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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054925 | 54,925 | Glucose-binding protein GlcS | GlcS_GBP | Family | 56 | true | false | The Glucose-binding protein GlcS is a component of the ABC transporter complex GlcSTUV, which is involved in glucose uptake in Saccharolobus solfataricus. This protein binds glucose and can also bind galactose and mannose. The binding of glucose by GlcS is strongly inhibited by the presence of galactose and mannose. Gl... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040930"
] | [
"GlcS_GBP"
] | [
56
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013790",
"PUB00106073"
] | [
"11260467",
"10400586"
] | [
"Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters.",
"Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein."
] | [
2001,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
56
] | 1 | [] | [] | 0 | true | Family | Glucose-binding protein GlcS | Glucose-binding protein GlcS | GlcS_GBP | 4 |
IPR054926 | 54,926 | Citrate synthase family | Cit_synThplmales | Family | 60 | true | false | Citrate synthase is an enzyme that catalyzes the first step of the citric acid cycle (Krebs cycle), which is the synthesis of citrate from oxaloacetate and acetyl-CoA. This enzyme is allosterically inhibited by NADH, indicating a regulatory role in cellular metabolism. Members of the citrate synthase family are found a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041157"
] | [
"Cit_synThplmales"
] | [
60
] | 1 | [] | [] | [] | 0 | [
"1o7x",
"1vgm",
"2ifc",
"2r26",
"2r9e",
"4ybo",
"6abv",
"6abw"
] | 8 | [
"PUB00106208",
"PUB00106209"
] | [
"2269303",
"7704526"
] | [
"Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene.",
"The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum."
] | [
1990,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
60
] | 1 | [] | [] | 0 | true | Family | Citrate synthase family | Citrate synthase family | Cit_synThplmales | 7 |
IPR054927 | 54,927 | Glucose ABC transporter permease GlcU | GlcU_transporter | Family | 58 | true | false | This entry represents the glucose import system permease protein GlcU, which is part of the ABC transporter complex GlcSTUV involved in glucose uptake. The protein is responsible for the translocation of glucose across the membrane. It belongs to the binding-protein-dependent transport system permease family. The prote... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040932"
] | [
"GlcU_transporter"
] | [
58
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013790",
"PUB00106073"
] | [
"11260467",
"10400586"
] | [
"Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters.",
"Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein."
] | [
2001,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
58
] | 1 | [] | [] | 0 | true | Family | Glucose ABC transporter permease GlcU | Glucose ABC transporter permease GlcU | GlcU_transporter | 8 |
IPR054928 | 54,928 | Fatty-acid--CoA ligase FadD21 | FAAL_FadD21 | Family | 62 | true | false | This entry represents the fatty-acid--CoA ligase FadD21, also known as fatty-acid--AMP ligase FAAL21/FadD21. These enzymes belong to the ATP-dependent AMP-binding enzyme family and are involved in the activation of fatty acids by forming a fatty acyl-CoA thioester. The proteins matched by this entry are found in variou... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF038337"
] | [
"FAAL_FadD21"
] | [
62
] | 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"... | [
"6.2.1.-",
"PWY-301",
"PWY-5045",
"PWY-5136",
"PWY-5660",
"PWY-5752",
"PWY-5922",
"PWY-5923",
"PWY-5924",
"PWY-5927",
"PWY-5958",
"PWY-6457",
"PWY-6593",
"PWY-6670",
"PWY-6722",
"PWY-6799",
"PWY-6926",
"PWY-6948",
"PWY-7007",
"PWY-7288",
"PWY-735",
"PWY-7462",
"PWY-7536",... | [
"EC:6.2.1.-",
"METACYC:PWY-301",
"METACYC:PWY-5045",
"METACYC:PWY-5136",
"METACYC:PWY-5660",
"METACYC:PWY-5752",
"METACYC:PWY-5922",
"METACYC:PWY-5923",
"METACYC:PWY-5924",
"METACYC:PWY-5927",
"METACYC:PWY-5958",
"METACYC:PWY-6457",
"METACYC:PWY-6593",
"METACYC:PWY-6670",
"METACYC:PWY-67... | 53 | [] | 0 | [
"PUB00077564",
"PUB00095586"
] | [
"25124040",
"19182784"
] | [
"Biosynthesis and translocation of unsulfated acyltrehaloses in Mycobacterium tuberculosis.",
"Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis."
] | [
2014,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Mycobacterium"
] | [
62
] | 1 | [] | [] | 0 | true | Family | Fatty-acid--CoA ligase FadD21 | Fatty-acid--CoA ligase FadD21 | FAAL_FadD21 | 6 |
IPR054929 | 54,929 | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | dPGM_arch | Family | 63 | true | false | This entry represents 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, an enzyme that catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. This enzyme belongs to the phosphoglycerate mutase family and is found in Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 1... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF038349"
] | [
"dPGM_arch"
] | [
63
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00055097"
] | [
"17576516"
] | [
"Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
63
] | 1 | [] | [] | 0 | true | Family | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | dPGM_arch | 2 |
IPR054930 | 54,930 | GTP-dependent dephospho-CoA kinase family | deph_CoA_kin_Thcocales | Family | 44 | true | false | GTP-dependent dephospho-CoA kinase (DPCK) catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). This enzyme is a member of the GTP-dependent DPCK family and is found in various archaeal species, including Pyrococcus horikoshii, Pyrococcus abyssi, Thermococ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041125"
] | [
"deph_CoA_kin_Thcocales"
] | [
44
] | 1 | [
"EC",
"METACYC"
] | [
"2.7.1.237",
"PWY-8342"
] | [
"EC:2.7.1.237",
"METACYC:PWY-8342"
] | 2 | [
"8jvc",
"8jvf",
"8jvg"
] | 3 | [
"PUB00093757"
] | [
"31337720"
] | [
"Identification of Dephospho-Coenzyme A (Dephospho-CoA) Kinase in Thermococcus kodakarensis and Elucidation of the Entire CoA Biosynthesis Pathway in Archaea."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
44
] | 1 | [] | [] | 0 | true | Family | GTP-dependent dephospho-CoA kinase family | GTP-dependent dephospho-CoA kinase family | deph_CoA_kin_Thcocales | 8 |
IPR054931 | 54,931 | Lysyl aminopeptidase | lys_aminopep_Arch | Family | 42 | true | false | Lysyl aminopeptidase is an enzyme that hydrolyzes di-, tri- and tetrapeptides with a lysine as the N-terminal amino acid and with Gly, Lys, Ala, Phe or Glu in the second position. This enzyme belongs to the peptidase M42 family and is found in Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). The enz... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040822"
] | [
"lys_aminopep_Arch"
] | [
42
] | 1 | [] | [] | [] | 0 | [
"2pe3",
"2wzn",
"4x8i"
] | 3 | [
"PUB00105996"
] | [
"15743956"
] | [
"Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
42
] | 1 | [] | [] | 0 | true | Family | Lysyl aminopeptidase | Lysyl aminopeptidase | lys_aminopep_Arch | 7 |
IPR054932 | 54,932 | Rhamnosyl O-methyltransferase family | RhmsylMtase | Family | 72 | true | false | Rhamnosyl O-methyltransferase enzymes catalyze the O-methylation of the hydroxyl group located on C-2 of the first rhamnosyl residue linked to the phenolic group of glycosylated phenolphthiocerol dimycocerosates (PGL) and p-hydroxybenzoic acid derivatives (p-HBAD). These enzymes are found in various strains of Mycobact... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045824"
] | [
"RhmsylMtase"
] | [
72
] | 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"... | [
"2.1.1.-",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601",
"PWY-6045"... | [
"EC:2.1.1.-",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",
"METACYC:PWY-5... | 146 | [] | 0 | [
"PUB00053670"
] | [
"15292265"
] | [
"Molecular dissection of the role of two methyltransferases in the biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the Mycobacterium tuberculosis complex."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Mycobacteriaceae"
] | [
72
] | 1 | [] | [] | 0 | true | Family | Rhamnosyl O-methyltransferase family | Rhamnosyl O-methyltransferase family | RhmsylMtase | 1 |
IPR054933 | 54,933 | Oxalate oxidoreductase subunit delta | OxalOxred_delta | Family | 37 | true | false | Oxalate oxidoreductase subunit delta is an enzyme that catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. This enzyme does not require coenzyme A as a cosubstrate and enables anaerobic growth on oxalate, wh... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045790"
] | [
"OxalOxred_delta"
] | [
37
] | 1 | [] | [] | [] | 0 | [
"5c4i",
"5exd",
"5exe"
] | 3 | [
"PUB00078738"
] | [
"20956531"
] | [
"Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
37
] | 1 | [] | [] | 0 | true | Family | Oxalate oxidoreductase subunit delta | Oxalate oxidoreductase subunit delta | OxalOxred_delta | 4 |
IPR054934 | 54,934 | Leucine/methionine racemase | LeuMetRace | Family | 41 | true | false | Leucine/methionine racemase is an amino acid racemase with moderate substrate specificity. It is primarily active toward leucine, which is the preferred substrate, and methionine. The enzyme also exhibits lower levels of activity toward phenylalanine, alanine, and serine. It belongs to the class-III pyridoxal-phosphate... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045634"
] | [
"LeuMetRace"
] | [
41
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154767"
] | [
"33468590"
] | [
"TK1211 Encodes an Amino Acid Racemase towards Leucine and Methionine in the Hyperthermophilic Archaeon Thermococcus kodakarensis."
] | [
2021
] | 1 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
41
] | 1 | [] | [] | 0 | true | Family | Leucine/methionine racemase | Leucine/methionine racemase | LeuMetRace | 1 |
IPR054935 | 54,935 | Polysaccharide lyase 17 family | Alg_lyase | Family | 49 | true | false | Alginate lyase is an enzyme that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. This enzyme acts specifically on alginate and each of its block structures, with the highest activity toward poly-beta-D-mannuronate (p... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042990"
] | [
"Alg_lyase"
] | [
49
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153625"
] | [
"26913076"
] | [
"Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Knufia peltigerae",
"Lysobacteraceae"
] | [
1,
48
] | 2 | [] | [] | 0 | true | Family | Polysaccharide lyase 17 family | Polysaccharide lyase 17 family | Alg_lyase | 2 |
IPR054936 | 54,936 | O6-methylguanine-DNA methyltransferase | DNA_protcyst_Mta_Thcoc | Family | 42 | true | false | Methylated-DNA--protein-cysteine methyltransferase (MGMT) is involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. This enzyme repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue i... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041132"
] | [
"DNA_protcyst_Mta_Thcoc"
] | [
42
] | 1 | [
"EC"
] | [
"2.1.1.63"
] | [
"EC:2.1.1.63"
] | 1 | [
"1mgt"
] | 1 | [
"PUB00027330",
"PUB00106190"
] | [
"10497033",
"9613574"
] | [
"Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.",
"The O6-methylguanine-DNA methyltransferase from the hyperthermophilic archaeon Pyrococcus sp. KOD1: a thermostable repair enzyme."
