1 | [] | [] | 0 | true | Domain | DUF8073, N-terminal domain | DUF8073, N-terminal domain | DUF8073_N | 2 |
IPR058812 | 58,812 | RhsPI | RhsPI | Domain | 30 | false | false | This entry represents RhsPI which forms a toxin-immunity pair with RhsP. This proteins is a member of the SUKH superfamily, members of which are known to function as immunity proteins in bacterial toxin systems. RhsPI forms a heterodimer with RhsP and neutralises the RhsP WHH active site via electrostatic interactions ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26352"
] | [
"RhsPI"
] | [
30
] | 1 | [] | [] | [] | 0 | [
"8bd1"
] | 1 | [
"PUB00161432"
] | [
"36476863"
] | [
"Vibrio parahaemolyticus prey targeting requires autoproteolysis-triggered dimerization of the type VI secretion system effector RhsP."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
30
] | 1 | [] | [] | 0 | true | Domain | RhsPI | RhsPI | RhsPI | 9 |
IPR058813 | 58,813 | ScoMcrA-like, DNA sulfur-binding domain | DNA-SBD_ScoMcrA | Domain | 1,929 | false | false | This entry represents the DNA sulfur-binding domain (SBD) found in the endonuclease ScoMcrA and related type IV restriction enzymes. This domain recognises the sulfur atom in phosphorothioated DNA (PT-DNA). The recognition of the PT-DNA by SBD is phosphorothioate-dependent and also DNA sequence-specific [ , ]. Residues... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26340"
] | [
"DNA-SBD_ScoMcrA"
] | [
1929
] | 1 | [] | [] | [] | 0 | [
"5zmm",
"5zmn",
"5zmo",
"7cc9",
"7ccd",
"7ccj",
"8h0l"
] | 7 | [
"PUB00154747",
"PUB00161216"
] | [
"30409991",
"32621606"
] | [
"Structural basis for the recognition of sulfur in phosphorothioated DNA.",
"DNA backbone interactions impact the sequence specificity of DNA sulfur-binding domains: revelations from structural analyses."
] | [
2018,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudovirales sp. ctilw2",
"ecological metagenomes"
] | [
1922,
1,
6
] | 3 | [] | [] | 0 | true | Domain | ScoMcrA-like, DNA sulfur-binding domain | ScoMcrA-like, DNA sulfur-binding domain | DNA-SBD_ScoMcrA | 4 |
IPR058814 | 58,814 | ZIG1/7, N-terminal | ZIG1/7_N | Domain | 249 | false | false | This entry represents the N-terminal immunoglobulin domain of the Zwei Ig-1 and 7 (ZIG1 and ZIG7) proteins, which contain two immunoglobulin domains. Members of this group are specific to nematodes. ZIG proteins are either secreted or membrane-associated molecules that play important roles in maintaining the structure ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26428"
] | [
"Zwei_Ig_N"
] | [
249
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00086969",
"PUB00161562"
] | [
"22829780",
"19737747"
] | [
"The secreted immunoglobulin domain proteins ZIG-5 and ZIG-8 cooperate with L1CAM/SAX-7 to maintain nervous system integrity.",
"The small, secreted immunoglobulin protein ZIG-3 maintains axon position in Caenorhabditis elegans."
] | [
2012,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Ecdysozoa"
] | [
249
] | 1 | [
"Caenorhabditis elegans"
] | [
3
] | 1 | true | Domain | ZIG1/7, N-terminal | ZIG1/7, N-terminal | ZIG1/7_N | 6 |
IPR058815 | 58,815 | BAM-2-like, concanavalin A-like domain | ConA_BAM2-like | Domain | 97 | false | false | This entry represents a concanavalin A-like domain widely distributed in proteins from nematodes, including Neurexin-related protein bam-2 (BAM-2) from Caenorhabditis elegans. BAM-2 is a neurexin-related transmembrane protein that functions in the development of neural circuits. It is specifically required for proper a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26430"
] | [
"ConA_BAM2"
] | [
97
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161187",
"PUB00161188"
] | [
"14551437",
"28901288"
] | [
"A Neurexin-related protein, BAM-2, terminates axonal branches in C. elegans.",
"Multiple conserved cell adhesion protein interactions mediate neural wiring of a sensory circuit in <i>C. elegans</i>."
