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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR010861 | 10,861 | Protein of unknown function DUF1492 | DUF1492 | Family | 1,301 | false | false | This entry includes Streptococcus phage 7201, Orf19. The characteristics of the protein distribution suggest prophage matches in addition to the phage matches. This entry consists of several hypothetical, highly conserved Streptococcal and related phage proteins. The function of this family is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07374"
] | [
"DUF1492"
] | [
1301
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"Viruses",
"bioreactor metagenome"
] | [
1039,
4,
247,
11
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF1492 | Protein of unknown function DUF1492 | DUF1492 | 3 |
IPR010862 | 10,862 | Protein of unknown function DUF1493 | DUF1493 | Family | 3,233 | false | false | This family consists of several bacterial proteins of around 115 residues in length. Members of this family are largely found in Salmonella and Yersinia species and several have been described as being putative cytoplasmic proteins. The function of this family is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07377"
] | [
"DUF1493"
] | [
3233
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Erwinia phage EtG",
"ecological metagenomes"
] | [
3230,
1,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF1493 | Protein of unknown function DUF1493 | DUF1493 | 1 |
IPR010863 | 10,863 | Regulator EarA-like | EarA-like | Family | 124 | false | false | This entry represents Uncharacterized protein MJ0905, EarA from Methanococcus maripaludis (MMP1718, ) and similar sequences widely distributed in archaea except for extreme halophiles [ ]. EarA is a transcriptional activator that directly regulates the fla operon, which contains genes involved in archaella formation [ ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07381"
] | [
"EarA"
] | [
124
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00158985",
"PUB00158986",
"PUB00158987"
] | [
"27314758",
"28535845",
"28769898"
] | [
"Identification of the first transcriptional activator of an archaellum operon in a euryarchaeon.",
"Phylogenetic distribution of the euryarchaeal archaellum regulator EarA and complementation of a <i>Methanococcus maripaludis ∆earA</i> mutant with heterologous <i>earA</i> homologues.",
"Bypassing the Need for ... | [
2016,
2017,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"marine sediment metagenome"
] | [
109,
10,
5
] | 3 | [] | [] | 0 | true | Family | Regulator EarA-like | Regulator EarA-like | EarA-like | 1 |
IPR010864 | 10,864 | D-lyxose isomerase | D-lyxose_isomer | Family | 2,076 | false | false | Members of this family of sugar isomerases belong to the cupin superfamily [ ]. The enzyme from Cohnella laevoribosii has been shown to be specific for D-lyxose, L-ribose, and D-mannose [ ]. E. coli sugar isomerase (EcSI) has been structurally and functionally characterised and shows a preference for D-lyxose and D-man... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07385"
] | [
"Lyx_isomer"
] | [
2076
] | 1 | [
"EC"
] | [
"5.3.1.15"
] | [
"EC:5.3.1.15"
] | 1 | [
"2y0o",
"3kmh",
"3mpb"
] | 3 | [
"PUB00055252",
"PUB00075374",
"PUB00103833"
] | [
"20615418",
"17189362",
"34422783"
] | [
"Structure-based annotation of a novel sugar isomerase from the pathogenic E. coli O157:H7.",
"Characterization of a novel D-lyxose isomerase from Cohnella laevoribosii RI-39 sp. nov.",
"Biochemical and Structural Characterisation of a Novel D-Lyxose Isomerase From the Hyperthermophilic Archaeon <i>Thermofilum<... | [
2010,
2007,
2021
] | 3 | [] | [
"IPR047581"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
8,
2028,
10,
30
] | 4 | [] | [] | 0 | true | Family | D-lyxose isomerase | D-lyxose isomerase | D-lyxose_isomer | 5 |
IPR010865 | 10,865 | Protein of unknown function DUF1499 | DUF1499 | Family | 6,223 | false | false | This family consists of several hypothetical bacterial and plant proteins of around 125 residues in length. The function of this family is unknown. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07386",
"PIRSF026426"
] | [
"DUF1499",
"DUF1499"
] | [
6223,
1398
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9,
4816,
1325,
73
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
3,
2,
9
] | 4 | true | Family | Protein of unknown function DUF1499 | Protein of unknown function DUF1499 | DUF1499 | 2 |
IPR010866 | 10,866 | Alpha-2,8-polysialyltransferase | A-2_8-polyST | Family | 1,960 | false | false | This family contains the bacterial enzyme alpha-2,8-polysialyltransferase (approximately 500 residues long). This catalyses the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07388"
] | [
"A-2_8-polyST"
] | [
1960
] | 1 | [] | [] | [] | 0 | [
"5wc6",
"5wc8",
"5wcn",
"5wd7"
] | 4 | [
"PUB00013124"
] | [
"12578835"
] | [
"Functional relationships of the sialyltransferases involved in expression of the polysialic acid capsules of Escherichia coli K1 and K92 and Neisseria meningitidis groups B or C."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)",
"metagenomes"
] | [
1936,
15,
1,
8
] | 4 | [] | [] | 0 | true | Family | Alpha-2,8-polysialyltransferase | Alpha-2,8-polysialyltransferase | A-2_8-polyST | 5 |
IPR010867 | 10,867 | NPR nonapeptide | NPR_nonapeptide | Repeat | 45 | false | false | This is a nine residue repeat, which was called NPR after NonaPeptide Repeat. It is found in two malarial proteins and has the consensus EEhhEEhhP where h stands for a hydrophobic amino acid. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07391"
] | [
"NPR"
] | [
45
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Plasmodium (Laverania)"
] | [
45
] | 1 | [] | [] | 0 | true | Repeat | NPR nonapeptide | NPR nonapeptide | NPR_nonapeptide | 7 |
IPR010868 | 10,868 | Tumor suppressor ARF | Tumor_suppres_ARF | Family | 111 | false | false | ARF (also known as p14ARF in the human and p19ARF in the mouse) is an alternative transcript of the INK4a/ARF tumour-suppressor locus that encodes p16INK4a, an inhibitor of cyclin dependent kinases. ARFs are tumour suppressors participating in p53-dependent or independent pathways that restrain abnormal cell growth and... | [
"GO:0006915",
"GO:0008285",
"GO:0051726"
] | [
"apoptotic process",
"negative regulation of cell population proliferation",
"regulation of cell cycle"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF07392"
] | [
"P19Arf_N"
] | [
111
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-111471",
"R-HSA-2559580",
"R-HSA-2559585",
"R-HSA-3108214",
"R-HSA-3232118",
"R-HSA-6804757",
"R-HSA-69541",
"R-HSA-8941858",
"R-HSA-9645722",
"R-HSA-9646303",
"R-HSA-9646304",
"R-HSA-9759194"
] | [
"REACTOME:R-HSA-111471",
"REACTOME:R-HSA-2559580",
"REACTOME:R-HSA-2559585",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-3232118",
"REACTOME:R-HSA-6804757",
"REACTOME:R-HSA-69541",
"REACTOME:R-HSA-8941858",
"REACTOME:R-HSA-9645722",
"REACTOME:R-HSA-9646303",
"REACTOME:R-HSA-9646304",
"REACTOME:R... | 12 | [
"1hn3"
] | 1 | [
"PUB00013126",
"PUB00074539",
"PUB00074542",
"PUB00074545",
"PUB00074546"
] | [
"12660818",
"16600663",
"20082327",
"25723571",
"11331246"
] | [
"p14ARF induces G2 arrest and apoptosis independently of p53 leading to regression of tumours established in nude mice.",
"The ARF tumour suppressor.",
"p14ARF interacts with E2F factors to form p14ARF-E2F/partner-DNA complexes repressing E2F-dependent transcription.",
"MDM2-mediated degradation of p14ARF: a ... | [
2003,
2006,
2010,
2015,
2001
] | 5 | [] | [] | 0 | 0 | null | [
"Theria"
] | [
111
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
1,
3
] | 3 | true | Family | Tumor suppressor ARF | Tumor suppressor ARF | Tumor_suppres_ARF | 3 |
IPR010870 | 10,870 | Phosphate-selective porin O/P | Porin_O/P | Family | 9,157 | false | false | This entry represents the bacterial phosphate-selective porins O and P. These are anion-specific porins, the binding sites of which has a higher affinity for phosphate than chloride ions. Porin O has a higher affinity for polyphosphates, while porin P has a higher affinity for orthophosphate [ ]. In Pseudomonas aerugin... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07396"
] | [
"Porin_O_P"
] | [
9157
] | 1 | [] | [] | [] | 0 | [
"2o4v",
"4rjw",
"4rjx"
] | 3 | [
"PUB00013129",
"PUB00013130"
] | [
"1370289",
"1406271"
] | [
"Overexpression in Escherichia coli and functional analysis of a novel PPi-selective porin, oprO, from Pseudomonas aeruginosa.",
"Polyphosphate-selective porin OprO of Pseudomonas aeruginosa: expression, purification and sequence."
] | [
1992,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
8965,
3,
8,
181
] | 4 | [] | [] | 0 | true | Family | Phosphate-selective porin O/P | Phosphate-selective porin O/P | Porin_O/P | 8 |
IPR010872 | 10,872 | MDMPI C-terminal | MDMPI_C-term_domain | Domain | 8,067 | false | false | This domain is found at the C terminus of the mycothiol maleylpyruvate isomerase enzyme (MDMPI). The structure of this protein has been solved [ ]. This domain appears weakly similar to . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07398"
] | [
"MDMPI_C"
] | [
8067
] | 1 | [] | [] | [] | 0 | [
"2nsf",
"2nsg"
] | 2 | [
"PUB00042028"
] | [
"17428791"
] | [
"Crystal structures and site-directed mutagenesis of a mycothiol-dependent enzyme reveal a novel folding and molecular basis for mycothiol-mediated maleylpyruvate isomerization."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Aduncisulcus paluster",
"Bacteria",
"metagenomes"
] | [
1,
7997,
69
] | 3 | [] | [] | 0 | true | Domain | MDMPI C-terminal | MDMPI C-terminal | MDMPI_C-term_domain | 4 |
IPR010874 | 10,874 | Telomere-binding protein subunit beta | TEBB | Family | 25 | false | false | Telomeres are specialised protein-DNA complexes that compose the ends of eukaryotic chromosomes. Telomeres protect chromosome termini from degradation and recombination and act together with telomerase to ensure complete genome replication. TEBP beta forms a complex with TEBP alpha and this complex is able to recognise... | [
"GO:0042162",
"GO:0000781"
] | [
"telomeric DNA binding",
"chromosome, telomeric region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PIRSF"
] | [
"PF07404",
"PIRSF018412"
] | [
"TEBP_beta",
"TEBP_beta"
] | [
25,
7
] | 2 | [] | [] | [] | 0 | [
"1jb7",
"1otc",
"1pa6",
"1ph1",
"1ph2",
"1ph3",
"1ph4",
"1ph5",
"1ph6",
"1ph7",
"1ph8",
"1ph9",
"1phj",
"2i0q"
] | 14 | [
"PUB00013133"
] | [
"9875850"
] | [
"Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Spirotrichea"
] | [
25
] | 1 | [] | [] | 0 | true | Family | Telomere-binding protein subunit beta | Telomere-binding protein subunit beta | TEBB | 6 |
IPR010875 | 10,875 | Protein of unknown function DUF1506 | DUF1506 | Family | 139 | false | false | This entry represents proteins found primarily in Borrelia species. Their function is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07405"
] | [
"DUF1506"
] | [
139
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Borreliaceae",
"Theileria annulata"
] | [
137,
2
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF1506 | Protein of unknown function DUF1506 | DUF1506 | 7 |
IPR010876 | 10,876 | Lipid transport auxiliary protein 1 | LTAP1 | Family | 1,937 | false | false | This entry represents Lipid transport auxiliary protein 1 (LTAP1) found in eukaryotes. LTAP1 is required for the formation of endoplasmic reticulum-plasma membrane junctions and functions as an accessory protein for bridge-like lipid transfer protein BLTP1, participating in lipid delivery between endoplasmic reticulum ... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07406",
"PTHR21425"
] | [
"NICE-3",
""
] | [
1918,
1749
] | 2 | [] | [] | [] | 0 | [
"9cap"
] | 1 | [
"PUB00013134",
"PUB00101871",
"PUB00163246"
] | [
"11230159",
"31540829",
"40269155"
] | [
"Identification of human epidermal differentiation complex (EDC)-encoded genes by subtractive hybridization of entire YACs to a gridded keratinocyte cDNA library.",
"Systematic Identification of Host Cell Regulators of Legionella pneumophila Pathogenesis Using a Genome-wide CRISPR Screen.",
"Structural basis of... | [
2001,
2019,
2025
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1937
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
2,
7,
5,
5
] | 6 | true | Family | Lipid transport auxiliary protein 1 | Lipid transport auxiliary protein 1 | LTAP1 | 3 |
IPR010877 | 10,877 | Bacteriophage Mu, Baseplate protein gp46 | Phage_Mu_Gp46 | Family | 2,125 | false | false | This entry represents Baseplate protein gp46 from Bacteriophage Mu (also known as Gene product V or GpV), a probable connector between the central and peripheral parts of the baseplate that may be involved in tail assembly [ ]. This protein family also includes proteins from bacterial prophages, such as Mu-like prophag... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07409"
] | [
"GP46"
] | [
2125
] | 1 | [
"GP"
] | [
"GenProp0208"
] | [
"GP:GenProp0208"
] | 1 | [
"8fqc",
"9ki1"
] | 2 | [
"PUB00099998"
] | [
"27555589"
] | [
"Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
2082,
21,
8,
14
] | 4 | [] | [] | 0 | true | Family | Bacteriophage Mu, Baseplate protein gp46 | Bacteriophage Mu, Baseplate protein gp46 | Phage_Mu_Gp46 | 7 |
IPR010878 | 10,878 | Protein of unknown function Gp111 | Gp111 | Family | 241 | false | false | This family consists of several proteins whose function is not known. It is named after the Streptococcus bacteriophage Gp111 protein. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07410"
] | [
"Phage_Gp111"
] | [
241
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"bioreactor metagenome"
] | [
198,
42,
1
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function Gp111 | Protein of unknown function Gp111 | Gp111 | 1 |
IPR010879 | 10,879 | Domain of unknown function DUF1508 | DUF1508 | Domain | 6,436 | false | false | This entry represents a domain that is often found as tandem repeats in proteins such as YegP from Escherichia coli. This domain covers the whole length of the protein in HVO_2922 from Haloferax volcanii ({swissprot:D4GXU1]), a small protein whose expression seem to be stress-regulated. It shows four β-strands and one ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07411"
] | [
"DUF1508"
] | [
6436
] | 1 | [] | [] | [] | 0 | [
"2k49",
"2k7i",
"2k8e",
"3bid",
"6q2z"
] | 5 | [
"PUB00101007"
] | [
"31161645"
] | [
"Solution Structure and Dynamics of the Small Protein HVO_2922 from Haloferax volcanii."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
5690,
67,
6,
602,
71
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Domain of unknown function DUF1508 | Domain of unknown function DUF1508 | DUF1508 | 6 |
IPR010880 | 10,880 | Herpesvirus UL37, HHV-5-related | Herpes_UL37_HHV-5-rel | Family | 180 | false | false | This family consists of several Betaherpesvirus immediate-early glycoprotein UL37 sequences. The human cytomegalovirus (HCMV) UL37 immediate-early regulatory protein is a type I integral membrane N-glycoprotein which traffics through the ER and the Golgi network [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07413"
] | [
"Herpes_UL37_2"
] | [
180
] | 1 | [
"REACTOME"
] | [
"R-HSA-9609690"
] | [
"REACTOME:R-HSA-9609690"
] | 1 | [] | 0 | [
"PUB00013136"
] | [
"8794367"
] | [
"The human cytomegalovirus UL37 immediate-early regulatory protein is an integral membrane N-glycoprotein which traffics through the endoplasmic reticulum and Golgi apparatus."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Herpesvirales",
"Homo sapiens"
] | [
179,
1
] | 2 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Herpesvirus UL37, HHV-5-related | Herpesvirus UL37, HHV-5-related | Herpes_UL37_HHV-5-rel | 7 |
IPR010881 | 10,881 | Gammaherpesvirus latent membrane protein 2 | Herpes_LMP2 | Family | 465 | false | false | This family consists of several Gammaherpesvirus latent membrane protein (LMP2) proteins. Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4) is a human gammaherpesvirus that infects and establishes latency in B lymphocytes in vivo. The latent membrane protein 2 (LMP2) gene is expressed in latently infected B... | [
"GO:0019042",
"GO:0033644"
] | [
"viral latency",
"host cell membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF07415"
] | [
"Herpes_LMP2"
] | [
465
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013138",
"PUB00095178",
"PUB00095179"
] | [
"11961256",
"17035319",
"26067064"
] | [
"Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells.",
"Epstein-barr virus latent membrane protein 2B (LMP2B) modulates LMP2A activity.",
"Latent Membrane Protein LMP2A Impairs Recognition of EBV-Infected Cells by CD8+ T Cells."