] | [
1999,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
42
] | 1 | [] | [] | 0 | true | Family | O6-methylguanine-DNA methyltransferase | O6-methylguanine-DNA methyltransferase | DNA_protcyst_Mta_Thcoc | 1 |
IPR054937 | 54,937 | CoaD family phosphopantetheine adenylyltransferase | CoaD_Thcocales | Family | 41 | true | false | Phosphopantetheine adenylyltransferase (CoaD) is an enzyme that reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. This enzyme belongs to the eukaryotic CoaD family and is found in various thermophilic archaea, including Thermococcus kodakarensis,... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041124"
] | [
"CoaD_Thcocales"
] | [
41
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.7.7.3",
"PWY-7851",
"PWY-8342"
] | [
"EC:2.7.7.3",
"METACYC:PWY-7851",
"METACYC:PWY-8342"
] | 3 | [] | 0 | [
"PUB00093757"
] | [
"31337720"
] | [
"Identification of Dephospho-Coenzyme A (Dephospho-CoA) Kinase in Thermococcus kodakarensis and Elucidation of the Entire CoA Biosynthesis Pathway in Archaea."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
41
] | 1 | [] | [] | 0 | true | Family | CoaD family phosphopantetheine adenylyltransferase | CoaD family phosphopantetheine adenylyltransferase | CoaD_Thcocales | 9 |
IPR054939 | 54,939 | 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | KDG_KDGal_kin | Family | 52 | true | false | This entry represents 2-dehydro-3-deoxygluconokinase (KDGK) and 2-dehydro-3-deoxygalactonokinase (KDGalK) enzymes. These enzymes are involved in the degradation of glucose and galactose via the semi-phosphorylative Entner-Doudoroff pathway. They catalyze the phosphorylation of 2-keto-3-deoxygluconate (KDG) and 2-keto-3... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040938"
] | [
"KDG_KDGal_kin"
] | [
52
] | 1 | [] | [] | [] | 0 | [
"1wye",
"2dcn",
"2v78",
"2var"
] | 4 | [
"PUB00106077",
"PUB00106078"
] | [
"16794308",
"19018105"
] | [
"Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway.",
"The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase."
] | [
2006,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoproteati"
] | [
52
] | 1 | [] | [] | 0 | true | Family | 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | KDG_KDGal_kin | 9 |
IPR054940 | 54,940 | L-prolyl-[peptidyl-carrier protein] dehydrogenase | ProlPCPDhRedW | Family | 64 | true | false | L-prolyl-[peptidyl-carrier protein] dehydrogenase, also known as L-prolyl-[prolyl-carrier protein] dehydrogenase, is an enzyme involved in the biosynthesis of undecylprodigiosin in Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). This enzyme catalyzes the desaturation of L-prolyl-[prolyl-carrier protein] t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045652"
] | [
"ProlPCPDhRedW"
] | [
64
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00096314",
"PUB00096315"
] | [
"11880032",
"11514230"
] | [
"Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during undecylprodigiosin and pyoluteorin biosynthesis.",
"Analysis of the prodiginine biosynthesis gene cluster of Streptomyces coelicolor A3(2): new mechanisms for chain initiation and termination in modular multienzymes."
] | [
2002,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
64
] | 1 | [] | [] | 0 | true | Family | L-prolyl-[peptidyl-carrier protein] dehydrogenase | L-prolyl-[peptidyl-carrier protein] dehydrogenase | ProlPCPDhRedW | 6 |
IPR054941 | 54,941 | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit gamma | sulfhyd_HydG | Family | 39 | true | false | This entry represents the gamma subunit of NADPH-dependent hydrogenase/sulfhydrogenase 1, also known as sulfhydrogenase 1 subunit gamma. This enzyme complex is found in Pyrococcus furiosus and functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. The beta and gamma subunits form t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040835"
] | [
"sulfhyd_HydG"
] | [
39
] | 1 | [] | [] | [] | 0 | [
"9nez",
"9nf0"
] | 2 | [
"PUB00033242",
"PUB00106003",
"PUB00106005"
] | [
"7704275",
"11265463",
"8389482"
] | [
"Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases.",
"Hydrogenases I and II from Pyrococcus furiosus.",
"Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase o... | [
1995,
2001,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
39
] | 1 | [] | [] | 0 | true | Family | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit gamma | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit gamma | sulfhyd_HydG | 1 |
IPR054942 | 54,942 | Tungsten-containing formylmethanofuran dehydrogenase subunit FwdC | FMH_DH_FwdC | Family | 50 | true | false | This entry represents the tungsten-containing formylmethanofuran dehydrogenase subunit FwdC. Proteins in this family catalyze the reversible oxidation of CO2 and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile and belongs to the FwdC/FmdC family. The activity of this enzyme is crucial... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042910"
] | [
"FMH_DH_FwdC"
] | [
50
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.2.7.12",
"PWY-5209",
"PWY-7784",
"PWY-8305"
] | [
"EC:1.2.7.12",
"METACYC:PWY-5209",
"METACYC:PWY-7784",
"METACYC:PWY-8305"
] | 4 | [
"5t5i",
"5t5m",
"5t61"
] | 3 | [
"PUB00015859",
"PUB00153614"
] | [
"8575452",
"27846502"
] | [
"The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide.",
"The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters."
] | [
1995,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Methanomada group"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Tungsten-containing formylmethanofuran dehydrogenase subunit FwdC | Tungsten-containing formylmethanofuran dehydrogenase subunit FwdC | FMH_DH_FwdC | 8 |
IPR054943 | 54,943 | Chemoreceptor glutamine deamidase/glutamate methylesterase CheD | CheD_Thtga | Family | 41 | true | false | Chemoreceptor glutamine deamidase/glutamate methylesterase CheD is an enzyme found in Thermotoga maritima, which plays a crucial role in the modification of chemoreceptors (MCPs). CheD deamidates glutamine residues on MCPs, a modification necessary for the proper transmission of conformational signals to the CheA kinas... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041119"
] | [
"CheD_Thtga"
] | [
41
] | 1 | [] | [] | [] | 0 | [
"2f9z"
] | 1 | [
"PUB00040594"
] | [
"16469702"
] | [
"A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Thermotogae",
"bioreactor metagenome"
] | [
40,
1
] | 2 | [] | [] | 0 | true | Family | Chemoreceptor glutamine deamidase/glutamate methylesterase CheD | Chemoreceptor glutamine deamidase/glutamate methylesterase CheD | CheD_Thtga | 4 |
IPR054944 | 54,944 | Cell wall elongation/penicillin-binding protein regulator TseB | regulator_TseB | Family | 67 | true | false | This entry represents the cell wall elongation/penicillin-binding protein regulator TseB. The TseB protein is involved in the regulation of cell wall elongation and penicillin-binding proteins in Bacillus subtilis (strain 168). The exact function of TseB remains uncharacterized, but it is believed to play a role in mai... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040668"
] | [
"regulator_TseB"
] | [
67
] | 1 | [] | [] | [] | 0 | [
"2gu3"
] | 1 | [
"PUB00105891",
"PUB00105892"
] | [
"25954268",
"34411374"
] | [
"Tetracycline hypersensitivity of an ezrA mutant links GalE and TseB (YpmB) to cell division.",
"Characterization of TseB: A new actor in cell wall elongation in Bacillus subtilis."
] | [
2015,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
67
] | 1 | [] | [] | 0 | true | Family | Cell wall elongation/penicillin-binding protein regulator TseB | Cell wall elongation/penicillin-binding protein regulator TseB | regulator_TseB | 1 |
IPR054945 | 54,945 | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit alpha | sulfhyd_HydA | Family | 39 | true | false | This entry represents the alpha subunit of NADPH-dependent hydrogenase/sulfhydrogenase 1, also known as sulfhydrogenase 1 subunit alpha. This protein is part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. It may play a role in hydrogen ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040832"
] | [
"sulfhyd_HydA"
] | [
39
] | 1 | [] | [] | [] | 0 | [
"5yxy",
"5yy0",
"9e15",
"9e1j",
"9nez",
"9nf0"
] | 6 | [
"PUB00033242",
"PUB00106003",
"PUB00106004"
] | [
"7704275",
"11265463",
"11054105"
] | [
"Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases.",
"Hydrogenases I and II from Pyrococcus furiosus.",
"Enzymes of hydrogen metabolism in Pyrococcus furiosus."
] | [
1995,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
39
] | 1 | [] | [] | 0 | true | Family | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit alpha | NADPH-dependent hydrogenase/sulfhydrogenase 1 subunit alpha | sulfhyd_HydA | 4 |
IPR054946 | 54,946 | Pantoate kinase Mhun_0831 | Mhun_0831 | Family | 38 | true | true | This entry represents Pantoate kinase found in Methanospirillum hungatei JF-1. Pantoate kinase (PoK) is an enzyme that belongs to the GHMP kinase family, specifically the PoK subfamily. It is responsible for phosphorylating (R)-pantoate to form (R)-4-phosphopantoate, a crucial step in the coenzyme A (CoA) biosynthesis ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040725"
] | [
"Panto_kinase"
] | [
38
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00060435",
"PUB00105931"
] | [
"19666462",
"23200110"
] | [
"Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea.",
"Identification of pantoate kinase and phosphopantothenate synthetase from Methanospirillum hungatei."
] | [
2009,
2013
] | 2 | [
"IPR012043"
] | [] | 1 | 0 | 1 | [
"Methanomicrobiales"
] | [
38
] | 1 | [] | [] | 0 | true | Family | Pantoate kinase Mhun_0831 | Pantoate kinase Mhun_0831 | Mhun_0831 | 6 |
IPR054947 | 54,947 | Glucose import system permease protein GlcT | GlcT_permease | Family | 45 | true | false | This entry represents the glucose import system permease protein GlcT, which is part of the ABC transporter complex GlcSTUV involved in glucose uptake. The protein is responsible for the translocation of glucose across the membrane. It belongs to the binding-protein-dependent transport system permease family. The prote... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040931"
] | [
"GlcT_permease"
] | [
45
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013790",
"PUB00106073"
] | [
"11260467",
"10400586"
] | [
"Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters.",
"Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein."