] | [
2003,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
97
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | BAM-2-like, concanavalin A-like domain | BAM-2-like, concanavalin A-like domain | ConA_BAM2-like | 7 |
IPR058816 | 58,816 | PH domain-like | PH_39 | Domain | 42 | false | false | This entry represents a PH domain found in some a group of bacterial uncharacterised proteins that contain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26565"
] | [
"PH_39"
] | [
42
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
42
] | 1 | [] | [] | 0 | true | Domain | PH domain-like | PH domain-like | PH_39 | 3 |
IPR058817 | 58,817 | Protein of unknown function DUF8155, C-terminal domain | DUF8155_C | Domain | 344 | false | false | This entry represents the C-terminal domain from a family of uncharacterised proteins from halophilic archaea. The proteins in this entry are predominantly found in the class Halobacteria, which includes families such as Natrialbaceae, Haloferacaceae, and Haloarculaceae. The proteins in this entry are generally around ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26483"
] | [
"DUF8155_C"
] | [
344
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"marine sediment metagenome"
] | [
337,
6,
1
] | 3 | [] | [] | 0 | true | Domain | Protein of unknown function DUF8155, C-terminal domain | Protein of unknown function DUF8155, C-terminal domain | DUF8155_C | 5 |
IPR058819 | 58,819 | UvrD domain-like | UvrD_dom-like | Family | 73 | false | false | This entry represents a set of uncharacterised proteins in halobacteria. Structure comparison shows that this family is most similar to the 1A domain of the D.radiodurans UvrD protein. UvrD is a DNA helicase involved in several DNA repair pathways. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26510"
] | [
"Halo_UvrD_like"
] | [
73
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
73
] | 1 | [] | [] | 0 | true | Family | UvrD domain-like | UvrD domain-like | UvrD_dom-like | 6 |
IPR058820 | 58,820 | Leucine-rich domain | LRR_16 | Domain | 46 | false | false | This domain is found in uncharacterised proteins mainly from Trypanosomatida. Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ ]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26020"
] | [
"LRR_16"
] | [
46
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001625",
"PUB00001898",
"PUB00007147",
"PUB00017058"
] | [
"1657640",
"2176636",
"11751054",
"14747988"
] | [
"A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a beta-sheet structure.",
"slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains.",
"The leucine-rich repeat as a protein reco... | [
1991,
1990,
2001,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
46
] | 1 | [] | [] | 0 | true | Domain | Leucine-rich domain | Leucine-rich domain | LRR_16 | 3 |
IPR058821 | 58,821 | Double winged helix-containing, halobacteria | Double_WHD-containing_halo | Family | 282 | false | false | This entry represents a family of uncharacterised proteins found in halobacteria. These proteins have two copies of a winged helix domain, suggesting they may act as transcriptional regulators. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25947"
] | [
"WHD_halo_double"
] | [
282
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Halobacteriales"
] | [
6,
276
] | 2 | [] | [] | 0 | true | Family | Double winged helix-containing, halobacteria | Double winged helix-containing, halobacteria | Double_WHD-containing_halo | 1 |
IPR058822 | 58,822 | Major fimbrium tip subunit FimD, third Ig-like domain | Ig-like_FimD_3rd | Domain | 157 | false | false | This entry represents the third domain found in Major fimbrium tip subunit FimD protein from Porphyromonas gingivalis and similar proteins from bacteroidales. FimD is though to be a component of the fimbrium tip, which mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26306"
] | [
"FimD_3rd"
] | [
157
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161686",
"PUB00161687"
] | [
"17526848",
"19506009"
] | [
"Involvement of minor components associated with the FimA fimbriae of Porphyromonas gingivalis in adhesive functions.",
"Host adhesive activities and virulence of novel fimbrial proteins of Porphyromonas gingivalis."