... | [
2002,
2007,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Lymphocryptovirus"
] | [
4,
461
] | 2 | [] | [] | 0 | true | Family | Gammaherpesvirus latent membrane protein 2 | Gammaherpesvirus latent membrane protein 2 | Herpes_LMP2 | 8 |
IPR010882 | 10,882 | Acidic phosphoprotein PCEMA1 | PCEMA1 | Family | 228 | false | false | This family consists of several acidic phosphoprotein precursor PCEMA1 sequences which appear to be found exclusively in Plasmodium. PCEMA1 is an antigen that is associated with the membrane of the infected erythrocyte throughout the entire intraerythrocytic cycle [ ]. The exact function of this family is unclear. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07418"
] | [
"PCEMA1"
] | [
228
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013140"
] | [
"1475002"
] | [
"Structure of a Plasmodium chabaudi acidic phosphoprotein that is associated with the host erythrocyte membrane."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Plasmodium (Vinckeia)"
] | [
228
] | 1 | [] | [] | 0 | true | Family | Acidic phosphoprotein PCEMA1 | Acidic phosphoprotein PCEMA1 | PCEMA1 | 4 |
IPR010883 | 10,883 | Marek disease virus, LORF3 | Marek_disease_virus_LORF3 | Family | 22 | false | false | This family consists of several uncharacterised viral proteins, which include LORF2 from the Marek's disease-like viruses (Meleagrid herpesvirus 1 (MeHV-1) and LORF3 from Gallid herpesvirus 2. Members of this family are typically around 400 residues in length. The function of this family is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07420"
] | [
"DUF1509"
] | [
22
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphaherpesvirinae"
] | [
22
] | 1 | [] | [] | 0 | true | Family | Marek disease virus, LORF3 | Marek disease virus, LORF3 | Marek_disease_virus_LORF3 | 2 |
IPR010884 | 10,884 | 6-Cysteine (6-Cys) domain | 6_CYS_dom | Domain | 1,778 | false | false | This entry represents the 6-Cys domain. The 6-Cysteine (6-Cys) domain is found in Plasmodium proteins that are expressed in all stages of the parasite life cycle in both the vertebrate and mosquito hosts. The domain is of roughly 120 amino acids and contains six positionally conserved cysteines. It might occur in 1-14 ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF07422",
"PS51701",
"SM00970"
] | [
"s48_45",
"6_CYS",
"s48_45"
] | [
1579,
1682,
1458
] | 3 | [] | [] | [] | 0 | [
"2loe",
"2ymo",
"4ys4",
"6e62",
"6e63",
"6h5n",
"6ohg",
"7jum",
"7kj7",
"7kjh",
"7kji",
"7s7q",
"7s7r",
"7u9e",
"7u9w",
"7ua2",
"7ua8",
"7ubs",
"7uc8",
"7ucq",
"7ufw",
"7ui1",
"7unb",
"7usr",
"7uss",
"7ust",
"7usv",
"7uvh",
"7uvi",
"7uvo",
"7uvq",
"7uvs"... | 48 | [
"PUB00013141",
"PUB00072570",
"PUB00072571",
"PUB00072572",
"PUB00072573"
] | [
"11163248",
"16155126",
"20386715",
"22493233",
"23511632"
] | [
"A central role for P48/45 in malaria parasite male gamete fertility.",
"Structural models for the protein family characterized by gamete surface protein Pfs230 of Plasmodium falciparum.",
"Three members of the 6-cys protein family of Plasmodium play a role in gamete fertility.",
"Structure of the Plasmodium ... | [
2001,
2005,
2010,
2012,
2013
] | 5 | [] | [] | 0 | 0 | null | [
"Borreliaceae",
"Eukaryota"
] | [
43,
1735
] | 2 | [] | [] | 0 | true | Domain | 6-Cysteine (6-Cys) domain | 6-Cysteine (6-Cys) domain | 6_CYS_dom | 9 |
IPR010886 | 10,886 | Histone H1-like Hc1 | Hc1 | Family | 2,277 | false | false | This entry represents a family that includes Histone H1-like protein HC1 from Chlamydia pneumoniae and similar proteins from bacteria and some archaeal species. The gene coding for HC1 is expressed only during the late stages of the chlamydial life cycle concomitant with the reorganisation of chlamydial reticulate bodi... | [
"GO:0003677",
"GO:0030527"
] | [
"DNA binding",
"structural constituent of chromatin"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF07432"
] | [
"Hc1"
] | [
2277
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013148"
] | [
"2023942"
] | [
"Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"metagenomes"
] | [
2148,
33,
9,
30,
57
] | 5 | [] | [] | 0 | true | Family | Histone H1-like Hc1 | Histone H1-like Hc1 | Hc1 | 3 |
IPR010888 | 10,888 | CblD-like pilus biogenesis initiator | CblD | Family | 681 | false | false | This family consists of several minor pilin proteins including CblD from Burkholderia cepacia which is known to CblD be the initiator of pilus biogenesis [ ]. The family also contains a variety of Enterobacterial minor pilin proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07434"
] | [
"CblD"
] | [
681
] | 1 | [] | [] | [] | 0 | [
"2hb0",
"3f83",
"3vac",
"6k73"
] | 4 | [
"PUB00013149"
] | [
"12686638"
] | [
"Identification and molecular analysis of cable pilus biosynthesis genes in Burkholderia cepacia."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
678,
3
] | 2 | [] | [] | 0 | true | Family | CblD-like pilus biogenesis initiator | CblD-like pilus biogenesis initiator | CblD | 3 |
IPR010889 | 10,889 | Protein of unknown function DUF1515 | DUF1515 | Family | 197 | false | false | This family consists of several hypothetical bacterial proteins of around 130 residues in length. Members of this family seem to be found exclusively in Rhizobium species. The function of this family is unknown. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07439",
"PIRSF033399"
] | [
"DUF1515",
"DUF1515"
] | [
197,
19
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Hyphomicrobiales",
"Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)"
] | [
196,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF1515 | Protein of unknown function DUF1515 | DUF1515 | 8 |
IPR010890 | 10,890 | PriC | PriC | Family | 2,424 | false | false | This family contains the bacterial primosomal replication proteins PriC (approximately 180 residues long). Replication restart protein PriC is involved in the reactivation of stalled replication forks by facilitating the reloading of the DnaB replicative helicase at sites other than the origin of replication [ , , ]. I... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07445"
] | [
"PriC"
] | [
2424
] | 1 | [
"GP",
"GP"
] | [
"GenProp1187",
"GenProp1208"
] | [
"GP:GenProp1187",
"GP:GenProp1208"
] | 2 | [
"2ncj",
"2rt6"
] | 2 | [
"PUB00013155",
"PUB00099781",
"PUB00104543",
"PUB00104544",
"PUB00160805",
"PUB00160806",
"PUB00160807"
] | [
"10613856",
"27387236",
"10540288",
"10835375",
"22636770",
"23629733",
"27382050"
] | [
"Role of PriA in replication fork reactivation in Escherichia coli.",
"DnaT is a PriC-binding protein.",
"dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12.",
"Multiple genetic pathways for restarting DNA replica... | [
2000,
2016,
1999,
2000,
2012,
2013,
2016
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2380,
42,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | PriC | PriC | PriC | 3 |
IPR010892 | 10,892 | Secreted phosphoprotein 24 | Spp-24 | Family | 833 | false | false | This entry represents a conserved region approximately 140 residues long within secreted phosphoprotein 24 (Spp-24), which seems to be restricted to vertebrates [ ]. This is a non-collagenous protein found in bone that is related in sequence to the cystatin family of thiol protease inhibitors. This suggests that Spp-24... | [
"GO:0046849",
"GO:0005576"
] | [
"bone remodeling",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF07448",
"PTHR15444"
] | [
"Spp-24",
""
] | [
807,
822
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-BTA-381426",
"R-BTA-8957275",
"R-HSA-114608",
"R-HSA-381426",
"R-HSA-8957275",
"R-MMU-114608",
"R-MMU-381426",
"R-MMU-8957275",
"R-RNO-114608",
"R-RNO-381426",
"R-RNO-8957275"
] | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-8957275",
"REACTOME:R-RNO-114608",
"REACTOME:R-RNO-381426",
"REACTOME:R-RNO-... | 12 | [] | 0 | [
"PUB00013157",
"PUB00033902"
] | [
"7814406",
"15062857"
] | [
"Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors.",
"Characterization of the human secreted phosphoprotein 24 gene (SPP2) and comparison of the protein sequence in nine species."
] | [
1995,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
833
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
4,
5
] | 4 | true | Family | Secreted phosphoprotein 24 | Secreted phosphoprotein 24 | Spp-24 | 7 |
IPR010894 | 10,894 | Stage V sporulation AD | SpoVAD | Family | 3,562 | false | false | This family contains the bacterial stage V sporulation protein AD (SpoVAD), which is approximately 340 residues long. This is one of six proteins encoded by the spoVA operon, which is transcribed exclusively in the forespore at about the time of dipicolinic acid (DPA) synthesis in the mother cell. The functions of the ... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM",
"PIRSF",
"NCBIFAM"
] | [
"NF006160",
"PF07451",
"PIRSF011570",
"TIGR02845"
] | [
"PRK08304.1",
"SpoVAD",
"SpoVAD",
"spore_V_AD"
] | [
3319,
3562,
3304,
2896
] | 4 | [
"GP"
] | [
"GenProp0610"
] | [
"GP:GenProp0610"
] | 1 | [
"3lm6",
"3lma"
] | 2 | [
"PUB00008450"
] | [
"11751839"
] | [
"The products of the spoVA operon are involved in dipicolinic acid uptake into developing spores of Bacillus subtilis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3525,
3,
34
] | 3 | [] | [] | 0 | true | Family | Stage V sporulation AD | Stage V sporulation AD | SpoVAD | 6 |
IPR010895 | 10,895 | CHRD | CHRD | Domain | 7,058 | false | false | CHRD (after SWISS-PROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. This family includes bacterial homologues. It is anticipated to have an immunoglobulin-like β-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF07452",
"PS50933",
"SM00754"
] | [
"CHRD",
"CHRD",
"CHRD"
] | [
6614,
4721,
5966
] | 3 | [
"PROSITEDOC"
] | [
"PDOC50933"
] | [
"PROSITEDOC:PDOC50933"
] | 1 | [] | 0 | [
"PUB00013160"
] | [
"13678956"
] | [
"CHRD, a novel domain in the BMP inhibitor chordin, is also found in microbial proteins."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
85,
4144,
2756,
19,
54
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
9,
6,
4
] | 5 | true | Domain | CHRD | CHRD | CHRD | 4 |
IPR010896 | 10,896 | Nuclease-associated modular DNA-binding 1 | NUMOD1 | Domain | 1,698 | false | false | This helix-turn-helix-containing DNA-binding domain is found associated in homing nucleases [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07453"
] | [
"NUMOD1"
] | [
1698
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013165"
] | [
"13678957"
] | [
"New types of conserved sequence domains in DNA-binding regions of homing endonucleases."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
297,
1014,
344,
43
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2,
1
] | 2 | true | Domain | Nuclease-associated modular DNA-binding 1 | Nuclease-associated modular DNA-binding 1 | NUMOD1 | 9 |
IPR010897 | 10,897 | Sporulation stage II, protein P | Spore_II_P | Family | 3,739 | false | false | This family contains the bacterial stage II sporulation protein P (SpoIIP) (approximately 350 residues long). It has been shown that a block in polar cytokinesis in Bacillus subtilis is mediated partly by transcription of spoIID, spoIIM and spoIIP. This inhibition of polar division is involved in the locking in of asym... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF07454",
"TIGR02867"
] | [
"SpoIIP",
"spore_II_P"
] | [
3739,
3371
] | 2 | [
"GP"
] | [
"GenProp0610"
] | [
"GP:GenProp0610"
] | 1 | [] | 0 | [
"PUB00012907",
"PUB00013161",
"PUB00034447",
"PUB00034448",
"PUB00034449"
] | [
"12662922",
"11886548",
"8501064",
"7836306",
"3011962"
] | [
"The sigmaE regulon and the identification of additional sporulation genes in Bacillus subtilis.",
"A three-protein inhibitor of polar septation during sporulation in Bacillus subtilis.",
"Physical and functional characterization of the Bacillus subtilis spoIIM gene.",
"Identification and characterization of ... | [
2003,
2001,
1993,
1995,
1986
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
3705,
34
] | 2 | [] | [] | 0 | true | Family | Sporulation stage II, protein P | Sporulation stage II, protein P | Spore_II_P | 8 |
IPR010898 | 10,898 | Heptaprenyl diphosphate synthase component I | Hpre_diP_synth_I | Family | 2,841 | false | false | This family contains component I of bacterial heptaprenyl diphosphate synthase ( ) (approximately 170 residues long). This is one of the two dissociable subunits that form the enzyme, both of which are required for the catalysis of the biosynthesis of the side chain of menaquinone-7 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07456"
] | [
"Hpre_diP_synt_I"
] | [
2841
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013095"
] | [
"9748348"
] | [
"Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex."
] | [
1998
] | 1 | [] | [
"IPR014535"
] | 0 | 1 | 0 | [
"Bacteria",
"Trichuris trichiura",
"unclassified sequences"
] | [
2781,
1,
59
] | 3 | [] | [] | 0 | true | Family | Heptaprenyl diphosphate synthase component I | Heptaprenyl diphosphate synthase component I | Hpre_diP_synth_I | 4 |
IPR010899 | 10,899 | Protein of unknown function UPF0344 | UPF0344 | Family | 1,728 | false | false | This family contains a number of hypothetical bacterial proteins of unknown function approximately 120 residues long. | [] | [] | [] | 0 | [
"HAMAP",
"PFAM"
] | [
"MF_01536",
"PF07457"
] | [
"UPF0344",
"DUF1516"
] | [
958,
1728
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
1727,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function UPF0344 | Protein of unknown function UPF0344 | UPF0344 | 5 |
IPR010900 | 10,900 | Nicotine adenine dinucleotide glycohydrolase, catalytic domain | NA_dinucl_GlycHdrlase_cat | Domain | 100 | false | false | This family consists of several bacterial nicotine adenine dinucleotide glycohydrolase (NGA) proteins which appear to be specific to Streptococcus pyogenes. NAD glycohydrolase (NADase) is a potential virulence factor. Streptococcal NADase may contribute to virulence by its ability to cleave beta-NAD at the ribose-nicot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07461"
] | [
"NADase_NGA"
] | [
100
] | 1 | [] | [] | [] | 0 | [
"3pnt",
"4kt6",
"7wvh"
] | 3 | [
"PUB00013166"
] | [
"10979908"
] | [
"Molecular epidemiology of nga and NAD glycohydrolase/ADP-ribosyltransferase activity among Streptococcus pyogenes causing streptococcal toxic shock syndrome."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
100
] | 1 | [] | [] | 0 | true | Domain | Nicotine adenine dinucleotide glycohydrolase, catalytic domain | Nicotine adenine dinucleotide glycohydrolase, catalytic domain | NA_dinucl_GlycHdrlase_cat | 8 |
IPR010901 | 10,901 | Merozoite surface 1, C-terminal | MSP1_C | Domain | 1,972 | false | false | This entry represents the C-terminal region of merozoite surface protein 1 (MSP1), which is found in a number of Plasmodium species. MSP-1 is a 200kDa protein expressed on the surface of the Plasmodium vivax merozoite. MSP-1 of Plasmodium species is synthesised as a high-molecular-weight precursor and then processed in... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF07462"
] | [
"MSP1_C"
] | [
1972
] | 1 | [] | [] | [] | 0 | [
"6zbc",
"6zbd",
"6zbe",
"6zbf",
"6zbg",
"6zbh",
"6zbj",
"6zbl"
] | 8 | [
"PUB00013167"
] | [
"12466500"
] | [
"Mosaic organization and heterogeneity in frequency of allelic recombination of the Plasmodium vivax merozoite surface protein-1 locus."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Plasmodium"
] | [
1972
] | 1 | [] | [] | 0 | true | Domain | Merozoite surface 1, C-terminal | Merozoite surface 1, C-terminal | MSP1_C | 9 |
IPR010902 | 10,902 | NUMOD4 | NUMOD4 | Domain | 3,245 | false | false | NUMOD4 is a putative DNA-binding motif found in homing endonucleases and related proteins [ ]. | [
"GO:0016788"
] | [
"hydrolase activity, acting on ester bonds"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07463"
] | [
"NUMOD4"
] | [
3245
] | 1 | [] | [] | [] | 0 | [
"1u3e"
] | 1 | [
"PUB00013165"
] | [
"13678957"
] | [
"New types of conserved sequence domains in DNA-binding regions of homing endonucleases."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1886,
105,
1144,
110
] | 4 | [] | [] | 0 | true | Domain | NUMOD4 | NUMOD4 | NUMOD4 | 1 |
IPR010903 | 10,903 | Protein of unknown function DUF1517 | DUF1517 | Family | 2,373 | false | false | This family consists of several hypothetical glycine rich plant and bacterial proteins of around 300 residues in length. This entry includes the Fluctuating-Light-Acclimation Protein 1 (FLAP1). FLAP1 is conserved in oxygenic phototrophs. FLAP1 is associated with chloroplast thylakoid and envelope membranes and is invol... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07466",
"PIRSF037221"
] | [
"DUF1517",
"DUF1517"
] | [
2373,
721
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153170",
"PUB00153171"
] | [
"29016945",
"37339934"
] | [
"FLUCTUATING-LIGHT-ACCLIMATION PROTEIN1, Conserved in Oxygenic Phototrophs, Regulates H+ Homeostasis and Non-Photochemical Quenching in Chloroplasts.",
"Arabidopsis mutants lacking DLDG1 and non-photochemical quenching-related proteins reveal the regulatory role of DLDG1 in chloroplast pH homeostasis."
