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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR024899 | 24,899 | Nitrogen fixation-sustaining protein CowN | CowN | Family | 343 | false | false | Nitrogen fixation is catalysed by the nitrogenase complex and can be inhibited by carbon monoxide. The CowN protein protects against this inhibition, allowing nitrogen fixation-dependent growth to occur in the presence of carbon monoxide [ ]. Disruption of CowN specifically impaires Mo-nitrogenase-dependent growth at c... | [
"GO:0009399"
] | [
"nitrogen fixation"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"NCBIFAM",
"PFAM"
] | [
"MF_02117",
"NF033689",
"PF20543"
] | [
"CowN",
"N2Fix_CO_CowN",
"CowN"
] | [
330,
340,
343
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00056771",
"PUB00105245"
] | [
"21115659",
"25070737"
] | [
"Sustaining N2-dependent growth in the presence of CO.",
"NifA- and CooA-coordinated cowN expression sustains nitrogen fixation by Rhodobacter capsulatus in the presence of carbon monoxide."
] | [
2011,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"mine drainage metagenome"
] | [
342,
1
] | 2 | [] | [] | 0 | true | Family | Nitrogen fixation-sustaining protein CowN | Nitrogen fixation-sustaining protein CowN | CowN | 1 |
IPR024901 | 24,901 | FAPy deformylase | FAPy_deformylase | Family | 76 | false | false | This entry represents FAPy deformylase ( ) , which catalyses the second step of the riboflavin and coenzyme F0 biosynthetic pathway in archaea [ ]. | [
"GO:0008198",
"GO:0016811",
"GO:0009231",
"GO:0052645"
] | [
"ferrous iron binding",
"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides",
"riboflavin biosynthetic process",
"F420-0 metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP"
] | [
"MF_02116"
] | [
"FAPy_deform"
] | [
76
] | 1 | [
"EC",
"METACYC"
] | [
"3.5.1.102",
"PWY-6167"
] | [
"EC:3.5.1.102",
"METACYC:PWY-6167"
] | 2 | [] | 0 | [
"PUB00056772"
] | [
"19309161"
] | [
"An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin."
] | [
2009
] | 1 | [
"IPR003785"
] | [] | 1 | 0 | 1 | [
"Methanomada group"
] | [
76
] | 1 | [] | [] | 0 | true | Family | FAPy deformylase | FAPy deformylase | FAPy_deformylase | 2 |
IPR024902 | 24,902 | FAD synthase RibL | FAD_synth_RibL | Family | 646 | false | false | FAD synthases convert flavin mononucleotide (FMN) to flavin adenine dinucleotide (FAD) by the addition of the AMP portion of ATP. RibL is, currently, the only identified archaeal FAD synthase [ ]. This protein is not related to the eukarytoic or bacterial enzymes and contains no known motifs for FMN or FAD binding, sug... | [
"GO:0003919",
"GO:0006747",
"GO:0046444"
] | [
"FMN adenylyltransferase activity",
"FAD biosynthetic process",
"FMN metabolic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP"
] | [
"MF_02115"
] | [
"FAD_synth_arch"
] | [
646
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.7.7.2",
"PWY-6167",
"PWY-6168"
] | [
"EC:2.7.7.2",
"METACYC:PWY-6167",
"METACYC:PWY-6168"
] | 3 | [
"3glv"
] | 1 | [
"PUB00056773"
] | [
"20822113"
] | [
"Archaeal RibL: a new FAD synthetase that is air sensitive."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
639,
7
] | 2 | [] | [] | 0 | true | Family | FAD synthase RibL | FAD synthase RibL | FAD_synth_RibL | 6 |
IPR024903 | 24,903 | Putrescine carbamoyltransferase PtcA | PtcA | Family | 414 | false | false | Many bacterial species are capable of utilising agmatine (a decarboxylated derivative of arginine) as an energy source via the agamtine deiminase pathway. Agmatine deiminase converts agmatine to carbamoyl putrescine, which is subsequently phosphorylised to carbamoyl phosphate and putrescine by putrescine carbamoyltrans... | [
"GO:0050231",
"GO:0033390"
] | [
"putrescine carbamoyltransferase activity",
"putrescine biosynthetic process from arginine via N-carbamoylputrescine"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02102",
"TIGR04384"
] | [
"PTCase",
"putr_carbamoyl"
] | [
195,
414
] | 2 | [
"EC"
] | [
"2.1.3.6"
] | [
"EC:2.1.3.6"
] | 1 | [
"3txx",
"4a8h",
"4a8p",
"4a8t",
"4am8"
] | 5 | [
"PUB00041924"
] | [
"17028272"
] | [
"The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction."
] | [
2007
] | 1 | [
"IPR002292"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"bioreactor metagenome"
] | [
413,
1
] | 2 | [] | [] | 0 | true | Family | Putrescine carbamoyltransferase PtcA | Putrescine carbamoyltransferase PtcA | PtcA | 9 |
IPR024904 | 24,904 | Ornithine carbamoyltransferase | OTCase_ArgI | Family | 23,712 | false | false | Ornithine carbamoyltransferases catalyse the production of citrulline from carbamoyl-phosphate and ornithine [ ]. This reaction is part of the arginine biosynthetic pathway, and in some organisms the reaction is also part of the arginine deaminase pathway [ ]. In most prokaryotes, and some lower eukaryotes, the enzyme ... | [
"GO:0004585",
"GO:0006591"
] | [
"ornithine carbamoyltransferase activity",
"ornithine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01109"
] | [
"OTCase"
] | [
23712
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.3.3",
"PWY-4984",
"PWY-6344",
"PWY-7400",
"PWY-8187"
] | [
"EC:2.1.3.3",
"METACYC:PWY-4984",
"METACYC:PWY-6344",
"METACYC:PWY-7400",
"METACYC:PWY-8187"
] | 5 | [
"1a1s",
"1akm",
"1duv",
"1dxh",
"1ort",
"1pvv",
"1vlv",
"2ef0",
"2i6u",
"2otc",
"2p2g",
"2w37",
"3gd5",
"3tpf",
"3upd",
"4amu",
"4anf",
"4ep1",
"4f2g",
"4h31",
"4jfr",
"4jhx",
"4jqo",
"4kwt",
"4nf2",
"4oh7",
"6ovw",
"7nnf",
"7nnv",
"7nnw",
"7nny",
"7nnz"... | 44 | [
"PUB00001352",
"PUB00001353",
"PUB00001795",
"PUB00003720"
] | [
"3109911",
"3038540",
"2121620",
"3020372"
] | [
"Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli.",
"Nucleotide sequence of the ARG3 gene of the yeast Saccharomyces cerevisiae encoding ornithine carbamo... | [
1987,
1987,
1990,
1986
] | 4 | [
"IPR002292"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
847,
22009,
609,
247
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
2,
2,
7
] | 4 | true | Family | Ornithine carbamoyltransferase | Ornithine carbamoyltransferase | OTCase_ArgI | 3 |
IPR024905 | 24,905 | Sec-independent protein translocase protein TatE | TatE | Family | 902 | false | false | Translocation of proteins across the two membranes of Gram-negative bacteria can be carried out via a number of routes. Most proteins marked for export carry a secretion signal at their N terminus, and are secreted by the general secretory pathway. The signal peptide is cleaved as they pass through the outer membrane. ... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00903"
] | [
"TatE"
] | [
902
] | 1 | [
"GP"
] | [
"GenProp1136"
] | [
"GP:GenProp1136"
] | 1 | [] | 0 | [
"PUB00007662",
"PUB00007663"
] | [
"9649434",
"10652088"
] | [
"Overlapping functions of components of a bacterial Sec-independent protein export pathway.",
"The Tat protein export pathway."
] | [
1998,
2000
] | 2 | [
"IPR006312"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta"
] | [
900,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Sec-independent protein translocase protein TatE | Sec-independent protein translocase protein TatE | TatE | 6 |
IPR024906 | 24,906 | Enoyl reductase FAD binding domain | Eno_Rdtase_FAD-bd_dom | Domain | 4,646 | false | false | This entry represents the C-terminal domain of trans-2-enoyl-CoA reductase that binds to FAD. The activity was characterised in Euglena where an unusual fatty acid synthesis path-way in mitochondria performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07055"
] | [
"Eno-Rase_FAD_bd"
] | [
4646
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.3.1.9",
"PWY-5971",
"PWY-5973",
"PWY-5989",
"PWY-6282",
"PWY-6519",
"PWY-7663",
"PWY-7664",
"PWY-7858",
"PWY-8173",
"PWY-8174",
"PWY-8175",
"PWY-8203",
"PWYG-321"
] | [
"EC:1.3.1.9",
"METACYC:PWY-5971",
"METACYC:PWY-5973",
"METACYC:PWY-5989",
"METACYC:PWY-6282",
"METACYC:PWY-6519",
"METACYC:PWY-7663",
"METACYC:PWY-7664",
"METACYC:PWY-7858",
"METACYC:PWY-8173",
"METACYC:PWY-8174",
"METACYC:PWY-8175",
"METACYC:PWY-8203",
"METACYC:PWYG-321"
] | 14 | [
"3s8m",
"3zu2",
"3zu3",
"3zu4",
"3zu5",
"4bko",
"4bkq",
"4bkr",
"4eue",
"4euf",
"4euh",
"4fbg",
"4ggo",
"4ggp",
"5g2o",
"5jai",
"5jam",
"5jaq",
"5xi0",
"8rcz"
] | 20 | [
"PUB00056785"
] | [
"15569691"
] | [
"Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4591,
17,
38
] | 3 | [] | [] | 0 | true | Domain | Enoyl reductase FAD binding domain | Enoyl reductase FAD binding domain | Eno_Rdtase_FAD-bd_dom | 1 |
IPR024909 | 24,909 | Cysteinyl-tRNA synthetase/mycothiol ligase | Cys-tRNA/MSH_ligase | Family | 43,472 | false | false | This entry represents a subgroup of the class-I aminoacyl-tRNA synthetase family. It includes cysteinyl-tRNA synthetase and the related enzyme mycothiol ligase [ ]. Cysteine-tRNA ligase (also known as Cysteinyl-tRNA synthetase) ( ) is an alpha monomer and belongs to class Ia [ ]. It is highly specific despite not posse... | [] | [] | [] | 0 | [
"PRINTS",
"PANTHER"
] | [
"PR00983",
"PTHR10890"
] | [
"TRNASYNTHCYS",
""
] | [
41568,
43429
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1.16",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-9725370",
"R-MTU-879299"
] | [
"EC:6.1.1.16",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-9725370",
"REACTOME:R-MTU-879299"
] | 5 | [
"1li5",
"1li7",
"1u0b",
"3c8z",
"3sp1",
"3tqo",
"6ujd",
"8hfm",
"8hfn",
"8hfo",
"8qhp",
"9yru",
"9yrw",
"9yrx",
"9yrz",
"9ys0",
"9ys1",
"9ys2",
"9yt2",
"9yt3",
"9yt5"
] | 21 | [
"PUB00028887",
"PUB00042967",
"PUB00056788",
"PUB00056789"
] | [
"12032090",
"16674910",
"1992490",
"12033919"
] | [
"Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase.",
"A coupled spectrophotometric assay for l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase and its application for inhibitor screening.",
"Sequence determination and modeling of structural motifs ... | [
2002,
2006,
1991,
2002
] | 4 | [] | [
"IPR015803",
"IPR017812"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
897,
31837,
9592,
33,
1113
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
4,
4,
2,
1,
18,
14,
1,
11,
15,
1,
1,
53
] | 13 | true | Family | Cysteinyl-tRNA synthetase/mycothiol ligase | Cysteinyl-tRNA synthetase/mycothiol ligase | Cys-tRNA/MSH_ligase | 8 |
IPR024910 | 24,910 | Trans-2-enoyl-CoA reductase catalytic domain, putative | Enoyl-CoA_Rdtase_cat_dom | Domain | 4,693 | false | false | This entry represents a putative catalytic domain of trans-2-enoyl-CoA reductases ( ). In Euglena where the enzyme has been characterised it catalyses the reduction of enoyl-CoA to acyl-CoA in an unusual fatty acid pathway in mitochondria. The whole path performs a malonyl-CoA independent synthesis of fatty acids leadi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12241"
] | [
"Enoyl_reductase"
] | [
4693
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.3.1.9",
"PWY-5971",
"PWY-5973",
"PWY-5989",
"PWY-6282",
"PWY-6519",
"PWY-7663",
"PWY-7664",
"PWY-7858",
"PWY-8173",
"PWY-8174",
"PWY-8175",
"PWY-8203",
"PWYG-321"
] | [
"EC:1.3.1.9",
"METACYC:PWY-5971",
"METACYC:PWY-5973",
"METACYC:PWY-5989",
"METACYC:PWY-6282",
"METACYC:PWY-6519",
"METACYC:PWY-7663",
"METACYC:PWY-7664",
"METACYC:PWY-7858",
"METACYC:PWY-8173",
"METACYC:PWY-8174",
"METACYC:PWY-8175",
"METACYC:PWY-8203",
"METACYC:PWYG-321"
] | 14 | [
"3s8m",
"3zu2",
"3zu3",
"3zu4",
"3zu5",
"4bko",
"4bkq",
"4bkr",
"4eue",
"4euf",
"4euh",
"4fbg",
"4ggo",
"4ggp",
"5g2o",
"5jai",
"5jam",
"5jaq",
"5xi0",
"8rcz"
] | 20 | [
"PUB00056785"
] | [
"15569691"
] | [
"Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4634,
20,
39
] | 3 | [] | [] | 0 | true | Domain | Trans-2-enoyl-CoA reductase catalytic domain, putative | Trans-2-enoyl-CoA reductase catalytic domain, putative | Enoyl-CoA_Rdtase_cat_dom | 7 |
IPR024911 | 24,911 | DNA gyrase inhibitor | SmbC | Family | 972 | false | false | DNA gyrase, a type II topoisomerase, negatively supercoils DNA and is essential for the survival of bacterial cells. This entry represents DNA gyrase inhibitor from Escherichia coli (SmbC) and similar sequences from enterobacterales. SmbC, also known as GyrI, is a protein which inhibits the supercoiling activity of DNA... | [
"GO:0008657"
] | [
"DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01896"
] | [
"DNA_gyrase_inhibitor"
] | [
972
] | 1 | [] | [] | [] | 0 | [
"1jyh"
] | 1 | [
"PUB00056797",
"PUB00056798",
"PUB00056799"
] | [
"9442027",
"11850398",
"13680098"
] | [
"Identification of DNA gyrase inhibitor (GyrI) in Escherichia coli.",
"GyrI: a counter-defensive strategy against proteinaceous inhibitors of DNA gyrase.",
"Chromosomally encoded gyrase inhibitor GyrI protects Escherichia coli against DNA-damaging agents."