] | [
2007,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteroidales",
"Siphoviridae sp. ctBLh2",
"human gut metagenome"
] | [
155,
1,
1
] | 3 | [] | [] | 0 | true | Domain | Major fimbrium tip subunit FimD, third Ig-like domain | Major fimbrium tip subunit FimD, third Ig-like domain | Ig-like_FimD_3rd | 6 |
IPR058823 | 58,823 | Orfx1, TULIPs domain | Orfx1 | Domain | 40 | false | false | This domain is found in the Orfx1, a protein encoded in the orfX gene cluster from certain strains of Clostridium botulinum, specifically those producing botulinum neurotoxin type E (BoNT/E1). OrfX1 adopts the so-called TULIPs (Tubular lipid binding proteins) domain fold, which is characteristic of a superfamily of lip... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26542"
] | [
"Orfx1"
] | [
40
] | 1 | [] | [] | [] | 0 | [
"8bgm",
"8fbd",
"8fbe"
] | 3 | [
"PUB00161176",
"PUB00161382"
] | [
"36653893",
"36403098"
] | [
"Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1.",
"Crystal structure of the OrfX1-OrfX3 complex from the PMP1 neurotoxin gene cluster."
] | [
2023,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
40
] | 1 | [] | [] | 0 | true | Domain | Orfx1, TULIPs domain | Orfx1, TULIPs domain | Orfx1 | 3 |
IPR058824 | 58,824 | Orfx2, N-terminal TULIPs domain | Orfx2_N | Domain | 49 | false | false | This domain is found N-terminal in the Orfx2, a protein encoded in the orfX gene cluster from certain strains of Clostridium botulinum, specifically those producing botulinum neurotoxin type E (BoNT/E1). The N-terminal domain of OrfX2 adopts the so-called TULIPs (Tubular lipid binding proteins) domain fold, which is ch... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26543"
] | [
"Orfx2_N"
] | [
49
] | 1 | [] | [] | [] | 0 | [
"6ekv",
"8fbf",
"9arj",
"9ark",
"9arl"
] | 5 | [
"PUB00161176"
] | [
"36653893"
] | [
"Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
49
] | 1 | [] | [] | 0 | true | Domain | Orfx2, N-terminal TULIPs domain | Orfx2, N-terminal TULIPs domain | Orfx2_N | 5 |
IPR058825 | 58,825 | MDM34, N-terminal domain | MDM34_N | Domain | 1,835 | false | false | This domain is found N-terminal in the Mitochondrial distribution and morphology protein 34 and related proteins. MDM34 is a component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. MDM34 is required for the interaction of the ER-resident membrane pro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26545"
] | [
"Mdm34_N"
] | [
1835
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00033261",
"PUB00055950",
"PUB00064827"
] | [
"11907266",
"19556461",
"14981098"
] | [
"Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae.",
"An ER-mitochondria tethering complex revealed by a synthetic biology screen.",
"Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids."
] | [
2002,
2009,
2004
] | 3 | [
"IPR031468"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1835
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Domain | MDM34, N-terminal domain | MDM34, N-terminal domain | MDM34_N | 8 |
IPR058828 | 58,828 | CARF/NKRF, DSRM domain | DSRM_CARF/NKRF | Domain | 1,784 | false | false | This entry represents a dsRNA binding domain found in human CDKN2A-interacting protein (CARF), NF-kappa-B-repressing factor (NKRF) and similar proteins from vertebrates. CARF fegulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and sen... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26535"
] | [
"DSRM_CARF"
] | [
1784
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00082542",
"PUB00087114",
"PUB00087115",
"PUB00100847",
"PUB00161217"
] | [
"10562553",
"15109303",
"24825908",
"32179686",
"12381793"
] | [
"Constitutive silencing of IFN-beta promoter is mediated by NRF (NF-kappaB-repressing factor), a nuclear inhibitor of NF-kappaB.",