] | [
2017,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
822,
1551
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
10,
8
] | 3 | true | Family | Protein of unknown function DUF1517 | Protein of unknown function DUF1517 | DUF1517 | 9 |
IPR010905 | 10,905 | Glycosyl hydrolase, family 88 | Glyco_hydro_88 | Family | 21,385 | false | false | Unsaturated glucuronyl hydrolase catalyses the hydrolytic release of unsaturated glucuronic acids from oligosaccharides produced by the reactions of polysaccharide lyases [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07470"
] | [
"Glyco_hydro_88"
] | [
21385
] | 1 | [
"EC"
] | [
"3.2.1"
] | [
"EC:3.2.1"
] | 1 | [
"1nc5",
"1vd5",
"2ahf",
"2ahg",
"2d5j",
"2d8l",
"2fuz",
"2fv0",
"2fv1",
"2gh4",
"2zzr",
"3ani",
"3anj",
"3ank",
"3k11",
"3pmm",
"3qwt",
"3vxd",
"3wiw",
"3wux",
"4ce7",
"4q88",
"4wu0",
"4xuv",
"5noa"
] | 25 | [
"PUB00013171"
] | [
"12777820"
] | [
"Crystallization and preliminary X-ray analysis of a novel unsaturated glucuronyl hydrolase from Bacillus sp. GL1."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Aureococcus anophagefferens virus",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
82,
1,
16921,
4239,
142
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Family | Glycosyl hydrolase, family 88 | Glycosyl hydrolase, family 88 | Glyco_hydro_88 | 2 |
IPR010906 | 10,906 | Bacteriophage lambda, Nu1, terminase small subunit | Phage_lambda_Nu1_terminase-ssu | Family | 1,168 | false | false | Terminase, the DNA packaging enzyme of bacteriophage lambda, is a heteromultimer composed of subunits Nu1 and A. The smaller Nu1 terminase subunit has a low-affinity ATPase stimulated by non-specific DNA [ ]. This entry is representes Bacteriophage lambda Nu1 and related proteins. The characteristics of the protein dis... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07471"
] | [
"Phage_Nu1"
] | [
1168
] | 1 | [] | [] | [] | 0 | [
"1j9i",
"6hn7",
"7lw0",
"7lwr",
"7lxs"
] | 5 | [
"PUB00013172"
] | [
"10600592"
] | [
"A mutation correcting the DNA interaction defects of a mutant phage lambda terminase, gpNu1 K35A terminase."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobrevibacter smithii DSM 2374",
"Protostomia",
"Viruses",
"organismal metagenomes"
] | [
1126,
1,
2,
33,
6
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Bacteriophage lambda, Nu1, terminase small subunit | Bacteriophage lambda, Nu1, terminase small subunit | Phage_lambda_Nu1_terminase-ssu | 5 |
IPR010908 | 10,908 | Longin domain | Longin_dom | Domain | 23,816 | false | false | VAMPs (and its homologue synaptobrevins) define a group of SNARE proteins that contain a C-terminal coiled-coil/SNARE domain, in combination with variable N-terminal domains that are used to classify VAMPs: those containing longin N-terminal domains (~150 aa) are referred to as longins, while those with shorter N-termi... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF13774",
"PS50859",
"SM01270",
"cd14824"
] | [
"Longin",
"LONGIN",
"Longin",
"Longin"
] | [
22453,
23532,
21460,
22231
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50859",
"R-BTA-204005",
"R-BTA-6807878",
"R-BTA-6811438",
"R-BTA-8980692",
"R-BTA-9013148",
"R-BTA-9013149",
"R-BTA-9013408",
"R-BTA-9013423",
"R-DDI-199992",
"R-DRE-204005",
"R-DRE-6807878",
"R-DRE-6811434",
"R-DRE-6811438",
"R-GGA-204005",
"R-GGA-432720",
"R-GGA-432722",
"R-... | [
"PROSITEDOC:PDOC50859",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811438",
"REACTOME:R-BTA-8980692",
"REACTOME:R-BTA-9013148",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013408",
"REACTOME:R-BTA-9013423",
"REACTOME:R-DDI-199992",
"REACTOME:R-DRE-204005",
"REACTOME:R-D... | 85 | [
"1h8m",
"1ifq",
"1iou",
"2dmw",
"2nup",
"2nut",
"2vx8",
"3bw6",
"3egd",
"3egx",
"3kyq",
"4afi",
"4b93",
"5vne",
"5vnf",
"5vng",
"5vnh",
"5vni",
"5vnj",
"5vnk",
"5vnl",
"5vnm",
"5vnn",
"5vno",
"6j74",
"6j7f",
"6j7x",
"8hr0"
] | 28 | [
"PUB00013945"
] | [
"12914952"
] | [
"Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Odinarchaeota yellowstonii (strain LCB_4)",
"unclassified Klosneuvirinae",
"viral metagenome"
] | [
44,
23767,
1,
3,
1
] | 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... | [
65,
2,
11,
7,
29,
13,
3,
41,
21,
2,
2,
91
] | 12 | true | Domain | Longin domain | Longin domain | Longin_dom | 1 |
IPR010909 | 10,909 | PLAC | PLAC | Domain | 20,489 | false | false | The PLAC (protease and lacunin) domain is a six-cysteine region of about 40 residues that is present at or near the C-terminal of various enzymes and matrix proteins, including: mammalian PACE4 (paired basic amino acid cleaving enzyme 4), mammalian PCSK5 (proprotein convertase subtilisin/kexin type 5), mammalian metall... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08686",
"PS50900"
] | [
"PLAC",
"PLAC"
] | [
12441,
20383
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50900",
"R-BTA-1650814",
"R-BTA-5173214",
"R-HSA-1181150",
"R-HSA-1474228",
"R-HSA-1650814",
"R-HSA-167060",
"R-HSA-5083635",
"R-HSA-5173214",
"R-HSA-6809371",
"R-HSA-8963889",
"R-HSA-9768727",
"R-MMU-1650814",
"R-MMU-5173214",
"R-RNO-167060",
"R-RNO-5173214",
"R-RNO-8963889",
... | [
"PROSITEDOC:PDOC50900",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-5173214",
"REACTOME:R-HSA-1181150",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-1650814",
"REACTOME:R-HSA-167060",
"REACTOME:R-HSA-5083635",
"REACTOME:R-HSA-5173214",
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-8963889",
"REACTOME:R... | 18 | [
"6buc"
] | 1 | [
"PUB00013946"
] | [
"11867212"
] | [
"Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains."
] | [
2002
] | 1 | [] | [
"IPR056270"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
20489
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
73,
13,
41,
52,
51
] | 6 | true | Domain | PLAC | PLAC | PLAC | 6 |
IPR010910 | 10,910 | Nitrate/nitrite sensing protein, bacterial | Nitrate/nitrite_sensing_bac | Domain | 5,702 | false | false | The nitrate and nitrite-sensing (NIT) domain is a (~250 aa) sensor domain found in various receptor components of signal transduction pathways from different bacterial lineages [ ]. Proteins containing a NIT domain belong to one of four known classes of prokaryotic signal transduction proteins: intracellular transcript... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50906"
] | [
"NIT"
] | [
5702
] | 1 | [
"PROSITEDOC"
] | [
"PDOC50906"
] | [
"PROSITEDOC:PDOC50906"
] | 1 | [
"4akk"
] | 1 | [
"PUB00013947"
] | [
"12633990"
] | [
"The NIT domain: a predicted nitrate-responsive module in bacterial sensory receptors."
] | [
2003
] | 1 | [
"IPR013587"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
5679,
23
] | 2 | [] | [] | 0 | true | Domain | Nitrate/nitrite sensing protein, bacterial | Nitrate/nitrite sensing protein, bacterial | Nitrate/nitrite_sensing_bac | 8 |
IPR010911 | 10,911 | Rab-binding domain | Rab_BD | Domain | 17,604 | false | false | This entry represents the Rab-binding domain. Rab are small GTPases implicated in vesicle trafficking. Like the other small GTPases, Rab proteins act as molecular switches, with an active GTP-bound form that interacts with its target or effector protein and an inactive GDP-bound form. A subgroup of Rab effectors contai... | [
"GO:0031267",
"GO:0006886"
] | [
"small GTPase binding",
"intracellular protein transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROFILE"
] | [
"PS50916"
] | [
"RABBD"
] | [
17604
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50916",
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-210500",
"R-CEL-212676",
"R-CEL-264642",
"R-CEL-888590",
"R-HSA-114608",
"R-HSA-181429",
"R-HSA-181430",
"R-HSA-210500",
"R-HSA-212676",
"R-HSA-264642",
"R-HSA-264876",
"R-HSA-8854214",
"R-HSA-888590",
"R-HSA-9824585",
"R-MMU-1146... | [
"PROSITEDOC:PDOC50916",
"REACTOME:R-CEL-181429",
"REACTOME:R-CEL-181430",
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-264642",
"REACTOME:R-CEL-888590",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-181430",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-2126... | 34 | [
"1zbd",
"2zet",
"3bc1",
"7opp",
"7opq",
"7opr",
"8p3g",
"8p3h",
"8p3i",
"8p3j",
"8p3k"
] | 11 | [
"PUB00008096",
"PUB00013948"
] | [
"10025402",
"12578829"
] | [
"Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A.",
"Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2."
] | [
1999,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
17599
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
227,
17,
68,
48,
74
] | 6 | true | Domain | Rab-binding domain | Rab-binding domain | Rab_BD | 8 |
IPR010912 | 10,912 | Spen paralogue/orthologue C-terminal, metazoa | SPOC_met | Domain | 6,459 | false | false | Spen (split end) proteins regulate the expression of key transcriptional effectors in diverse signalling pathways. They are large proteins characterised by N-terminal RNA-binding motifs and a highly conserved C-terminal SPOC (Spen paralog and ortholog C-terminal) domain. The function of the SPOC domain is unknown, but ... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50917"
] | [
"SPOC"
] | [
6459
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50917",
"R-DME-9013422",
"R-HSA-9013422",
"R-MMU-9013422"
] | [
"PROSITEDOC:PDOC50917",
"REACTOME:R-DME-9013422",
"REACTOME:R-HSA-9013422",
"REACTOME:R-MMU-9013422"
] | 4 | [
"1ow1",
"2rt5",
"7z1k",
"7z27"
] | 4 | [
"PUB00013949"
] | [
"12897056"
] | [
"A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling."
] | [
2003
] | 1 | [
"IPR012921"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
76,
6383
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
13,
8,
10,
5,
11
] | 6 | true | Domain | Spen paralogue/orthologue C-terminal, metazoa | Spen paralogue/orthologue C-terminal, metazoa | SPOC_met | 1 |
IPR010915 | 10,915 | Polyhydroxyalkanoate depolymerase | PHB_depoly_PhaZ | Family | 5,328 | false | false | This entry represents an intracellular depolymerase for polyhydroxyalkanoate (PHA), a carbon and energy storing polyester that accumulates in granules in many bacterial species when carbon sources are abundant but other nutrients are limiting. | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF020818",
"TIGR01849"
] | [
"PHB_depoly_PhaZ",
"PHB_depoly_PhaZ"
] | [
5149,
5244
] | 2 | [
"GP"
] | [
"GenProp0055"
] | [
"GP:GenProp0055"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5293,
4,
31
] | 3 | [] | [] | 0 | true | Family | Polyhydroxyalkanoate depolymerase | Polyhydroxyalkanoate depolymerase | PHB_depoly_PhaZ | 5 |
IPR010916 | 10,916 | TonB box, conserved site | TonB_box_CS | Conserved_site | 23,185 | false | false | This entry describes a short conserved region at the N terminus called the tonB-box [ , , ], which is involved in the interaction of the protein with the TonB protein [ ]. In Escherichia coli the TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptak... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00430"
] | [
"TONB_DEPENDENT_REC_1"
] | [
23185
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00354",
"R-DME-425393",
"R-DME-5223345",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-1474228",
"R-HSA-8963896",
"R-HSA-9638334",
"R-HSA-9638482"
] | [
"PROSITEDOC:PDOC00354",
"REACTOME:R-DME-425393",
"REACTOME:R-DME-5223345",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-8963896",
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9638482"
] | 9 | [
"1kmo",
"1kmp",
"6tav",
"7o7l",
"7o7m",
"7o7n",
"7o7o",
"7o7p",
"7o7q",
"7o7r",
"7o7s"
] | 11 | [
"PUB00002063",
"PUB00002072",
"PUB00002093",
"PUB00002420"
] | [
"2439491",
"2644220",
"2687240",
"3015941"
] | [
"Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors.",
"Evolutionary relationship between the TonB-dependent outer membrane transport proteins: nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene.",
"Point mu... | [
1987,
1989,
1989,
1986
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
218,
21597,
1220,
29,
121
] | 5 | [
"Arabidopsis thaliana",
"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"
] | [
5,
2,
7,
6,
2,
1,
1,
16
] | 8 | true | Conserved_site | TonB box, conserved site | TonB box, conserved site | TonB_box_CS | 5 |
IPR010917 | 10,917 | TonB-dependent receptor, conserved site | TonB_rcpt_CS | Conserved_site | 45,755 | false | false | This conserved site is found at the C terminus of outer membrane receptors which interact with the TonB [ ]. In Escherichia coli the TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. These substrates a... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01156"
] | [
"TONB_DEPENDENT_REC_2"
] | [
45755
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC00354",
"R-HSA-9638334",
"R-HSA-9638482"
] | [
"PROSITEDOC:PDOC00354",
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9638482"
] | 3 | [
"1by3",
"1by5",
"1fcp",
"1fep",
"1fi1",
"1kmo",
"1kmp",
"1nqe",
"1nqf",
"1nqg",
"1nqh",
"1pnz",
"1po0",
"1po3",
"1qff",
"1qfg",
"1qjq",
"1qkc",
"1ujw",
"1xkh",
"1xkw",
"2fcp",
"2grx",
"2gsk",
"2guf",
"2hdf",
"2hdi",
"2iah",
"2o5p",
"2w16",
"2w6t",
"2w6u"... | 76 | [
"PUB00002093"
] | [
"2687240"
] | [
"Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina mazei",
"Viruses",
"unclassified sequences"
] | [
45344,
61,
1,
2,
347
] | 5 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Conserved_site | TonB-dependent receptor, conserved site | TonB-dependent receptor, conserved site | TonB_rcpt_CS | 3 |
IPR010918 | 10,918 | PurM-like, C-terminal domain | PurM-like_C_dom | Domain | 101,851 | false | false | This domain is found in carbamoyl dehydratase HypE, which is involved in the maturation of NifE hydrogenase; AIR synthase (PurM) and FGAM synthase (PurL), which are involved in de novo purine biosynthesis; and selenide, water dikinase, an enzyme which synthesizes selenophosphate from selenide and ATP. In PurM this doma... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02769"
] | [
"AIRS_C"
] | [
101851
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-73817",
"R-CEL-2408557",
"R-CEL-73817",
"R-DDI-2408557",
"R-DDI-73817",
"R-DME-2408557",
"R-DME-73817",
"R-DRE-2408557",
"R-GGA-419140",
"R-HSA-2408557",
"R-HSA-73817",
"R-MMU-2408557",
"R-MMU-73817",
"R-SCE-73817",
"R-SPO-73817",
"R-SSC-2408557"
] | [
"REACTOME:R-BTA-73817",
"REACTOME:R-CEL-2408557",
"REACTOME:R-CEL-73817",
"REACTOME:R-DDI-2408557",
"REACTOME:R-DDI-73817",
"REACTOME:R-DME-2408557",
"REACTOME:R-DME-73817",
"REACTOME:R-DRE-2408557",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-2408557",
"REACTOME:R-HSA-73817",
"REACTOME:R-MMU-240... | 16 | [
"1cli",
"1t3t",
"1vk3",
"2btu",
"2hru",
"2hry",
"2hs0",
"2hs3",
"2hs4",
"2i6r",
"2rb9",
"2v9y",
"2yxz",
"2yye",
"2z01",
"2z1e",
"2z1f",
"2z1t",
"2z1u",
"2zau",
"2zod",
"3d54",
"3fd5",
"3fd6",
"3kiz",
"3m84",
"3mcq",
"3mdo",
"3p4e",
"3qty",
"3u0o",
"3ugj"... | 79 | [
"PUB00014643"
] | [
"10508786"
] | [
"X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4245,
82866,
12419,
314,
2007
] | 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,
3,
8,
10,
5,
19,
10,
2,
8,
11,
2,
2,
22
] | 13 | true | Domain | PurM-like, C-terminal domain | PurM-like, C-terminal domain | PurM-like_C_dom | 4 |
IPR010919 | 10,919 | SAND-like domain superfamily | SAND-like_dom_sf | Homologous_superfamily | 13,116 | false | false | The SAND domain (named after Sp100, AIRE-1, NucP41/75, DEAF-1) is a conserved ~80 residue region found in a number of nuclear proteins, many of which function in chromatin-dependent transcriptional control. These include proteins linked to various human diseases, such as the Sp100 (Speckled protein 100kDa), NUDR (Nucle... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.10.390.10",
"SSF63763"
] | [
"",
""
] | [
13048,
12595
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-201451",
"R-HSA-2173795",
"R-HSA-3108214",
"R-HSA-877300",
"R-MMU-201451",
"R-MMU-2173795",
"R-MMU-3108214"
] | [
"REACTOME:R-HSA-201451",
"REACTOME:R-HSA-2173795",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-201451",
"REACTOME:R-MMU-2173795",
"REACTOME:R-MMU-3108214"
] | 7 | [
"1h5p",
"1mr1",
"1oqj",
"1ufn",
"5c4v",
"8j70",
"8j71"
] | 7 | [
"PUB00005483",
"PUB00007101",
"PUB00013959"
] | [
"9697411",
"11427895",
"12419246"
] | [
"The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor.",
"The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.",
"Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Sk... | [
1998,
2001,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Avian erythroblastosis virus (strain Sloan-Kettering)",
"Bacillales",
"Eukaryota",
"marine sediment metagenome"
] | [
1,
8,
13106,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
5,
95,
13,
43,
47,
58
] | 7 | true | Homologous_superfamily | SAND-like domain superfamily | SAND-like domain superfamily | SAND-like_dom_sf | 4 |
IPR010920 | 10,920 | LSM domain superfamily | LSM_dom_sf | Homologous_superfamily | 199,748 | false | false | This domain superfamily is found as the core structure in Lsm (like-Sm) proteins and bacterial Lsm-related Hfq proteins, and as the middle domain of the mechanosensitive channel protein MscS. In each case, the domain adopts a core structure consisting of an open β-barrel with an SH3-like topology. Lsm proteins have div... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50182"
] | [
""
] | [
199748
] | 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-111367",
"R-BTA-191859",
"R-BTA-430039",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-73856",
"R-BTA-77588",
"R-CEL-111367",
"R-CEL-191859",
"R-CEL-430039",
"R-CEL-72163",
"R-CEL-72165",
"R-CEL-73856",
"R-CEL-77588",
"R-DDI-111367",
"R-DDI-430039",
"R-DDI-72163",
"R-DDI-73856",
"R... | [
"REACTOME:R-BTA-111367",
"REACTOME:R-BTA-191859",
"REACTOME:R-BTA-430039",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72165",
"REACTOME:R-BTA-73856",
"REACTOME:R-BTA-77588",
"REACTOME:R-CEL-111367",
"REACTOME:R-CEL-191859",
"REACTOME:R-CEL-430039",
"REACTOME:R-CEL-72163",
"REACTOME:R-CEL-72165",
... | 57 | [
"1b34",
"1d3b",
"1h64",
"1hk9",
"1i4k",
"1i5l",
"1i81",
"1i8f",
"1jbm",
"1jri",
"1kq1",
"1kq2",
"1ljo",
"1lnx",
"1loj",
"1m5q",
"1m8v",
"1mgq",
"1n9r",
"1n9s",
"1th7",
"1u1s",
"1u1t",
"1ycy",
"2fb7",
"2jn0",
"2k57",
"2oau",
"2qtx",
"2ra2",
"2rb6",
"2rd1"... | 325 | [
"PUB00013954",
"PUB00013956",
"PUB00016606",
"PUB00016607",
"PUB00016608"
] | [
"12093755",
"12446901",
"10801455",
"12438310",
"15130578"
] | [
"Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.",
"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel.",
"Functions of Lsm proteins in mRNA degradation and splicing.",
"Lsm Proteins are required for norma... | [
2002,
2002,
2000,
2003,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5433,
99280,
93777,
10,
1248
] | 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",... | [
151,
21,
34,
45,
9,
88,
60,
21,
81,
102,
17,
19,
188
] | 13 | true | Homologous_superfamily | LSM domain superfamily | LSM domain superfamily | LSM_dom_sf | 5 |
IPR010921 | 10,921 | Trp repressor/replication initiator | Trp_repressor/repl_initiator | Homologous_superfamily | 62,011 | false | false | The Trp repressor (TrpR) binds to at least five operators in the Escherichia coli genome, repressing gene expression. The operators at which it binds vary considerably in DNA sequence and location within the promoter; when bound to the Trp operon it recognises the sequence 5'-ACTAGT-3' and acts to prevent the initiatio... | [
"GO:0043565"
] | [
"sequence-specific DNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.1750.10",
"SSF48295"
] | [
"",
""
] | [
28860,
61979
] | 2 | [] | [] | [] | 0 | [
"1co0",
"1j1v",
"1jhg",
"1l8q",
"1mi7",
"1rcs",
"1tro",
"1trr",
"1wrp",
"1wrs",
"1wrt",
"1zt9",
"2hcb",
"2jrt",
"2oa4",
"2oz9",
"2xdi",
"2z4r",
"2z4s",
"3frw",
"3g1c",
"3kor",
"3pvp",
"3pvv",
"3r8f",
"3ssw",
"3ssx",
"3wrp",
"5tm0",
"6ejw",
"6ejz",
"6ekp"... | 42 | [
"PUB00013953",
"PUB00013960"
] | [
"12475235",
"12234917"
] | [
"Trp repressor-operator binding: NMR and electrophoretic mobility shift studies of the effect of DNA sequence and corepressor binding on two Trp repressor-operator complexes.",
"The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation."