] | [
1998,
2002,
2003
] | 3 | [
"IPR050908"
] | [] | 1 | 0 | 1 | [
"Callosobruchus maculatus",
"Gammaproteobacteria"
] | [
1,
971
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DNA gyrase inhibitor | DNA gyrase inhibitor | SmbC | 3 |
IPR024912 | 24,912 | Protein translocase subunit SecD, archaeal | SecD_arc | Family | 604 | false | false | Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component [ ]. From there, the mature proteins are either targeted to the outer membra... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01463_A"
] | [
"SecD_A"
] | [
604
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007064",
"PUB00007065",
"PUB00007066",
"PUB00007187",
"PUB00008120",
"PUB00053868"
] | [
"2202721",
"11336818",
"10418149",
"12167867",
"9694879",
"16452406"
] | [
"The sec and prl genes of Escherichia coli.",
"SecB, a molecular chaperone with two faces.",
"Effects of pre-protein overexpression on SecB synthesis in Escherichia coli.",
"Three-dimensional structure of the bacterial protein-translocation complex SecYEG.",
"SecDF of Bacillus subtilis, a molecular Siamese ... | [
1990,
2001,
1999,
2002,
1998,
2006
] | 6 | [
"IPR022813"
] | [] | 1 | 0 | 1 | [
"Methanobacteriota",
"ecological metagenomes"
] | [
599,
5
] | 2 | [] | [] | 0 | true | Family | Protein translocase subunit SecD, archaeal | Protein translocase subunit SecD, archaeal | SecD_arc | 5 |
IPR024913 | 24,913 | tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS | tRNA_Ile2__agm2C_synt | Family | 860 | false | false | TiaS is an archaeal ATP-dependent agmatine transferase that catalyses the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2) [ ]. This modified base specifically recognises AUA codons. | [
"GO:0016879",
"GO:0002101"
] | [
"ligase activity, forming carbon-nitrogen bonds",
"tRNA wobble cytosine modification"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01892"
] | [
"tRNA_Ile2_agm2C_synt"
] | [
860
] | 1 | [
"EC"
] | [
"6.3.4.22"
] | [
"EC:6.3.4.22"
] | 1 | [
"3amt",
"3amu",
"3au7",
"4rvz",
"5xob",
"6agg"
] | 6 | [
"PUB00056803"
] | [
"20139989"
] | [
"Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Geodia barretti",
"unclassified sequences"
] | [
845,
1,
14
] | 3 | [] | [] | 0 | true | Family | tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS | tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS | tRNA_Ile2__agm2C_synt | 6 |
IPR024915 | 24,915 | 23S rRNA (guanosine-2-O-)-methyltransferase RlmB | 23S_rRNA_MeTrfase_RlmB | Family | 5,908 | false | false | 23S rRNA (guanosine-2-O-)-methyltransferase RlmB specifically methylates the ribose of guanosine 2251 in 23S rRNA [ ]. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01887"
] | [
"23SrRNA_methyltr_B"
] | [
5908
] | 1 | [
"EC"
] | [
"2.1.1.185"
] | [
"EC:2.1.1.185"
] | 1 | [
"1gz0"
] | 1 | [
"PUB00028132"
] | [
"11698387"
] | [
"The rlmB gene is essential for formation of Gm2251 in 23S rRNA but not for ribosome maturation in Escherichia coli."
] | [
2001
] | 1 | [
"IPR004441"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Fungi",
"unclassified sequences"
] | [
5859,
2,
47
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 23S rRNA (guanosine-2-O-)-methyltransferase RlmB | 23S rRNA (guanosine-2-O-)-methyltransferase RlmB | 23S_rRNA_MeTrfase_RlmB | 6 |
IPR024918 | 24,918 | 3'-5' ssDNA/RNA exonuclease TatD | Exonuc_TatD | Family | 1,348 | false | false | TatD is a Mg(2+)-dependent 3'-5' exonuclease that not only degrades chromosomal DNA during apoptosis but also processes single-stranded DNA during DNA repair [ ]. In E. coli TatD is encoded by a operon that encodes Tat proteins, including TatA, TatB, and TatC, for protein transport via the Tat (Twin-Arginine Translocat... | [
"GO:0008408"
] | [
"3'-5' exonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00901",
"NF007745"
] | [
"TatD_exonuclease",
"PRK10425.1"
] | [
1240,
1348
] | 2 | [
"EC",
"EC"
] | [
"3.1.11.-",
"3.1.13.-"
] | [
"EC:3.1.11.-",
"EC:3.1.13.-"
] | 2 | [
"1xwy",
"4p5u",
"4pe8"
] | 3 | [
"PUB00007123",
"PUB00077112"
] | [
"10747959",
"25114049"
] | [
"TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export.",
"Structure and function of TatD exonuclease in DNA repair."
] | [
2000,
2014
] | 2 | [
"IPR001130"
] | [] | 1 | 0 | 1 | [
"Anopheles maculatus",
"Gammaproteobacteria"
] | [
1,
1347
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 3'-5' ssDNA/RNA exonuclease TatD | 3'-5' ssDNA/RNA exonuclease TatD | Exonuc_TatD | 6 |
IPR024919 | 24,919 | ECF transporter transmembrane protein EcfT | EcfT | Family | 3,526 | false | false | Energy-coupling factor (ECF) transporters consist of a substrate-specific component (known as the S component), and an energy-coupling module [ ]. The substrate-binding component is a small integral membrane protein which captures specific substrates and forms an active transporter in the presence of the energy-couplin... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_01461"
] | [
"EcfT"
] | [
3526
] | 1 | [] | [] | [] | 0 | [
"4huq",
"4hzu",
"4rfs",
"5d3m",
"5jsz",
"6fnp",
"6zg3",
"7nnt",
"7nnu",
"8bmp",
"8bmq",
"8bmr",
"8bms",
"9kym"
] | 14 | [
"PUB00056162",
"PUB00056815"
] | [
"18931129",
"19717603"
] | [
"A novel class of modular transporters for vitamins in prokaryotes.",
"Two essential arginine residues in the T components of energy-coupling factor transporters."
] | [
2009,
2009
] | 2 | [
"IPR003339"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
3518,
8
] | 2 | [] | [] | 0 | true | Family | ECF transporter transmembrane protein EcfT | ECF transporter transmembrane protein EcfT | EcfT | 5 |
IPR024920 | 24,920 | Dihydroorotate dehydrogenase, class 1 | Dihydroorotate_DH_1 | Family | 8,932 | false | false | Dihydroorotate dehydrogenase (DHOD), also known as dihydroorotate oxidase, catalyses the fourth step in de novo pyrimidine biosynthesis, the stereospecific oxidation of (S)-dihydroorotate to orotate, which is the only redox reaction in this pathway. DHODs can be divided into two mains classes: class 1 cytosolic enzymes... | [
"GO:0004152",
"GO:0006221",
"GO:0005737"
] | [
"dihydroorotate dehydrogenase activity",
"pyrimidine nucleotide biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_00224"
] | [
"DHO_dh_type1"
] | [
8932
] | 1 | [
"EC",
"METACYC"
] | [
"1.3.1.14",
"PWY-7791"
] | [
"EC:1.3.1.14",
"METACYC:PWY-7791"
] | 2 | [
"1dor",
"1ep1",
"1ep2",
"1ep3",
"1jqv",
"1jqx",
"1jrb",
"1jrc",
"1jub",
"1jue",
"1ovd",
"2bsl",
"2bx7",
"2dor",
"3oix",
"5ksw",
"5ue9"
] | 17 | [
"PUB00005052",
"PUB00024104",
"PUB00024613",
"PUB00033267",
"PUB00033268",
"PUB00056837"
] | [
"9655329",
"10673429",
"11188687",
"9405053",
"12220493",
"8021180"
] | [
"The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function.",
"Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents.",
"Structure of dihydroorotate dehydrogenase B: electron tr... | [
1998,
2000,
2000,
1997,
2002,
1994
] | 6 | [
"IPR012135"
] | [
"IPR033886",
"IPR033888"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
499,
8040,
67,
326
] | 4 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Dihydroorotate dehydrogenase, class 1 | Dihydroorotate dehydrogenase, class 1 | Dihydroorotate_DH_1 | 8 |
IPR024921 | 24,921 | Protein-export membrane protein SecF | SecF | Family | 626 | false | false | This family consists of various archaeal SecF proteins. They show a high degree of structural and functional similarity to their bacterial homologues, despite the different composition of their translocation machineries [ ]. Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein tr... | [
"GO:0065002",
"GO:0016020"
] | [
"intracellular protein transmembrane transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP"
] | [
"MF_01464_A"
] | [
"SecF_A"
] | [
626
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00007064",
"PUB00007065",
"PUB00007066",
"PUB00007187",
"PUB00008120",
"PUB00053868"
] | [
"2202721",
"11336818",
"10418149",
"12167867",
"9694879",
"16452406"
] | [
"The sec and prl genes of Escherichia coli.",
"SecB, a molecular chaperone with two faces.",
"Effects of pre-protein overexpression on SecB synthesis in Escherichia coli.",
"Three-dimensional structure of the bacterial protein-translocation complex SecYEG.",
"SecDF of Bacillus subtilis, a molecular Siamese ... | [
1990,
2001,
1999,
2002,
1998,
2006
] | 6 | [
"IPR022813"
] | [] | 1 | 0 | 1 | [
"Aerophobetes bacterium",
"Archaea",
"ecological metagenomes"
] | [
1,
617,
8
] | 3 | [] | [] | 0 | true | Family | Protein-export membrane protein SecF | Protein-export membrane protein SecF | SecF | 9 |
IPR024922 | 24,922 | Rubredoxin | Rubredoxin | Family | 7,148 | false | false | Rubredoxin is a low molecular weight iron-containing bacterial and archaeal protein that is involved in electron transfer [ , ], sometimes replacing ferredoxin as an electron carrier [ ]. The 3D structures of a number of rubredoxins have been solved [ , ]. The fold belongs to the α+β class, with 2 α-helices and 2-3 β-s... | [
"GO:0005506",
"GO:0009055"
] | [
"iron ion binding",
"electron transfer activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF"
] | [
"PIRSF000071"
] | [
"Rubredoxin"
] | [
7148
] | 1 | [] | [] | [] | 0 | [
"1b13",
"1b2j",
"1b2o",
"1be7",
"1bfy",
"1bq8",
"1bq9",
"1brf",
"1c09",
"1caa",
"1cad",
"1e8j",
"1fhh",
"1fhm",
"1irn",
"1iro",
"1iu5",
"1iu6",
"1r0f",
"1r0g",
"1r0h",
"1r0i",
"1r0j",
"1rb9",
"1rdg",
"1rdv",
"1rwd",
"1smm",
"1smu",
"1smw",
"1t9o",
"1t9p"... | 70 | [
"PUB00000489",
"PUB00003266",
"PUB00008022",
"PUB00008023",
"PUB00008024"
] | [
"2244884",
"1992166",
"7726577",
"1303768",
"3441010"
] | [
"Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data.",
"Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution.",
"Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, He... | [
1990,
1991,
1995,
1992,
1987
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
294,
6697,
4,
153
] | 4 | [] | [] | 0 | true | Family | Rubredoxin | Rubredoxin | Rubredoxin | 1 |
IPR024923 | 24,923 | Peptidoglycan biosynthesis protein, SpoVB-type | PG_synth_SpoVB | Family | 11,559 | false | false | This entry represents a group of peptidoglycan biosynthesis proteins including stage V sporulation protein B (SpoVB), sporulation protein YkvU and probable cell division protein YtgP [ ]. The integral membrane protein SpoVB has been implicated in the biosynthesis of the peptidoglycan component of the spore cortex in Ba... | [] | [] | [] | 0 | [
"PIRSF",
"CDD"
] | [
"PIRSF038958",
"cd13124"
] | [
"PG_synth_SpoVB",
"MATE_SpoVB_like"
] | [
9909,
10877
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005697",
"PUB00056820"
] | [
"1744050",
"19648239"
] | [
"Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis.",
"Homologues of the Bacillus subtilis SpoVB protein are involved in cell wall metabolism."
] | [
1991,
2009
] | 2 | [
"IPR002797"
] | [
"IPR014249"
] | 1 | 1 | 0 | [
"Bacteria",
"Methanobacteriales",
"unclassified sequences"
] | [
11515,
16,
28
] | 3 | [] | [] | 0 | true | Family | Peptidoglycan biosynthesis protein, SpoVB-type | Peptidoglycan biosynthesis protein, SpoVB-type | PG_synth_SpoVB | 7 |
IPR024924 | 24,924 | 7-carboxy-7-deazaguanine synthase-like | 7-CO-7-deazaguanine_synth-like | Family | 16,084 | false | false | This entry represents 7-carboxy-7-deazaguanine synthase and related uncharacterised proteins that are thought to have the same function. 7-deazapurines are compounds that contain pyrrolopyrimidine functional groups (similar to purines, but lacking one of the nitrogens in the pentameric ring). These compounds form a str... | [] | [] | [] | 0 | [
"HAMAP",
"PIRSF"
] | [
"MF_00917",
"PIRSF000370"
] | [
"QueE",
"QueE"
] | [
16081,
14882
] | 2 | [
"EC",
"METACYC"
] | [
"4.3.99.3",
"PWY-6703"
] | [
"EC:4.3.99.3",
"METACYC:PWY-6703"
] | 2 | [
"4njg",
"4njh",
"4nji",
"4njj",
"4njk",
"5tgs",
"5th5",
"6nhl"
] | 8 | [
"PUB00035932",
"PUB00056816"
] | [
"14660578",
"19354300"
] | [
"Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine.",
"The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of PreQ(0) from guanosine 5'-triphosphate in four steps."