"Alternative reading frame protein (ARF)-independent function of CARF (collaborator of ARF) involves its interactions with p53: evidence for a novel p53-activation pathway and its neg... | [
1999,
2004,
2014,
2020,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Waterburya agarophytonicola KI4"
] | [
1783,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
10,
3,
8
] | 4 | true | Domain | CARF/NKRF, DSRM domain | CARF/NKRF, DSRM domain | DSRM_CARF/NKRF | 1 |
IPR058829 | 58,829 | Anti-CRISPR Type I-F ADP-ribosyltransferase AcrIF11-like | AcrIF11-like | Family | 95 | false | false | This entry represents a group of proteins from tailed bacteriophages and proteobacteria, including AcrIF11 from Pseudomonas aeruginosa, an ADP-ribosyltransferase that function as anti-CRISPR protein targeting Type I-F CRISPR-Cas systems. Members of this family inhibit CRISPR-Cas immune systems by ADP-ribosylating the C... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26151"
] | [
"AcrIF11_ADP_ribosyl"
] | [
95
] | 1 | [] | [] | [] | 0 | [
"6kyf",
"8dwq"
] | 2 | [
"PUB00161659"
] | [
"33049228"
] | [
"A Type I-F Anti-CRISPR Protein Inhibits the CRISPR-Cas Surveillance Complex by ADP-Ribosylation."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome",
"unclassified Caudoviricetes"
] | [
90,
2,
3
] | 3 | [] | [] | 0 | true | Family | Anti-CRISPR Type I-F ADP-ribosyltransferase AcrIF11-like | Anti-CRISPR Type I-F ADP-ribosyltransferase AcrIF11-like | AcrIF11-like | 8 |
IPR058830 | 58,830 | LolA-like domain 1 | LolA-like_dom_1st | Domain | 119 | false | false | This entry represents a LolA-like domain that is found at the N terminus of a family of large nematode proteins. These uncharacterised proteins are composed of two LolA-like domains followed by a third C-terminal domain. Members of this group are though to be membrane anchored and glycosylated. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25897"
] | [
"LolA_1st_nematode"
] | [
119
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Chromadorea"
] | [
119
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | LolA-like domain 1 | LolA-like domain 1 | LolA-like_dom_1st | 8 |
IPR058831 | 58,831 | LolA-like domain 2 | LolA-like_dom_2nd | Domain | 1,093 | false | false | This entry represents a LolA-like domain that is found in the middle of a family of large metazoan proteins. These proteins are composed of two LolA-like domains followed by a third C-terminal domain. These proteins are membrane anchored and glycosylated. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25898"
] | [
"LolA_2nd_metazoa"
] | [
1093
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1093
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | LolA-like domain 2 | LolA-like domain 2 | LolA-like_dom_2nd | 2 |
IPR058832 | 58,832 | PTX3-like, N-terminal domain | PTX3_N | Domain | 801 | false | false | This domain is found at the N-terminal end of human Pentraxin-related protein PTX3 and similar sequences from vertebrates. PTX3 plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility [ ]. This domain, which is often found asso... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26206"
] | [
"PTX3_N"
] | [
801
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-6798695",
"R-MMU-6798695"
] | [
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695"
] | 2 | [
"7zl1",
"8s50"
] | 2 | [
"PUB00161425",
"PUB00161426"
] | [
"12763682",
"9407058"
] | [
"Pentraxin 3, a non-redundant soluble pattern recognition receptor involved in innate immunity.",
"Multimer formation and ligand recognition by the long pentraxin PTX3. Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component."