] | [
2001,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
45
] | 1 | [] | [] | 0 | true | Family | Glucose import system permease protein GlcT | Glucose import system permease protein GlcT | GlcT_permease | 9 |
IPR054948 | 54,948 | alpha-IPM synthase | IPMS | Family | 56 | true | false | 2-isopropylmalate synthase (IPMS) is an enzyme that catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). This reaction represents the first step in the leucine biosynthesis pathway. Members of thi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041069"
] | [
"IPMS"
] | [
56
] | 1 | [
"EC",
"METACYC"
] | [
"2.3.3.13",
"PWY-6871"
] | [
"EC:2.3.3.13",
"METACYC:PWY-6871"
] | 2 | [] | 0 | [
"PUB00106155"
] | [
"31330039"
] | [
"Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoproteati"
] | [
56
] | 1 | [] | [] | 0 | true | Family | alpha-IPM synthase | alpha-IPM synthase | IPMS | 5 |
IPR054949 | 54,949 | HTH-type transcriptional regulator CatM | HTH_CatM | Family | 50 | true | false | The HTH-type transcriptional regulator CatM is a protein found in Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). It positively regulates the expression of catA, catBCIJFD, and benPK in response to cis,cis-muconate. CatM binds to the catB-catM intercistronic region, a specific sequence upstream of catA, and th... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040710"
] | [
"HTH_CatM"
] | [
50
] | 1 | [] | [] | [] | 0 | [
"2h98"
] | 1 | [
"PUB00047583",
"PUB00105920",
"PUB00105922"
] | [
"19400783",
"16517618",
"14684899"
] | [
"Inducer responses of BenM, a LysR-type transcriptional regulator from Acinetobacter baylyi ADP1.",
"CatM regulation of the benABCDE operon: functional divergence of two LysR-type paralogs in Acinetobacter baylyi ADP1.",
"Crystallization of the effector-binding domains of BenM and CatM, LysR-type transcriptiona... | [
2009,
2006,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Acinetobacter"
] | [
50
] | 1 | [] | [] | 0 | true | Family | HTH-type transcriptional regulator CatM | HTH-type transcriptional regulator CatM | HTH_CatM | 1 |
IPR054950 | 54,950 | Methane monooxygenase component C | MethMoxCompC | Family | 49 | true | false | Methane monooxygenase component C (mmoC) from Methylococcus capsulatus is responsible for the initial oxygenation of methane to methanol in methanotrophs. This enzyme also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic, and heterocyclic compounds. The component C is the iron-su... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045803"
] | [
"MethMoxCompC"
] | [
49
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001791",
"PUB00154631",
"PUB00154633"
] | [
"2205538",
"1845980",
"1785954"
] | [
"The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath).",
"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction.",
"The methane monooxygenase gene cluster of Methylosinus trichosporium... | [
1990,
1991,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
49
] | 1 | [] | [] | 0 | true | Family | Methane monooxygenase component C | Methane monooxygenase component C | MethMoxCompC | 1 |
IPR054951 | 54,951 | Cell division protein CdvC | cell_div_CdvC | Family | 48 | true | false | Cell division protein CdvC is a member of the AAA ATPase family and is involved in the cell division machinery of Sulfolobus acidocaldarius. The CdvA, CdvB, and CdvC proteins polymerize between segregating nucleoids and persist throughout cell division, forming a successively smaller structure during constriction. The ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041006"
] | [
"cell_div_CdvC"
] | [
48
] | 1 | [] | [] | [] | 0 | [
"4lcb"
] | 1 | [
"PUB00050019",
"PUB00083231"
] | [
"19008417",
"18987308"
] | [
"A role for the ESCRT system in cell division in archaea.",
"A unique cell division machinery in the Archaea."
] | [
2008,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoprotei"
] | [
48
] | 1 | [] | [] | 0 | true | Family | Cell division protein CdvC | Cell division protein CdvC | cell_div_CdvC | 6 |
IPR054952 | 54,952 | Oxalate oxidoreductase subunit beta | OxalOxred_beta | Family | 37 | true | false | Oxalate oxidoreductase subunit beta is an enzyme that catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. This enzyme does not require coenzyme A as a cosubstrate and enables anaerobic growth on oxalate, whi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045792"
] | [
"OxalOxred_beta"
] | [
37
] | 1 | [] | [] | [] | 0 | [
"5c4i",
"5exd",
"5exe"
] | 3 | [
"PUB00078738"
] | [
"20956531"
] | [
"Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
37
] | 1 | [] | [] | 0 | true | Family | Oxalate oxidoreductase subunit beta | Oxalate oxidoreductase subunit beta | OxalOxred_beta | 9 |
IPR054953 | 54,953 | Methane monooxygenase component A gamma chain | MethMoxGammaMmoZ | Family | 43 | true | false | Methane monooxygenase (MMO) is an enzyme complex found in methanotrophic bacteria that catalyzes the initial oxygenation of methane to methanol. The gamma chain of the methane monooxygenase component A, also known as mmoZ, plays a crucial role in this process. This subunit is responsible for the monohydroxylation of a ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045805"
] | [
"MethMoxGammaMmoZ"
] | [
43
] | 1 | [] | [] | [] | 0 | [
"1fyz",
"1fz0",
"1fz1",
"1fz2",
"1fz3",
"1fz4",
"1fz5",
"1fz6",
"1fz7",
"1fz8",
"1fz9",
"1fzh",
"1fzi",
"1mhy",
"1mhz",
"1mmo",
"1mty",
"1xmf",
"1xmg",
"1xmh",
"1xu3",
"1xu5",
"1xvb",
"1xvc",
"1xvd",
"1xve",
"1xvf",
"1xvg",
"4gam",
"6d7k",
"6vk4",
"6vk5"... | 50 | [
"PUB00019847",
"PUB00154630",
"PUB00154631",
"PUB00154632"
] | [
"8255292",
"2505721",
"1845980",
"1904125"
] | [
"Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.",
"Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath).",
"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. ... | [
1993,
1989,
1991,
1991
] | 4 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
43
] | 1 | [] | [] | 0 | true | Family | Methane monooxygenase component A gamma chain | Methane monooxygenase component A gamma chain | MethMoxGammaMmoZ | 1 |
IPR054954 | 54,954 | Carbonic anhydrase, gamma-class | carb_anhyd | Family | 32 | true | false | Carbonic anhydrases (CAs) are enzymes that catalyze the reversible hydration of carbon dioxide. This entry represents the gamma-class carbonic anhydrase family, which includes enzymes that are important for growth on acetate. In Methanosarcina thermophila, the carbonic anhydrase (MSTHT_0588) is likely an extracellular ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040597"
] | [
"carb_anhyd"
] | [
32
] | 1 | [] | [] | [] | 0 | [
"1qq0",
"1qre",
"1qrf",
"1qrg",
"1qrl",
"1qrm",
"1thj",
"3otm",
"3otz",
"3ou9",
"3oup",
"3ow5",
"9lin"
] | 13 | [
"PUB00105846"
] | [
"8041719"
] | [
"A carbonic anhydrase from the archaeon Methanosarcina thermophila."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Methanosarcinaceae",
"bioreactor metagenome"
] | [
31,
1
] | 2 | [] | [] | 0 | true | Family | Carbonic anhydrase, gamma-class | Carbonic anhydrase, gamma-class | carb_anhyd | 4 |
IPR054955 | 54,955 | Methane monooxygenase regulatory protein B | MethMoxRegMmoB | Family | 42 | true | false | Methane monooxygenase regulatory protein B (MmoB) is a component of the soluble methane monooxygenase (sMMO) complex found in methanotrophic bacteria such as Methylosinus trichosporium and Methylococcus capsulatus. The MmoB protein acts as a regulator of electron flow through the sMMO complex, switching the enzyme from... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045804"
] | [
"MethMoxRegMmoB"
] | [
42
] | 1 | [] | [] | [] | 0 | [
"1ckv",
"2mob",
"4gam",
"6vk4",
"6vk5",
"6vk8",
"6yd0",
"6ydi",
"6ydu",
"6yy3",
"7m8q",
"7m8r",
"7s6q",
"7s6r",
"7s6s",
"7s6t",
"7s7h",
"8xiw"
] | 18 | [
"PUB00154630",
"PUB00154631",
"PUB00154632",
"PUB00154634"
] | [
"2505721",
"1845980",
"1904125",
"10381404"
] | [
"Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath).",
"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction.",
"Molecular analysis of the methane monooxygenase (MMO) gene cl... | [
1989,
1991,
1991,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
42
] | 1 | [] | [] | 0 | true | Family | Methane monooxygenase regulatory protein B | Methane monooxygenase regulatory protein B | MethMoxRegMmoB | 4 |
IPR054956 | 54,956 | Methane monooxygenase component A beta chain | MethMoxA_beta | Family | 45 | true | false | Methane monooxygenase component A beta chain is responsible for the initial oxygenation of methane to methanol in methanotrophs. This enzyme also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic, and heterocyclic compounds. The enzyme is found in species such as Methylosinus tric... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045802"
] | [
"MethMoxA_beta"
] | [
45
] | 1 | [] | [] | [] | 0 | [
"1fyz",
"1fz0",
"1fz1",
"1fz2",
"1fz3",
"1fz4",
"1fz5",
"1fz6",
"1fz7",
"1fz8",
"1fz9",
"1fzh",
"1fzi",
"1mhy",
"1mhz",
"1mmo",
"1mty",
"1xmf",
"1xmg",
"1xmh",
"1xu3",
"1xu5",
"1xvb",
"1xvc",
"1xvd",
"1xve",
"1xvf",
"1xvg",
"4gam",
"6d7k",
"6vk4",
"6vk5"... | 50 | [
"PUB00019847",
"PUB00154630",
"PUB00154631",
"PUB00154632"
] | [
"8255292",
"2505721",
"1845980",
"1904125"
] | [
"Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.",
"Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath).",
"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. ... | [
1993,
1989,
1991,
1991
] | 4 | [] | [] | 0 | 0 | null | [
"Plasmodium yoelii yoelii",
"Pseudomonadota"
] | [
1,
44
] | 2 | [] | [] | 0 | true | Family | Methane monooxygenase component A beta chain | Methane monooxygenase component A beta chain | MethMoxA_beta | 2 |
IPR054957 | 54,957 | Phospho-furanose lactonase | PhFuoseLconase | Family | 50 | true | false | Phospho-furanose lactonase catalyzes the hydrolysis of D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. It is also capable of hydrolyzing carboxy 1,4-lactones. This enzyme belongs to the metallo-dependent hydrolases superfamily, specifically the phosphotriesterase family. The enzyme is found in M... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045706"
] | [
"PhFuoseLconase"
] | [
50
] | 1 | [] | [] | [] | 0 | [
"3msr",
"3ovg"
] | 2 | [
"PUB00085013"
] | [
"24955762"
] | [
"Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Phospho-furanose lactonase | Phospho-furanose lactonase | PhFuoseLconase | 6 |
IPR054958 | 54,958 | NurA family nuclease | NurA_nuclease | Family | 30 | true | false | The DNA double-strand break repair nuclease NurA is involved in the repair of DNA double-strand breaks (DSBs). It likely acts in conjunction with HerA to stimulate the resection of the 5' strand, producing the long 3' single-strand required for RadA loading. NurA exhibits 5' endonuclease activity as well as both 5' and... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041032"
] | [
"NurA_nuclease"
] | [
30
] | 1 | [] | [] | [] | 0 | [
"3tai",
"3tal",
"3taz"
] | 3 | [
"PUB00105991",
"PUB00106139"
] | [
"18957200",
"22064858"
] | [
"The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break.",
"Crystal structure of the NurA-dAMP-Mn2+ complex."