] | [
2004,
2009
] | 2 | [] | [
"IPR017742",
"IPR023868",
"IPR027609",
"IPR027621",
"IPR030977"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
744,
14871,
36,
151,
282
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 7-carboxy-7-deazaguanine synthase-like | 7-carboxy-7-deazaguanine synthase-like | 7-CO-7-deazaguanine_synth-like | 7 |
IPR024925 | 24,925 | Malonyl CoA-acyl carrier protein transacylase | Malonyl_CoA-ACP_transAc | Family | 22,649 | false | false | Malonyl CoA-acyl carrier protein transacylases transfer the malonyl moiety from coenzyme A to acyl-carrier protein. These include proteins involved in fatty acid biosynthesis (FabD), antibiotic biosynthesis (PksC) and the McdH subunit of malonate decarboxylase [ , , ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000446"
] | [
"Mct"
] | [
22649
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.39",
"PWY-4381",
"PWY-6799",
"PWY-8012",
"PWY-8047",
"PWY-8049",
"PWY-8438"
] | [
"EC:2.3.1.39",
"METACYC:PWY-4381",
"METACYC:PWY-6799",
"METACYC:PWY-8012",
"METACYC:PWY-8047",
"METACYC:PWY-8049",
"METACYC:PWY-8438"
] | 7 | [
"1mla",
"2c2n",
"2cdh",
"2cf2",
"2cuy",
"2g1h",
"2g2o",
"2g2y",
"2g2z",
"2h1y",
"3ezo",
"3h0p",
"3hjv",
"3im8",
"3im9",
"3k89",
"3ptw",
"3qat",
"3r97",
"3rgi",
"3sbm",
"3tqe",
"4rr5",
"5dz6",
"5dz7",
"5ypv",
"5zk4",
"6apf",
"6apg",
"6apk",
"6mhp",
"6smd"... | 33 | [
"PUB00056817",
"PUB00056818",
"PUB00056819"
] | [
"1314802",
"16757561",
"9914491"
] | [
"Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase.",
"Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis.",
"Formation of catalytically a... | [
1992,
2006,
1999
] | 3 | [] | [
"IPR004410",
"IPR017554"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
21901,
461,
21,
266
] | 4 | [
"Escherichia coli (strain K12)",
"Zea mays"
] | [
1,
1
] | 2 | true | Family | Malonyl CoA-acyl carrier protein transacylase | Malonyl CoA-acyl carrier protein transacylase | Malonyl_CoA-ACP_transAc | 2 |
IPR024926 | 24,926 | Nucleolar GTP-binding protein 1 | NOG1 | Family | 4,240 | false | false | Nucleolar GTP-binding protein 1 is involved in the biogenesis of the 60S ribosomal subunit [ ]. It is found as part of the pre-60S complex in nucleolus [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF038919"
] | [
"NOG1"
] | [
4240
] | 1 | [] | [] | [] | 0 | [
"3jct",
"4v7f",
"5jcs",
"6c0f",
"6elz",
"6em1",
"6em5",
"6ft6",
"6lss",
"6lu8",
"6m62",
"6n8j",
"6n8k",
"6n8l",
"6ylg",
"6ylh",
"6ylx",
"6yly",
"7bt6",
"7btb",
"7nac",
"7nad",
"7of1",
"7oh3",
"7ohp",
"7ohq",
"7ohr",
"7ohs",
"7oht",
"7ohu",
"7ohv",
"7ohw"... | 112 | [
"PUB00019935",
"PUB00056203"
] | [
"11112701",
"12808088"
] | [
"A novel nucleolar G-protein conserved in eukaryotes.",
"Sequential protein association with nascent 60S ribosomal particles."
] | [
2001,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4240
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
1,
3,
4,
1,
1,
3,
2,
1,
1,
5
] | 12 | true | Family | Nucleolar GTP-binding protein 1 | Nucleolar GTP-binding protein 1 | NOG1 | 3 |
IPR024927 | 24,927 | Purple acid phosphatase | Acid_PPase | Family | 3,852 | false | false | This entry includes purple acid phosphatases ( ), which are metal dependent, binding two metal ions. Metal binding ligands and residues involved in resistance to tartrate inhibition are conserved [ ]. Purple acid phosphatase 3, 4, 7, 8 and 17 are found in plants, bind zinc and iron, and the genes are predominantly tran... | [
"GO:0003993"
] | [
"acid phosphatase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"CDD"
] | [
"PIRSF000898",
"cd07378"
] | [
"Acid_Ptase_5",
"MPP_ACP5"
] | [
3387,
3298
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.2",
"PWY-6348",
"R-HSA-196843",
"R-MMU-196843",
"R-RNO-196843",
"R-SSC-196843"
] | [
"EC:3.1.3.2",
"METACYC:PWY-6348",
"REACTOME:R-HSA-196843",
"REACTOME:R-MMU-196843",
"REACTOME:R-RNO-196843",
"REACTOME:R-SSC-196843"
] | 6 | [
"1qfc",
"1qhw",
"1ute",
"1war",
"2bq8",
"3tgh",
"5uq6",
"7ov2",
"7ov3",
"7ov8"
] | 10 | [
"PUB00038058",
"PUB00087904",
"PUB00088904",
"PUB00088905",
"PUB00103626"
] | [
"15993892",
"18940929",
"10504579",
"16244908",
"22387043"
] | [
"Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.",
"Acid phosphatase 5 is responsible for removing the mannose 6-phosphate recognition marker from lysosomal proteins.",
"A type 5 acid phosphatase gene from Arabidopsis thaliana i... | [
2005,
2008,
1999,
2005,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
625,
3224,
3
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
30,
1,
5,
4,
1,
9,
5,
20
] | 8 | true | Family | Purple acid phosphatase | Purple acid phosphatase | Acid_PPase | 8 |
IPR024928 | 24,928 | E3 ubiquitin-protein ligase, SMURF1 type | E3_ub_ligase_SMURF1 | Family | 13,631 | false | false | This entry represents a set of E3 ubiquitin-protein ligases which accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates, like SMURF1 [ ], Pub1 [ ] and RSP5 [ ]. All of them contain a HECT domain [ ]. | [
"GO:0061630",
"GO:0006511"
] | [
"ubiquitin protein ligase activity",
"ubiquitin-dependent protein catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF001569"
] | [
"E3_ub_ligase_SMURF1"
] | [
13631
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.26",
"PWY-7511",
"R-CEL-1253288",
"R-CEL-2672351",
"R-CEL-8948751",
"R-CEL-9013406",
"R-CEL-9013420",
"R-CEL-983168",
"R-DME-1169408",
"R-DME-1253288",
"R-DME-2122948",
"R-DME-2173795",
"R-DME-8939236",
"R-DME-8948747",
"R-DME-8948751",
"R-DME-9013406",
"R-DME-9013420",
"R-D... | [
"EC:2.3.2.26",
"METACYC:PWY-7511",
"REACTOME:R-CEL-1253288",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CEL-8948751",
"REACTOME:R-CEL-9013406",
"REACTOME:R-CEL-9013420",
"REACTOME:R-CEL-983168",
"REACTOME:R-DME-1169408",
"REACTOME:R-DME-1253288",
"REACTOME:R-DME-2122948",
"REACTOME:R-DME-2173795",
... | 88 | [
"5xmc",
"9gik",
"9gim"
] | 3 | [
"PUB00027961",
"PUB00056821",
"PUB00056822",
"PUB00056823"
] | [
"10998601",
"11956316",
"10458166",
"9858558"
] | [
"The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases.",
"The novel HECT-type ubiquitin-protein ligase Pub2p shares partially overlapping function with Pub1p in Schizosaccharomyces pombe.",
"A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation.",
"... | [
2000,
2002,
1999,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
13631
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
2,
52,
8,
21,
28,
1,
35,
1,
3
] | 9 | true | Family | E3 ubiquitin-protein ligase, SMURF1 type | E3 ubiquitin-protein ligase, SMURF1 type | E3_ub_ligase_SMURF1 | 2 |
IPR024929 | 24,929 | Nucleolar GTP-binding protein 2, circularly permuted GTPase motif | GNL2_CP_dom | Domain | 4,477 | false | false | This entry represents the circularly permuted GTPase motif of Nucleolar GTP-binding protein 2 (GNL2, also known as NGP-1) from animals and fungi. GNL2 is a GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation [ ]. This group of proteins also inc... | [
"GO:0005730"
] | [
"nucleolus"
] | [
"cellular_component"
] | 1 | [
"CDD"
] | [
"cd01858"
] | [
"NGP_1"
] | [
4477
] | 1 | [] | [] | [] | 0 | [
"3jct",
"6ft6",
"6lss",
"6lu8",
"6m62",
"6n8j",
"6ylg",
"6ylh",
"7bt6",
"7btb",
"7of1",
"7oh3",
"7ohq",
"7oht",
"7ug6",
"7uoo",
"7uqb",
"7uqz",
"7uui",
"7v08",
"8fkz",
"8fl0",
"8fl2",
"8fl3",
"8fl4",
"8fl6",
"8fl7",
"8fl9",
"8hfr",
"8idt",
"8idy",
"8ie3"... | 52 | [
"PUB00056824",
"PUB00072522",
"PUB00101554"
] | [
"11707418",
"21205822",
"32669547"
] | [
"Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps.",
"Nuclear/nucleolar GTPase 2 proteins as a subfamily of YlqF/YawG GTPases function in pre-60S ribosomal subunit maturation of mono- and dicotyledonous plants.",
"Structural snapshots of human pre-60S ribosoma... | [
2001,
2011,
2020
] | 3 | [
"IPR030378"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4477
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
2,
1,
1,
4,
4,
1,
1,
2,
1,
1,
6
] | 12 | true | Domain | Nucleolar GTP-binding protein 2, circularly permuted GTPase motif | Nucleolar GTP-binding protein 2, circularly permuted GTPase motif | GNL2_CP_dom | 2 |
IPR024930 | 24,930 | Skp domain superfamily | Skp_dom_sf | Homologous_superfamily | 18,566 | false | false | This superfamily represents the Skp (also known as OmpH) domain, named after the Skp protein which functions as a periplasmic chaperone for newly synthesised outer-membrane proteins [ , ]. Three hairpin-shaped α-helical extensions reach out by approximately 60 A from a trimerisation region, which is composed of three i... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.910.20",
"SSF111384"
] | [
"",
""
] | [
18287,
18508
] | 2 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9760173",
"R-PFA-6791226"
] | [
"REACTOME:R-HSA-9760173",
"REACTOME:R-PFA-6791226"
] | 2 | [
"1sg2",
"1u2m",
"4kqt",
"8gl8"
] | 4 | [
"PUB00015159",
"PUB00015160"
] | [
"15304217",
"15361861"
] | [
"Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.",
"Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture."
] | [
2004,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
25,
17976,
151,
414
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Skp domain superfamily | Skp domain superfamily | Skp_dom_sf | 3 |
IPR024931 | 24,931 | Importin subunit alpha | Importin_alpha | Family | 15,676 | false | false | The exchange of macromolecules between the nucleus and cytoplasm takes place through nuclear pore complexes within the nuclear membrane. Active transport of large molecules through these pore complexes require carrier proteins, called karyopherins (importins and exportins), which shuttle between the two compartments. M... | [
"GO:0061608",
"GO:0006606",
"GO:0005737"
] | [
"nuclear import signal receptor activity",
"protein import into nucleus",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF005673"
] | [
"Importin_alpha"
] | [
15676
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-140342",
"R-BTA-68616",
"R-BTA-909733",
"R-DDI-909733",
"R-DME-5693548",
"R-HSA-111932",
"R-HSA-1169408",
"R-HSA-140342",
"R-HSA-162592",
"R-HSA-168271",
"R-HSA-168276",
"R-HSA-180910",
"R-HSA-442729",
"R-HSA-5693548",
"R-HSA-68616",
"R-HSA-9018519",
"R-HSA-909733",
"R-HSA-9... | [
"REACTOME:R-BTA-140342",
"REACTOME:R-BTA-68616",
"REACTOME:R-BTA-909733",
"REACTOME:R-DDI-909733",
"REACTOME:R-DME-5693548",
"REACTOME:R-HSA-111932",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-140342",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-168271",
"REACTOME:R-HSA-168276",
"REACTOME:R-HSA-18... | 28 | [
"1ejl",
"1ejy",
"1ial",
"1iq1",
"1pjm",
"1pjn",
"1q1s",
"1q1t",
"1un0",
"1wa5",
"2c1t",
"2jdq",
"2ynr",
"2yns",
"3fex",
"3fey",
"3knd",
"3oqs",
"3q5u",
"3rz9",
"3rzx",
"3tj3",
"3tpo",
"3ukw",
"3ukx",
"3uky",
"3ukz",
"3ul0",
"3ul1",
"3uvu",
"3zin",
"3zio"... | 161 | [
"PUB00004894",
"PUB00034676"
] | [
"8692858",
"17170104"
] | [
"The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence.",
"Classical nuclear localization signals: definition, function, and interaction with importin alpha."