] | [
2002,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid Ti",
"Viruses",
"unclassified sequences"
] | [
43,
59477,
1165,
1,
188,
1137
] | 6 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Homo sapiens"
] | [
1,
3,
1
] | 3 | true | Homologous_superfamily | Trp repressor/replication initiator | Trp repressor/replication initiator | Trp_repressor/repl_initiator | 7 |
IPR010923 | 10,923 | tRNA threonylcarbamoyladenosine biosynthesis protein SUA5 | T(6)A37_SUA5 | Family | 12,615 | false | false | The yeast SUA5 protein is part of the YrdC/SUA5 family is required for the formation of threonylcarbamoyladenosine in tRNA [ ]. SUA5 has been shown to be required for translational regulation [ ] and telomere recombination [ ] and replication [ ] in yeast. Members of this group contain two domains: a YrdC-like domain a... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF004930"
] | [
"Tln_factor_SUA5"
] | [
12615
] | 1 | [
"EC"
] | [
"2.7.7.87"
] | [
"EC:2.7.7.87"
] | 1 | [
"2eqa",
"3aje",
"4e1b",
"6f87",
"6f89",
"6f8y",
"9dg5",
"9dsq",
"9dsv",
"9dsw"
] | 10 | [
"PUB00011086",
"PUB00011089",
"PUB00054278",
"PUB00063343",
"PUB00063344",
"PUB00063360"
] | [
"11206077",
"1325384",
"19287007",
"20309016",
"19884342",
"19369944"
] | [
"The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.",
"Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae.",
"The universal YrdC/Sua5 family is required for the formation of threonylcarbamoy... | [
2000,
1992,
2009,
2010,
2010,
2009
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
280,
11090,
1036,
209
] | 4 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1
] | 2 | true | Family | tRNA threonylcarbamoyladenosine biosynthesis protein SUA5 | tRNA threonylcarbamoyladenosine biosynthesis protein SUA5 | T(6)A37_SUA5 | 1 |
IPR010924 | 10,924 | DNA-directed RNA polymerase subunit Rpo4 | Rpo4 | Family | 927 | false | false | Eukaryotic RNA polymerase II (RNAPII) is composed of a ten-subunit core and an Rpb4-Rpb7 heterodimer that reversibly associates with the core [ ]. The heterodimer both binds RNA and serves to stabilise the transcription complex. The Rpb4 and Rpb7 homologues in Archaea are known as subunits F and E, and have been more r... | [] | [] | [] | 0 | [
"HAMAP",
"PIRSF",
"PANTHER"
] | [
"MF_00864",
"PIRSF005053",
"PTHR39646"
] | [
"RNApol_arch_Rpo4",
"RNA_pol_F_arch",
""
] | [
866,
849,
915
] | 3 | [
"EC"
] | [
"2.7.7.6"
] | [
"EC:2.7.7.6"
] | 1 | [
"1go3",
"2pmz",
"2waq",
"2wb1",
"2y0s",
"3hkz",
"4ayb",
"4qiw",
"4qjf",
"4v8s",
"6kf3",
"6kf4",
"6kf9",
"7ok0",
"7oq4",
"7oqy",
"8cro",
"8oki",
"8orq",
"8p2i",
"8rbo",
"9bct",
"9bcu"
] | 23 | [
"PUB00007873",
"PUB00010734",
"PUB00010735",
"PUB00010736",
"PUB00059148",
"PUB00059149"
] | [
"11741548",
"11909517",
"10400604",
"11058130",
"19419240",
"19880312"
] | [
"Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex.",
"The RNA polymerase II machinery: structure illuminates function.",
"Methanobacterium thermoautotrophicum RNA polymerase and transcription in vitro.",
"Archaeal RNA polymerase subunits F and P are bona fide homologs of ... | [
2001,
2002,
1999,
2000,
2009,
2009
] | 6 | [
"IPR005574"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Metazoa",
"ecological metagenomes"
] | [
891,
2,
34
] | 3 | [] | [] | 0 | true | Family | DNA-directed RNA polymerase subunit Rpo4 | DNA-directed RNA polymerase subunit Rpo4 | Rpo4 | 9 |
IPR010926 | 10,926 | Class I myosin tail homology domain | Myosin_TH1 | Domain | 17,176 | false | false | Class I myosins (Myo1s) are widely expressed in eukaryotic cells. Myo1s exist as monomers and can sense cellular mechanical forces and function as tension- sensitive anchors or transporters. Each Myo1 contains from N terminus to C terminus, a motor domain, a neck region consisting of several calmodulin (CaM)-binding IQ... | [
"GO:0003774",
"GO:0016459"
] | [
"cytoskeletal motor activity",
"myosin complex"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF06017",
"PS51757"
] | [
"Myosin_TH1",
"TH1"
] | [
17067,
16973
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2029482",
"R-BTA-5250924",
"R-HSA-1445148",
"R-HSA-2029482",
"R-HSA-5250924",
"R-HSA-9662360",
"R-HSA-9662361",
"R-HSA-9664422",
"R-MMU-2029482",
"R-MMU-5250924",
"R-RNO-2029482",
"R-RNO-5250924"
] | [
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-5250924",
"REACTOME:R-HSA-1445148",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-5250924",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361",
"REACTOME:R-HSA-9664422",
"REACTOME:R-MMU-2029482",
"REACTOME:R-MMU-5250924",
"REACTOME:R-RNO-2029482",
"REACTOM... | 12 | [
"4r8g"
] | 1 | [
"PUB00077755",
"PUB00077756"
] | [
"25437912",
"20071333"
] | [
"Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.",
"Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)."
] | [
2015,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
17176
] | 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,
3,
42,
7,
31,
26,
1,
2,
40,
2,
1,
4
] | 12 | true | Domain | Class I myosin tail homology domain | Class I myosin tail homology domain | Myosin_TH1 | 9 |
IPR010927 | 10,927 | Type IV conjugative transfer system protein TraH | T4SS_TraH | Family | 3,003 | false | false | Six Tra proteins encoded by the F plasmid and required by F(+) cells to elaborate F pili. The six proteins are TraH, TraF, TraW, TraU, TrbI, and TrbB. Except for TrbI, these proteins were all identified as hallmarks of F-like type IV secretion systems (TFSSs), with no homologues among TFSS genes of P-type or I-type sys... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06122"
] | [
"TraH"
] | [
3003
] | 1 | [
"GP"
] | [
"GenProp0484"
] | [
"GP:GenProp0484"
] | 1 | [] | 0 | [
"PUB00020459",
"PUB00034400",
"PUB00044763",
"PUB00044764"
] | [
"2656408",
"1355084",
"15292150",
"11914349"
] | [
"Nucleotide sequence of the F plasmid transfer gene, traH: identification of a new gene and a promoter within the transfer operon.",
"Characterization, localization, and sequence of F transfer region products: the pilus assembly gene product TraW and a new product, TrbI.",
"Tra proteins characteristic of F-like... | [
1989,
1992,
2004,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2968,
18,
17
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Type IV conjugative transfer system protein TraH | Type IV conjugative transfer system protein TraH | T4SS_TraH | 3 |
IPR010928 | 10,928 | Tyrosinase co-factor MelC1 | MelC1 | Family | 1,080 | false | false | This family consists of several tyrosinase co-factor MELC1 proteins from a number of Streptomyces species. The melanin operon (melC) of Streptomyces antibioticus contains two genes, melC1 and melC2 (apotyrosinase). It is thought that MelC1 forms a transient binary complex with the downstream apotyrosinase MelC2 to faci... | [
"GO:0005507",
"GO:0042438"
] | [
"copper ion binding",
"melanin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF06236"
] | [
"MelC1"
] | [
1080
] | 1 | [] | [] | [] | 0 | [
"1wx2",
"1wx4",
"1wx5",
"1wxc",
"2ahk",
"2ahl",
"2zmx",
"2zmy",
"2zmz",
"2zwd",
"2zwe",
"2zwf",
"2zwg",
"3aws",
"3awt",
"3awu",
"3awv",
"3aww",
"3awx",
"3awy",
"3awz",
"3ax0",
"5z0d",
"5z0e",
"5z0f",
"5z0g",
"5z0h",
"5z0i",
"5z0j",
"5z0k",
"5z0l",
"5z0m"... | 35 | [
"PUB00012298"
] | [
"8360164"
] | [
"Mutational study of Streptomyces tyrosinase trans-activator MelC1. MelC1 is likely a chaperone for apotyrosinase."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
1080
] | 1 | [] | [] | 0 | true | Family | Tyrosinase co-factor MelC1 | Tyrosinase co-factor MelC1 | MelC1 | 6 |
IPR010929 | 10,929 | CDR ABC transporter | PDR_CDR_ABC | Domain | 14,887 | false | false | In yeast, the PDR and CDR ABC transporters display extensive sequence homology, and confer resistance to several anti-fungal compounds by actively transporting their substrates out of the cell. These transporters have two homologous halves, each with an N-terminal intracellular hydrophilic region that contains an ATP-b... | [
"GO:0005524",
"GO:0042626",
"GO:0055085",
"GO:0016020"
] | [
"ATP binding",
"ATPase-coupled transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF06422"
] | [
"PDR_CDR"
] | [
14887
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-DDI-1369062",
"R-DDI-8964058"
] | [
"REACTOME:R-DDI-1369062",
"REACTOME:R-DDI-8964058"
] | 2 | [
"7p03",
"7p04",
"7p05",
"7p06",
"9iuk",
"9iul",
"9ium"
] | 7 | [
"PUB00004290",
"PUB00014769",
"PUB00014928",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"9872322",
"9873074",
"12709320",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"Functional similarities and differences between Candida albicans Cdr1p and Cdr2p transporters.",
"ABC tra... | [
1998,
1999,
2003,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2001
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
7,
14878,
2
] | 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)"
] | [
4,
8,
2
] | 3 | true | Domain | CDR ABC transporter | CDR ABC transporter | PDR_CDR_ABC | 1 |
IPR010930 | 10,930 | Flagellar basal-body/hook protein, C-terminal domain | Flg_bb/hook_C_dom | Domain | 66,728 | false | false | This functionally uncharacterised domain is found in the C terminus of flagellar basal-body rod and flagellar hook proteins in which is often present at the extreme N terminus. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06429"
] | [
"Flg_bbr_C"
] | [
66728
] | 1 | [] | [] | [] | 0 | [
"3a69",
"4ut1",
"5jxl",
"5npy",
"5wrh",
"6jzr",
"6jzt",
"6k3i",
"6k9q",
"6kfk",
"7bin",
"7cbm",
"7cg0",
"7cgb",
"7cgo",
"7e80",
"7e82",
"7nvg",
"8wk3",
"8wki",
"8wkk",
"8wkq",
"8wl2",
"8wlh",
"8wln",
"8wlp",
"8wlq",
"8wlt",
"8wo5",
"8woe",
"8z5s",
"8z5u"... | 39 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
65886,
2,
85,
755
] | 4 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Domain | Flagellar basal-body/hook protein, C-terminal domain | Flagellar basal-body/hook protein, C-terminal domain | Flg_bb/hook_C_dom | 8 |
IPR010931 | 10,931 | Lactococcus lactis RepB, C-terminal | L_lactis_RepB_C | Domain | 557 | false | false | This entry represents the C-terminal region of RepB proteins from Lactococcus lactis. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06430"
] | [
"L_lactis_RepB_C"
] | [
557
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
556,
1
] | 2 | [] | [] | 0 | true | Domain | Lactococcus lactis RepB, C-terminal | Lactococcus lactis RepB, C-terminal | L_lactis_RepB_C | 4 |
IPR010933 | 10,933 | NADH dehydrogenase subunit 2, C-terminal | NADH_DH_su2_C | Domain | 68,943 | false | false | This entry represents the C-terminal region specific to the animal NADH dehydrogenase subunit 2 protein, also known as NADH-ubiquinone oxidoreductase chain 2. This protein is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyses electron transfer from NADH through... | [
"GO:0008137",
"GO:0006120"
] | [
"NADH dehydrogenase (ubiquinone) activity",
"mitochondrial electron transport, NADH to ubiquinone"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF06444"
] | [
"NADH_dehy_S2_C"
] | [
68943
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"7.1.1.2",
"PWY-3781",
"PWY-4302",
"PWY-5083",
"PWY-6692",
"R-DME-5419276",
"R-DME-611105",
"R-DME-6799198",
"R-DRE-611105",
"R-GGA-5419276",
"R-GGA-611105",
"R-GGA-6799198",
"R-HSA-5419276",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9837999",
"R-MMU-5419276",
"R-MMU-611105",
"R-MM... | [
"EC:7.1.1.2",
"METACYC:PWY-3781",
"METACYC:PWY-4302",
"METACYC:PWY-5083",
"METACYC:PWY-6692",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DRE-611105",
"REACTOME:R-GGA-5419276",
"REACTOME:R-GGA-611105",
"REACTOME:R-GGA-6799198",
"REACTOME:R-HSA-541... | 25 | [
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtc",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6q9b",
"6qa9",
"6qbx",
"6qc2",
"6qc3",
"6qc4",
"6qc5",
"6qc6",
"6qc7",
"6qc8",
"6qc9",
"6qca",
"6qcf",
"6zka",
"6zkb",
"6zkc",
"6zkd",
"6zke",
"6zkf"... | 209 | [
"PUB00103885"
] | [
"16996290"
] | [
"Mutated ND2 impairs mitochondrial complex I assembly and leads to Leigh syndrome."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillus yapensis",
"Opisthokonta"
] | [
1,
68942
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
14,
977,
24,
11
] | 5 | true | Domain | NADH dehydrogenase subunit 2, C-terminal | NADH dehydrogenase subunit 2, C-terminal | NADH_DH_su2_C | 9 |
IPR010935 | 10,935 | SMCs flexible hinge | SMC_hinge | Domain | 39,205 | false | false | This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that its precise structure is an essential determinant of the specificity of the DNA-protein interaction [ ]. This... | [
"GO:0005515",
"GO:0005524",
"GO:0051276",
"GO:0005694"
] | [
"protein binding",
"ATP binding",
"chromosome organization",
"chromosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"SMART"
] | [
"PF06470",
"SM00968"
] | [
"SMC_hinge",
"SMC_hinge"
] | [
38586,
36750
] | 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-2467813",
"R-BTA-2468052",
"R-BTA-2470946",
"R-BTA-2500257",
"R-BTA-3108214",
"R-CEL-2299718",
"R-CEL-2468052",
"R-CEL-2470946",
"R-CEL-2500257",
"R-CEL-3108214",
"R-DDI-2299718",
"R-DDI-2468052",
"R-DDI-2470946",
"R-DDI-2500257",
"R-DDI-2514853",
"R-DDI-3108214",
"R-HSA-12216... | [
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2468052",
"REACTOME:R-BTA-2470946",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-3108214",
"REACTOME:R-CEL-2299718",
"REACTOME:R-CEL-2468052",
"REACTOME:R-CEL-2470946",
"REACTOME:R-CEL-2500257",
"REACTOME:R-CEL-3108214",
"REACTOME:R-DDI-2299718",
"REACTOM... | 47 | [
"1gxj",
"1gxk",
"1gxl",
"2wd5",
"3l51",
"3nwc",
"4rsi",
"4rsj",
"4u4p",
"5h69",
"6n64",
"6wg3",
"6wg4",
"6wg6",
"6wge",
"6yuf",
"6yvd",
"6yvu",
"6yvv",
"7dg5",
"7ogt",
"7q2x",
"7q2y",
"7qen",
"7w1m",
"9f5w"
] | 26 | [
"PUB00012621",
"PUB00154981"
] | [
"12411491",
"23653445"
] | [
"Hinge-mediated dimerization of SMC protein is essential for its dynamic interaction with DNA.",
"Factors required for activation of urease as a virulence determinant in Cryptococcus neoformans."