] | [
2008,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
30
] | 1 | [] | [] | 0 | true | Family | NurA family nuclease | NurA family nuclease | NurA_nuclease | 7 |
IPR054959 | 54,959 | Sarcosine reductase complex component B subunit beta | Sarcosine_GrdF | Family | 39 | true | false | Sarcosine reductase complex component B subunit beta is involved in the first step of sarcosine reductase. The substrate is bound to component PB via a Schiff base intermediate. The PB-activated substrate is then nucleophilically attacked by the selenol anion of component PA, transforming it into a carboxymethylated se... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040794"
] | [
"Sarcosine_GrdF"
] | [
39
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105967"
] | [
"24926057"
] | [
"Complete Genome Sequence of Amino Acid-Utilizing Eubacterium acidaminophilum al-2 (DSM 3953)."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
39
] | 1 | [] | [] | 0 | true | Family | Sarcosine reductase complex component B subunit beta | Sarcosine reductase complex component B subunit beta | Sarcosine_GrdF | 8 |
IPR054961 | 54,961 | MPN499 protein | MPN499 | Family | 62 | true | true | This entry represents the MPN499 family protein, which is currently uncharacteriσed. The protein is found in Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) and is encoded by the MPN_499 gene. The specific function of this protein family remains unknown. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045754",
"PF26924"
] | [
"MPN499",
"MPN_499"
] | [
51,
62
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154763"
] | [
"22373819"
] | [
"Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
62
] | 1 | [] | [] | 0 | true | Family | MPN499 protein | MPN499 protein | MPN499 | 3 |
IPR054963 | 54,963 | Trehalase 2 | Trehalase_2 | Family | 35 | true | false | Trehalase 2 is an enzyme that catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose. It belongs to the glycosyl hydrolase 15 family and is found in Sulfolobus acidocaldarius. This enzyme plays a crucial role in carbohydrate metabolism by breaking down trehalose, a disaccharide sugar. The act... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041085"
] | [
"Trehalase_2"
] | [
35
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106167"
] | [
"29574614"
] | [
"Two trehalose-hydrolyzing enzymes from Crenarchaeon Sulfolobus acidocaldarius exhibit distinct activities and affinities toward trehalose."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
35
] | 1 | [] | [] | 0 | true | Family | Trehalase 2 | Trehalase 2 | Trehalase_2 | 3 |
IPR054964 | 54,964 | Preflagellin peptidase | Arch_preflagellin_pept | Family | 35 | true | false | Preflagellin peptidases, also known as FlaK, are enzymes that cleave the N-terminal leader peptide from preflagellins. This processing is necessary for the assembly of flagellins into a flagellum structure. These enzymes belong to the peptidase A24 family, specifically the archaeal preflagellin peptidase subfamily. The... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040695"
] | [
"Arch_preflagellin_pept"
] | [
35
] | 1 | [
"EC"
] | [
"3.4.23.52"
] | [
"EC:3.4.23.52"
] | 1 | [
"3s0x"
] | 1 | [
"PUB00010516",
"PUB00066803"
] | [
"11934494",
"21765428"
] | [
"FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity.",
"The crystal structure of GXGD membrane protease FlaK."
] | [
2002,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Methanococcales"
] | [
35
] | 1 | [] | [] | 0 | true | Family | Preflagellin peptidase | Preflagellin peptidase | Arch_preflagellin_pept | 5 |
IPR054965 | 54,965 | HTH-type sugar sensing transcriptional regulator TrmB | tran_reg_TrmB | Family | 22 | true | false | The HTH-type sugar sensing transcriptional regulator TrmB is a protein family involved in the regulation of sugar metabolism in archaea. Members of this family, such as those found in Pyrococcus furiosus (Q9HGZ9) and Thermococcus litoralis (Q7LYW4), contain an N-terminal DNA-binding domain and a C-terminal sugar-bindin... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040851"
] | [
"tran_reg_TrmB"
] | [
22
] | 1 | [] | [] | [] | 0 | [
"3qph"
] | 1 | [
"PUB00015607",
"PUB00060975",
"PUB00106022"
] | [
"12426307",
"16135241",
"17504272"
] | [
"TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis.",
"TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers.",
... | [
2003,
2005,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
22
] | 1 | [] | [] | 0 | true | Family | HTH-type sugar sensing transcriptional regulator TrmB | HTH-type sugar sensing transcriptional regulator TrmB | tran_reg_TrmB | 3 |
IPR054966 | 54,966 | 4-epi-cubebol synthase | epi-cubol_syn | Family | 58 | true | false | 4-epi-cubebol synthase is an enzyme that belongs to the terpene synthase family. It catalyses the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpenol 4-epi-cubebol via a 1,10-cyclization. This process requires the abstraction of the pyrophosphate from FPP to yield a (E,E)-germacradieny... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042951"
] | [
"epi-cubol_syn"
] | [
58
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00151349",
"PUB00151350"
] | [
"27829890",
"27666571"
] | [
"Mechanistic investigations on six bacterial terpene cyclases.",
"Lessons from 1,3-Hydride Shifts in Sesquiterpene Cyclizations."
] | [
2016,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Streptosporangiaceae"
] | [
58
] | 1 | [] | [] | 0 | true | Family | 4-epi-cubebol synthase | 4-epi-cubebol synthase | epi-cubol_syn | 9 |
IPR054968 | 54,968 | 1-deoxy-11-beta-hydroxypentalenate dehydrogenase | HdxpentlteDhPtlF | Family | 30 | true | false | This entry represents 1-deoxy-11-beta-hydroxypentalenate dehydrogenase, an enzyme involved in the biosynthesis of pentalenolactone antibiotics. The enzyme catalyzes the oxidation of 1-deoxy-11-beta-hydroxypentalenic acid to 1-deoxy-11-oxopentalenic acid. Members of this family belong to the short-chain dehydrogenases/r... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045814"
] | [
"HdxpentlteDhPtlF"
] | [
30
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.340",
"PWY-6915",
"PWY-6919"
] | [
"EC:1.1.1.340",
"METACYC:PWY-6915",
"METACYC:PWY-6919"
] | 3 | [] | 0 | [
"PUB00154689",
"PUB00154691",
"PUB00154693"
] | [
"21284395",
"21250661",
"17178094"
] | [
"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone.",
"Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in t... | [
2011,
2011,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
30
] | 1 | [] | [] | 0 | true | Family | 1-deoxy-11-beta-hydroxypentalenate dehydrogenase | 1-deoxy-11-beta-hydroxypentalenate dehydrogenase | HdxpentlteDhPtlF | 4 |
IPR054969 | 54,969 | Pentalenene synthase | PentlnSyn | Family | 29 | true | false | Pentalenene synthase is an enzyme that catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene. This reaction is a key step in the biosynthesis of the pentalenolactone family of antibiotics, which are produced by various Streptomyces species. The enzyme belongs to the terpene ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045811"
] | [
"PentlnSyn"
] | [
29
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.2.3.7",
"PWY-6915",
"PWY-6919"
] | [
"EC:4.2.3.7",
"METACYC:PWY-6915",
"METACYC:PWY-6919"
] | 3 | [
"1hm4",
"1hm7",
"1ps1",
"6wkc",
"6wkd",
"6wke",
"6wkf",
"6wkg",
"6wkh",
"6wki",
"6wkj",
"9c7k",
"9c7l",
"9c7m"
] | 14 | [
"PUB00022455",
"PUB00154688",
"PUB00154689",
"PUB00154690"
] | [
"9295272",
"16681390",
"21284395",
"8180213"
] | [
"Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.",
"A gene cluster for biosynthesis of the sesquiterpenoid antibiotic pentalenolactone in Streptomyces avermitilis.",
"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidat... | [
1997,
2006,
2011,
1994
] | 4 | [
"IPR034686"
] | [] | 1 | 0 | 1 | [
"Actinomycetes"
] | [
29
] | 1 | [] | [] | 0 | true | Family | Pentalenene synthase | Pentalenene synthase | PentlnSyn | 7 |
IPR054970 | 54,970 | Alpha-L-rhamnosidase, ulvan degradation | Rhamnosidase_Flavobac | Family | 40 | true | false | Alpha-L-rhamnosidase is an enzyme that may be involved in the degradation of ulvan, the main polysaccharide component of the cell wall of Ulvales (green seaweed). Ulvan is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xyl... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041572"
] | [
"Rhamnosidase_Flavobac"
] | [
40
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00093668"
] | [
"31285597"
] | [
"A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Flavobacteriaceae"
] | [
40
] | 1 | [] | [] | 0 | true | Family | Alpha-L-rhamnosidase, ulvan degradation | Alpha-L-rhamnosidase, ulvan degradation | Rhamnosidase_Flavobac | 6 |
IPR054971 | 54,971 | 1-deoxypentalenic acid 11-beta-hydroxylase | DxPntBtaHylase | Family | 30 | true | false | 1-deoxypentalenic acid 11-beta-hydroxylase is an enzyme that catalyzes the conversion of 1-deoxypentalenic acid to 11-beta-hydroxy-1-deoxypentalenic acid. This reaction is a key step in the biosynthesis of the antibiotic pentalenolactone. The enzyme belongs to the PhyH family and is found in various Streptomyces specie... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045813"
] | [
"DxPntBtaHylase"
] | [
30
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.14.11.35",
"PWY-6915",
"PWY-6919"
] | [
"EC:1.14.11.35",
"METACYC:PWY-6915",
"METACYC:PWY-6919"
] | 3 | [
"2rdn",
"2rdq",
"2rdr",
"2rds"
] | 4 | [
"PUB00154689",
"PUB00154691",
"PUB00154692"
] | [
"21284395",
"21250661",
"16704250"
] | [
"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone.",
"Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in t... | [
2011,
2011,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
30
] | 1 | [] | [] | 0 | true | Family | 1-deoxypentalenic acid 11-beta-hydroxylase | 1-deoxypentalenic acid 11-beta-hydroxylase | DxPntBtaHylase | 2 |
IPR054973 | 54,973 | Pentalenolactone F synthase | PentlctneF_syn | Family | 29 | true | false | This entry represents pentalenolactone F synthase, an enzyme that catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F. This enzyme is involved in the biosynthesis of the pentalenolactone antibiotic. Additionally, it can catalyze the oxidation of pentalenolactone ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045815"
] | [
"PentlctneF_syn"
] | [
29
] | 1 | [
"EC"
] | [
"1.14.11.36"
] | [
"EC:1.14.11.36"
] | 1 | [] | 0 | [
"PUB00154689",
"PUB00154691"
] | [
"21284395",
"21250661"
] | [
"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone.",
"Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in t... | [
2011,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
29
] | 1 | [] | [] | 0 | true | Family | Pentalenolactone F synthase | Pentalenolactone F synthase | PentlctneF_syn | 7 |