] | [
1996,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"unclassified dsDNA viruses"
] | [
15674,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
2,
11,
12,
22,
12,
1,
16,
29,
1,
2,
24
] | 12 | true | Family | Importin subunit alpha | Importin subunit alpha | Importin_alpha | 2 |
IPR024932 | 24,932 | Flavin transferase ApbE | ApbE | Family | 25,239 | false | false | ApbE is a Mg2+-dependent flavin transferase that catalyses covalent attachment of FMN to a threonine residue in bacterial flavoproteins [ ]. | [
"GO:0017013"
] | [
"protein flavinylation"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF02424",
"PIRSF006268",
"PTHR30040"
] | [
"ApbE",
"ApbE",
""
] | [
25222,
18379,
24937
] | 3 | [
"EC"
] | [
"2.7.1.180"
] | [
"EC:2.7.1.180"
] | 1 | [
"1vrm",
"2o18",
"3pnd",
"4ifu",
"4ifw",
"4ifx",
"4ifz",
"4ig1",
"4xdr",
"4xdt",
"4xdu",
"4xgv",
"4xgw",
"4xgx",
"5mgy",
"6nxi",
"6nxj",
"7esa",
"7esb",
"7esc",
"7f2u",
"7f39",
"7mgt"
] | 23 | [
"PUB00070984"
] | [
"23558683"
] | [
"Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
103,
24348,
169,
619
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Family | Flavin transferase ApbE | Flavin transferase ApbE | ApbE | 9 |
IPR024934 | 24,934 | Rubredoxin-like domain | Rubredoxin-like_dom | Domain | 26,671 | false | false | Rubredoxin is a low molecular weight iron-containing bacterial protein involved in electron transfer [ , ], sometimes replacing ferredoxin as an electron carrier [ ]. Rubredoxins possess a 45- to 55-residue domain containing one iron atom tetrahedrally coordinated to four cysteinyl residues. Structural analysis of the ... | [
"GO:0005506"
] | [
"iron ion binding"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS50903"
] | [
"RUBREDOXIN_LIKE"
] | [
26671
] | 1 | [] | [] | [] | 0 | [
"1b13",
"1b2j",
"1b2o",
"1b71",
"1be7",
"1bfy",
"1bq8",
"1bq9",
"1brf",
"1c09",
"1caa",
"1cad",
"1dvb",
"1dx8",
"1e8j",
"1fhh",
"1fhm",
"1h7v",
"1irn",
"1iro",
"1iu5",
"1iu6",
"1jyb",
"1lkm",
"1lko",
"1lkp",
"1nnq",
"1qcv",
"1qyb",
"1r0f",
"1r0g",
"1r0h"... | 140 | [
"PUB00000489",
"PUB00003266",
"PUB00008022",
"PUB00008023",
"PUB00008024",
"PUB00008767",
"PUB00018378"
] | [
"2244884",
"1992166",
"7726577",
"1303768",
"3441010",
"8646540",
"7830611"
] | [
"Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data.",
"Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution.",
"Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, He... | [
1990,
1991,
1995,
1992,
1987,
1996,
1994
] | 7 | [] | [
"IPR024935",
"IPR048574"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1272,
22442,
2361,
13,
583
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
1,
7,
25
] | 4 | true | Domain | Rubredoxin-like domain | Rubredoxin-like domain | Rubredoxin-like_dom | 6 |
IPR024935 | 24,935 | Rubredoxin domain | Rubredoxin_dom | Domain | 16,857 | false | false | Rubredoxin is a low molecular weight iron-containing bacterial protein involved in electron transfer [ , ], sometimes replacing ferredoxin as an electron carrier [ ]. Rubredoxins possess a 45- to 55-residue domain containing one iron atom tetrahedrally coordinated to four cysteinyl residues. Structural analysis of the ... | [
"GO:0005506"
] | [
"iron ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"CDD"
] | [
"PF00301",
"PR00163",
"cd00730"
] | [
"Rubredoxin",
"RUBREDOXIN",
"rubredoxin"
] | [
16456,
14139,
16480
] | 3 | [] | [] | [] | 0 | [
"1b13",
"1b2j",
"1b2o",
"1be7",
"1bfy",
"1bq8",
"1bq9",
"1brf",
"1c09",
"1caa",
"1cad",
"1dx8",
"1e8j",
"1fhh",
"1fhm",
"1h7v",
"1irn",
"1iro",
"1iu5",
"1iu6",
"1qcv",
"1r0f",
"1r0g",
"1r0h",
"1r0i",
"1r0j",
"1rb9",
"1rdg",
"1rdv",
"1rwd",
"1s24",
"1smm"... | 118 | [
"PUB00000489",
"PUB00003266",
"PUB00008022",
"PUB00008023",
"PUB00008024",
"PUB00008767",
"PUB00018378"
] | [
"2244884",
"1992166",
"7726577",
"1303768",
"3441010",
"8646540",
"7830611"
] | [
"Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data.",
"Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution.",
"Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, He... | [
1990,
1991,
1995,
1992,
1987,
1996,
1994
] | 7 | [
"IPR024934"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
582,
14823,
1150,
299,
3
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
5,
18
] | 4 | true | Domain | Rubredoxin domain | Rubredoxin domain | Rubredoxin_dom | 1 |
IPR024936 | 24,936 | Cyclophilin-type peptidyl-prolyl cis-trans isomerase | Cyclophilin-type_PPIase | Family | 46,377 | false | false | Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity ( ), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ , ]. They also have protein chaperone-like functions [ ] and are the major high-affinity binding proteins for the immu... | [
"GO:0003755"
] | [
"peptidyl-prolyl cis-trans isomerase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF001467"
] | [
"Peptidylpro_ismrse"
] | [
46377
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.2.1.8",
"R-BTA-210991",
"R-BTA-6798695",
"R-BTA-72163",
"R-CEL-72163",
"R-DDI-72163",
"R-GGA-72163",
"R-HSA-114608",
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-173107",
"R-HSA-175474",
"R-HSA-180689",
"R-HSA-2025928",
... | [
"EC:5.2.1.8",
"REACTOME:R-BTA-210991",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-72163",
"REACTOME:R-CEL-72163",
"REACTOME:R-DDI-72163",
"REACTOME:R-GGA-72163",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACT... | 32 | [
"1a33",
"1a58",
"1ak4",
"1awq",
"1awr",
"1aws",
"1awt",
"1awu",
"1awv",
"1bck",
"1c5f",
"1clh",
"1cwa",
"1cwb",
"1cwc",
"1cwf",
"1cwh",
"1cwi",
"1cwj",
"1cwk",
"1cwl",
"1cwm",
"1cwo",
"1cyn",
"1dyw",
"1e3b",
"1e8k",
"1fgl",
"1h0p",
"1ist",
"1j2a",
"1lop"... | 435 | [
"PUB00000320",
"PUB00017852",
"PUB00021063",
"PUB00056846",
"PUB00056847",
"PUB00089651"
] | [
"2186809",
"14731520",
"15998457",
"21309470",
"21295323",
"20676357"
] | [
"The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.",
"Cyclophilins: a new family of proteins involved in intracellular folding.",
"The cyclophilins.",
"An overview of cyclophilins in human cancers.",
"Emerging picture of ho... | [
1990,
1992,
2005,
2010,
2011,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
653,
21761,
23583,
7,
373
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
23,
10,
14,
10,
1,
32,
18,
3,
22,
18,
3,
4,
41
] | 13 | true | Family | Cyclophilin-type peptidyl-prolyl cis-trans isomerase | Cyclophilin-type peptidyl-prolyl cis-trans isomerase | Cyclophilin-type_PPIase | 2 |
IPR024937 | 24,937 | Domain X | Domain_X | Domain | 132,697 | false | false | Group II introns are widespread in plant cell organelles [ ]. In vivo, most plant group II introns do not self-splice, but require the assistance of proteinaceous splicing factors, known as maturases. In higher plants, maturases are encoded for in the nuclear genes [ ], but are otherwise encoded by organellar introns. ... | [
"GO:0006397"
] | [
"mRNA processing"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01348"
] | [
"Intron_maturas2"
] | [
132697
] | 1 | [] | [] | [] | 0 | [
"5g2x",
"7d0f",
"7d0g",
"7d1a",
"8h2h"
] | 5 | [
"PUB00004435",
"PUB00004450",
"PUB00043292",
"PUB00043293"
] | [
"8255751",
"8029012",
"16763758",
"12527773"
] | [
"Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function.",
"Splicing defective mutants of the COXI gene of yeast mitochondrial DNA: initial definition of the maturase domain of the group II intron aI2.",
"Evolutionary o... | [
1993,
1994,
2006,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Haloferax sulfurifontis",
"unclassified sequences"
] | [
1899,
130770,
1,
27
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
35,
17,
2,
1,
17
] | 5 | true | Domain | Domain X | Domain X | Domain_X | 4 |
IPR024940 | 24,940 | Transcription factor TCF/LEF | TCF/LEF | Family | 11,383 | false | false | Members of this family of HMG box containing factors play an essential role in the Wnt/Wingless signalling cascade. They are known to associate with beta-catenin in the nucleus to mediate Wnt signaling [ , ]. This family exist in vertebrates, Drosophila melanogaster and Caenorhabditis elegans, and includes transcriptio... | [
"GO:0016055"
] | [
"Wnt signaling pathway"
] | [
"biological_process"
] | 1 | [
"PANTHER"
] | [
"PTHR10373"
] | [
""
] | [
11383
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-201722",
"R-CEL-3769402",
"R-CEL-4086398",
"R-CEL-4641265",
"R-CEL-8853884",
"R-CEL-8951430",
"R-CEL-9825892",
"R-DME-201722",
"R-DME-209421",
"R-DME-209441",
"R-DME-3769402",
"R-DME-4086398",
"R-DME-4641265",
"R-DME-8853884",
"R-DME-8951430",
"R-DME-9825892",
"R-DRE-201722",
... | [
"REACTOME:R-CEL-201722",
"REACTOME:R-CEL-3769402",
"REACTOME:R-CEL-4086398",
"REACTOME:R-CEL-4641265",
"REACTOME:R-CEL-8853884",
"REACTOME:R-CEL-8951430",
"REACTOME:R-CEL-9825892",
"REACTOME:R-DME-201722",
"REACTOME:R-DME-209421",
"REACTOME:R-DME-209441",
"REACTOME:R-DME-3769402",
"REACTOME:R-... | 52 | [
"1g3j",
"1jdh",
"1jpw",
"2gl7",
"2lef",
"3ouw",
"3oux"
] | 7 | [
"PUB00056864",
"PUB00069213",
"PUB00069267"
] | [
"11934263",
"10209158",
"9433138"
] | [
"TCF: Lady Justice casting the final verdict on the outcome of Wnt signalling.",
"Regulation of LEF-1/TCF transcription factors by Wnt and other signals.",
"TCF/LEF factor earn their wings."
] | [
2002,
1999,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Metazoa",
"bird metagenome"
] | [
11382,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
80,
5,
55,
30,
34
] | 6 | true | Family | Transcription factor TCF/LEF | Transcription factor TCF/LEF | TCF/LEF | 2 |
IPR024942 | 24,942 | Maturase MatK, N-terminal domain | Maturase_MatK_N | Domain | 141,502 | false | false | Group II introns are widespread in plant cell organelles [ ]. In vivo, most plant group II introns do not self-splice, but require the assistance of proteinaceous splicing factors, known as maturases. In higher plants, maturases are encoded for in the nuclear genes [ ], but are otherwise encoded by organellar introns. ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01824"
] | [
"MatK_N"
] | [
141502
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00004435",
"PUB00043292",
"PUB00043293"
] | [
"8255751",
"16763758",
"12527773"
] | [
"Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function.",
"Evolutionary origin of a plant mitochondrial group II intron from a reverse transcriptase/maturase-encoding ancestor.",
"Putative proteins related to group II ... | [
1993,
2006,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unidentified"
] | [
7,
141490,
5
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
14,
6,
3
] | 3 | true | Domain | Maturase MatK, N-terminal domain | Maturase MatK, N-terminal domain | Maturase_MatK_N | 1 |
IPR024943 | 24,943 | Enhancer of polycomb protein | Enhancer_polycomb | Family | 8,784 | false | false | The enhancer of polycomb gene of Drosophila encodes a chromatin protein conserved in yeast and mammals [ ]. The homologous yeast protein, known as enhancer of polycomb-like protein 1 (Epl1), is a subunit of the NuA4 histone acetyltransferase (HAT) complex, which is involved in transcriptional activation of selected gen... | [
"GO:0006357",
"GO:0035267"
] | [
"regulation of transcription by RNA polymerase II",
"NuA4 histone acetyltransferase complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR14898"
] | [
""
] | [
8784
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-3214847",
"R-HSA-8953750",
"R-MMU-8953750"
] | [
"REACTOME:R-HSA-3214847",
"REACTOME:R-HSA-8953750",
"REACTOME:R-MMU-8953750"
] | 3 | [
"5j9q",
"5j9t",
"5j9u",
"5j9w",
"7vvu",
"7vvy",
"7vvz",
"7yfn",
"7yfp",
"7zvw",
"8esc",
"8qr1",
"8xvg",
"8xvt",
"9c57",
"9c62",
"9c6n",
"9cac"
] | 18 | [
"PUB00012820",
"PUB00035439",
"PUB00056868"
] | [
"9735366",
"14966270",
"12782659"
] | [
"The enhancer of polycomb gene of Drosophila encodes a chromatin protein conserved in yeast and mammals.",
"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans.",
"Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin."