] | [
2003,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Gnathostomata",
"Pseudomonadati"
] | [
792,
9
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
1,
3
] | 4 | true | Domain | PTX3-like, N-terminal domain | PTX3-like, N-terminal domain | PTX3_N | 3 |
IPR058833 | 58,833 | ALG44, helical loop domain | Hl_ALG44 | Domain | 668 | false | false | This domain is found in Alg44 from Pseudomonas aeruginosa and related proteins. Alg44 is a membrane protein that along Alg8 is required in vivo for the polymerisation reaction leading to alginate production [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25891"
] | [
"Hl_ALG44"
] | [
668
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161135"
] | [
"18524915"
] | [
"Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadaceae"
] | [
668
] | 1 | [] | [] | 0 | true | Domain | ALG44, helical loop domain | ALG44, helical loop domain | Hl_ALG44 | 1 |
IPR058834 | 58,834 | ALG44, beta-barrel domain | Beta-barrel_ALG44 | Domain | 771 | false | false | This domain is found in Alg44 from Pseudomonas aeruginosa and related proteins. The domain represented in this entry folds into a six-stranded closed β-barrel with a greek-key topology which has a structural similarity to the C-terminal domain of alanine racemase. This domain is interrupted by the barrel-sandwich hybri... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25965"
] | [
"Beta-barrel_ALG44"
] | [
771
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161135"
] | [
"18524915"
] | [
"Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
771
] | 1 | [] | [] | 0 | true | Domain | ALG44, beta-barrel domain | ALG44, beta-barrel domain | Beta-barrel_ALG44 | 2 |
IPR058835 | 58,835 | ALG44, barrel-sandwich hybrid domain | BSH_ALG44 | Domain | 752 | false | false | This domain is found in Alg44 from Pseudomonas aeruginosa and related proteins. Alg44 is a membrane protein that along Alg8 is required in vivo for the polymerisation reaction leading to alginate production [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25964"
] | [
"BSH_ALG44"
] | [
752
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161135"
] | [
"18524915"
] | [
"Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
752
] | 1 | [] | [] | 0 | true | Domain | ALG44, barrel-sandwich hybrid domain | ALG44, barrel-sandwich hybrid domain | BSH_ALG44 | 8 |
IPR058836 | 58,836 | DUF8183, C-terminal HTH domain | DUF8183_C | Domain | 49 | false | false | This entry represents a presumed helix-turn-helix (HTH) domain of unknown function found in uncharacterised proteins in archaea. The domain is typically around 60-70 amino acids in length. DUF8183 contains a SycN-like N-terminal domain and an HTH C-terminal domain . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26555"
] | [
"HTH_78"
] | [
49
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eisenbergiella massiliensis"
] | [
47,
2
] | 2 | [] | [] | 0 | true | Domain | DUF8183, C-terminal HTH domain | DUF8183, C-terminal HTH domain | DUF8183_C | 4 |
IPR058837 | 58,837 | Magnetosome protein MamS/MamX domain | MamS_MamX_dom | Domain | 332 | false | false | This entry represents the C-terminal region of Magnetosome protein MamX, MamS and similar bacterial proteins. This domain is crucial for its function [ ], and it likely interacts with FtsZ-like proteins and MamY. It is predicted to fold into a small five-stranded β-barrel. The MamS/MamX protein family is involved in th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26390"
] | [
"MamS_MamX"
] | [
332
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093603",
"PUB00093606",
"PUB00106118",
"PUB00106121",
"PUB00161334"
] | [
"23889511",
"24816605",
"20212111",
"24020498",
"30367002"
] | [
"The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense.",
"Genetic dissection of the mamAB and mms6 operons reveals a gene set essential for magnetosome biogenesis in Magnetospirillum gryphiswaldense.",
"Comprehensive geneti... | [
2013,
2014,
2010,
2013,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Aduncisulcus paluster",
"Bacteria",
"ecological metagenomes"
] | [
1,
324,
7
] | 3 | [] | [] | 0 | true | Domain | Magnetosome protein MamS/MamX domain | Magnetosome protein MamS/MamX domain | MamS_MamX_dom | 6 |
IPR058838 | 58,838 | SH3 domain, actinomycetes | SH3_actinomycetes | Domain | 3,966 | false | false | This predicted SH3 domain is found in a group of uncharacterised proteins mainly from actinomycetes that also have and . Many members of this family are annotated as magnesium transporters. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26205"
] | [
"SH3_actinomycetes"
] | [
3966
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Acrobeloides nanus",
"Bacteria",
"metagenomes"
] | [
1,
3850,
115
] | 3 | [] | [] | 0 | true | Domain | SH3 domain, actinomycetes | SH3 domain, actinomycetes | SH3_actinomycetes | 2 |