IPR054974 | 54,974 | Pectinesterase B | Pectinest_B | Family | 50 | true | false | Pectinesterase B (PemB) is an enzyme that belongs to the pectinesterase family. It is involved in the degradation of methylated oligogalacturonides present in the periplasm. This enzyme is more active on methylated oligogalacturides than on pectin. Pectinesterase B is found in bacteria such as Dickeya dadantii (strain ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041901"
] | [
"Pectinest_B"
] | [
50
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00152933"
] | [
"8830237"
] | [
"Characterization of pectin methylesterase B, an outer membrane lipoprotein of Erwinia chrysanthemi 3937."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
50
] | 1 | [] | [] | 0 | true | Family | Pectinesterase B | Pectinesterase B | Pectinest_B | 4 |
IPR054976 | 54,976 | Pentalenolactone synthase | PentlenlactSyn | Family | 24 | true | false | Pentalenolactone synthase is an enzyme that catalyzes the final step in the biosynthesis of the sesquiterpenoid antibiotic pentalenolactone. This enzyme mediates the oxidative rearrangement of pentalenolactone F to pentalenolactone. It belongs to the cytochrome P450 family, which is known for its role in the oxidative ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045816"
] | [
"PentlenlactSyn"
] | [
24
] | 1 | [] | [] | [] | 0 | [
"5l1o",
"5l1p",
"5l1q",
"5l1r",
"5l1s",
"5l1t",
"5l1u",
"5l1v",
"5l1w"
] | 9 | [
"PUB00154689"
] | [
"21284395"
] | [
"Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
24
] | 1 | [] | [] | 0 | true | Family | Pentalenolactone synthase | Pentalenolactone synthase | PentlenlactSyn | 2 |
IPR054977 | 54,977 | Uncharacterized protein CT_504-like | CT_504-like | Family | 47 | false | false | This entry represents several uncharacterised proteins such as CT_504 from Chlamydia trachomatis, TC_0791 from Chlamydia muridarum and CPn_0623 from Chlamydia pneumoniae, and related proteins from Chlamydiaceae lineage. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045799",
"PF28261"
] | [
"GrgA",
"GrgA_tf"
] | [
31,
47
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154808",
"PUB00154809",
"PUB00154810",
"PUB00154811",
"PUB00154812"
] | [
"33940135",
"38112466",
"34342542",
"30061357",
"23027952"
] | [
"GrgA overexpression inhibits Chlamydia trachomatis growth through sigma<sup>66</sup>- and sigma<sup>28</sup>-dependent mechanisms.",
"Requirement of GrgA for <i>Chlamydia</i> infectious progeny production, optimal growth, and efficient plasmid maintenance.",
"Identification of a GrgA-Euo-HrcA Transcriptional R... | [
2021,
2024,
2021,
2018,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
46,
1
] | 2 | [] | [] | 0 | true | Family | Uncharacterized protein CT_504-like | Uncharacterized protein CT_504-like | CT_504-like | 3 |
IPR054978 | 54,978 | Endo-beta-N-acetylglucosaminidase F3 | Endoglyc_F3 | Family | 21 | true | false | Endo-beta-N-acetylglucosaminidase F3 (Endo F3) is an enzyme that catalyzes the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. It is capable of hydrolyzing bi- and triantennary glycans. The presence of a core-bound fucose significantly enhances Endo F3 activity on bian... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045481"
] | [
"Endoglyc_F3"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"1eok",
"1eom"
] | 2 | [
"PUB00153667",
"PUB00153668"
] | [
"7768917",
"7768916"
] | [
"Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum.",
"Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteroidota"
] | [
21
] | 1 | [] | [] | 0 | true | Family | Endo-beta-N-acetylglucosaminidase F3 | Endo-beta-N-acetylglucosaminidase F3 | Endoglyc_F3 | 6 |
IPR054979 | 54,979 | Uncharacterized protein MG241/MG241-like | MG241/MG241-like | Family | 45 | true | true | This entry represents the uncharacterised proteins MG241 and MG242 from Mycoplasma genitalium and their homologues from Mycoplasma pneumoniae. The exact function of these proteins is currently unknown. | [] | [] | [] | 0 | [
"NCBIFAM",
"NCBIFAM",
"PFAM"
] | [
"NF045749",
"NF045750",
"PF28262"
] | [
"MPN337",
"MPN338_fam_protein",
"MPN337"
] | [
23,
28,
45
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154763",
"PUB00154765"
] | [
"22373819",
"32732422"
] | [
"Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.",
"In-cell architecture of an actively transcribing-translating expressome."
] | [
2012,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
45
] | 1 | [] | [] | 0 | true | Family | Uncharacterized protein MG241/MG241-like | Uncharacterized protein MG241/MG241-like | MG241/MG241-like | 9 |
IPR054980 | 54,980 | Nine-heme cytochrome c | 9HemeCytC | Family | 15 | true | false | Nine-heme cytochrome c proteins are characterized by the presence of nine heme groups arranged into two tetraheme clusters, with an additional heme located asymmetrically between the two regions. These proteins may form part of a transmembrane redox complex, facilitating electron transfer to the cytoplasm for the reduc... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045784"
] | [
"9HemeCytC"
] | [
15
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00023222",
"PUB00154813"
] | [
"10368280",
"10471375"
] | [
"The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family.",
"Sequencing the gene encoding desulfovibrio desulfuricans ATCC 27774 nine-heme cytochrome c."
] | [
1999,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Desulfovibrio"
] | [
15
] | 1 | [] | [] | 0 | true | Family | Nine-heme cytochrome c | Nine-heme cytochrome c | 9HemeCytC | 7 |
IPR054981 | 54,981 | Indoleacetate decarboxylase activating enzyme | Ind_deCO2_activ | Family | 14 | true | false | This entry represents the indoleacetate decarboxylase activating enzyme. This enzyme catalyzes the activation of indoleacetate decarboxylase under anaerobic conditions by generating an organic free radical on a glycine residue through the homolytic cleavage of S-adenosyl-L-methionine (SAM). The enzyme belongs to the or... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF033719"
] | [
"Ind_deCO2_activ"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
14
] | 1 | [] | [] | 0 | true | Family | Indoleacetate decarboxylase activating enzyme | Indoleacetate decarboxylase activating enzyme | Ind_deCO2_activ | 1 |
IPR054982 | 54,982 | Chondroitinase-AC | ChondaseAC | Family | 14 | true | false | Chondroitinase-AC, also known as chondroitinase AC, is an enzyme that belongs to the polysaccharide lyase 8 family. This enzyme is involved in the degradation of chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix of animal tissues. Chondroitinase-AC specifically cleaves the glycosidic bonds in c... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043001"
] | [
"ChondaseAC"
] | [
14
] | 1 | [] | [] | [] | 0 | [
"1cb8",
"1hm2",
"1hm3",
"1hmu",
"1hmw"
] | 5 | [
"PUB00010617",
"PUB00153666"
] | [
"11327856",
"10618199"
] | [
"Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.",
"Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium... | [
2001,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteroidota"
] | [
14
] | 1 | [] | [] | 0 | true | Family | Chondroitinase-AC | Chondroitinase-AC | ChondaseAC | 5 |
IPR054983 | 54,983 | Iron transporter MagA | FeTrans_MagA | Family | 12 | true | false | Iron transporter MagA is a protein found in Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1). It plays a crucial role in the synthesis of bacterial magnetic particles (BMPs) by transporting iron from the environment into the cytoplasm across the cell membrane, and subsequently from the cytoplasm into the BM... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045626"
] | [
"FeTrans_MagA"
] | [
12
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154760",
"PUB00154761"
] | [
"8537318",
"7499342"
] | [
"Iron-regulated expression and membrane localization of the magA protein in Magnetospirillum sp. strain AMB-1.",
"An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Rhodospirillales"
] | [
12
] | 1 | [] | [] | 0 | true | Family | Iron transporter MagA | Iron transporter MagA | FeTrans_MagA | 7 |
IPR054984 | 54,984 | Digeranylgeranylglycerophospholipid reductase family | DGGPL_reductase | Family | 10 | true | false | Digeranylgeranylglycerophospholipid reductase is an enzyme involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. This enzyme catalyzes the formation of archaetidic acid ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041160"
] | [
"DGGPL_reductase"
] | [
10
] | 1 | [
"EC",
"METACYC"
] | [
"1.3.1.101",
"PWY-6141"
] | [
"EC:1.3.1.101",
"METACYC:PWY-6141"
] | 2 | [
"3oz2"
] | 1 | [
"PUB00054596",
"PUB00106211"
] | [
"16788058",
"20869368"
] | [
"Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum.",
"Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme i... | [
2006,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoplasmatales"
] | [
10
] | 1 | [] | [] | 0 | true | Family | Digeranylgeranylglycerophospholipid reductase family | Digeranylgeranylglycerophospholipid reductase family | DGGPL_reductase | 6 |
IPR054985 | 54,985 | Hexaprenyl-diphosphate synthase large subunit | HxpDPsynlarge | Family | 21 | true | false | Hexaprenyl-diphosphate synthase large subunit catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. The large subunit, Hexs-B, is responsible for the condensa... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045628"
] | [
"HxpDPsynlarge"
] | [
21
] | 1 | [] | [] | [] | 0 | [
"3aqb",
"3aqc"
] | 2 | [
"PUB00057665",
"PUB00154814"
] | [
"21068379",
"9515931"
] | [
"Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation.",
"Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Microc... | [
2011,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
21
] | 1 | [] | [] | 0 | true | Family | Hexaprenyl-diphosphate synthase large subunit | Hexaprenyl-diphosphate synthase large subunit | HxpDPsynlarge | 5 |
IPR054987 | 54,987 | 3(1)-hydroxy-L-isoleucine 4-dioxygenase | Il_dioxgen_HilB | Family | 19 | true | false | This entry represents the enzyme 3(1)-hydroxy-L-isoleucine 4-dioxygenase, also known as HilB, from Pantoea ananatis (strain AJ13355). HilB belongs to the iron/ascorbate-dependent oxidoreductase family and catalyzes the hydroxylation of L-4'-hydroxyisoleucine (4'-HIL) at the C-4 position to form L-4,4'-dihydroxyisoleuci... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042428"
] | [
"Il_dioxgen_HilB"
] | [
19
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100360",
"PUB00109260"
] | [
"23554367",
"22448874"
] | [
"A novel l-isoleucine-4'-dioxygenase and l-isoleucine dihydroxylation cascade in Pantoea ananatis.",
"A novel family of bacterial dioxygenases that catalyse the hydroxylation of free L-amino acids."