] | [
1998,
2004,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Candidatus Anaerobiospirillum pullicola",
"Eukaryota"
] | [
1,
8783
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
24,
1,
8,
5,
12,
8,
1,
11,
11,
1,
1,
77
] | 12 | true | Family | Enhancer of polycomb protein | Enhancer of polycomb protein | Enhancer_polycomb | 7 |
IPR024945 | 24,945 | Spt5 C-terminal domain | Spt5_C_dom | Domain | 3,526 | false | false | The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD dom... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"SMART"
] | [
"SM01104"
] | [
"CTD"
] | [
3526
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-72086",
"R-CEL-75955",
"R-CEL-77075",
"R-DME-112382",
"R-DME-113418",
"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-45... | [
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-72086",
"REACTOME:R-CEL-75955",
"REACTOME:R-CEL-77075",
"REACTOME:R-DME-112382",
"REACTOME:R-DME-113418",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-15923... | 68 | [
"5mqf",
"5oik",
"5xjc",
"5yzg",
"5z56",
"5z57",
"6ff4",
"6ff7",
"6gmh",
"6gml",
"6icz",
"6ted",
"6zym",
"7a5p",
"7dvq",
"7nkx",
"7nky",
"7okx",
"7oky",
"7ol0",
"7pks",
"7qtt",
"7unc",
"7und",
"7w59",
"7w5a",
"7w5b",
"7ycx",
"8a3y",
"8c6j",
"8ch6",
"8i0r"... | 74 | [
"PUB00053692"
] | [
"19460865"
] | [
"Characterization of the Schizosaccharomyces pombe Spt5-Spt4 complex."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
3525,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
5,
2,
9,
3,
1,
11,
1,
1
] | 9 | true | Domain | Spt5 C-terminal domain | Spt5 C-terminal domain | Spt5_C_dom | 4 |
IPR024949 | 24,949 | Bet v I type allergen | Bet_v_I_allergen | Family | 7,758 | false | false | This family consists of a number of plant proteins that are structurally related [ , , ] and seem to be involved in pathogen defence response. These proteins include: Bet v I, the major pollen allergen from white birch. Bet v I is the main cause of type I allergic reactions observed in early spring. Aln g I, the major ... | [
"GO:0004864",
"GO:0010427",
"GO:0038023",
"GO:0009738"
] | [
"protein phosphatase inhibitor activity",
"abscisic acid binding",
"signaling receptor activity",
"abscisic acid-activated signaling pathway"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PRINTS",
"PROSITE"
] | [
"PR00634",
"PS00451"
] | [
"BETALLERGEN",
"PATHOGENESIS_BETVI"
] | [
7722,
2937
] | 2 | [] | [] | [] | 0 | [
"1b6f",
"1btv",
"1bv1",
"1e09",
"1fm4",
"1fsk",
"1h2o",
"1icx",
"1ifv",
"1llt",
"1qmr",
"1tw0",
"1txc",
"1xdf",
"2bk0",
"2flh",
"2k7h",
"2lpx",
"2qim",
"2wql",
"3c0v",
"3e85",
"3ie5",
"4a80",
"4a81",
"4a83",
"4a84",
"4a85",
"4a86",
"4a87",
"4a88",
"4a8g"... | 101 | [
"PUB00001168",
"PUB00004549",
"PUB00004554"
] | [
"2571499",
"1371403",
"1627770"
] | [
"The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene.",
"Characterization of a stress-induced, developmentally regulated gene family from soybean.",
"Characterisation of a wound-induced transcript from the monocot asparagus that shares simila... | [
1989,
1992,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
6,
7752
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
9,
15
] | 3 | true | Family | Bet v I type allergen | Bet v I type allergen | Bet_v_I_allergen | 7 |
IPR024951 | 24,951 | Sulphate adenylyltransferase catalytic domain | Sulfurylase_cat_dom | Domain | 13,057 | false | false | This domain is the catalytic domain of ATP-sulfurylase or sulphate adenylyltransferase ( ). ATP-sulfurylase catalyses the synthesis of adenosine-phosphosulphate (APS) from ATP and inorganic sulphate [ ]. Sometimes is found as part of a bifunctional polypeptide chain associated with adenylylsulphate kinase ( ). Both enz... | [
"GO:0004781"
] | [
"sulfate adenylyltransferase (ATP) activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01747"
] | [
"ATP-sulfurylase"
] | [
13057
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.4",
"GenProp1392",
"PWY-5278",
"PWY-5340",
"PWY-6683",
"PWY-6932",
"R-CEL-174362",
"R-HSA-174362",
"R-HSA-2408550",
"R-HSA-3560796",
"R-HSA-6802952",
"R-MMU-174362"
] | [
"EC:2.7.7.4",
"GP:GenProp1392",
"METACYC:PWY-5278",
"METACYC:PWY-5340",
"METACYC:PWY-6683",
"METACYC:PWY-6932",
"REACTOME:R-CEL-174362",
"REACTOME:R-HSA-174362",
"REACTOME:R-HSA-2408550",
"REACTOME:R-HSA-3560796",
"REACTOME:R-HSA-6802952",
"REACTOME:R-MMU-174362"
] | 12 | [
"1g8f",
"1g8g",
"1g8h",
"1i2d",
"1j70",
"1jec",
"1jed",
"1jee",
"1jhd",
"1m8p",
"1r6x",
"1v47",
"1x6v",
"1xjq",
"1xnj",
"2gks",
"2qjf",
"3cr8",
"4dnx",
"4maf",
"7fh3",
"7fha",
"8a8d",
"8a8g"
] | 24 | [
"PUB00001859",
"PUB00004924"
] | [
"8522184",
"9671738"
] | [
"A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities.",
"A member of a family of sulfate-activating enzymes causes murine brachymorphism."
] | [
1995,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
234,
4609,
7993,
10,
211
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
12,
1,
5,
5,
7,
7,
1,
7,
9,
1,
1,
22
] | 12 | true | Domain | Sulphate adenylyltransferase catalytic domain | Sulphate adenylyltransferase catalytic domain | Sulfurylase_cat_dom | 3 |
IPR024952 | 24,952 | Lipoprotein LPP20-like domain | LPP20-like_dom | Domain | 1,482 | false | false | This entry represents a domain covering almost the full length of LPP20, which belongs to the non-essential class of lipoproteins [ ]. It is also found in close homologues, and associated to other domains in a related group of sequences that have not yet been experimentally characterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02169"
] | [
"LPP20"
] | [
1482
] | 1 | [] | [] | [] | 0 | [
"4kzs",
"5ok8"
] | 2 | [
"PUB00002256"
] | [
"7928954"
] | [
"Molecular characterization of a conserved 20-kilodalton membrane-associated lipoprotein antigen of Helicobacter pylori."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Protostomia",
"ecological metagenomes"
] | [
1405,
4,
73
] | 3 | [] | [] | 0 | true | Domain | Lipoprotein LPP20-like domain | Lipoprotein LPP20-like domain | LPP20-like_dom | 9 |
IPR024953 | 24,953 | Polyphosphate kinase middle domain | PP_kinase_middle | Domain | 22,620 | false | false | Polyphosphate kinase (Ppk) catalyses the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate molecules [ ]. This entry represents the Ppk middle domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02503"
] | [
"PP_kinase"
] | [
22620
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"2.7.4.1",
"GenProp0840",
"PWY-8138"
] | [
"EC:2.7.4.1",
"GP:GenProp0840",
"METACYC:PWY-8138"
] | 3 | [
"1xdo",
"1xdp",
"2o8r"
] | 3 | [
"PUB00020166"
] | [
"9501429"
] | [
"Transcription of ppk from Acinetobacter sp. strain ADP1, encoding a putative polyphosphate kinase, is induced by phosphate starvation."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
21887,
84,
345,
304
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Polyphosphate kinase middle domain | Polyphosphate kinase middle domain | PP_kinase_middle | 3 |
IPR024954 | 24,954 | SSRP1, dimerization domain | SSRP1_DD | Domain | 5,185 | false | false | This is the dimerization domain found in structure-specific recognition protein SSRP1 (POB3 in yeast) and related proteins, which are components of the FACT complex - a general chromatin factor that acts to reorganise nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03531"
] | [
"SSrecog"
] | [
5185
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-112382",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-6804756",
"R-CEL-75955",
"R-DDI-674695",
"R-DDI-6796648",
"R-DDI-6804756",
"R-DME-112382",
"R-DME-674695",
"R-DME-6796648",
"R-DME-6804756",
"R-DME-75955",
"R-HSA-112382",
"R-HSA-167152",
"R-HSA-167200",
"R-HSA-167238",
"R-HSA... | [
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6804756",
"REACTOME:R-CEL-75955",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6796648",
"REACTOME:R-DDI-6804756",
"REACTOME:R-DME-112382",
"REACTOME:R-DME-674695",
"REACTOME:R-DME-6796648",
"REACTOME:R-DME... | 41 | [
"3f5r",
"4khb",
"6upk",
"6upl",
"7nky",
"7xsx",
"7xt7",
"7xtd",
"7xti",
"8xgc",
"9eh2",
"9s3g"
] | 12 | [
"PUB00033374",
"PUB00088205",
"PUB00088206",
"PUB00088207",
"PUB00101032",
"PUB00101047"
] | [
"12934006",
"14585989",
"10924459",
"9489704",
"31775157",
"26966247"
] | [
"FACT facilitates transcription-dependent nucleosome alteration.",
"The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo.",
"POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae.",
"FACT, a f... | [
2003,
2003,
2000,
1998,
2020,
2016
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5185
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
2,
2,
22,
4,
3,
1,
2,
4,
1,
1,
9
] | 12 | true | Domain | SSRP1, dimerization domain | SSRP1, dimerization domain | SSRP1_DD | 4 |
IPR024956 | 24,956 | tRNAHis guanylyltransferase catalytic domain | tRNAHis_GuaTrfase_cat | Domain | 5,681 | false | false | The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His [ ]. The catalytic domain of Thg1 contains a RRM (ferredoxin) fold palm domain, just like the viral RNA-dependent RNA polymerases, reverse transcriptases, family A and B DNA polymerases, adenylyl cyclases, d... | [
"GO:0000287",
"GO:0008193",
"GO:0006400"
] | [
"magnesium ion binding",
"tRNA guanylyltransferase activity",
"tRNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF04446"
] | [
"Thg1"
] | [
5681
] | 1 | [
"EC",
"REACTOME"
] | [
"2.7.7.79",
"R-HSA-6782315"
] | [
"EC:2.7.7.79",
"REACTOME:R-HSA-6782315"
] | 2 | [
"3otb",
"3otc",
"3otd",
"3ote",
"3wbz",
"3wc0",
"3wc1",
"3wc2",
"4kgk",
"4kgm",
"5axk",
"5axl",
"5axm",
"5axn",
"5xox",
"7cv1"
] | 16 | [
"PUB00020433",
"PUB00057251",
"PUB00057252"
] | [
"14633974",
"20591188",
"21059936"
] | [
"tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis.",
"Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.",
"tRNA(His) guanylyltransferase (THG1), a u... | [
2003,
2010,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
207,
577,
4775,
95,
27
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
33,
2,
1,
3,
4,
1,
4,
6,
1,
1,
9
] | 11 | true | Domain | tRNAHis guanylyltransferase catalytic domain | tRNAHis guanylyltransferase catalytic domain | tRNAHis_GuaTrfase_cat | 6 |
IPR024957 | 24,957 | Cep57 centrosome microtubule-binding domain | Cep57_MT-bd_dom | Domain | 3,456 | false | false | This C-terminal domain of Cep57 binds, nucleates and bundles microtubules. The N-terminal part of the protein is the centrosome localisation domain [ ]. | [
"GO:0008017"
] | [
"microtubule binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF06657"
] | [
"Cep57_MT_bd"
] | [
3456
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2565942",
"R-HSA-380259",
"R-HSA-380270",
"R-HSA-380284",
"R-HSA-380320",
"R-HSA-5620912",
"R-HSA-8854518",
"R-MMU-2565942",
"R-MMU-380259",
"R-MMU-380270",
"R-MMU-380284",
"R-MMU-380320",
"R-MMU-5620912",
"R-MMU-8854518",
"R-RNO-2565942",
"R-RNO-380259",
"R-RNO-380270",
"R-... | [
"REACTOME:R-HSA-2565942",
"REACTOME:R-HSA-380259",
"REACTOME:R-HSA-380270",
"REACTOME:R-HSA-380284",
"REACTOME:R-HSA-380320",
"REACTOME:R-HSA-5620912",
"REACTOME:R-HSA-8854518",
"REACTOME:R-MMU-2565942",
"REACTOME:R-MMU-380259",
"REACTOME:R-MMU-380270",
"REACTOME:R-MMU-380284",
"REACTOME:R-MMU... | 21 | [
"4l0r",
"8ibh"
] | 2 | [
"PUB00057253"
] | [
"18294141"
] | [
"Cep57, a multidomain protein with unique microtubule and centrosomal localization domains."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3456
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
7,
10,
10,
1,
14,
1
] | 6 | true | Domain | Cep57 centrosome microtubule-binding domain | Cep57 centrosome microtubule-binding domain | Cep57_MT-bd_dom | 2 |
IPR024958 | 24,958 | GRASP-type PDZ domain | GRASP_PDZ | Domain | 5,648 | false | false | The Golgi apparatus is a highly dynamic organelle responsible for sorting out proteins and other biomolecules to the cell surface and to the extracellular milieu. The Golgi apparatus is comprised of flattened membrane-bound compartments called cisternae, which are apposed to one another to form a Golgi stack. The struc... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF04495",
"PS51865"
] | [
"GRASP55_65",
"PDZ_GRASP"
] | [
5639,
5372
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162658",
"R-HSA-204005",
"R-HSA-6807878",
"R-MMU-162658",
"R-MMU-204005",
"R-MMU-6807878",
"R-RNO-162658",
"R-RNO-204005",
"R-RNO-6807878",
"R-SCE-162658",
"R-SCE-204005",
"R-SPO-162658",
"R-SPO-204005"
] | [
"REACTOME:R-HSA-162658",
"REACTOME:R-HSA-204005",
"REACTOME:R-HSA-6807878",
"REACTOME:R-MMU-162658",
"REACTOME:R-MMU-204005",
"REACTOME:R-MMU-6807878",
"REACTOME:R-RNO-162658",
"REACTOME:R-RNO-204005",
"REACTOME:R-RNO-6807878",
"REACTOME:R-SCE-162658",
"REACTOME:R-SCE-204005",
"REACTOME:R-SPO-... | 13 | [
"3rle",
"4edj",
"4kfv",
"4kfw",
"4rey",
"5gmi",
"5gmj",
"5gml",
"5h3j",
"6g8t",
"6g8w",
"6g8y"
] | 12 | [
"PUB00094770",
"PUB00094772",
"PUB00094773",
"PUB00094774"
] | [
"21235525",
"27436376",
"21515684",
"23940043"
] | [
"The multiple facets of the Golgi reassembly stacking proteins.",
"New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.",
"Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis.",
"Structural insight into Golg... | [
2011,
2016,
2011,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Spirosoma"
] | [
5635,
13
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
7,
1,
26,
10,