IPR058839 | 58,839 | DNA helicase B, winged helix domain | WHD_HELB | Domain | 899 | false | false | This entry represents the winged helix domain found in DNA helicase B (HELB). HELB is a 5'-3' DNA helicase that functions in cellular homologous recombination and DNA damage response. It accumulates on chromatin in cells exposed to DNA damage and interacts with RPA. HELB promotes homologous recombination in vivo and st... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25894"
] | [
"WHD_HELB"
] | [
899
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00062763",
"PUB00062764",
"PUB00062765",
"PUB00161523",
"PUB00161524",
"PUB00161525",
"PUB00161526"
] | [
"12181327",
"7794903",
"7596831",
"22194613",
"25617833",
"26774285",
"11557815"
] | [
"A dominant-negative mutant of human DNA helicase B blocks the onset of chromosomal DNA replication.",
"Stimulation of DNA synthesis by mouse DNA helicase B in a DNA replication system containing eukaryotic replication origins.",
"Stimulation of mouse DNA primase-catalyzed oligoribonucleotide synthesis by mouse... | [
2002,
1995,
1995,
2012,
2015,
2016,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
899
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
2,
2
] | 4 | true | Domain | DNA helicase B, winged helix domain | DNA helicase B, winged helix domain | WHD_HELB | 3 |
IPR058840 | 58,840 | tRNA 2-selenouridine synthase, AAA domain | AAA_SelU | Domain | 7,004 | false | false | This entry represents the AAA domain in SelU proteins. tRNA 2-selenouridine synthase (SelU) is a monomeric enzyme involved in the post-transcriptional modification of uridine at the wobble position (U34) of tRNA\textsuperscript{Lys}, tRNA\textsuperscript{Glu}, and tRNA\textsuperscript{Gln}, where it catalyses the two-s... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26341"
] | [
"AAA_SelU"
] | [
7004
] | 1 | [
"EC"
] | [
"2.9.1.3"
] | [
"EC:2.9.1.3"
] | 1 | [] | 0 | [
"PUB00043071",
"PUB00093754",
"PUB00093755",
"PUB00093756"
] | [
"14594807",
"24971911",
"22983156",
"29862510"
] | [
"Functional diversity of the rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase.",
"Transformation of a wobble 2-thiouridine to 2-selenouridine via S-geranyl-2-thiouridine as a possible cellular pathway.",
"Discovery and biological charact... | [
2004,
2014,
2012,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanococcales",
"metagenomes"
] | [
6695,
187,
41,
81
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | tRNA 2-selenouridine synthase, AAA domain | tRNA 2-selenouridine synthase, AAA domain | AAA_SelU | 1 |
IPR058841 | 58,841 | PEX14-like, helix-turn-helix domain | HTH_76 | Domain | 1,666 | false | false | This helix-turn-helix domain is found in one or two copies at the N-terminal of proteins that contain a domain. These proteins are largely found in fungal proteins and annotated as putative Peroxisomal membrane protein PEX14-like KPWE domain-containing proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25871"
] | [
"HTH_76"
] | [
1666
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1666
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | PEX14-like, helix-turn-helix domain | PEX14-like, helix-turn-helix domain | HTH_76 | 7 |
IPR058842 | 58,842 | E3 ubiquitin-protein ligase DCST1-like, C-terminal domain | DCST1_C | Domain | 1,652 | false | false | This RING zinc finger domain is found at the C-terminal end of human E3 ubiquitin-protein ligase DCST1 and DSCT2 and related proteins mostly from animals. DCST1 mediates 'Lys-48'-linked ubiquitination of STAT2 and induces its proteasomal degradation thereby negatively regulating type-I-interferon signalling [ ]. DSCT1 ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26037"
] | [
"zf-RING_DCST1_C"
] | [
1652
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00161553"
] | [
"27782195"
] | [
"Global functional profiling of human ubiquitome identifies E3 ubiquitin ligase DCST1 as a novel negative regulator of Type-I interferon signaling."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Thermofilum adornatum"
] | [
1650,
2
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
42,
6,
4,
2,
4
] | 5 | true | Domain | E3 ubiquitin-protein ligase DCST1-like, C-terminal domain | E3 ubiquitin-protein ligase DCST1-like, C-terminal domain | DCST1_C | 8 |
IPR058843 | 58,843 | DAAF9, PH domain | PH_DAAF9 | Domain | 977 | false | false | This entry describes the PH domain in human DAAF9 and related proteins. This domain is usually present in proteins that bind to short peptide motifs and are involved in cell signalling. Dynein axonemal assembly factor 9 DNAAF9 (Shulin) is a dynein axonemal assembly factor that regulates the transport and activation of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26246"
] | [
"PH_DAAF9"
] | [
977
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00069901",
"PUB00109577"
] | [
"22085962",
"33632841"
] | [
"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium.",
"Shulin packages axonemal outer dynein arms for ciliary targeting."