] | [
2013,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
19
] | 1 | [] | [] | 0 | true | Family | 3(1)-hydroxy-L-isoleucine 4-dioxygenase | 3(1)-hydroxy-L-isoleucine 4-dioxygenase | Il_dioxgen_HilB | 4 |
IPR054988 | 54,988 | Aldehyde dehydrogenase AldH | AldDh_AldH | Family | 16 | true | false | This entry represents aldehyde dehydrogenase (AldH) proteins, which belong to the aldehyde dehydrogenase family. These enzymes are capable of oxidizing various aldehydes such as formaldehyde, glyceraldehyde, butyraldehyde, glutaraldehyde, and benzaldehyde in vitro. They are likely involved in the oxidative D-xylose deg... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042989"
] | [
"AldDh_AldH"
] | [
16
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00095194"
] | [
"23063486"
] | [
"Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
16
] | 1 | [] | [] | 0 | true | Family | Aldehyde dehydrogenase AldH | Aldehyde dehydrogenase AldH | AldDh_AldH | 7 |
IPR054989 | 54,989 | MG267/MG319-like | MG267/MG319-like | Family | 22 | false | false | This entry represents a group of unchareacterised proteins for Mycoplasmatota, including MG267 and MG319 from Mycoplasma genitalium and its homologues from Mycoplasma pneumoniae. The exact function of these proteins is currently unknown. | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF045771",
"PF28263"
] | [
"MPN454_MG319",
"MPN454_MG319"
] | [
22,
22
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
22
] | 1 | [] | [] | 0 | true | Family | MG267/MG319-like | MG267/MG319-like | MG267/MG319-like | 6 |
IPR054990 | 54,990 | DNA double-strand break repair ATPase Rad50 | Rad50_ATPase_DNA_repair | Family | 14 | true | false | The DNA double-strand break repair ATPase Rad50 is a crucial component of the Rad50/Mre11 complex, which plays a significant role in the early stages of DNA double-strand break (DSB) repair. This complex is thought to facilitate the opening of processed DNA ends, aiding in the recruitment of other proteins such as HerA... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041034"
] | [
"Rad50_ATPase_DNA_repair"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106138"
] | [
"18294364"
] | [
"The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
14
] | 1 | [] | [] | 0 | true | Family | DNA double-strand break repair ATPase Rad50 | DNA double-strand break repair ATPase Rad50 | Rad50_ATPase_DNA_repair | 6 |
IPR054991 | 54,991 | Cyclohexane-1-carbonyl-CoA dehydrogenase | CyhCrbnylCoADH | Family | 8 | true | false | Cyclohexane-1-carbonyl-CoA dehydrogenase is an enzyme that belongs to the acyl-CoA dehydrogenase family. This enzyme is involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). It catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA). In G... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043006"
] | [
"CyhCrbnylCoADH"
] | [
8
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153596"
] | [
"23667239"
] | [
"Cyclohexanecarboxyl-coenzyme A (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Thermodesulfobacteriota"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Cyclohexane-1-carbonyl-CoA dehydrogenase | Cyclohexane-1-carbonyl-CoA dehydrogenase | CyhCrbnylCoADH | 1 |
IPR054992 | 54,992 | 46 kDa surface antigen | SurfProtP46 | Family | 10 | true | false | The 46 kDa surface antigen (P46) is a protein found in Mesomycoplasma hyopneumoniae, specifically in strains J (ATCC 25934 / NCTC 10110) and 232. This protein is implicated in the surface structure of the bacterium, potentially playing a role in host-pathogen interactions. The P46 protein is 416 amino acids in length a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045705"
] | [
"SurfProtP46"
] | [
10
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154777",
"PUB00154778"
] | [
"32355038",
"7896725"
] | [
"Structure of P46, an immunodominant surface protein from Mycoplasma hyopneumoniae: interaction with a monoclonal antibody.",
"Molecular cloning of a 46-kilodalton surface antigen (P46) gene from Mycoplasma hyopneumoniae: direct evidence of CGG codon usage for arginine."
] | [
2020,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Mesomycoplasma"
] | [
10
] | 1 | [] | [] | 0 | true | Family | 46 kDa surface antigen | 46 kDa surface antigen | SurfProtP46 | 9 |
IPR054993 | 54,993 | Bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD | FolD_Thplmales | Family | 10 | true | false | This entry represents the bifunctional protein FolD, which belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family. The FolD enzyme catalyzes two sequential reactions in the folate metabolism pathway: the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate, followed by the hydrolysi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041156"
] | [
"FolD_Thplmales"
] | [
10
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.5.1.5",
"3.5.4.9",
"PWY-1722",
"PWY-2201",
"PWY-3841",
"PWY-5030",
"PWY-5497",
"PWY-6613",
"PWY-7909",
"PWY-8303"
] | [
"EC:1.5.1.5",
"EC:3.5.4.9",
"METACYC:PWY-1722",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"METACYC:PWY-6613",
"METACYC:PWY-7909",
"METACYC:PWY-8303"
] | 10 | [
"3ngl",
"3ngx"
] | 2 | [
"PUB00055732",
"PUB00106207"
] | [
"21333632",
"8436115"
] | [
"Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum.",
"Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum."
] | [
2011,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoplasmatales"
] | [
10
] | 1 | [] | [] | 0 | true | Family | Bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD | Bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD | FolD_Thplmales | 6 |
IPR054994 | 54,994 | Dimethylsulfonioproprionate lyase DddY | DimsulpropLyDddY | Family | 6 | true | true | Dimethylsulfonioproprionate lyase DddY is an enzyme found in Alcaligenes faecalis that cleaves dimethylsulfonioproprionate (DMSP), releasing dimethyl sulfide (DMS). DMS is the principal form by which sulfur is transported from oceans to the atmosphere. This enzyme plays a crucial role in the global sulfur cycle by faci... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043049"
] | [
"DimsulpropLyDddY"
] | [
6
] | 1 | [] | [] | [] | 0 | [
"5xkx",
"5xky",
"5y4k",
"8hle"
] | 4 | [
"PUB00076456"
] | [
"21248856"
] | [
"DddY, a periplasmic dimethylsulfoniopropionate lyase found in taxonomically diverse species of Proteobacteria."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
6
] | 1 | [] | [] | 0 | true | Family | Dimethylsulfonioproprionate lyase DddY | Dimethylsulfonioproprionate lyase DddY | DimsulpropLyDddY | 1 |
IPR054995 | 54,995 | Esterase EstD | Esterase_EstD | Family | 10 | true | false | Esterase EstD from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) is a member of the AB hydrolase superfamily, specifically the Esterase 10 family. This enzyme exhibits significant esterase activity with a preference for short acyl chain esters (C4-C8) in vitro. Its physiological fu... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041096"
] | [
"Esterase_EstD"
] | [
10
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075373"
] | [
"17466017"
] | [
"Characterization and structural modeling of a new type of thermostable esterase from Thermotoga maritima."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Thermotogales"
] | [
10
] | 1 | [] | [] | 0 | true | Family | Esterase EstD | Esterase EstD | Esterase_EstD | 3 |
IPR054996 | 54,996 | Glycerate 2-kinase | Gly_kinase | Family | 8 | true | false | Glycerate 2-kinase (EC 2.7.1.165) catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. This enzyme belongs to the glycerate kinase type-1 family and is involved in the glycerate pathway. It can also partially utilize GTP, CTP, or UTP as phosphate donors. The enzyme is found in various organ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040791"
] | [
"Gly_kinase"
] | [
8
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105964"
] | [
"16684110"
] | [
"Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoplasmatales"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Glycerate 2-kinase | Glycerate 2-kinase | Gly_kinase | 4 |
IPR054997 | 54,997 | Cytochrome c-554 Puf2C | Cyt554Puf2C | Family | 9 | true | false | Cytochrome c-554, encoded by the puf2C gene in Chloroflexus aurantiacus, serves as the immediate electron donor to the oxidized bacteriochlorophyll dimer (BChl2) during the initial step of light-induced charge separation. This protein can also oxidize low-potential substrates, playing a crucial role in the electron tra... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043009"
] | [
"Cyt554Puf2C"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"8ydm"
] | 1 | [
"PUB00153489",
"PUB00153490"
] | [
"1660302",
"7535995"
] | [
"The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus.",
"Cloning and sequencing of the genes encoding the light-harvesting B806-866 polypeptides and initial studies on the transcriptional organization of puf2B, puf2A and puf2C in Chloroflexus aurantiacus."