] | [
2002,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
717,
16029,
22089,
370
] | 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... | [
27,
5,
10,
38,
27,
18,
4,
13,
24,
4,
4,
52
] | 12 | true | Domain | SMCs flexible hinge | SMCs flexible hinge | SMC_hinge | 5 |
IPR010938 | 10,938 | Protein of unknown function DUF1131 | DUF1131 | Family | 1,518 | false | false | This entry consists of several hypothetical bacterial proteins of unknown function. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF007990",
"PF06572"
] | [
"PRK10718.1",
"DUF1131"
] | [
1343,
1518
] | 2 | [] | [] | [] | 0 | [
"2qzb"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
1515,
2,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Protein of unknown function DUF1131 | Protein of unknown function DUF1131 | DUF1131 | 9 |
IPR010940 | 10,940 | Magnesium-protoporphyrin IX methyltransferase, C-terminal | Mg_prot_MeTrfase_C | Domain | 1,732 | false | false | This entry represents the C terminus (approximately 100 residues) of bacterial and eukaryotic magnesium-protoporphyrin IX methyltransferase ( ). This converts magnesium-protoporphyrin IX to magnesium-protoporphyrin IX metylester using S-adenosyl-L-methionine as a cofactor [ ]. | [
"GO:0046406",
"GO:0015995"
] | [
"magnesium protoporphyrin IX methyltransferase activity",
"chlorophyll biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF07109"
] | [
"Mg-por_mtran_C"
] | [
1732
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.1.1.11",
"PWY-5531",
"PWY-7159"
] | [
"EC:2.1.1.11",
"METACYC:PWY-5531",
"METACYC:PWY-7159"
] | 3 | [
"4qdj",
"4qdk"
] | 2 | [
"PUB00013004"
] | [
"8071204"
] | [
"Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"freshwater sediment metagenome"
] | [
1053,
678,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
5,
3
] | 3 | true | Domain | Magnesium-protoporphyrin IX methyltransferase, C-terminal | Magnesium-protoporphyrin IX methyltransferase, C-terminal | Mg_prot_MeTrfase_C | 4 |
IPR010941 | 10,941 | Poly-beta-hydroxybutyrate polymerase, N-terminal domain | PhaC_N | Domain | 9,984 | false | false | This entry represents the central domain of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulphur, becomes limiti... | [
"GO:0042619"
] | [
"poly-hydroxybutyrate biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF07167"
] | [
"PhaC_N"
] | [
9984
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
"PWY-5794"... | [
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"METACYC:PWY-53... | 219 | [
"5xav",
"6k3c",
"9knj",
"9knk",
"9knl"
] | 5 | [
"PUB00013025"
] | [
"10427049"
] | [
"Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
25,
9862,
22,
75
] | 4 | [] | [] | 0 | true | Domain | Poly-beta-hydroxybutyrate polymerase, N-terminal domain | Poly-beta-hydroxybutyrate polymerase, N-terminal domain | PhaC_N | 1 |
IPR010943 | 10,943 | Xanthosine phosphorylase | Xanthosine_phosphorylase | Family | 933 | false | false | This entry represents purine nucleotide phosphorylases in the gammaproteobacteria. The gene is part of an operon for the degradation of xanthosine and is induced by xanthosine [ ]. The enzyme is also capable of acting on inosine and guanosine, but not adenosine. | [
"GO:0004731",
"GO:0055086",
"GO:0005737"
] | [
"purine-nucleoside phosphorylase activity",
"nucleobase-containing small molecule metabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01699"
] | [
"XAPA"
] | [
933
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP"
] | [
"GenProp1235",
"GenProp1255",
"GenProp1278",
"GenProp1469",
"GenProp1528",
"GenProp1611",
"GenProp1753"
] | [
"GP:GenProp1235",
"GP:GenProp1255",
"GP:GenProp1278",
"GP:GenProp1469",
"GP:GenProp1528",
"GP:GenProp1611",
"GP:GenProp1753"
] | 7 | [
"1yqq",
"1yqu",
"1yr3",
"3odg"
] | 4 | [
"PUB00002280"
] | [
"7559336"
] | [
"Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli."
] | [
1995
] | 1 | [
"IPR011268"
] | [] | 1 | 0 | 1 | [
"Beauveria bassiana D1-5",
"Pseudomonadota"
] | [
1,
932
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Xanthosine phosphorylase | Xanthosine phosphorylase | Xanthosine_phosphorylase | 5 |
IPR010944 | 10,944 | AMP nucleosidase, putative | AMN-like | Family | 1,327 | false | false | AMP nucleosidase (AMN) catalyses the hydrolysis of AMP to form adenine and ribose 5-phosphate. It is only found in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation [ ]. The gene for AMP nucleosidase from Escherichia coli (amn) encodes a protein of 483 amino acids. A... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01721"
] | [
"AMN-like"
] | [
1327
] | 1 | [] | [] | [] | 0 | [
"1ybf"
] | 1 | [
"PUB00013804",
"PUB00031378"
] | [
"2690948",
"15296732"
] | [
"Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli.",
"Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases."
] | [
1989,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
1305,
3,
19
] | 3 | [] | [] | 0 | true | Family | AMP nucleosidase, putative | AMP nucleosidase, putative | AMN-like | 7 |
IPR010945 | 10,945 | Malate dehydrogenase, type 2 | Malate_DH_type2 | Family | 20,555 | false | false | Malate dehydrogenases catalyse the interconversion of malate and oxaloacetate using dinucleotide cofactors [ ]. The enzymes in this entry are found in archaea, bacteria and eukaryotes and fall into two distinct groups. The first group are cytoplasmic, NAD-dependent enzymes which participate in the citric acid cycle ( )... | [
"GO:0016615",
"GO:0006108"
] | [
"malate dehydrogenase activity",
"malate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_01517",
"PTHR23382",
"TIGR01759"
] | [
"Malate_dehydrog_2",
"",
"MalateDH-SF1"
] | [
8284,
20530,
13296
] | 3 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.37",
"GenProp0033",
"GenProp1584",
"GenProp1612",
"GenProp1693",
"PWY-1622",
"PWY-5392",
"PWY-561",
"PWY-5690",
"PWY-6728",
"PWY-6969",
"PWY-7115",
"PWY-7383",
"PWY-8086",
"R-BTA-9856872",
"R-CEL-9856872",
"R-DDI-9856872",
"R-GGA-352875",
"R-HSA-9856872",
"R-M... | [
"EC:1.1.1",
"EC:1.1.1.37",
"GP:GenProp0033",
"GP:GenProp1584",
"GP:GenProp1612",
"GP:GenProp1693",
"METACYC:PWY-1622",
"METACYC:PWY-5392",
"METACYC:PWY-561",
"METACYC:PWY-5690",
"METACYC:PWY-6728",
"METACYC:PWY-6969",
"METACYC:PWY-7115",
"METACYC:PWY-7383",
"METACYC:PWY-8086",
"REACTOM... | 24 | [
"1b8p",
"1b8u",
"1b8v",
"1bdm",
"1bmd",
"1civ",
"1iz9",
"1wze",
"1wzi",
"1y7t",
"2cvq",
"3d5t",
"3fi9",
"4h7p",
"4i1i",
"4kde",
"4kdf",
"4mdh",
"4tvo",
"4uul",
"4uum",
"4uun",
"4uuo",
"4uup",
"5a1t",
"5kvv",
"5mdh",
"5nue",
"5nuf",
"6itk",
"6pbl",
"6um4"... | 37 | [
"PUB00013757",
"PUB00019781",
"PUB00021232",
"PUB00023558",
"PUB00023967",
"PUB00027655"
] | [
"10194350",
"10075524",
"8471603",
"10206992",
"10196131",
"7849603"
] | [
"Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form.",
"Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and... | [
1999,
1999,
1993,
1999,
1999,
1994
] | 6 | [
"IPR001557"
] | [
"IPR011272",
"IPR011273",
"IPR011274"
] | 1 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified Candidatus Thermoprofundales",
"unclassified sequences"
] | [
7102,
13281,
1,
7,
164
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
22,
1,
18,
2,
11,
4,
8,
9,
29
] | 9 | true | Family | Malate dehydrogenase, type 2 | Malate dehydrogenase, type 2 | Malate_DH_type2 | 4 |
IPR010946 | 10,946 | Geranylgeranylglyceryl phosphate synthase | GGGP_synth | Family | 1,596 | false | false | This entry represents geranylgeranylglyceryl phosphate synthase from bacteroidetes and archaea. It catalyses the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P) [ ]. In archaea, it catalyses the first committed step in the synthesis of ether... | [
"GO:0000287",
"GO:0047294",
"GO:0006650",
"GO:0005737"
] | [
"magnesium ion binding",
"phosphoglycerol geranylgeranyltransferase activity",
"glycerophospholipid metabolic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"NCBIFAM"
] | [
"TIGR01769"
] | [
"GGGP"
] | [
1596
] | 1 | [
"EC",
"METACYC"
] | [
"2.5.1.41",
"PWY-6349"
] | [
"EC:2.5.1.41",
"METACYC:PWY-6349"
] | 2 | [
"4jej",
"4mm1",
"5ndy",
"5nez",
"5nf1",
"6jo3",
"6nke"
] | 7 | [
"PUB00013822",
"PUB00088866"
] | [
"11732904",
"24684232"
] | [
"Geranylgeranylglyceryl phosphate synthase. Characterization of the recombinant enzyme from Methanobacterium thermoautotrophicum.",
"A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary struc... | [
2001,
2014
] | 2 | [
"IPR008205"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
496,
1048,
2,
50
] | 4 | [] | [] | 0 | true | Family | Geranylgeranylglyceryl phosphate synthase | Geranylgeranylglyceryl phosphate synthase | GGGP_synth | 7 |
IPR010948 | 10,948 | TonB-dependent lactoferrin/transferrin receptor | TonB_lacto/transferrin_rcpt | Family | 447 | false | false | This family of TonB-dependent receptors are responsible for import of iron from the mammalian iron carriers lactoferrin and transferrin across the outer membrane. These receptors are found only in bacteria which can infect mammals, examples are Moraxella, Mannheimia, Neisseria, Actinobacillus, Pasteurella, Haemophilus ... | [
"GO:0015091",
"GO:0006826",
"GO:0019867"
] | [
"ferric iron transmembrane transporter activity",
"iron ion transport",
"outer membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01776"
] | [
"TonB-tbp-lbp"
] | [
447
] | 1 | [] | [] | [] | 0 | [
"3v89",
"3v8x"
] | 2 | [
"PUB00087366",
"PUB00087367",
"PUB00087368"
] | [
"25286931",
"12399483",
"9620956"
] | [
"The structure of lactoferrin-binding protein B from Neisseria meningitidis suggests roles in iron acquisition and neutralization of host defences.",
"Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB.",
"Preparation and characterization of Ne... | [
2014,
2002,
1998
] | 3 | [
"IPR010949"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
447
] | 1 | [] | [] | 0 | true | Family | TonB-dependent lactoferrin/transferrin receptor | TonB-dependent lactoferrin/transferrin receptor | TonB_lacto/transferrin_rcpt | 4 |
IPR010949 | 10,949 | TonB-dependent haemoglobin/transferrin/lactoferrin receptor | TonB_Hb/transfer/lactofer_rcpt | Family | 6,857 | false | false | This entry represents a family of TonB-dependent outer membrane receptor/transporters acting on iron-containing proteins such as haemoglobin, transferrin and lactoferrin. It contains the haem/haemoglobin receptor family and the transferrin/lactoferrin receptor family. Nearly all of the species, which contain sequences ... | [
"GO:0022857",
"GO:0055085",
"GO:0019867"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"outer membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01786"
] | [
"TonB-hemlactrns"
] | [
6857
] | 1 | [] | [] | [] | 0 | [
"3csl",
"3csn",
"3ddr",
"3fhh",
"3v89",
"3v8x",
"5c58",
"8the",
"9dhe",
"9dir",
"9dis"
] | 11 | [
"PUB00095094"
] | [
"22327295"
] | [
"Structural basis for iron piracy by pathogenic Neisseria."
] | [
2012
] | 1 | [
"IPR039426"
] | [
"IPR010948",
"IPR011276"
] | 1 | 2 | 0 | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
6828,
4,
25
] | 3 | [] | [] | 0 | true | Family | TonB-dependent haemoglobin/transferrin/lactoferrin receptor | TonB-dependent haemoglobin/transferrin/lactoferrin receptor | TonB_Hb/transfer/lactofer_rcpt | 8 |
IPR010950 | 10,950 | Chorismate mutase, archaeal | Chorismate_mutase_arc | Domain | 288 | false | false | This entry represents archaeal chorismate mutases. Chorismate mutase catalyses the conversion of chorismate into prephenate which is subsequently converted into either phenylalanine or tyrosine. In Sulfolobus solfataricus this gene is found as a fusion with prephenate dehydrogenase ( ) which is the next enzyme in the t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01791"
] | [
"CM_archaeal"
] | [
288
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00070219"
] | [
"19082689"
] | [
"Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus."