] | [
2011,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
977
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
5,
5
] | 4 | true | Domain | DAAF9, PH domain | DAAF9, PH domain | PH_DAAF9 | 4 |
IPR058844 | 58,844 | DAAF9, pita-bread-like domain | PB_DAAF9 | Domain | 1,077 | false | false | This domain is found in human DAAF9 and related proteins. This domain shows a fold similar to that of aminopeptidase, prolidase, and related proteins, collectively referred to as the "pita bread" fold [ ]. Dynein axonemal assembly factor 9 DNAAF9 (Shulin) is a dynein axonemal assembly factor that regulates the transpor... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25203"
] | [
"PB_DAAF9"
] | [
1077
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044073",
"PUB00069901",
"PUB00109577"
] | [
"8146141",
"22085962",
"33632841"
] | [
"Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.",
"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium.",
"Shulin packages axonemal outer dynein arms for ciliary targeting."
] | [
1994,
2011,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1077
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
6,
5
] | 4 | true | Domain | DAAF9, pita-bread-like domain | DAAF9, pita-bread-like domain | PB_DAAF9 | 1 |
IPR058845 | 58,845 | Kringle-like domain | Kringle_2 | Domain | 181 | false | false | This entry represents a Kringle-like domain found in a range of nematode proteins of unknown function. This domain likely forms three disulphide bridges. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25866"
] | [
"Kringle_2"
] | [
181
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
181
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Domain | Kringle-like domain | Kringle-like domain | Kringle_2 | 5 |
IPR058846 | 58,846 | PAS-like domain | PAS-like | Domain | 1,969 | false | false | This domain is found in uncharacterised proteins mainly from fungi. It has very remote similarity to PAS domains and it is predicted to adopt similar structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26131"
] | [
"PAS-like"
] | [
1969
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1969
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | PAS-like domain | PAS-like domain | PAS-like | 4 |
IPR058848 | 58,848 | Endo-acting ulvan lyase, C-terminal domain | Ulvan_lyase_C | Domain | 366 | false | false | This entry represents the C-terminal domain of ulvan lyase. Endo-acting ulvan lyases are enzymes that play a crucial role in the degradation of ulvan, a major polysaccharide component of the cell walls of green seaweeds belonging to the Ulvales order. These enzymes specifically catalyse the endolytic cleavage of the gl... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26374"
] | [
"Ulvan_lyaseC"
] | [
366
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093668"
] | [
"31285597"
] | [
"A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halogranum amylolyticum",
"metagenomes"
] | [
358,
1,
7
] | 3 | [] | [] | 0 | true | Domain | Endo-acting ulvan lyase, C-terminal domain | Endo-acting ulvan lyase, C-terminal domain | Ulvan_lyase_C | 3 |
IPR058849 | 58,849 | Endo-acting ulvan lyase, 2nd domain | Ulvan_lyase_2nd | Domain | 433 | false | false | This entry represents the second domain found in the ulvan lyase protein. Endo-acting ulvan lyases are enzymes that play a crucial role in the degradation of ulvan, a major polysaccharide component of the cell walls of green seaweeds belonging to the Ulvales order. These enzymes specifically catalyse the endolytic clea... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26377"
] | [
"Ulvan_lyase_2nd"
] | [
433
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093668"
] | [
"31285597"
] | [
"A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
426,
7
] | 2 | [] | [] | 0 | true | Domain | Endo-acting ulvan lyase, 2nd domain | Endo-acting ulvan lyase, 2nd domain | Ulvan_lyase_2nd | 2 |