] | [
1991,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Chloroflexineae"
] | [
9
] | 1 | [] | [] | 0 | true | Family | Cytochrome c-554 Puf2C | Cytochrome c-554 Puf2C | Cyt554Puf2C | 2 |
IPR054998 | 54,998 | Nucleoside kinase | NucKin | Family | 7 | true | false | This entry represents nucleoside kinases, which belong to the carbohydrate kinase PfkB family. These enzymes catalyze the phosphorylation of various nucleosides to their corresponding nucleoside 5'-mono-phosphates in the presence of phosphate donors and divalent cations. The nucleoside kinase from Thermoplasma acidophi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041164"
] | [
"NucKin"
] | [
7
] | 1 | [] | [] | [] | 0 | [
"3bf5"
] | 1 | [
"PUB00106214"
] | [
"23161756"
] | [
"A broad specificity nucleoside kinase from Thermoplasma acidophilum."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoplasmatales"
] | [
7
] | 1 | [] | [] | 0 | true | Family | Nucleoside kinase | Nucleoside kinase | NucKin | 2 |
IPR054999 | 54,999 | Hexaprenyl-diphosphate synthase, small subunit | HexA | Family | 9 | false | false | This entry represents the small subunit of Hexaprenyl-diphosphate synthase (HexA) found in bacterial proteins. It is composed of mostly antiparallel α-helices joined by connecting loops [ ]. Hexaprenyl-diphosphate synthase from Micrococcus luteus is made of a small subunit (HexA) and a large subunit (HexB). HexA cataly... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045627"
] | [
"HxpDPsynsmall"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"3aqb",
"3aqc"
] | 2 | [
"PUB00057665",
"PUB00154814"
] | [
"21068379",
"9515931"
] | [
"Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation.",
"Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Microc... | [
2011,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
9
] | 1 | [] | [] | 0 | true | Family | Hexaprenyl-diphosphate synthase, small subunit | Hexaprenyl-diphosphate synthase, small subunit | HexA | 9 |
IPR055000 | 55,000 | Uncharacterised protein MPN160 family | MPN160_family | Family | 8 | true | false | This entry represents a family of uncharacterised proteins, including the uncharacterised protein MG147 homolog from Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) and the uncharacterised protein MG147 from Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37). The function of these pro... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045740"
] | [
"MPN160_family"
] | [
8
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Uncharacterised protein MPN160 family | Uncharacterised protein MPN160 family | MPN160_family | 2 |
IPR055001 | 55,001 | L-2-amino-4-chloropent-4-enoate dechlorinase/desaturase | PAGG_Syn_BesB | Family | 10 | true | true | This entry represents the enzyme L-2-amino-4-chloropent-4-enoate dechlorinase/desaturase, also known as BesB, from Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057). This enzyme is involved in the biosynthesis of terminal alkyne-containing amino acids such as L-proparg... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042918"
] | [
"PAGG_Syn_BesB"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"9aua",
"9aub"
] | 2 | [
"PUB00093050"
] | [
"30867596"
] | [
"Discovery of a pathway for terminal-alkyne amino acid biosynthesis."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Streptomycetaceae"
] | [
10
] | 1 | [] | [] | 0 | true | Family | L-2-amino-4-chloropent-4-enoate dechlorinase/desaturase | L-2-amino-4-chloropent-4-enoate dechlorinase/desaturase | PAGG_Syn_BesB | 6 |
IPR055003 | 55,003 | GLD-3, KH3 domain | KH-I_CeGLD3_3rd | Domain | 18 | false | false | GLD-3 from C.elegans, also called defective in germ line development protein 3, is a Bicaudal-C (Bic-C) homologue that is involved in the translational control of germline-specific mRNAs during embryogenesis. It interacts with the cytoplasmic poly(A)-polymerase GLD-2. The two proteins cooperate to recognize target mRNA... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22467"
] | [
"KH_GLD-3_3rd"
] | [
18
] | 1 | [] | [] | [] | 0 | [
"3n89"
] | 1 | [
"PUB00091480"
] | [
"20823118"
] | [
"Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Caenorhabditis"
] | [
18
] | 1 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | GLD-3, KH3 domain | GLD-3, KH3 domain | KH-I_CeGLD3_3rd | 4 |
IPR055004 | 55,004 | CFAP410, C-terminal domain | CFAP410_C | Domain | 41 | false | false | This entry represents the C-terminal domain of Trypanosoma brucei cilia and flagella associated protein 410 (CFAP410) and related proteins. This domain is involved in oligomerisation and self-associates to form a tetrameric helical bundle composed of a dimer of two interlocking dimers. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22800"
] | [
"CFAP410_C"
] | [
41
] | 1 | [] | [] | [] | 0 | [
"8axo"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Metakinetoplastina"
] | [
41
] | 1 | [] | [] | 0 | true | Domain | CFAP410, C-terminal domain | CFAP410, C-terminal domain | CFAP410_C | 5 |
IPR055005 | 55,005 | S-layer protein, domain II | SlpA_D2 | Domain | 150 | false | false | This domain is found in S-layer protein (SlpA) from Lactobacillus acidophilus and similar sequences. This domain is involved in the self-assembly and dimerisation of the S-layer. It adopts an α/β structure consisting of a curved mixed β-sheet and two α-helices packed on it. It has a partial structural similarity to the... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22797"
] | [
"SlpA_D2"
] | [
150
] | 1 | [] | [] | [] | 0 | [
"7qec",
"7qfl",
"8bt9"
] | 3 | [
"PUB00154867"
] | [
"38838019"
] | [
"The molecular architecture of <i>Lactobacillus</i> S-layer: Assembly and attachment to teichoic acids."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Lactobacillaceae"
] | [
150
] | 1 | [] | [] | 0 | true | Domain | S-layer protein, domain II | S-layer protein, domain II | SlpA_D2 | 5 |
IPR055006 | 55,006 | S-layer protein, N-terminal domain | SlpA_N | Domain | 113 | false | false | This entry represents the N-terminal domain of S-layer protein SlpA from Lactobacillus amylovorus and related proteins. This domain adopts unusual topology composed of β-strands arranged in a barrel-sandwich fold [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22796"
] | [
"SlpA_N"
] | [
113
] | 1 | [] | [] | [] | 0 | [
"7qld",
"7qle",
"7qlh",
"8q1o"
] | 4 | [
"PUB00154867"
] | [
"38838019"
] | [
"The molecular architecture of <i>Lactobacillus</i> S-layer: Assembly and attachment to teichoic acids."
] | [
2024
] | 1 | [] | [] | 0 | 0 | null | [
"Lactobacillus"
] | [
113
] | 1 | [] | [] | 0 | true | Domain | S-layer protein, N-terminal domain | S-layer protein, N-terminal domain | SlpA_N | 7 |
IPR055007 | 55,007 | NACHT-associated inactive Restriction Endonuclease 2 domain | NA-iREase2_dom | Domain | 70 | false | false | This entry represents a predicted sensor domain in bacterial NACHT conflict systems. It is likely to bind a ligand which could contribute to activation of enzymatic domains additionally fused to the N terminus of the NACHT module [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22723"
] | [
"NA-iREase2"
] | [
70
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154095"
] | [
"37160116"
] | [
"Bacterial NLR-related proteins protect against phage."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
69,
1
] | 2 | [] | [] | 0 | true | Domain | NACHT-associated inactive Restriction Endonuclease 2 domain | NACHT-associated inactive Restriction Endonuclease 2 domain | NA-iREase2_dom | 1 |
IPR055008 | 55,008 | MrpR, C-terminal catalytic domain | MrpR_C_cat | Domain | 277 | false | false | This family includes the MrpR protein from Bacillus subtilis (also known as SPbeta prophage-derived protein YopR), the master repressor of the lytic cycle of the temperate phage SPbeta. MrpR, a DNA-binding protein that has lost its recombinase function, shows a tyrosine recombinase fold with an N-terminal all-α domain ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22823"
] | [
"MrpR_C_cat"
] | [
277
] | 1 | [] | [] | [] | 0 | [
"8a0a",
"8bj6",
"8bjv",
"8bpz"
] | 4 | [
"PUB00154082"
] | [
"37602373"
] | [
"Structural and functional characterization of MrpR, the master repressor of the Bacillus subtilis prophage SPβ."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Viruses"
] | [
258,
19
] | 2 | [] | [] | 0 | true | Domain | MrpR, C-terminal catalytic domain | MrpR, C-terminal catalytic domain | MrpR_C_cat | 9 |
IPR055011 | 55,011 | Tag1, C-terminal domain | Tag1_C | Domain | 1,152 | false | false | This entry represents the C-terminal Ig-like domain of yeast Tag1 (also known as YLR173W). It shows homology to LEA-2 domain, and together with TMEM106B from humans and Vac7 from yeast, are all predicted to be lipid transfer proteins [ ]. Tag1 is a vacuolar membrane protein involved in termination of autophagy. It regu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22786"
] | [
"Tag1_C"
] | [
1152
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100166",
"PUB00100170"
] | [
"34347309",
"33536246"
] | [
"TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.",
"Vacuolar protein Tag1 and Atg1-Atg13 regulate autophagy termination during persistent starvation in <i>S. cerevisiae</i>."
] | [
2022,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1152
] | 1 | [
"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 | Tag1, C-terminal domain | Tag1, C-terminal domain | Tag1_C | 5 |
IPR055012 | 55,012 | Tag1, N-terminal domain | Tag1_N | Domain | 67 | false | false | This entry represents the N-terminal domain of yeast Tag1 (also known as YLR173W). Tag1 is a vacuolar membrane protein involved in termination of autophagy. It regulates autophagy termination during persistent nitrogen starvation through Atg1p-mediated re-phosphorylation of Atg13p and PAS disassembly. It shows homology... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF20775"
] | [
"Tag1_N"
] | [
67
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00100166",
"PUB00100170"
] | [
"34347309",
"33536246"
] | [
"TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.",
"Vacuolar protein Tag1 and Atg1-Atg13 regulate autophagy termination during persistent starvation in <i>S. cerevisiae</i>."
] | [
2022,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
67
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Tag1, N-terminal domain | Tag1, N-terminal domain | Tag1_N | 4 |
IPR055013 | 55,013 | Cobalt-zinc-cadmium resistance protein CzcI | CzcI | Family | 175 | false | false | This entry represents a group of proteins from betaproteobacteria, including Cobalt-zinc-cadmium resistance protein CzcI from Cupriavidus metallidurans. CzcI is a component of the czc cation-efflux system that confers resistance to cobalt, zinc and cadmium [ , , ]. This protein may have a regulatory function. | [
"GO:0046686"
] | [
"response to cadmium ion"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"NF045614"
] | [
"efflu_CzcI_Cupr"
] | [
175
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00046109",
"PUB00154772",
"PUB00154773"
] | [
"7766206",
"32117100",
"1459958"
] | [
"The czc operon of Alcaligenes eutrophus CH34: from resistance mechanism to the removal of heavy metals.",
"Comparative Insights Into the Complete Genome Sequence of Highly Metal Resistant <i>Cupriavidus metallidurans</i> Strain BS1 Isolated From a Gold-Copper Mine.",
"CzcR and CzcD, gene products affecting reg... | [
1995,
2020,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Betaproteobacteria"
] | [
175
] | 1 | [] | [] | 0 | true | Family | Cobalt-zinc-cadmium resistance protein CzcI | Cobalt-zinc-cadmium resistance protein CzcI | CzcI | 5 |
IPR055014 | 55,014 | BapA/Bap-like, C-terminal domain | BapA_Bap-like_C | Domain | 1,956 | false | false | This entry represents a conserved C-terminal region shared by a number of large adhesins of Gram-negative genera mainly from gammaproteobacteria. Most members of this entry have repeat domains N-terminal to the region described here, including bacterial Ig-like domains. Notable members of the family include biofilm-ass... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045619"
] | [
"adhes_GNV_Cterm"
] | [
1956
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105145",
"PUB00154621",
"PUB00154622"
] | [
"18024522",
"21557055",
"22083703"
] | [
"Identification and characterization of an Acinetobacter baumannii biofilm-associated protein.",
"Adhesive mechanisms of Salmonella enterica.",
"The Acinetobacter baumannii biofilm-associated protein plays a role in adherence to human epithelial cells."