] | [
2009
] | 1 | [
"IPR002701"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
274,
11,
3
] | 3 | [] | [] | 0 | true | Domain | Chorismate mutase, archaeal | Chorismate mutase, archaeal | Chorismate_mutase_arc | 8 |
IPR010953 | 10,953 | Citrate synthase, type I | Citrate_synthase_typ-I | Family | 16,852 | false | false | This entry describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Ps... | [
"GO:0005737"
] | [
"cytoplasm"
] | [
"cellular_component"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR01798",
"cd06114"
] | [
"cit_synth_I",
"EcCS_like"
] | [
16752,
15503
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP"
] | [
"2.3.3.16",
"GenProp0033",
"GenProp1265",
"GenProp1267",
"GenProp1710"
] | [
"EC:2.3.3.16",
"GP:GenProp0033",
"GP:GenProp1265",
"GP:GenProp1267",
"GP:GenProp1710"
] | 5 | [
"1nxe",
"1nxg",
"1owb",
"1owc",
"2h12",
"3msu",
"4e6y",
"4g6b",
"4jad",
"4jae",
"4jaf",
"4jag",
"4tvm",
"4xgh",
"6zu0",
"7e8n"
] | 16 | [] | [] | [] | [] | 0 | [
"IPR024176"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4,
16447,
199,
202
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Citrate synthase, type I | Citrate synthase, type I | Citrate_synthase_typ-I | 2 |
IPR010954 | 10,954 | Chorismate mutase, Firmicutes/Deinococcus | Chorismate_mutase_GmP-bac | Domain | 1,706 | false | false | This entry represents the chorismate mutase (CM) domains N-terminally fused to the first enzyme in the chorismate pathway, 2-dehydro-3-deoxyphosphoheptanoate aldolase (DAHP synthetase, AroA) which are found in some Gram-positive species and Deinococcus. Only in Deinococcus, where this domain is the sole CM domain in th... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01801"
] | [
"CM_A"
] | [
1706
] | 1 | [] | [] | [] | 0 | [
"2d8d",
"2d8e",
"3nvt",
"3tfc",
"5gmu",
"5go2",
"5j6f"
] | 7 | [] | [] | [] | [] | 0 | [
"IPR002701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"human gut metagenome"
] | [
1703,
2,
1
] | 3 | [] | [] | 0 | true | Domain | Chorismate mutase, Firmicutes/Deinococcus | Chorismate mutase, Firmicutes/Deinococcus | Chorismate_mutase_GmP-bac | 4 |
IPR010957 | 10,957 | Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain | G/b/e-P-prot_chorismate_mutase | Domain | 4,795 | false | false | This entry primarily represents the chorismate mutase domain of the gamma, beta and epsilon proteobacterial 'P-protein', which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. | [
"GO:0004106",
"GO:0009094",
"GO:0005737"
] | [
"chorismate mutase activity",
"L-phenylalanine biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01807"
] | [
"CM_P2"
] | [
4795
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.51",
"5.4.99.5",
"PWY-3461",
"PWY-3462",
"PWY-6120",
"PWY-6627",
"PWY-7432",
"PWY-7626"
] | [
"EC:4.2.1.51",
"EC:5.4.99.5",
"METACYC:PWY-3461",
"METACYC:PWY-3462",
"METACYC:PWY-6120",
"METACYC:PWY-6627",
"METACYC:PWY-7432",
"METACYC:PWY-7626"
] | 8 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR002701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_68_B04"
] | [
4653,
23,
118,
1
] | 4 | [] | [] | 0 | true | Domain | Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain | Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain | G/b/e-P-prot_chorismate_mutase | 7 |
IPR010958 | 10,958 | Chorismate mutase, high GC Gram-positive bacteria/archaeal | Chorismate_mutase_highGC-bac | Domain | 2,285 | false | false | This entry represents prokaryotic, primarily monofunctional, chorismate mutases of the AroQ class from high GC Gram-positive bacteria and archaea. In Corynebacterium and Pyrococcus, these are the apparently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genome... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01808"
] | [
"CM_M_hiGC-arch"
] | [
2285
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.99.5",
"PWY-3461",
"PWY-3462",
"PWY-6120",
"PWY-6627",
"PWY-7626"
] | [
"EC:5.4.99.5",
"METACYC:PWY-3461",
"METACYC:PWY-3462",
"METACYC:PWY-6120",
"METACYC:PWY-6627",
"METACYC:PWY-7626"
] | 6 | [
"1ybz",
"2qbv",
"2vkl",
"2w19",
"2w1a",
"5ckx",
"5hub",
"5hud",
"5mpv",
"6ygt"
] | 10 | [] | [] | [] | [] | 0 | [
"IPR002701"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Rhodosorus marinus",
"metagenomes"
] | [
15,
2265,
1,
4
] | 4 | [] | [] | 0 | true | Domain | Chorismate mutase, high GC Gram-positive bacteria/archaeal | Chorismate mutase, high GC Gram-positive bacteria/archaeal | Chorismate_mutase_highGC-bac | 3 |
IPR010960 | 10,960 | Flavocytochrome c | Flavocytochrome_c | Family | 6,732 | false | false | This entry describes a family of redox proteins related to the succinate dehydrogenases and fumarate reductases (FRDs) of Escherichia coli, mitochondria, and other well-characterised systems. A member of this family from Shewanella frigidimarina (strain NCIMB 400) is characterised as a water-soluble periplasmic protein... | [
"GO:0010181",
"GO:0016491"
] | [
"FMN binding",
"oxidoreductase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01813"
] | [
"flavo_cyto_c"
] | [
6732
] | 1 | [] | [] | [] | 0 | [
"1d4c",
"1d4d",
"1d4e",
"1e39",
"1jrx",
"1jry",
"1jrz",
"1kss",
"1ksu",
"1lj1",
"1m64",
"1p2e",
"1p2h",
"1q9i",
"1qjd",
"1qo8",
"1y0p",
"2b7r",
"2b7s",
"5glg",
"5zyn",
"6ku6",
"6t85",
"6t86",
"6t87",
"6t88"
] | 26 | [
"PUB00097228",
"PUB00097229"
] | [
"23078170",
"33107907"
] | [
"Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR-1.",
"A new water-soluble bacterial NADH: fumarate oxidoreductase."
] | [
2012,
2020
] | 2 | [
"IPR050315"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
3867,
2851,
14
] | 3 | [
"Caenorhabditis elegans",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
2,
1
] | 4 | true | Family | Flavocytochrome c | Flavocytochrome c | Flavocytochrome_c | 4 |
IPR010961 | 10,961 | Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase | 4pyrrol_synth_NH2levulA_synth | Domain | 9,193 | false | false | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including vitamin B12, haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [ ]. The first stage in tetrapyrrole synthesi... | [
"GO:0003870",
"GO:0030170",
"GO:0033014"
] | [
"5-aminolevulinate synthase activity",
"pyridoxal phosphate binding",
"tetrapyrrole biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01821"
] | [
"5aminolev_synth"
] | [
9193
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.37",
"GenProp0223",
"GenProp1525",
"PWY-5189",
"PWY-7536",
"R-BTA-189451",
"R-DRE-189451",
"R-GGA-421984",
"R-HSA-189451",
"R-HSA-1989781",
"R-HSA-2151201",
"R-HSA-9837999",
"R-MMU-189451",
"R-MMU-9837999",
"R-RNO-189451",
"R-RNO-9837999",
"R-SCE-189451",
"R-SPO-189451"
] | [
"EC:2.3.1.37",
"GP:GenProp0223",
"GP:GenProp1525",
"METACYC:PWY-5189",
"METACYC:PWY-7536",
"REACTOME:R-BTA-189451",
"REACTOME:R-DRE-189451",
"REACTOME:R-GGA-421984",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-189451"... | 18 | [
"2bwn",
"2bwo",
"2bwp",
"5qqq",
"5qqr",
"5qqs",
"5qqt",
"5qqu",
"5qqv",
"5qqw",
"5qqx",
"5qqy",
"5qqz",
"5qr0",
"5qr1",
"5qr2",
"5qr3",
"5qr4",
"5qr5",
"5qr6",
"5qr7",
"5qr8",
"5qr9",
"5qra",
"5qrb",
"5qrc",
"5qrd",
"5qre",
"5qt3",
"5txr",
"5txt",
"6hrh"... | 36 | [
"PUB00009744",
"PUB00035496",
"PUB00035498"
] | [
"11215515",
"17227226",
"16564539"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Tetrapyrrole biosynthesis in higher plants.",
"Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis."
] | [
2000,
2007,
2006
] | 3 | [
"IPR004839"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Thermococcaceae",
"metagenomes",
"uncultured Caudovirales phage"
] | [
4046,
5117,
2,
27,
1
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
2,
6,
9,
1,
11,
1,
1
] | 8 | true | Domain | Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase | Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase | 4pyrrol_synth_NH2levulA_synth | 2 |
IPR010962 | 10,962 | Putative 8-amino-7-oxononanoate synthase, Archaea/Firmicutes type | AONS_Archaea/Firmicutes | Family | 1,907 | false | false | This entry represents a group of putative 8-amino-7-oxononanoate synthases (AONS) mainly from Firmicutes and Archaea. They are related to the 8-amino-7-oxononanoate synthases from Proteobacteria ( ), which is a pyridoxal 5'-phosphate-dependent enzyme that catalyses the decarboxylative condensation of L-alanine with pim... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01825"
] | [
"gly_Cac_T_rel"
] | [
1907
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.47",
"PWY-6519",
"PWY-6578",
"PWY-7147",
"PWY-8203"
] | [
"EC:2.3.1.47",
"METACYC:PWY-6519",
"METACYC:PWY-6578",
"METACYC:PWY-7147",
"METACYC:PWY-8203"
] | 5 | [
"7poa",
"7pob",
"7poc",
"8s1y"
] | 4 | [
"PUB00024209"
] | [
"10642176"
] | [
"Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Phytophthora kernoviae 00238/432",
"ecological metagenomes"
] | [
61,
1838,
1,
7
] | 4 | [] | [] | 0 | true | Family | Putative 8-amino-7-oxononanoate synthase, Archaea/Firmicutes type | Putative 8-amino-7-oxononanoate synthase, Archaea/Firmicutes type | AONS_Archaea/Firmicutes | 3 |
IPR010964 | 10,964 | Peptidase M20A, peptidase V-related | M20A_pepV-rel | Family | 7,001 | false | false | This entry consists of Beta-Ala-Xaa dipeptidase (peptidase V, PepV) from Lactobacillus delbrueckii [ ] and other putative bacterial zinc dipeptidases belonging to the MEROPS peptidase family M20 (clan MH), subfamily M20A. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monome... | [
"GO:0008270",
"GO:0016805"
] | [
"zinc ion binding",
"dipeptidase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01887"
] | [
"dipeptidaselike"
] | [
7001
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.4.13.-",
"PWY-6842",
"PWY-7569",
"PWY-7570"
] | [
"EC:3.4.13.-",
"METACYC:PWY-6842",
"METACYC:PWY-7569",
"METACYC:PWY-7570"
] | 4 | [
"1lfw",
"3khx",
"3khz",
"3ki9"
] | 4 | [
"PUB00013828",
"PUB00079892"
] | [
"12176387",
"16962986"
] | [
"Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides.",
"Characterization and kinetic analysis of enzyme-substrate recognition by three recombinant lactococcal PepVs."
] | [
2002,
2006
] | 2 | [
"IPR002933"
] | [
"IPR011291"
] | 1 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Podoviridae sp. ctxJ29",
"metagenomes"
] | [
6976,
7,
1,
17
] | 4 | [] | [] | 0 | true | Family | Peptidase M20A, peptidase V-related | Peptidase M20A, peptidase V-related | M20A_pepV-rel | 3 |
IPR010965 | 10,965 | HesB-related, selonoprotein | HesB-rel_seleno | Family | 168 | false | false | This entry represents a family of small proteins related to HesB and its close homologues, which are likely to be involved in iron-sulphur cluster assembly. Several members are selenoproteins, with a TGA codon and Sec residue that aligns to the conserved Cys of the HesB domain. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01911"
] | [
"HesB_rel_seleno"
] | [
168
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Methanocaldococcus",
"bioreactor metagenome"
] | [
163,
4,
1
] | 3 | [] | [] | 0 | true | Family | HesB-related, selonoprotein | HesB-related, selonoprotein | HesB-rel_seleno | 6 |
IPR010966 | 10,966 | Na(+)-translocating NADH-quinone reductase subunit B | NqrB | Family | 4,384 | false | false | This entry represents the NqrB subunit of the six-protein (NqrA to NqrF), membrane-associated Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria [ ]. The Nqr complex catalyses the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport... | [
"GO:0010181",
"GO:0016655",
"GO:0022904",
"GO:0016020"
] | [
"FMN binding",
"oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor",
"respiratory electron transport chain",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM",
"PIRSF",
"NCBIFAM"
] | [
"MF_00426",
"NF003756",
"PIRSF016055",
"TIGR01937"
] | [
"NqrB",
"PRK05349.1",
"NADH-UbQ_OxRdtase_B_su",
"nqrB"
] | [
4338,
4309,
4112,
4369
] | 4 | [
"EC",
"GP"
] | [
"7.2.1.1",
"GenProp0129"
] | [
"EC:7.2.1.1",
"GP:GenProp0129"
] | 2 | [
"7xk3",
"7xk4",
"7xk5",
"7xk6",
"7xk7",
"8a1t",
"8a1u",
"8a1v",
"8a1w",
"8a1x",
"8a1y",
"8acw",
"8acy",
"8ad0",
"8evu",
"8ew3",
"9lrr",
"9u5g",
"9ud2",
"9ud3",
"9ud4",
"9ud5",
"9ud6",
"9ud8",
"9ud9",
"9uda",
"9udf",
"9udg",
"9uuu"
] | 29 | [
"PUB00005074",
"PUB00015145",
"PUB00015146",
"PUB00043561",
"PUB00045437"
] | [
"1470679",
"11163785",
"11888296",
"10940377",
"18394423"
] | [
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"FMN is covalently attached to a threonine residue in the NqrB and NqrC subunits of Na(+)-translocating NADH-quinone reductase from Vibrio alginolyticus.",
"Purification and characterization of the recombinant Na(+)-translocating NADH:quin... | [
1992,
2001,
2002,
2000,
2008
] | 5 | [
"IPR004338"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4321,
5,
58
] | 3 | [] | [] | 0 | true | Family | Na(+)-translocating NADH-quinone reductase subunit B | Na(+)-translocating NADH-quinone reductase subunit B | NqrB | 1 |
IPR010967 | 10,967 | Na(+)-translocating NADH-quinone reductase subunit E | NqrE | Family | 4,215 | false | false | This entry represents the Na(+)-translocating E subunit from NADH:ubiquinone oxidoreductase. NADH can be oxidized by the respiratory chain of bacteria via NADH:quinone oxidoreductases that belong to three distinct enzyme families: NDH-1, NDH-2, and NQR. The NQR-type enzymes are sodium-motive NADH:quinone oxidoreductase... | [
"GO:0016655",
"GO:0022904",
"GO:0009276",
"GO:0016020"
] | [
"oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor",
"respiratory electron transport chain",
"Gram-negative-bacterium-type cell wall",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00429",
"TIGR01940"
] | [
"NqrE",
"nqrE"
] | [
4031,
4214
] | 2 | [
"EC",
"GP"
] | [
"7.2.1.1",
"GenProp0129"
] | [
"EC:7.2.1.1",
"GP:GenProp0129"
] | 2 | [
"7xk3",
"7xk4",
"7xk5",
"7xk6",
"7xk7",
"8a1t",
"8a1u",
"8a1v",
"8a1w",
"8a1x",
"8a1y",
"8acw",
"8acy",
"8ad0",
"8evu",
"8ew3",
"9lrr",
"9u5g",
"9ud2",
"9ud3",
"9ud4",
"9ud5",
"9ud6",
"9ud8",
"9ud9",
"9uda",
"9udf",
"9udg",
"9uuu"
] | 29 | [
"PUB00005074",
"PUB00014919",
"PUB00043561",
"PUB00045437"
] | [
"1470679",
"15063750",
"10940377",
"18394423"
] | [
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae.",
"The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.",
"A... | [
1992,
2004,
2000,
2008
] | 4 | [
"IPR003667"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4144,
5,
66
] | 3 | [] | [] | 0 | true | Family | Na(+)-translocating NADH-quinone reductase subunit E | Na(+)-translocating NADH-quinone reductase subunit E | NqrE | 8 |
IPR010968 | 10,968 | Ion-translocating oxidoreductase complex subunit E | RnfE | Family | 6,220 | false | false | The six-subunit complex RnfABCDGE in Rhodobacter capsulatus (Rhodopseudomonas capsulata) encodes a NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation [ ]. A closely related complex in Escherichia coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superox... | [
"GO:0022900",
"GO:0016020"
] | [
"electron transport chain",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00478",
"TIGR01948"
] | [
"RsxE_RnfE",
"rnfE"
] | [
6175,
6159
] | 2 | [
"GP"
] | [
"GenProp0130"
] | [
"GP:GenProp0130"
] | 1 | [
"7zc6",
"8ahx",