1,
11,
1,
1
] | 9 | true | Domain | GRASP-type PDZ domain | GRASP-type PDZ domain | GRASP_PDZ | 6 |
IPR024960 | 24,960 | Phosphatidyl-N-methylethanolamine/Phosphatidylethanolamine N-methyltransferase | PEMT/MFAP | Family | 3,773 | false | false | This family includes yeast phosphatidyl-N-methylethanolamine N-methyltransferase CHO1/OPI3 [ ] and vertebrates phosphatidylethanolamine N-methyltransferases [ , ]. In yeast, this enzyme catalyzes the second two steps of the methylation pathway of phosphatidylcholine (PC) biosynthesis, the SAM-dependent methylation of p... | [
"GO:0008757",
"GO:0006656"
] | [
"S-adenosylmethionine-dependent methyltransferase activity",
"phosphatidylcholine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PROFILE",
"PANTHER"
] | [
"MF_03216",
"PIRSF005444",
"PS51599",
"PTHR15458"
] | [
"PLMT",
"PEMT",
"SAM_PEMT_PEM2",
""
] | [
3221,
2233,
2939,
3740
] | 4 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.17",
"2.1.1.71",
"PWY-6825",
"R-BTA-1483191",
"R-DDI-1483191",
"R-HSA-1483191",
"R-MMU-1483191",
"R-RNO-1483191",
"R-SCE-1483191",
"R-SPO-1483191"
] | [
"EC:2.1.1.17",
"EC:2.1.1.71",
"METACYC:PWY-6825",
"REACTOME:R-BTA-1483191",
"REACTOME:R-DDI-1483191",
"REACTOME:R-HSA-1483191",
"REACTOME:R-MMU-1483191",
"REACTOME:R-RNO-1483191",
"REACTOME:R-SCE-1483191",
"REACTOME:R-SPO-1483191"
] | 10 | [] | 0 | [
"PUB00009897",
"PUB00057255",
"PUB00087310"
] | [
"2445736",
"11420179",
"9755189"
] | [
"Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes.",
"Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene.",
"The Schizosaccharomyces pombe cho1+ gene encodes a phos... | [
1987,
2001,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
22,
3750,
1
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (st... | [
4,
7,
3,
3,
1,
3,
9,
1,
1,
2
] | 10 | true | Family | Phosphatidyl-N-methylethanolamine/Phosphatidylethanolamine N-methyltransferase | Phosphatidyl-N-methylethanolamine/Phosphatidylethanolamine N-methyltransferase | PEMT/MFAP | 1 |
IPR024961 | 24,961 | Type II secretion system protein GspC, N-terminal | T2SS_GspC_N | Domain | 4,715 | false | false | This is the N-terminal region of GspC proteins, which is part of the Type II secretion system. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interac... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11356"
] | [
"T2SSC"
] | [
4715
] | 1 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"2lnv",
"3oss",
"6hcg",
"7oio"
] | 4 | [
"PUB00051842",
"PUB00065447",
"PUB00093998",
"PUB00094002",
"PUB00094004"
] | [
"19217396",
"21931548",
"30767847",
"28258547",
"22523076"
] | [
"Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.",
"Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.",
"Architecture, Function, and Substrates of the Type II Secretion System.",
"1H, 1... | [
2009,
2011,
2019,
2017,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4624,
8,
83
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Type II secretion system protein GspC, N-terminal | Type II secretion system protein GspC, N-terminal | T2SS_GspC_N | 3 |
IPR024962 | 24,962 | YukD-like | YukD-like | Family | 6,942 | false | false | YukD adopts a ubiquitin-like fold [ ]. Usually, ubiquitin covalently binds to protein and flags them for protein degradation; however conjugation assays have indicated that the classical YukD lacks the capacity for covalent bond formation with other proteins [ ]. In firmicutes (Gram-positive bacteria), the YukD-like pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08817"
] | [
"YukD"
] | [
6942
] | 1 | [
"GP"
] | [
"GenProp0905"
] | [
"GP:GenProp0905"
] | 1 | [
"2bps",
"4kv2",
"4kv3",
"6lar",
"6sgw",
"6sgx",
"6sgz",
"6umm",
"7b7j",
"7b9f",
"7b9s",
"7np7",
"7npr",
"7npt",
"7npu",
"7npv"
] | 16 | [
"PUB00034476",
"PUB00035494",
"PUB00055111",
"PUB00057262"
] | [
"16859499",
"15978580",
"18554323",
"21547297"
] | [
"The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.",
"Crystal structure of the ubiquitin-like protein YukD from Bacillus subtilis.",
"EsaC substrate for the ESAT-6 secretion pathway and its role in persistent infections of Staphylococcus ... | [
2006,
2005,
2008,
2011
] | 4 | [] | [
"IPR006707",
"IPR014921"
] | 0 | 2 | 0 | [
"Bacteria",
"metagenomes"
] | [
6930,
12
] | 2 | [] | [] | 0 | true | Family | YukD-like | YukD-like | YukD-like | 3 |
IPR024964 | 24,964 | CTLH/CRA C-terminal to LisH motif domain | CTLH/CRA | Domain | 22,468 | false | false | RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. The RanBPM protein contains multiple conserved domains that provide potential protein-protein interaction sites [ ]. This entry represents a domain at the C terminus of RanBPM containing th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF10607"
] | [
"CTLH"
] | [
22468
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9861718",
"R-DDI-9861718",
"R-DME-9861718",
"R-DRE-5673001",
"R-DRE-8851805",
"R-DRE-9861718",
"R-GGA-9861718",
"R-HSA-373760",
"R-HSA-5673001",
"R-HSA-8851805",
"R-HSA-9861718",
"R-MMU-373760",
"R-MMU-5673001",
"R-MMU-8851805",
"R-MMU-9861718",
"R-RNO-9861718",
"R-SCE-9861718... | [
"REACTOME:R-BTA-9861718",
"REACTOME:R-DDI-9861718",
"REACTOME:R-DME-9861718",
"REACTOME:R-DRE-5673001",
"REACTOME:R-DRE-8851805",
"REACTOME:R-DRE-9861718",
"REACTOME:R-GGA-9861718",
"REACTOME:R-HSA-373760",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-8851805",
"REACTOME:R-HSA-9861718",
"REACTOME... | 22 | [
"6swy",
"7ns3",
"7ns4",
"7nsb",
"7nsc",
"7wug",
"8pjn",
"8pmq"
] | 8 | [
"PUB00007968",
"PUB00044453",
"PUB00057270"
] | [
"11734546",
"15381419",
"22094242"
] | [
"A new sequence motif linking lissencephaly, Treacher Collins and oral-facial-digital type 1 syndromes, microtubule dynamics and cell migration.",
"The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre.",
"Diverse roles of... | [
2001,
2004,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
22468
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
61,
3,
14,
10,
21,
13,
4,
18,
17,
4,
4,
52
] | 12 | true | Domain | CTLH/CRA C-terminal to LisH motif domain | CTLH/CRA C-terminal to LisH motif domain | CTLH/CRA | 4 |
IPR024965 | 24,965 | Putative integrase | Putative_integrase | Family | 472 | false | false | This entry represents a family of putative integrases found in association with IS elements. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13009"
] | [
"Integrase_2"
] | [
472
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Monodon slow growth-associated virus",
"marine sediment metagenome"
] | [
466,
2,
1,
3
] | 4 | [] | [] | 0 | true | Family | Putative integrase | Putative integrase | Putative_integrase | 1 |
IPR024966 | 24,966 | Primase helical domain | Primase_helical_domain | Domain | 20 | false | false | This α helical domain is found in a set of archaeal plasmid replication proteins [ ]. The domain is found to the C terminus of the primase/polymerase domain and is necessary for primase activity. Mutations in this domain can result in defective template binding, dinucleotide formation and conformation change prior to D... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13010"
] | [
"pRN1_helical"
] | [
20
] | 1 | [] | [] | [] | 0 | [
"3m1m",
"6gt7",
"6gvq",
"6gvt",
"6gvu"
] | 5 | [
"PUB00057275"
] | [
"20511586"
] | [
"The archaeo-eukaryotic primase of plasmid pRN1 requires a helix bundle domain for faithful primer synthesis."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoproteati"
] | [
20
] | 1 | [] | [] | 0 | true | Domain | Primase helical domain | Primase helical domain | Primase_helical_domain | 2 |
IPR024967 | 24,967 | DNA-binding domain, IS481-type | DNA-bd_IS481-type | Domain | 1,916 | false | false | This entry represents a DNA-binding domain found in a number of putative transposases. This domain can be found in the upstream region of the conjoined ORF AB of insertion element 481 from Bordetella pertusis [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13011"
] | [
"LZ_Tnp_IS481"
] | [
1916
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00069777"
] | [
"17065269"
] | [
"Prevalence and sequence variants of IS481 in Bordetella bronchiseptica: implications for IS481-based detection of Bordetella pertussis."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1905,
7,
4
] | 3 | [] | [] | 0 | true | Domain | DNA-binding domain, IS481-type | DNA-binding domain, IS481-type | DNA-bd_IS481-type | 4 |
IPR024968 | 24,968 | S-layer protein, C-terminal domain, lactobacillus | SlpA_C_lactobacillus | Domain | 2,692 | false | false | This short domain is found at the C-terminal end of Lactobacillus S-layer proteins [ ] and in a variety of bacterial cell surface proteins. The domain is about 60 residues in length (although previously defined as 2 copies of this domain). It usually occurs in tandem pairs. It may be distantly related to the SH3 domain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03217"
] | [
"SlpA"
] | [
2692
] | 1 | [] | [] | [] | 0 | [
"7qeh",
"7qfg",
"8alu",
"8aol"
] | 4 | [
"PUB00020346",
"PUB00154867"
] | [
"8522531",
"38838019"
] | [
"Identification, cloning, and nucleotide sequence of a silent S-layer protein gene of Lactobacillus acidophilus ATCC 4356 which has extensive similarity with the S-layer protein gene of this species.",
"The molecular architecture of <i>Lactobacillus</i> S-layer: Assembly and attachment to teichoic acids."
] | [
1995,
2024
] | 2 | [] | [] | 0 | 0 | null | [
"Anaeramoeba ignava",
"Bacillota"
] | [
2,
2690
] | 2 | [] | [] | 0 | true | Domain | S-layer protein, C-terminal domain, lactobacillus | S-layer protein, C-terminal domain, lactobacillus | SlpA_C_lactobacillus | 1 |
IPR024970 | 24,970 | Maelstrom domain | Maelstrom | Domain | 1,522 | false | false | Maelstrom is a germ-plasm component protein that is involved in the piRNA pathway, though its precise function is not known. This protein contains a novel domain, known as the Maelstrom domain, which adopts the RNaseH fold. Maelstrom is essential for Piwi-mediated silencing and acts downstream of or in parallel to H3K9... | [
"GO:0060964"
] | [
"regulation of miRNA-mediated gene silencing"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF13017"
] | [
"Maelstrom"
] | [
1522
] | 1 | [
"REACTOME"
] | [
"R-HSA-5601884"
] | [
"REACTOME:R-HSA-5601884"
] | 1 | [
"4ybg",
"5af0",
"9nhc",
"9nhd",
"9nhe",
"9nhs"
] | 6 | [
"PUB00085036"
] | [
"23159368"
] | [
"Transcriptional silencing of transposons by Piwi and maelstrom and its impact on chromatin state and gene expression."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1522
] | 1 | [
"Caenorhabditis elegans",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
11,
4,
2,
4
] | 5 | true | Domain | Maelstrom domain | Maelstrom domain | Maelstrom | 1 |
IPR024972 | 24,972 | HNS-dependent expression A | HdeA | Family | 208 | false | false | HNS (histone-like nucleoid structuring)-dependent expression A (HdeA) protein is a stress response protein found in highly acid resistant bacteria such as Shigella flexneri and Escherichia coli, but which is lacking in mildly acid tolerant bacteria such as Salmonella [ ]. HdeA is one of the most abundant proteins found... | [
"GO:0071468",
"GO:0030288"
] | [
"cellular response to acidic pH",
"outer membrane-bounded periplasmic space"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PIRSF"
] | [
"MF_00946",
"PIRSF009564"
] | [
"HdeA",
"HNS-dep_expression_A"
] | [
208,
104
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013251",
"PUB00013252"
] | [
"10623550",
"12694615"
] | [
"HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria.",
"Regulatory network of acid resistance genes in Escherichia coli."
] | [
2000,
2003
] | 2 | [
"IPR010486"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota",
"Trichuris trichiura"
] | [
207,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | HNS-dependent expression A | HNS-dependent expression A | HdeA | 4 |
IPR024973 | 24,973 | ESPR domain | ESPR | Domain | 11,508 | false | false | This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). ESPR sev... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13018"
] | [
"ESPR"
] | [
11508
] | 1 | [
"GP",
"REACTOME",
"REACTOME"
] | [
"GenProp1074",
"R-HSA-9760173",
"R-HSA-9927020"
] | [
"GP:GenProp1074",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-9927020"
] | 3 | [
"8vba",
"8vbb"
] | 2 | [
"PUB00066788"
] | [
"22337167"
] | [
"From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified Caudoviricetes"
] | [
11482,
13,
11,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | ESPR domain | ESPR domain | ESPR | 5 |
IPR024974 | 24,974 | Sde2, ubiquitin domain | Sde2_N | Domain | 1,330 | false | false | Sde2 (silencing defective 2) is a ubiquitin-fold-containing splicing regulator that supports splicing of selected pre-mRNAs in an intron-specific manner in Schizosaccharomyces pombe. Sde2 is translated as inactive precursor proteins harbouring the ubiquitin-fold domain linked through an invariant GGKGG motif to a C-ter... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13019"
] | [
"Sde2_N_Ubi_yeast"
] | [
1330
] | 1 | [] | [] | [] | 0 | [
"9l5r",
"9l5t"
] | 2 | [
"PUB00091018",
"PUB00101934"
] | [
"28947618",
"27906959"
] | [
"Sde2 is an intron-specific pre-mRNA splicing regulator activated by ubiquitin-like processing.",
"PCNA-Dependent Cleavage and Degradation of SDE2 Regulates Response to Replication Stress."