IPR058850 | 58,850 | Botulinum-like neurotoxin Wo, peptidase domain | Peptidase_M27_Wo | Domain | 1 | false | false | This entry represents the peptidase domain in BoNT/Wo. This domain is responsible for the zinc-dependent proteolytic activity of the toxin, specifically cleaving the VAMP2 protein between Trp89 and Trp90. The domain contains the conserved HExxH zinc-binding motif characteristic of the M27 metalloproteases family, but f... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26320"
] | [
"Peptidase_M27_Wo"
] | [
1
] | 1 | [] | [] | [] | 0 | [
"6rim",
"8c8g"
] | 2 | [
"PUB00161140",
"PUB00161141",
"PUB00161404",
"PUB00161646"
] | [
"27443638",
"37746829",
"31111466",
"38009421"
] | [
"The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain.",
"The cryo-EM structure of the BoNT/Wo-NTNH complex reveals two immunoglobulin-like domains.",
"Crystal structure of the catalytic domain of the Weissella oryzae botulinum-like toxin.",
"NTNH protein: more than a bo... | [
2016,
2024,
2019,
2024
] | 4 | [] | [] | 0 | 0 | null | [
"Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25)"
] | [
1
] | 1 | [] | [] | 0 | true | Domain | Botulinum-like neurotoxin Wo, peptidase domain | Botulinum-like neurotoxin Wo, peptidase domain | Peptidase_M27_Wo | 5 |
IPR058851 | 58,851 | Callose synthase, helical domain | CALS1_helical | Domain | 6,974 | false | false | This domain is found in Callose synthase 1 from Arabidopsis thaliana (CALS1) and similar sequences mainly found in plants. This domain is predicted to show an α-helical configuration. CALS1 is involved in callose synthesis at the forming cell plate during cytokinesis. It is not required for callose formation after woun... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25968"
] | [
"CALS1"
] | [
6974
] | 1 | [
"EC",
"METACYC"
] | [
"2.4.1.34",
"PWY-6773"
] | [
"EC:2.4.1.34",
"METACYC:PWY-6773"
] | 2 | [] | 0 | [
"PUB00062061",
"PUB00161162",
"PUB00161163",
"PUB00161164",
"PUB00161165",
"PUB00161166",
"PUB00161167",
"PUB00161168"
] | [
"14555698",
"16021399",
"16212660",
"15842618",
"18315544",
"12081364",
"12920300",
"20430748"
] | [
"An Arabidopsis Callose Synthase, GSL5, Is Required for Wound and Papillary Callose Formation.",
"Two callose synthases, GSL1 and GSL5, play an essential and redundant role in plant and pollen development and in fertility.",
"Callose (beta-1,3 glucan) is essential for Arabidopsis pollen wall patterning, but not... | [
2003,
2005,
2005,
2005,
2008,
2002,
2003,
2010
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6974
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
62,
26,
228
] | 3 | true | Domain | Callose synthase, helical domain | Callose synthase, helical domain | CALS1_helical | 3 |
IPR058852 | 58,852 | Winged helix-turn-helix domain 77 | HTH_77 | Domain | 12,230 | false | false | This entry represents a winged helix-turn-helix domain found in a range of bacterial proteins. These domains are often but not always involved in binding to DNA. Many proteins in this family include a P-loop domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF25872"
] | [
"HTH_77"
] | [
12230
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Dikarya",
"Stenosarchaea group",
"metagenomes"
] | [
12207,
3,
3,
17
] | 4 | [] | [] | 0 | true | Domain | Winged helix-turn-helix domain 77 | Winged helix-turn-helix domain 77 | HTH_77 | 3 |
IPR058854 | 58,854 | HI_0096-like, winged helix domain | HI_0096-like_WHD | Domain | 139 | false | false | This entry represents a winged helix domain found in a small family of uncharacterised bacterial proteins that often contain a methyltransferase domain, including HI_0096 from Haemophilus influenzae. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF26433"
] | [
"WH_HI_0096"
] | [
139
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
138,
1
] | 2 | [] | [] | 0 | true | Domain | HI_0096-like, winged helix domain | HI_0096-like, winged helix domain | HI_0096-like_WHD | 4 |
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