"8rb8",
"8rb9",
"8rbm",
"8rbq",
"9eri",
"9erj",
"9erk",
"9erl"
] | 10 | [
"PUB00008135",
"PUB00013513",
"PUB00087510",
"PUB00088392",
"PUB00088393"
] | [
"9492268",
"12773378",
"27114876",
"23269825",
"24045950"
] | [
"Overexpression in Escherichia coli of the rnf genes from Rhodobacter capsulatus--characterization of two membrane-bound iron-sulfur proteins.",
"A reducing system of the superoxide sensor SoxR in Escherichia coli.",
"The role of Rnf in ion gradient formation in Desulfovibrio alaskensis.",
"The Rnf complex of... | [
1998,
2003,
2016,
2012,
2013
] | 5 | [
"IPR003667"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanobacteriota",
"Opisthokonta",
"unclassified sequences"
] | [
6066,
41,
3,
110
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ion-translocating oxidoreductase complex subunit E | Ion-translocating oxidoreductase complex subunit E | RnfE | 6 |
IPR010969 | 10,969 | Cysteine desulfurase-related, unknown function | Cys_dSase-rel_unknwn_funct | Family | 2,652 | false | false | This entry describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N terminus. The functio... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01977"
] | [
"am_tr_V_EF2568"
] | [
2652
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cladocopium goreaui",
"Methanoculleus nereidis",
"Siphoviridae sp. ctub511",
"metagenomes"
] | [
2622,
1,
1,
1,
27
] | 5 | [] | [] | 0 | true | Family | Cysteine desulfurase-related, unknown function | Cysteine desulfurase-related, unknown function | Cys_dSase-rel_unknwn_funct | 5 |
IPR010970 | 10,970 | Cysteine desulfurase, SufS | Cys_dSase_SufS | Family | 26,932 | false | false | Cysteine desulfurases are pyridoxal-phosphate enzymes which catalyse the removal of sulphur from L-cysteine to form L-alanine and elemental sulphur. These enzymes have been shown to play an important role in the biosynthesis of iron-sulphur clusters, thionucleosides in tRNA, thiamine, biotin, lipoate and molydopterin [... | [
"GO:0030170",
"GO:0031071",
"GO:0006534"
] | [
"pyridoxal phosphate binding",
"cysteine desulfurase activity",
"cysteine metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01831",
"TIGR01979",
"cd06453"
] | [
"SufS_aminotrans_5",
"sufS",
"SufS_like"
] | [
1104,
21994,
26932
] | 3 | [
"EC",
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.8.1.7",
"4.4.1.16",
"GenProp0137",
"GenProp1333",
"PWY-6823",
"PWY-6892",
"PWY-7250",
"PWY-7892",
"PWY-8164",
"PWY-8165",
"PWY-8452"
] | [
"EC:2.8.1.7",
"EC:4.4.1.16",
"GP:GenProp0137",
"GP:GenProp1333",
"METACYC:PWY-6823",
"METACYC:PWY-6892",
"METACYC:PWY-7250",
"METACYC:PWY-7892",
"METACYC:PWY-8164",
"METACYC:PWY-8165",
"METACYC:PWY-8452"
] | 11 | [
"1c0n",
"1i29",
"1jf9",
"1kmj",
"1kmk",
"1t3i",
"4lw2",
"4lw4",
"4q75",
"4q76",
"4w91",
"5b7s",
"5b7u",
"5b87",
"5b89",
"5db5",
"5ft4",
"5ft5",
"5ft6",
"5ft8",
"5j8q",
"5vpr",
"5xt5",
"5xt6",
"5zs9",
"5zsk",
"5zso",
"6a6e",
"6a6g",
"6c9e",
"6kfy",
"6kfz"... | 77 | [
"PUB00016898",
"PUB00026361",
"PUB00028013",
"PUB00028014",
"PUB00028015",
"PUB00028016"
] | [
"9914259",
"11827487",
"12382038",
"11498000",
"10329673",
"15379559"
] | [
"Structure, evolution and action of vitamin B6-dependent enzymes.",
"Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation.",
"Bacterial cysteine desulfurases: their function and mechanisms.",
"Incorporation of iron-sulphur cluste... | [
1998,
2002,
2002,
2001,
1999,
2004
] | 6 | [
"IPR016454"
] | [
"IPR022471"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Tupanvirus",
"unclassified sequences"
] | [
832,
24862,
826,
4,
408
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
2,
4,
4
] | 4 | true | Family | Cysteine desulfurase, SufS | Cysteine desulfurase, SufS | Cys_dSase_SufS | 5 |
IPR010971 | 10,971 | Ubiquinone biosynthesis hydroxylase UbiH/COQ6 | UbiH/COQ6 | Family | 26,304 | false | false | This entry represents a family of FAD-dependent hydroxylases (monooxygenases), which are all believed to act in the aerobic ubiquinone biosynthesis pathway [ ]. In Escherichia coli, three enzyme activities have been described: UbiI, UbiH and UbiF [ ]. UbiH and UbiF are similar to one another and form the basis of this ... | [
"GO:0016705",
"GO:0050660",
"GO:0006744"
] | [
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen",
"flavin adenine dinucleotide binding",
"ubiquinone biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01988"
] | [
"Ubi-OHases"
] | [
26304
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.15.45",
"1.14.15.46",
"GenProp0136",
"GenProp1744",
"PDOC01008",
"R-BTA-2142789",
"R-CEL-2142789",
"R-DDI-2142789",
"R-DME-2142789",
"R-DRE-2142789",
"R-HSA-2142789",
"R-MMU-2142789",
"R-RNO-2142789",
"R-SCE-2142789",
"R-SPO-2142789",
"R-XTR-2142789"
] | [
"EC:1.14.15.45",
"EC:1.14.15.46",
"GP:GenProp0136",
"GP:GenProp1744",
"PROSITEDOC:PDOC01008",
"REACTOME:R-BTA-2142789",
"REACTOME:R-CEL-2142789",
"REACTOME:R-DDI-2142789",
"REACTOME:R-DME-2142789",
"REACTOME:R-DRE-2142789",
"REACTOME:R-HSA-2142789",
"REACTOME:R-MMU-2142789",
"REACTOME:R-RNO-... | 16 | [
"4k22",
"4n9x",
"7mwa"
] | 3 | [
"PUB00013761",
"PUB00013831",
"PUB00013848",
"PUB00068672"
] | [
"1339425",
"12721307",
"11583838",
"23709220"
] | [
"Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone.",
"The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis.",
"Ubiquinone... | [
1992,
2003,
2001,
2013
] | 4 | [] | [
"IPR000689",
"IPR011295"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
21795,
4319,
190
] | 3 | [
"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",... | [
9,
1,
4,
1,
3,
2,
3,
1,
4,
2,
1,
1,
10
] | 13 | true | Family | Ubiquinone biosynthesis hydroxylase UbiH/COQ6 | Ubiquinone biosynthesis hydroxylase UbiH/COQ6 | UbiH/COQ6 | 6 |
IPR010972 | 10,972 | Beta-phosphoglucomutase | Beta-PGM | Family | 4,669 | false | false | This entry represents the beta-phosphoglucomutase (Beta-PGM) enzyme which catalyses the interconversion of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerisation (alpha to beta or vice versa) while the 1-phosphate is not. A separate enzyme is responsible for... | [
"GO:0000287",
"GO:0008801",
"GO:0005975"
] | [
"magnesium ion binding",
"beta-phosphoglucomutase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR01990",
"cd02598"
] | [
"bPGM",
"HAD_BPGM"
] | [
4586,
4592
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.2.6",
"PWY-2721",
"PWY-2722",
"PWY-7459"
] | [
"EC:5.4.2.6",
"METACYC:PWY-2721",
"METACYC:PWY-2722",
"METACYC:PWY-7459"
] | 4 | [
"1lvh",
"1o03",
"1o08",
"1z4n",
"1z4o",
"1zol",
"2wf5",
"2wf6",
"2wf7",
"2wf8",
"2wf9",
"2wfa",
"2whe",
"3fm9",
"3nas",
"3zi4",
"4c4r",
"4c4s",
"4c4t",
"4g9b",
"4gib",
"4uw9",
"5o6p",
"5o6r",
"5ojz",
"5ok0",
"5ok1",
"5ok2",
"5olw",
"5olx",
"5oly",
"6h8u"... | 60 | [
"PUB00003337",
"PUB00009540",
"PUB00009589",
"PUB00014792"
] | [
"7966317",
"10956028",
"11601995",
"12637673"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and ca... | [
1994,
2000,
2001,
2003
] | 4 | [
"IPR006439"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Pyrococcus sp. ST04",
"Siphoviridae sp. ctYaH2",
"metagenomes"
] | [
4640,
5,
1,
1,
22
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Beta-phosphoglucomutase | Beta-phosphoglucomutase | Beta-PGM | 7 |
IPR010974 | 10,974 | Phosphotransferase system, N-acetylglucosamine-specific IIBC component | PTS_IIBC_nag | Domain | 5,422 | false | false | This entry represents the combined B and C domains of the PTS transport system enzyme II specific for N-acetylglucosamine transport [ ]. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name 'PTS system, N-acetylglucosamine-specific IIABC component'.... | [
"GO:0008982",
"GO:0015572",
"GO:0009401",
"GO:0016020",
"GO:0019866"
] | [
"protein-N(PI)-phosphohistidine-sugar phosphotransferase activity",
"N-acetylglucosamine transmembrane transporter activity",
"phosphoenolpyruvate-dependent sugar phosphotransferase system",
"membrane",
"organelle inner membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"NCBIFAM"
] | [
"TIGR01998"
] | [
"PTS-II-BC-nag"
] | [
5422
] | 1 | [
"EC",
"GP"
] | [
"2.7.1.193",
"GenProp0119"
] | [
"EC:2.7.1.193",
"GP:GenProp0119"
] | 2 | [] | 0 | [
"PUB00013785"
] | [
"3284790"
] | [
"Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase."
] | [
1988
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"metagenomes"
] | [
5418,
1,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Phosphotransferase system, N-acetylglucosamine-specific IIBC component | Phosphotransferase system, N-acetylglucosamine-specific IIBC component | PTS_IIBC_nag | 2 |
IPR010975 | 10,975 | Phosphotransferase system, alpha-glucoside-specific IIBC component | PTS_IIBC_a_glc | Family | 1,341 | false | false | This entry represents the fused PTS enzyme II B and C domains. A gene from Clostridium [ ] has been partially characterised as a maltose transporter, while genes from Fusobacterium and Klebsiella [ , ] have been proposed to transport the five non-standard isomers of sucrose. | [
"GO:0008982",
"GO:0009401"
] | [
"protein-N(PI)-phosphohistidine-sugar phosphotransferase activity",
"phosphoenolpyruvate-dependent sugar phosphotransferase system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02005"
] | [
"PTS-IIBC-alpha"
] | [
1341
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.-",
"GenProp0119",
"PWY-5129",
"PWY-6322",
"PWY-6369",
"PWY-6626",
"PWY-6682",
"PWY-6955",
"PWY-7077",
"PWY-7321",
"PWY-7740",
"PWY-7769",
"PWY-7886",
"PWY-7948",
"PWY-7975",
"PWY-8129",
"PWY-8324",
"PWY-8367",
"PWY-8392",
"PWY-8393",
"PWY-8394",
"PWY-8402"
] | [
"EC:2.7.1.-",
"GP:GenProp0119",
"METACYC:PWY-5129",
"METACYC:PWY-6322",
"METACYC:PWY-6369",
"METACYC:PWY-6626",
"METACYC:PWY-6682",
"METACYC:PWY-6955",
"METACYC:PWY-7077",
"METACYC:PWY-7321",
"METACYC:PWY-7740",
"METACYC:PWY-7769",
"METACYC:PWY-7886",
"METACYC:PWY-7948",
"METACYC:PWY-797... | 22 | [] | 0 | [
"PUB00013783",
"PUB00013817",
"PUB00013830"
] | [
"11473129",
"11882720",
"11781805"
] | [
"Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae. Participation and properties of sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase.",
"Metabolism of sucrose and its five isomers by Fusobacterium mortiferum.",
"Characterization of a maltose tra... | [
2001,
2002,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"bioreactor metagenome"
] | [
1337,
2,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphotransferase system, alpha-glucoside-specific IIBC component | Phosphotransferase system, alpha-glucoside-specific IIBC component | PTS_IIBC_a_glc | 9 |
IPR010976 | 10,976 | Beta-phosphoglucomutase hydrolase | B-phosphoglucomutase_hydrolase | Domain | 9,636 | false | false | Phosphoglucomutases interconvert D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction which is important for energy metabolism in many organisms and for cell wall biosynthesis in bacteria [ , ]. Beta-phosphoglucomutases are monomeric enzymes which interconvert the beta anomers of these compounds using Mg2+ as a ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02009"
] | [
"PGMB-YQAB-SF"
] | [
9636
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.2.6",
"PWY-2721",
"PWY-2722",
"PWY-7459"
] | [
"EC:5.4.2.6",
"METACYC:PWY-2721",
"METACYC:PWY-2722",
"METACYC:PWY-7459"
] | 4 | [
"1lvh",
"1o03",
"1o08",
"1z4n",
"1z4o",
"1zol",
"2wf5",
"2wf6",
"2wf7",
"2wf8",
"2wf9",
"2wfa",
"2whe",
"3fm9",
"3nas",
"3zi4",
"4c4r",
"4c4s",
"4c4t",
"4g9b",
"4gib",
"5o6p",
"5o6r",
"5ojz",
"5ok0",
"5ok1",
"5ok2",
"5olw",
"5olx",
"5oly",
"6h8u",
"6h8v"... | 60 | [
"PUB00022122",
"PUB00028017",
"PUB00028018"
] | [
"12081483",
"8071206",
"9084169"
] | [
"Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis.",
"Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp. lactis and their regulation in maltose- and glucose-utilizing cells.",
"Product formation and phosphoglucomutase act... | [
2002,
1994,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctYaH2",
"metagenomes"
] | [
7,
9574,
10,
1,
44
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Beta-phosphoglucomutase hydrolase | Beta-phosphoglucomutase hydrolase | B-phosphoglucomutase_hydrolase | 7 |
IPR010977 | 10,977 | Aromatic-L-amino-acid decarboxylase | Aromatic_deC | Family | 26,889 | false | false | A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group [ , ]. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptoph... | [
"GO:0016831",
"GO:0006520"
] | [
"carboxy-lyase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR00800",
"PTHR11999"
] | [
"YHDCRBOXLASE",
""
] | [
21339,
24780
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1",
"R-BTA-70921",
"R-DME-209905",
"R-DME-209931",
"R-DME-70921",
"R-HSA-209905",
"R-HSA-209931",
"R-HSA-70921",
"R-MMU-209905",
"R-MMU-209931",
"R-MMU-70921",
"R-RNO-209905",
"R-RNO-209931",
"R-RNO-70921"
] | [
"EC:4.1.1",
"REACTOME:R-BTA-70921",
"REACTOME:R-DME-209905",
"REACTOME:R-DME-209931",
"REACTOME:R-DME-70921",
"REACTOME:R-HSA-209905",
"REACTOME:R-HSA-209931",
"REACTOME:R-HSA-70921",
"REACTOME:R-MMU-209905",
"REACTOME:R-MMU-209931",
"REACTOME:R-MMU-70921",
"REACTOME:R-RNO-209905",
"REACTOME... | 14 | [
"1js3",
"1js6",
"3k40",
"3rbf",
"3rbl",
"3rch",
"4e1o",
"4obu",
"4obv",
"6eei",
"6eem",
"6eeq",
"6eew",
"6jrl",
"6khn",
"6kho",
"6khp",
"6liu",
"6liv",
"7eiw",
"7eix",
"7eiy",
"7xin",
"8or9",
"8ora",
"8x0o",
"8x0p",
"9dui",
"9gns",
"9hrh",
"9hri"
] | 31 | [
"PUB00001452",
"PUB00002358",
"PUB00003414",
"PUB00004715"
] | [
"8181483",
"8889823",
"2124279",
"2300558"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.",
"Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous.",
... | [
1994,
1996,
1990,
1990
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
86,
9073,
17432,
298
] | 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",
"Zea mays"
] | [
18,
9,
3,
15,
61,
7,
2,
20,
13,
17
] | 10 | true | Family | Aromatic-L-amino-acid decarboxylase | Aromatic-L-amino-acid decarboxylase | Aromatic_deC | 1 |
IPR010978 | 10,978 | Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm | tRNA-bd_arm | Homologous_superfamily | 88,749 | false | false | This superfamily represents an α-helical tRNA-binding arm found in class I and II aminoacyl-tRNA synthetase enzymes, as well as in the methicillin resistance protein FemA. The tRNA-binding arm domain is conserved between class I and class II aminoacyl-tRNA synthetase enzymes ( ), consisting of two α helices in an antip... | [
"GO:0000166"
] | [
"nucleotide binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF46589"
] | [
""
] | [
88749
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"R-HSA-2408557",
"R-HSA-379716",
"R-HSA-379726"
] | [
"EC:6.1.1",
"REACTOME:R-HSA-2408557",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726"
] | 4 | [
"1b70",
"1b7y",
"1eiy",
"1gax",
"1ivs",
"1iyw",
"1jjc",
"1lrz",
"1pys",
"1ser",
"1ses",
"1set",
"1sry",
"1wle",
"2dq0",
"2dq3",
"2iy5",
"2zr2",
"2zr3",
"3err",
"3hfz",
"3lsq",
"3lss",
"3pco",
"3qne",
"3qo5",
"3qo7",
"3qo8",
"3teh",
"3vbb",
"4l87",
"4p71"... | 94 | [
"PUB00014007",
"PUB00014008"
] | [
"12554880",
"12176388"
] | [
"Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase.",
"X-ray crystal structure of Staphylococcus aureus FemA."