] | [
2018,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Shewanella electrica"
] | [
1329,
1
] | 2 | [
"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"
] | [
1,
4,
1,
7
] | 4 | true | Domain | Sde2, ubiquitin domain | Sde2, ubiquitin domain | Sde2_N | 5 |
IPR024975 | 24,975 | Protein NO VEIN, C-terminal | NOV_C | Domain | 6,153 | false | false | This domain of unknown function is found at the C-terminal of Protein NO VEIN from Arabidopsis, a protein essential for cell fate determination during embryogenesis [ ]. It mediates this process through an auxin-dependent pathway [ ]. It is also found in some restriction endonucleases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13020"
] | [
"NOV_C"
] | [
6153
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00085159",
"PUB00097628"
] | [
"15266054",
"20729639"
] | [
"Identification of genes required for embryo development in Arabidopsis.",
"NO VEIN facilitates auxin-mediated development in Arabidopsis."
] | [
2004,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
162,
3942,
1975,
73,
1
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
15,
2,
5,
8
] | 4 | true | Domain | Protein NO VEIN, C-terminal | Protein NO VEIN, C-terminal | NOV_C | 2 |
IPR024976 | 24,976 | Domain of unknown function DUF3885 | DUF3885 | Domain | 1,567 | false | false | This short domain of unknown function is approximately 40 amino acids in length. There is a conserved YDDRG sequence motif and a single completely conserved aspartate residue that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13021"
] | [
"DUF3885"
] | [
1567
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1562,
2,
3
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3885 | Domain of unknown function DUF3885 | DUF3885 | 8 |
IPR024977 | 24,977 | Anaphase-promoting complex subunit 4-like, WD40 domain | Apc4-like_WD40_dom | Domain | 17,104 | false | false | This entry represents the N-terminal propeller-shaped WD40 domain of the anaphase-promoting complex subunit 4 (Apc4) and similar proteins. WD-40 repeats (also known as WD or beta-transducin repeats) are short ~40 amino acid motifs, often terminating in a Trp-Asp (W-D) dipeptide. WD40 repeats usually assume a 7-8 bladed... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12894"
] | [
"ANAPC4_WD40"
] | [
17104
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-983168",
"R-DDI-141430",
"R-DDI-174048",
"R-DDI-174084",
"R-DDI-174154",
"R-DDI-174178",
"R-DDI-174184",
"R-DDI-176407",
"R-DDI-176408",
"R-DDI-176409",
"R-DDI-176412",
"R-DDI-179409",
"R-DDI-2467813",
"R-DDI-2559582",
"R-DDI-3214841",
"R-DDI-69017",
"R-DDI-8951664",
"R-DDI-... | [
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-141430",
"REACTOME:R-DDI-174048",
"REACTOME:R-DDI-174084",
"REACTOME:R-DDI-174154",
"REACTOME:R-DDI-174178",
"REACTOME:R-DDI-174184",
"REACTOME:R-DDI-176407",
"REACTOME:R-DDI-176408",
"REACTOME:R-DDI-176409",
"REACTOME:R-DDI-176412",
"REACTOME:R-DDI-179... | 61 | [
"1r5m",
"3jb9",
"4ui9",
"5a31",
"5bpt",
"5bpw",
"5g04",
"5g05",
"5i2t",
"5khr",
"5khu",
"5l9t",
"5l9u",
"5lcw",
"5wlc",
"5wyj",
"5wyk",
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6nd4",
"6q6g",
"6q6h",
"6tlj",
"6tm5",
"6tnt",
"6zqa"... | 68 | [
"PUB00004188",
"PUB00005491",
"PUB00015237",
"PUB00094364",
"PUB00160279"
] | [
"8090199",
"10322433",
"11814058",
"30069656",
"23776530"
] | [
"The ancient regulatory-protein family of WD-repeat proteins.",
"The WD repeat: a common architecture for diverse functions.",
"WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases.",
"WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions.",
... | [
1994,
1999,
2001,
2018,
2013
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megamimivirinae",
"ecological metagenomes"
] | [
21,
1696,
15365,
9,
13
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
5,
13,
7,
12,
9,
2,
19,
5,
2,
4,
32
] | 12 | true | Domain | Anaphase-promoting complex subunit 4-like, WD40 domain | Anaphase-promoting complex subunit 4-like, WD40 domain | Apc4-like_WD40_dom | 3 |
IPR024978 | 24,978 | Homeodomain, phBC6A51-type | Homeodomain_phBC6A51-type | Domain | 498 | false | false | This domain, found in phage or prophage proteins, adopts a homeodomain fold with additional N and C-terminal helices and a C-terminal β-strand that forms an intersubunit β-barrel with a channel. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13022"
] | [
"HTH_Tnp_1_2"
] | [
498
] | 1 | [] | [] | [] | 0 | [
"2ao9"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanosarcinaceae",
"Viruses",
"metagenomes"
] | [
463,
2,
24,
9
] | 4 | [] | [] | 0 | true | Domain | Homeodomain, phBC6A51-type | Homeodomain, phBC6A51-type | Homeodomain_phBC6A51-type | 7 |
IPR024979 | 24,979 | Protein of unknown function DUF3884 | DUF3884 | Family | 305 | false | false | This family of proteins is functionally uncharacterised. Several of them are annotated as Tagatose 1,6-diphosphate aldolase, but there appears to be no direct evidence to support this. Proteins in this family are typically between 61 and 106 amino acids in length and have two completely conserved residues (Y and F) tha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13024"
] | [
"DUF3884"
] | [
305
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
305
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3884 | Protein of unknown function DUF3884 | DUF3884 | 3 |
IPR024980 | 24,980 | Protein of unknown function DUF3886 | DUF3886 | Family | 1,111 | false | false | This family of proteins is functionally uncharacterised. Proteins in this family are approximately 90 amino acids in length and contain two completely conserved L residues that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13025"
] | [
"DUF3886"
] | [
1111
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacilli",
"Phytophthora kernoviae 00238/432"
] | [
1110,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF3886 | Protein of unknown function DUF3886 | DUF3886 | 2 |
IPR024981 | 24,981 | Domain of unknown function DUF3887 | DUF3887 | Domain | 1,790 | false | false | This domain is found in bacteria and archaea, and is approximately 90 amino acids in length. This domain can be found in N-terminal of the EstD protein from Thermotoga maritima. EstD exhibits significant esterase activity with a preference for short acyl chain esters (C4-C8) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13026"
] | [
"DUF3887"
] | [
1790
] | 1 | [] | [] | [] | 0 | [
"2mc8",
"4hyz"
] | 2 | [
"PUB00075373"
] | [
"17466017"
] | [
"Characterization and structural modeling of a new type of thermostable esterase from Thermotoga maritima."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
100,
1652,
7,
31
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3887 | Domain of unknown function DUF3887 | DUF3887 | 5 |
IPR024982 | 24,982 | Rax2-like, C-terminal domain | Rax2-like_C | Domain | 1,989 | false | false | Diploid yeast cells repeatedly polarise and bud from their poles, due probably to the presence of highly stable membrane markers, and Rax2 is one such marker. It is inherited immutably at the cell cortex for multiple generations, and has a half-life exceeding several generations. The persistent inheritance of cortical ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12768"
] | [
"Rax2"
] | [
1989
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00057283",
"PUB00057284",
"PUB00057285",
"PUB00151895"
] | [
"11110666",
"15356260",
"17085965",
"23608319"
] | [
"Multigenerational cortical inheritance of the Rax2 protein in orienting polarity and division in yeast.",
"Interactions among Rax1p, Rax2p, Bud8p, and Bud9p in marking cortical sites for bipolar bud-site selection in yeast.",
"Function of rax2p in the polarized growth of fission yeast.",
"Rax2 is important f... | [
2000,
2004,
2006,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
186,
1797,
6
] | 3 | [
"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 | Rax2-like, C-terminal domain | Rax2-like, C-terminal domain | Rax2-like_C | 9 |
IPR024984 | 24,984 | Protein of unknown function DUF3888 | DUF3888 | Family | 1,172 | false | false | This family of proteins is functionally uncharacterised | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13027"
] | [
"DUF3888"
] | [
1172
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Nitrosarchaeum koreense MY1",
"bioreactor metagenome"
] | [
1164,
1,
7
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF3888 | Protein of unknown function DUF3888 | DUF3888 | 5 |
IPR024986 | 24,986 | Sister chromatid cohesion C-terminal domain | Nipped-B_C | Domain | 5,634 | false | false | This domain lies towards the C terminus of nipped-B or sister chromatid cohesion proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12830"
] | [
"Nipped-B_C"
] | [
5634
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-2470946",
"R-DME-2470946",
"R-HSA-2470946",
"R-MMU-2470946",
"R-SPO-2470946"
] | [
"REACTOME:R-CEL-2470946",
"REACTOME:R-DME-2470946",
"REACTOME:R-HSA-2470946",
"REACTOME:R-MMU-2470946",
"REACTOME:R-SPO-2470946"
] | 5 | [
"5me3",
"5t8v",
"6wg3",
"6wge",
"6yuf",
"6zz6",
"7w1m"
] | 7 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine sediment metagenome"
] | [
5632,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
5,
4,
3,
2,
1,
4,
3,
1,
1,
43
] | 12 | true | Domain | Sister chromatid cohesion C-terminal domain | Sister chromatid cohesion C-terminal domain | Nipped-B_C | 8 |
IPR024987 | 24,987 | Protein of unknown function DUF3889 | DUF3889 | Family | 1,099 | false | false | This family of proteins is functionally uncharacterised. Proteins in this family are approximately 110 amino acids in length and contain two completely conserved residues (A and Y) that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13028"
] | [
"DUF3889"
] | [
1099
] | 1 | [] | [] | [] | 0 | [
"2lyx"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
1099
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3889 | Protein of unknown function DUF3889 | DUF3889 | 5 |
IPR024988 | 24,988 | Domain of unknown function DUF3890 | DUF3890 | Domain | 140 | false | false | This presumed domain, approximately 70 amino acids in length, is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13029"
] | [
"DUF3890"
] | [
140
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Borreliaceae"
] | [
140
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3890 | Domain of unknown function DUF3890 | DUF3890 | 1 |
IPR024989 | 24,989 | Major facilitator superfamily associated domain | MFS_assoc_dom | Domain | 17,866 | false | false | This domain is found in a number of major facilitator superfamily proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF12832"
] | [
"MFS_1_like"
] | [
17866
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctVsq1",
"metagenomes"
] | [
61,
9673,
8037,
1,
94
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
13,
1,
8,
4,
6
] | 7 | true | Domain | Major facilitator superfamily associated domain | Major facilitator superfamily associated domain | MFS_assoc_dom | 9 |
IPR024990 | 24,990 | Anaphase-promoting complex subunit 1 | APC1 | Family | 6,097 | false | false | APC1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The APC/C complex mediates ubiquitination and degradation of target prote... | [
"GO:0005680"
] | [
"anaphase-promoting complex"
] | [
"cellular_component"
] | 1 | [
"PANTHER"
] | [
"PTHR12827"
] | [
""
] | [
6097
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-983168",
"R-DDI-141430",
"R-DDI-174048",
"R-DDI-174084",
"R-DDI-174154",
"R-DDI-174178",
"R-DDI-174184",
"R-DDI-176407",
"R-DDI-176408",
"R-DDI-176409",
"R-DDI-176412",
"R-DDI-179409",
"R-DDI-2467813",
"R-DDI-2559582",
"R-DDI-69017",
"R-DDI-983168",
"R-HSA-141430",
"R-HSA-17... | [
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-141430",
"REACTOME:R-DDI-174048",
"REACTOME:R-DDI-174084",
"REACTOME:R-DDI-174154",
"REACTOME:R-DDI-174178",
"REACTOME:R-DDI-174184",
"REACTOME:R-DDI-176407",
"REACTOME:R-DDI-176408",
"REACTOME:R-DDI-176409",
"REACTOME:R-DDI-176412",
"REACTOME:R-DDI-179... | 52 | [
"4ui9",
"5a31",
"5g04",
"5g05",
"5khr",
"5khu",
"5l9t",
"5l9u",
"5lcw",
"5lgg",
"6q6g",
"6q6h",
"6tlj",
"6tm5",
"6tnt",
"8a3t",
"8a5y",
"8a61",
"8pkp",
"8tar",
"8tau",
"9gaw",
"9n9r",
"9n9s"
] | 24 | [
"PUB00055977",
"PUB00057287",
"PUB00057288",
"PUB00091489",
"PUB00098994"
] | [
"16896351",
"11179667",
"17942546",
"26083744",
"27601667"
] | [
"The anaphase promoting complex/cyclosome: a machine designed to destroy.",
"Characterisation of the human APC1, the largest subunit of the anaphase-promoting complex.",
"Accumulation of substrates of the anaphase-promoting complex (APC) during human cytomegalovirus infection is associated with the phosphorylat... | [
2006,
2001,
2008,
2015,
2016
] | 5 | [] | [] | 0 | 0 | null | [
"Candidatus Phytoplasma melaleucae",
"Eukaryota"
] | [
1,
6096
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
2,
4,
2,
5,
5,
1,
4,
4,
1,
1,
13
] | 12 | true | Family | Anaphase-promoting complex subunit 1 | Anaphase-promoting complex subunit 1 | APC1 | 8 |
IPR024991 | 24,991 | Anaphase-promoting complex subunit 11, RING-H2 finger | RING-H2_APC11 | Domain | 3,456 | false | false | Apc11 is one of the subunits of the anaphase-promoting complex or cyclosome (APC) [ ]. The APC subunits are cullin family proteins with ubiquitin ligase activity [ ]. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enz... | [
"GO:0008270",
"GO:0061630",
"GO:0097602",
"GO:0031145",
"GO:0005680"
] | [
"zinc ion binding",
"ubiquitin protein ligase activity",
"cullin family protein binding",
"anaphase-promoting complex-dependent catabolic process",
"anaphase-promoting complex"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM",
"CDD"
] | [
"PF12861",
"cd16456"
] | [
"zf-ANAPC11",
"RING-H2_APC11"
] | [
3450,
2913
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-141430",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-176407",
"R-BTA-176408",
"R-BTA-176409",
"R-BTA-176412",
"R-BTA-179409",
"R-BTA-2467813",
"R-BTA-2559582",
"R-BTA-68867",
"R-BTA-69017",
"R-BTA-983168",
"R-CEL-983168",
"R-DDI-141... | [
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-174184",
"REACTOME:R-BTA-176407",
"REACTOME:R-BTA-176408",
"REACTOME:R-BTA-176409",
"REACTOME:R-BTA-176412",
"REACTOME:R-BTA-179409",
"REACTOME:R-BTA-246... | 68 | [
"2mt5",
"4r2y",
"4ui9",
"5a31",
"5g04",
"5g05",
"5jg6",
"5khr",
"5khu",
"5l9t",
"5l9u",
"5lcw",
"6q6g",
"6q6h",
"6tlj",
"6tm5",
"6tnt",
"8a3t",
"8a5y",
"8a61",
"8pkp",
"8tar",
"8tau",
"9gaw",
"9n9r",
"9n9s"
] | 26 | [
"PUB00055977",
"PUB00057289",
"PUB00057290",
"PUB00094953"
] | [
"16896351",
"10230407",
"10888670",
"25306923"
] | [
"The anaphase promoting complex/cyclosome: a machine designed to destroy.",
"ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity.",
"The APC11 RING-H2 finger mediates E2-dependent ubiquitination.",
"Mechanism of polyubiquitination by human anaphase-pro... | [
2006,
1999,
2000,
2014
] | 4 | [
"IPR001841"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Meridianimarinicoccus aquatilis",
"Nucleocytoviricota",
"metagenomes"
] | [
3446,
1,
3,
6
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
13,
1,
2,
1,
4,
1,
1,
4,
2,
1,
1,
2
] | 12 | true | Domain | Anaphase-promoting complex subunit 11, RING-H2 finger | Anaphase-promoting complex subunit 11, RING-H2 finger | RING-H2_APC11 | 3 |
IPR024992 | 24,992 | Protein of unknown function DUF3891 | DUF3891 | Family | 1,441 | false | false | This family consists of proteins that have not yet been functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13030"
] | [
"DUF3891"
] | [
1441
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
1406,
4,
22,
9
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF3891 | Protein of unknown function DUF3891 | DUF3891 | 2 |
IPR024993 | 24,993 | Protein of unknown function DUF3894 | DUF3894 | Family | 128 | false | false | This family of bacterial proteins is functionally uncharacterised. They contain two conserved sequence motifs: FNIC and MALLNLT. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13033"
] | [
"DUF3894"
] | [
128
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
128
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3894 | Protein of unknown function DUF3894 | DUF3894 | 5 |
IPR024994 | 24,994 | Protein of unknown function DUF3896 | DUF3896 | Family | 189 | false | false | This family of bacterial proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13035"
] | [
"DUF3896"
] | [
189
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
189
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3896 | Protein of unknown function DUF3896 | DUF3896 | 6 |
IPR024995 | 24,995 | Protein of unknown function DUF3895 | DUF3895 | Family | 250 | false | false | This family of bacterial proteins is functionally uncharacterised. There are two completely conserved residues (Y and L) that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13034"
] | [
"DUF3895"
] | [
250
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
250
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3895 | Protein of unknown function DUF3895 | DUF3895 | 3 |
IPR024996 | 24,996 | pPIWI_RE, RNaseH domain | RNaseH_pPIWI_RE | Domain | 958 | false | false | This entry represents the RNaseH domain of the pPIWI_RE PIWI/Argonaute module. pPIWI_RE is found in a conserved three-gene island that also contains a DinG-type helicase and an REase nuclease. This three gene island is predicted to form a conflict system which targets R-loop formation of invasive plasmids during plasmi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13032"
] | [
"RNaseH_pPIWI_RE"
] | [
958
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091016"
] | [
"23758928"
] | [
"Two novel PIWI families: roles in inter-genomic conflicts in bacteria and Mediator-dependent modulation of transcription in eukaryotes."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
957,
1
] | 2 | [] | [] | 0 | true | Domain | pPIWI_RE, RNaseH domain | pPIWI_RE, RNaseH domain | RNaseH_pPIWI_RE | 2 |
IPR024997 | 24,997 | Protein of unknown function DUF3892 | DUF3892 | Family | 2,379 | false | false | DUF3892 is related to the truncated RNaseH fold-containing ribosome hibernation factors. Predicted to function as a possible conflict effector domain at the ribosome, based on comparable genome contextual associations with DUF2188, including repeated association with nucleotide-activated effector conflict systems [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13031"
] | [
"DUF3892"
] | [
2379
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00097693"
] | [
"32868406"
] | [
"Identification of Uncharacterized Components of Prokaryotic Immune Systems and Their Diverse Eukaryotic Reformulations."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"metagenomes"
] | [
45,
2302,
7,
25
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF3892 | Protein of unknown function DUF3892 | DUF3892 | 4 |
IPR024998 | 24,998 | Protein of unknown function DUF3906 | DUF3906 | Family | 428 | false | false | This family of bacterial proteins is functionally uncharacterised. Family members are approximately 70 amino acids in length. There is a conserved EKK sequence motif. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13046"
] | [
"DUF3906"
] | [
428
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
428
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3906 | Protein of unknown function DUF3906 | DUF3906 | 1 |
IPR024999 | 24,999 | Protein of unknown function DUF3905 | DUF3905 | Family | 562 | false | false | This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 110 amino acids in length. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13045"
] | [
"DUF3905"
] | [
562
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
562
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3905 | Protein of unknown function DUF3905 | DUF3905 | 3 |
IPR025000 | 25,000 | Protein of unknown function DUF3903 | DUF3903 | Family | 146 | false | false | This family is functionally uncharacterised. Proteins in this family are found in bacteria, and they are approximately 40 amino acids in length. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13043"
] | [
"DUF3903"
] | [
146
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
146
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3903 | Protein of unknown function DUF3903 | DUF3903 | 5 |
IPR025001 | 25,001 | Protein of unknown function DUF3902 | DUF3902 | Family | 271 | false | false | This family of proteins found in firmicutes is functionally uncharacterised. Proteins in this family are approximately 170 amino acids in length. There is a conserved LGI sequence motif. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13042"
] | [
"DUF3902"
] | [
271
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
271
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3902 | Protein of unknown function DUF3902 | DUF3902 | 4 |
IPR025002 | 25,002 | Domain of unknown function DUF3972 | DUF3972 | Domain | 323 | false | false | This entry represents a domain whose function is not currently known. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13118"
] | [
"DUF3972"
] | [
323
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
304,
11,
8
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3972 | Domain of unknown function DUF3972 | DUF3972 | 3 |
IPR025003 | 25,003 | Domain of unknown function DUF3973 | DUF3973 | Domain | 220 | false | false | This presumed domain, approximately 40 amino acids in length, is functionally uncharacterised. It contains a conserved YCI sequence motif. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13119"
] | [
"DUF3973"
] | [
220
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
220
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3973 | Domain of unknown function DUF3973 | DUF3973 | 2 |
IPR025004 | 25,004 | Transcriptional regulatory protein SenN/SenS | SenN/SenS | Family | 1,388 | false | false | This family of bacterial proteins includes the transcriptional regulatory proteins senN and senS, which regulate the expression of extracellular-protein genes of Bacillus subtilis [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13040"
] | [
"Fur_reg_FbpB"
] | [
1388
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00057383",
"PUB00057384"
] | [
"3269394",
"2108127"
] | [
"Cloning and nucleotide sequence of senN, a novel 'Bacillus natto' (B. subtilis) gene that regulates expression of extracellular protein genes.",
"Complex character of senS, a novel gene regulating expression of extracellular-protein genes of Bacillus subtilis."
] | [
1988,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
1388
] | 1 | [] | [] | 0 | true | Family | Transcriptional regulatory protein SenN/SenS | Transcriptional regulatory protein SenN/SenS | SenN/SenS | 7 |
IPR025005 | 25,005 | Domain of unknown function DUF3974 | DUF3974 | Domain | 172 | false | false | This presumed domain, approximately 130 amino acids in length, is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13120"
] | [
"DUF3974"
] | [
172
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
172
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3974 | Domain of unknown function DUF3974 | DUF3974 | 2 |
IPR025006 | 25,006 | Protein of unknown function DUF3900 | DUF3900 | Family | 701 | false | false | This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria. Proteins in this family are approximately 360 amino acids in length. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13039"
] | [
"DUF3900"
] | [
701
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Candidatus Methanogaster sp."
] | [
700,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF3900 | Protein of unknown function DUF3900 | DUF3900 | 3 |
IPR025007 | 25,007 | Domain of unknown function DUF3899 | DUF3899 | Domain | 1,436 | false | false | This domain is found in uncharacterised bacterial sequences, some described as possible tryptophanyl-tRNA synthetases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13038"
] | [
"DUF3899"
] | [
1436
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Panagrolaimus sp. ES5",
"Sepunavirus",
"bioreactor metagenome"
] | [
1428,
1,
3,
4
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3899 | Domain of unknown function DUF3899 | DUF3899 | 5 |
IPR025008 | 25,008 | Domain of unknown function DUF3976 | DUF3976 | Domain | 133 | false | false | This presumed domain, approximately 40 amino acids in length, is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13121"
] | [
"DUF3976"
] | [
133
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
133
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3976 | Domain of unknown function DUF3976 | DUF3976 | 6 |
IPR025009 | 25,009 | Protein of unknown function DUF3977 | DUF3977 | Family | 325 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13122"
] | [
"DUF3977"
] | [
325
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"viral metagenome"
] | [
324,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF3977 | Protein of unknown function DUF3977 | DUF3977 | 8 |
IPR025010 | 25,010 | Protein of unknown function DUF3978 | DUF3978 | Family | 152 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13123"
] | [
"DUF3978"
] | [
152
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
152
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3978 | Protein of unknown function DUF3978 | DUF3978 | 9 |
IPR025014 | 25,014 | Protein of unknown function DUF3958 | DUF3958 | Family | 495 | false | false | This family of proteins is functionally uncharacterised. Proteins in this family are approximately 120 amino acids in length and contain two conserved sequence motifs: RLF and TWH. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13125"
] | [
"DUF3958"
] | [
495
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Heterotrigona itama"
] | [
494,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF3958 | Protein of unknown function DUF3958 | DUF3958 | 7 |
IPR025015 | 25,015 | Protein of unknown function DUF3975 | DUF3975 | Family | 178 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13126"
] | [
"DUF3975"
] | [
178
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
178
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3975 | Protein of unknown function DUF3975 | DUF3975 | 1 |
IPR025016 | 25,016 | Domain of unknown function DUF3955 | DUF3955 | Domain | 1,948 | false | false | This entry represents a domain found in a family of bacterial and fungal proteins that are functionally uncharacterised. It contains two completely conserved residues (G and E) that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13127"
] | [
"DUF3955"
] | [
1948
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
885,
1050,
13
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Domain of unknown function DUF3955 | Domain of unknown function DUF3955 | DUF3955 | 7 |
IPR025018 | 25,018 | Protein of unknown function DUF3953 | DUF3953 | Family | 1,115 | false | false | This family of proteins has not yet been functionally characterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13129"
] | [
"DUF3953"
] | [
1115
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
1115
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3953 | Protein of unknown function DUF3953 | DUF3953 | 9 |
IPR025019 | 25,019 | Domain of unknown function DUF3952 | DUF3952 | Domain | 335 | false | false | This presumed domain is functionally uncharacterised, found in some species of Bacillus. It is approximately 110 amino acids in length and contains a conserved VMSAS sequence motif. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13130"
] | [
"DUF3952"
] | [
335
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
335
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3952 | Domain of unknown function DUF3952 | DUF3952 | 3 |
IPR025020 | 25,020 | Protein of unknown function DUF3908 | DUF3908 | Family | 211 | false | false | This family of proteins is functionally uncharacterised. There is a single completely conserved residue Y that may be functionally important. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13048"
] | [
"DUF3908"
] | [
211
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Svunavirus",
"bioreactor metagenome"
] | [
208,
2,
1
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF3908 | Protein of unknown function DUF3908 | DUF3908 | 7 |
IPR025021 | 25,021 | Protein of unknown function DUF3910 | DUF3910 | Family | 182 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13049"
] | [
"DUF3910"
] | [
182
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
182
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3910 | Protein of unknown function DUF3910 | DUF3910 | 4 |
IPR025022 | 25,022 | Protein of unknown function DUF3911 | DUF3911 | Family | 126 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13050"
] | [
"DUF3911"
] | [
126
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
126
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3911 | Protein of unknown function DUF3911 | DUF3911 | 9 |
IPR025023 | 25,023 | Protein of unknown function DUF3912 | DUF3912 | Family | 175 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13051"
] | [
"DUF3912"
] | [
175
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
175
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3912 | Protein of unknown function DUF3912 | DUF3912 | 2 |
IPR025024 | 25,024 | Protein of unknown function DUF3913 | DUF3913 | Family | 116 | false | false | This family of proteins is functionally uncharacterised. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF13052"
] | [
"DUF3913"
] | [
116
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
116
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF3913 | Protein of unknown function DUF3913 | DUF3913 | 2 |
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