] | [
2003,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
802,
75792,
10545,
32,
1578
] | 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",... | [
17,
1,
5,
2,
3,
11,
9,
2,
19,
8,
3,
2,
62
] | 13 | true | Homologous_superfamily | Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm | Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm | tRNA-bd_arm | 9 |
IPR010979 | 10,979 | Small ribosomal subunit protein uS13-like, H2TH | Ribosomal_uS13-like_H2TH | Homologous_superfamily | 83,501 | false | false | This superfamily represents the H2TH motif found in the small ribosomal subunit protein uS13. Small ribosomal subunit protein uS13 was previously known as Ribosomal protein S13 [ , ]. In Escherichia coli, S13 is known to be involved in binding fMet-tRNA and, hence, in the initiation of translation. S13 contains thee he... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF46946"
] | [
""
] | [
83501
] | 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-110329",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5649702",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CFA-156827",
"R-CFA-1799339",
"R-CFA-72649",
"R-CFA-72689",
"R-CFA-72695",
"R-CFA-72702",... | [
"REACTOME:R-BTA-110329",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5649702",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-97595... | 123 | [
"1ee8",
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1k3w",
"1k3x",
"1k82",
"1kfv",
"1l1t",
"1l1z",
"1l2b",
"1l2c",
"1l2d",
"1mj1",
"1ml5",
"1mu5",
"1mx0",
"1n32",
"1n33"... | 1,932 | [
"PUB00014009",
"PUB00014010",
"PUB00014011",
"PUB00080279"
] | [
"12464183",
"10921868",
"12505993",
"24524803"
] | [
"Selection of tRNA by the ribosome requires a transition from an open to a closed form.",
"Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.",
"Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase me... | [
2002,
2000,
2003,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1628,
64350,
16163,
91,
1269
] | 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",... | [
20,
1,
6,
3,
3,
6,
12,
3,
21,
16,
3,
3,
34
] | 13 | true | Homologous_superfamily | Small ribosomal subunit protein uS13-like, H2TH | Small ribosomal subunit protein uS13-like, H2TH | Ribosomal_uS13-like_H2TH | 1 |
IPR010980 | 10,980 | Cytochrome c/b562 | Cyt_c/b562 | Homologous_superfamily | 9,819 | false | false | Cytochromes are haem-containing proteins that function as electron carriers during electron transfer reactions. Cytochromes can be divided into types depending upon how the haem atom is bound: in c-type cytochromes the haem is covalently attached to the polypeptide, while in b-type cytochromes the haem is not covalentl... | [
"GO:0005506",
"GO:0009055",
"GO:0020037",
"GO:0022900"
] | [
"iron ion binding",
"electron transfer activity",
"heme binding",
"electron transport chain"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"SSF"
] | [
"SSF47175"
] | [
""
] | [
9819
] | 1 | [] | [] | [] | 0 | [
"1a7v",
"1apc",
"1bbh",
"1cgn",
"1cgo",
"1cpq",
"1cpr",
"1e83",
"1e84",
"1e85",
"1e86",
"1eky",
"1gqa",
"1jaf",
"1lm3",
"1m6t",
"1mqv",
"1nbb",
"1qpu",
"1qq3",
"1rcp",
"1s05",
"1yyj",
"1yyx",
"1yza",
"1yzc",
"256b",
"2bc5",
"2ccy",
"2j8w",
"2j9b",
"2qla"... | 767 | [
"PUB00013996",
"PUB00014012"
] | [
"11914078",
"12215425"
] | [
"A multigeneration analysis of cytochrome b(562) redox variants: evolutionary strategies for modulating redox potential revealed using a library approach.",
"Sequence conservation in families whose members have little or no sequence similarity: the four-helical cytokines and cytochromes."
] | [
2002,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctu6J18",
"unclassified sequences"
] | [
9628,
20,
1,
170
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Cytochrome c/b562 | Cytochrome c/b562 | Cyt_c/b562 | 5 |
IPR010981 | 10,981 | SinR repressor/SinI anti-repressor, dimerisation domain | SinR/SinI_dimer_dom | Domain | 2,410 | false | false | The SinR repressor is part of a group of Sin (sporulation inhibition) proteins in Bacillus subtilis that regulate the commitment to sporulation in response to extreme adversity [ ]. SinR is a tetrameric repressor protein that binds to the promoters of genes essential for entry into sporulation and prevents their transc... | [
"GO:0046983",
"GO:0006355"
] | [
"protein dimerization activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF08671",
"PS51500"
] | [
"SinI",
"SIN"
] | [
2249,
2405
] | 2 | [] | [] | [] | 0 | [
"1b0n",
"2yal",
"3zkc",
"5tmx",
"5tn2"
] | 5 | [
"PUB00014013"
] | [
"9799632"
] | [
"An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
2410
] | 1 | [] | [] | 0 | true | Domain | SinR repressor/SinI anti-repressor, dimerisation domain | SinR repressor/SinI anti-repressor, dimerisation domain | SinR/SinI_dimer_dom | 3 |
IPR010982 | 10,982 | Lambda repressor-like, DNA-binding domain superfamily | Lambda_DNA-bd_dom_sf | Homologous_superfamily | 858,641 | false | false | Bacteriophage lambda C1 repressor controls the expression of viral genes as part of the lysogeny/lytic growth switch. C1 is essential for maintaining lysogeny, where the phage replicates non-disruptively along with the host. If the host cell is threatened, then lytic growth is induced. The Lambda C1 repressor consists ... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.260.40",
"SSF47413"
] | [
"",
""
] | [
829458,
827439
] | 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-CEL-373752",
"R-CEL-418885",
"R-CEL-418886",
"R-DME-373752",
"R-DME-418885",
"R-DME-418886",
"R-DME-6804759",
"R-DME-6807505",
"R-DME-9018519",
"R-DRE-373752",
"R-DRE-418885",
"R-DRE-418886",
"R-HSA-111465",
"R-HSA-1839117",
"R-HSA-210744",
"R-HSA-210745",
"R-HSA-210747",
"R-HSA... | [
"REACTOME:R-CEL-373752",
"REACTOME:R-CEL-418885",
"REACTOME:R-CEL-418886",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-418885",
"REACTOME:R-DME-418886",
"REACTOME:R-DME-6804759",
"REACTOME:R-DME-6807505",
"REACTOME:R-DME-9018519",
"REACTOME:R-DRE-373752",
"REACTOME:R-DRE-418885",
"REACTOME:R-DRE-... | 54 | [
"1adr",
"1au7",
"1b0n",
"1bdh",
"1bdi",
"1cjg",
"1cop",
"1cqt",
"1d1l",
"1d1m",
"1dw9",
"1dwk",
"1e3o",
"1efa",
"1gt0",
"1hf0",
"1ic8",
"1jfs",
"1jft",
"1jh9",
"1jwl",
"1jye",
"1jyf",
"1l1m",
"1lbg",
"1lbh",
"1lbi",
"1lcc",
"1lcd",
"1lli",
"1lmb",
"1lqc"... | 472 | [
"PUB00007265",
"PUB00008198",
"PUB00014013",
"PUB00014015",
"PUB00014016",
"PUB00014017",
"PUB00014018",
"PUB00014019",
"PUB00014020"
] | [
"9009203",
"10801492",
"9799632",
"10892750",
"7973627",
"10700279",
"9237914",
"11583619",
"12453420"
] | [
"Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility.",
"Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.",
"An evolutionary link between sporulation and prophage induction in th... | [
1997,
2000,
1998,
2000,
1994,
2000,
1997,
2001,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
6164,
796639,
41434,
7237,
14,
7153
] | 6 | [
"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",... | [
11,
26,
209,
37,
36,
171,
85,
4,
6,
108,
1,
1,
19
] | 13 | true | Homologous_superfamily | Lambda repressor-like, DNA-binding domain superfamily | Lambda repressor-like, DNA-binding domain superfamily | Lambda_DNA-bd_dom_sf | 2 |
IPR010985 | 10,985 | Ribbon-helix-helix | Ribbon_hlx_hlx | Homologous_superfamily | 85,589 | false | false | This superfamily represents domains with a ribbon-helix-helix core topology consisting of four helices in an open array of two hairpins. Such domains are found in several bacterial and phage repressors, including the Escherichia coli methionine repressor (MetJ), which when combined with S-adenosylmethionine (SAM) repre... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF47598"
] | [
""
] | [
85589
] | 1 | [] | [] | [] | 0 | [
"1arq",
"1arr",
"1b01",
"1b28",
"1baz",
"1bdt",
"1bdv",
"1cma",
"1cmb",
"1cmc",
"1ea4",
"1irq",
"1mj2",
"1mjk",
"1mjl",
"1mjm",
"1mjo",
"1mjp",
"1mjq",
"1mnt",
"1myk",
"1myl",
"1nla",
"1p94",
"1par",
"1q5v",
"1qtg",
"1u9p",
"1x93",
"1xrx",
"1y9b",
"1zx3"... | 106 | [
"PUB00013999",
"PUB00014000",
"PUB00014001",
"PUB00014024",
"PUB00016689"
] | [
"1943695",
"9927650",
"7999761",
"11733997",
"15808743"
] | [
"Regulation of methionine synthesis in Escherichia coli.",
"Origins of DNA-binding specificity: role of protein contacts with the DNA backbone.",
"Solution structure of dimeric Mnt repressor (1-76).",
"Crystal structure of omega transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1... | [
1991,
1999,
1994,
2001,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
4903,
78644,
70,
446,
5,
1521
] | 6 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Homologous_superfamily | Ribbon-helix-helix | Ribbon-helix-helix | Ribbon_hlx_hlx | 9 |
IPR010989 | 10,989 | SNARE | SNARE | Homologous_superfamily | 58,609 | false | false | Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an α-helical coiled-coil domain called the SNARE motif [ ]. These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classi... | [
"GO:0016192",
"GO:0016020"
] | [
"vesicle-mediated transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"SSF"
] | [
"SSF47661"
] | [
""
] | [
58609
] | 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-181429",
"R-BTA-181430",
"R-BTA-204005",
"R-BTA-210500",
"R-BTA-212676",
"R-BTA-264642",
"R-BTA-449836",
"R-BTA-5682910",
"R-BTA-5694530",
"R-BTA-6807878",
"R-BTA-6811438",
"R-BTA-888590",
"R-BTA-8980692",
"R-BTA-9013106",
"R-BTA-9013408",
"R-BTA-9609523",
"R-CEL-114516",
"R... | [
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-264642",
"REACTOME:R-BTA-449836",
"REACTOME:R-BTA-5682910",
"REACTOME:R-BTA-5694530",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811438",
"REACTOME:R-BTA... | 138 | [
"1br0",
"1ez3",
"1fio",
"1hs7",
"1kil",
"1l4a",
"1lvf",
"1n7s",
"1s94",
"1sfc",
"1urq",
"1vcs",
"2c5i",
"2c5j",
"2c5k",
"2dnx",
"2m8r",
"2n1t",
"2qyw",
"2v8s",
"2xhe",
"3c98",
"3hd7",
"3ipd",
"3j96",
"3j97",
"3j98",
"3j99",
"3lg7",
"3onj",
"3onl",
"3rk2"... | 84 | [
"PUB00014049",
"PUB00014050",
"PUB00014051",
"PUB00014052",
"PUB00014055"
] | [
"12827282",
"10913252",
"11839791",
"11224573",
"12082176"
] | [
"The molecular machinery of synaptic vesicle exocytosis.",
"Structural analysis of the neuronal SNARE protein syntaxin-1A.",
"Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation.",
"Vam3p structure... | [
2003,
2000,
2002,
2001,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
16,
283,
58287,
9,
14
] | 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... | [
121,
9,
56,
23,
92,
62,
9,
61,
90,
8,
6,
144
] | 12 | true | Homologous_superfamily | SNARE | SNARE | SNARE | 5 |
IPR010991 | 10,991 | p53, tetramerisation domain | p53_tetrameristn | Domain | 4,735 | false | false | This entry represents the tetramerisation domain of p53. The tetramerisation domain of human p53 extends from residues 325 to 356, and has a 4-helical bundle fold. The tetramerisation domain is essential for DNA binding, protein-protein interactions, post-translational modifications, and p53 degradation [ , ]. The p53 ... | [
"GO:0051262"
] | [
"protein tetramerization"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF07710"
] | [
"P53_tetramer"
] | [
4735
] | 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-2559580",
"R-BTA-2559586",
"R-BTA-349425",
"R-BTA-5689880",
"R-BTA-5689896",
"R-BTA-5693565",
"R-BTA-6804754",
"R-BTA-6804756",
"R-BTA-6804757",
"R-BTA-6804758",
"R-BTA-6804759",
"R-BTA-6804760",
"R-BTA-6811555",
"R-BTA-69473",
"R-BTA-69481",
"R-BTA-69541",
"R-BTA-69895",
"R... | [
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-349425",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-5689896",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-6804754",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6804757",
"REACTOME:R-BTA-6804758",
"REACTOME:R-BTA-6804759",
"REACTOME... | 150 | [
"1a1u",
"1aie",
"1c26",
"1hs5",
"1olg",
"1olh",
"1pes",
"1pet",
"1sae",
"1saf",
"1sak",
"1sal",
"2j0z",
"2j10",
"2j11",
"2kby",
"2mw4",
"2nb1",
"2wqi",
"2wqj",
"2wtt",
"3q01",
"3q05",
"3q06",
"3sak",
"3ts8",
"3zy0",
"3zy1",
"4a9z",
"4cz5",
"4cz6",
"4cz7"... | 55 | [
"PUB00000596",
"PUB00001893",
"PUB00002729",
"PUB00004096",
"PUB00004490",
"PUB00014036",
"PUB00014037",
"PUB00054382"
] | [
"2142001",
"2137806",
"1639769",
"2046748",
"2142762",
"7878469",
"11420672",
"19815500"
] | [
"Tumor suppressor genes: the p53 and retinoblastoma sensitivity genes and gene products.",
"p53: oncogene or anti-oncogene?",
"The p53 tumor suppressor protein, a modulator of cell proliferation.",
"The p53 tumour suppressor gene.",
"Structural aspects of the p53 protein in relation to gene evolution.",
"... | [
1990,
1990,
1992,
1991,
1990,
1995,
2001,
2009
] | 8 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"bird metagenome"
] | [
4734,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
69,
45,
19,
15
] | 4 | true | Domain | p53, tetramerisation domain | p53, tetramerisation domain | p53_tetrameristn | 4 |
IPR010992 | 10,992 | Integration host factor (IHF)-like DNA-binding domain superfamily | IHF-like_DNA-bd_dom_sf | Homologous_superfamily | 69,105 | false | false | Integration host factor (IHF) ( , ) is a small heterodimeric protein that binds the minor groove of DNA in a sequence-specific manner and induces a large bend. This bending stabilises distinct DNA conformations that are required during several bacterial processes, such as recombination, transposition, replication and t... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:4.10.520.10",
"SSF47729"
] | [
"",
""
] | [
65642,
68981
] | 2 | [] | [] | [] | 0 | [
"1b8z",
"1dp3",
"1exe",
"1hue",
"1huu",
"1ihf",
"1mul",
"1ouz",
"1owf",
"1owg",
"1p51",
"1p71",
"1p78",
"1riy",
"1wtu",
"2ht0",
"2iie",
"2iif",
"2ndp",
"2np2",
"2o97",
"3omy",
"3on0",
"3rhi",
"4dky",
"4p3v",
"4pt4",
"4qjn",
"4qju",
"4qpo",
"4qpq",
"4yew"... | 59 | [
"PUB00010445",
"PUB00014038",
"PUB00014039",
"PUB00014040"
] | [
"11258958",
"12842466",
"12853489",
"10993726"
] | [
"Solution structure of the DNA-binding domain of TraM.",
"Integration host factor: putting a twist on protein-DNA recognition.",
"Flexible DNA bending in HU-DNA cocrystal structures.",
"Solution structure of a mutant of transcription factor 1: implications for enhanced DNA binding."
] | [
2001,
2003,
2003,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
45,
66555,
747,
460,
1298
] | 5 | [
"Escherichia coli (strain K12)",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
1,
3
] | 3 | true | Homologous_superfamily | Integration host factor (IHF)-like DNA-binding domain superfamily | Integration host factor (IHF)-like DNA-binding domain superfamily | IHF-like_DNA-bd_dom_sf | 3 |
IPR010994 | 10,994 | RuvA domain 2-like | RuvA_2-like | Homologous_superfamily | 191,711 | false | false | In prokaryotes, RuvA, RuvB, and RuvC process the universal DNA intermediate of homologous recombination, termed Holliday junction. The tetrameric DNA helicase RuvA specifically binds to the Holliday junction and facilitates the isomerization of the junction from the stacked folded configuration to the square-planar str... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF47781"
] | [
""
] | [
191711
] | 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-5685938",
"R-BTA-5696395",
"R-BTA-5696400",
"R-BTA-6782135",
"R-BTA-6783310",
"R-BTA-9833482",
"R-CEL-112382",
"R-CEL-674695",
"R-CEL-75955",
"R-DDI-5696395",
"R-DDI-6782135",
"R-DME-112382",
"R-DME-5632684",
"R-DME-5696395",
"R-DME-5696400",
"R-DME-674695",
"R-DME-6782135",
... | [
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-5696400",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6783310",
"REACTOME:R-BTA-9833482",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-75955",
"REACTOME:R-DDI-5696395",
"REACTOME:R-DDI-6782135",
"REACTOME:R-... | 55 | [
"1bdx",
"1c7y",
"1cuk",
"1d8l",
"1dgs",
"1hjp",
"1ixr",
"1kft",
"1v9p",
"1x2i",
"1z00",
"2a1j",
"2aq0",
"2bgw",
"2bhn",
"2csb",
"2csd",
"2edu",
"2h5x",
"2kn7",
"2lyh",
"2m9n",
"2mut",
"2nrt",
"2nrv",
"2nrw",
"2nrx",
"2nrz",
"2oce",
"2owo",
"2ztc",
"2ztd"... | 116 | [
"PUB00007386",
"PUB00013198",
"PUB00014056"
] | [
"10698952",
"12408833",
"12426397"
] | [
"Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications.",
"Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.",
"Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.col... | [
2000,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2752,
161729,
23512,
392,
3326
] | 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",... | [
35,
3,
47,
12,
7,
34,
16,
4,
11,
34,
2,
3,
53
] | 13 | true | Homologous_superfamily | RuvA domain 2-like | RuvA domain 2-like | RuvA_2-like | 1 |
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