] | [
2008,
2011,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Panagrolaimomorpha"
] | [
1954,
2
] | 2 | [] | [] | 0 | true | Domain | BapA/Bap-like, C-terminal domain | BapA/Bap-like, C-terminal domain | BapA_Bap-like_C | 6 |
IPR055015 | 55,015 | 3-coathanger stack domain | GCX_COOH | Domain | 914 | false | false | This entry represents a domain which is frequently found as C-terminal of a larger protein, typically with Gly-Cys-Xaa(-Xaa) as the last three (or four) amino acids, or just upstream from type IX secretion system (T9SS) C-terminal sorting signal domain. In from Spirosoma taeanense, a member of this group, this domain i... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045639"
] | [
"GCX_COOH"
] | [
914
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
912,
2
] | 2 | [] | [] | 0 | true | Domain | 3-coathanger stack domain | 3-coathanger stack domain | GCX_COOH | 1 |
IPR055016 | 55,016 | Uncharacterised protein Aq_1974-like | Aq_1974-like | Family | 5 | false | false | This protein family includes the uncharacterised protein Aq_1974 from Aquifex aeolicus and similar sequences from Aquificales. This protein has a tryptophan content five times the average. Its structure is mainly α-helical with a small two-stranded β-sheet forming a fold named 'Aromatic Claw' [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22323"
] | [
"Aq_1974-like"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"5syq"
] | 1 | [
"PUB00153823"
] | [
"27750371"
] | [
"Aromatic claw: A new fold with high aromatic content that evades structural prediction."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Aquificaceae"
] | [
5
] | 1 | [] | [] | 0 | true | Family | Uncharacterised protein Aq_1974-like | Uncharacterised protein Aq_1974-like | Aq_1974-like | 8 |
IPR055017 | 55,017 | Tailspike protein, C-terminal domain | G7C_C | Domain | 3 | false | false | This entry represents the Concanavalin-like C-terminal domain of Tail fibre protein from Escherichia phage vB_EcoP_G7C ( ), also known as domain 6 (d6) of the tailspike receptor-binding protein (RBP) gp63.1. This domain is structurally similar to carbohydrate-binding domains and is putatively involved in substrate bind... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22245"
] | [
"G7C_C"
] | [
3
] | 1 | [] | [] | [] | 0 | [
"4qnl"
] | 1 | [
"PUB00091258"
] | [
"28513100"
] | [
"Function of bacteriophage G7C esterase tailspike in host cell adsorption."
] | [
2017
] | 1 | [] | [] | 0 | 0 | null | [
"Caudoviricetes"
] | [
3
] | 1 | [] | [] | 0 | true | Domain | Tailspike protein, C-terminal domain | Tailspike protein, C-terminal domain | G7C_C | 3 |
IPR055018 | 55,018 | Zonadhesin, first cohesin-like domain | Zona_CL1 | Domain | 11 | false | false | This entry represents the first cohesin-like domain present in zonadhesin protein from Pichia pastoris [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22320"
] | [
"Zona_CL1"
] | [
11
] | 1 | [] | [] | [] | 0 | [
"5fx8"
] | 1 | [
"PUB00154340"
] | [
"27313058"
] | [
"Crystal structure of linoleate 13R-manganese lipoxygenase in complex with an adhesion protein."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Komagataella"
] | [
11
] | 1 | [] | [] | 0 | true | Domain | Zonadhesin, first cohesin-like domain | Zonadhesin, first cohesin-like domain | Zona_CL1 | 4 |
IPR055019 | 55,019 | Zonadhesin, second cohesin-like domain | Zona_CL2 | Domain | 12 | false | false | This entry represents the second cohesin-like domain present in zonadhesin protein from Pichia pastoris [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22321"
] | [
"Zona_CL2"
] | [
12
] | 1 | [] | [] | [] | 0 | [
"5fx8"
] | 1 | [
"PUB00154340"
] | [
"27313058"
] | [
"Crystal structure of linoleate 13R-manganese lipoxygenase in complex with an adhesion protein."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
12
] | 1 | [] | [] | 0 | true | Domain | Zonadhesin, second cohesin-like domain | Zonadhesin, second cohesin-like domain | Zona_CL2 | 2 |
IPR055020 | 55,020 | Avirulence protein AvrPiz-t | AvrPiz-t | Family | 13 | false | false | This entry represents avirulence protein AvrPiz-t from Magnaporthe oryzae [ ]. It is predicted to be secreted and it can suppress programmed cell death (PCD) induced by BAX in tobacco which suggests that it might contribute to the pathogenicity of M.oryzae. This domain adopts a six-stranded β-sandwich . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22347"
] | [
"AvrPiz-t"
] | [
13
] | 1 | [] | [] | [] | 0 | [
"2lw6"
] | 1 | [
"PUB00066029"
] | [
"23334361"
] | [
"Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Pyricularia"
] | [
13
] | 1 | [] | [] | 0 | true | Family | Avirulence protein AvrPiz-t | Avirulence protein AvrPiz-t | AvrPiz-t | 6 |
IPR055022 | 55,022 | Halocin C8-like, N-terminal domain | HalC8-like_N | Domain | 49 | false | false | This is a presumed domain found at the N-terminal of halocin C8 and similar sequences from archaea. Halocins are bacteriocin-like proteins or peptides produced by many species of the family Halobacteriaceae. Halocin C8 is derived from the C terminus of a 283 amino-acid prepro-protein (ProC8) [ ]. The N-terminal peptide... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22862"
] | [
"HalC8_like_N"
] | [
49
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074361",
"PUB00154869",
"PUB00154870"
] | [
"18658263",
"12811620",
"15978083"
] | [
"The helix-loop-helix motif at the N terminus of HalI is essential for its immunity function against halocin C8.",
"Purification and biological characterization of halocin C8, a novel peptide antibiotic from Halobacterium strain AS7092.",
"A single gene directs both production and immunity of halocin C8 in a ha... | [
2008,
2003,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
49
] | 1 | [] | [] | 0 | true | Domain | Halocin C8-like, N-terminal domain | Halocin C8-like, N-terminal domain | HalC8-like_N | 6 |
IPR055023 | 55,023 | Colicin-A, N-terminal domain | ColA_N | Domain | 15 | false | false | This entry represents the N-terminal translocation domain of colicin A, an endonuclease active on both single- and double-stranded DNA but with undefined specificity [ , ]. This domain interacts directly with TolAIII (C-terminal domain of TolA) which facilitates translocation through the cell envelope to reach their cy... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22348"
] | [
"ColA_N"
] | [
15
] | 1 | [] | [] | [] | 0 | [
"3iax",
"3qdr"
] | 2 | [
"PUB00058538",
"PUB00059427"
] | [
"19627502",
"22493500"
] | [
"The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins.",
"Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli Periplasm."
] | [
2010,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
15
] | 1 | [] | [] | 0 | true | Domain | Colicin-A, N-terminal domain | Colicin-A, N-terminal domain | ColA_N | 5 |
IPR055024 | 55,024 | Endo-beta-N-acetylglucosaminidase EndoS, helical bundle | EndoS_helical | Domain | 24 | false | false | This entry represents a three-helical up-and-down bundle domain of EndoS from Streptococcus pyogenes and similar bacterial proteins. EndoS is involved in immune evasion mechanisms and possesses a specific endoglycosidase activity that targets IgG antibodies [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22382"
] | [
"EndoS_helical"
] | [
24
] | 1 | [] | [] | [] | 0 | [
"4nuy",
"4nuz",
"6en3",
"8a49",
"8a64",
"8w4g",
"8w4i",
"8w4n",
"8x8g"
] | 9 | [
"PUB00151608",
"PUB00151610"
] | [
"24753590",
"29760474"
] | [
"Crystal structure of Streptococcus pyogenes EndoS, an immunomodulatory endoglycosidase specific for human IgG antibodies.",
"Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S."
] | [
2014,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Streptococcus"
] | [
24
] | 1 | [] | [] | 0 | true | Domain | Endo-beta-N-acetylglucosaminidase EndoS, helical bundle | Endo-beta-N-acetylglucosaminidase EndoS, helical bundle | EndoS_helical | 8 |
IPR055025 | 55,025 | ToxT, N-terminal cupin-like domain | ToxT_N | Domain | 13 | false | false | This entry represents a cupin-like domain present in ToxT from Vibrio Cholerae ( , ) [ , ]. ToxT serves as the culminating factor in the regulatory pathway, ensuring the coordinated production of two virulence factors: the toxin-coregulated pilus (TCP) and cholera toxin (CT), which are crucial for the pathogenicity of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22404"
] | [
"ToxT_N"
] | [
13
] | 1 | [] | [] | [] | 0 | [
"3gbg",
"4mlo",
"5suw",
"5sux",
"6p7r",
"6p7t",
"6pb9"
] | 7 | [
"PUB00097575",
"PUB00097576",
"PUB00154292",
"PUB00154293"
] | [
"20133655",
"27599865",
"31815195",
"21673111"
] | [
"Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes.",
"1.65 A resolution structure of the AraC-family transcriptional activator ToxT from Vibrio cholerae.",
"Structural basis for virulence regulation in <i>Vibrio cholerae</i> by unsaturated fatty acid components ... | [
2010,
2016,
2019,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Vibrio"
] | [
13
] | 1 | [] | [] | 0 | true | Domain | ToxT, N-terminal cupin-like domain | ToxT, N-terminal cupin-like domain | ToxT_N | 5 |
IPR055026 | 55,026 | AVR-Pik-like, HMA interaction domain | AVR-Pik_HID | Domain | 18 | false | false | This entry represents the HMA interaction domain of AVR-Pik { ), an effector protein from the rice blast fungus Pyricularia oryzae which binds and stabilizes rice HMA-domain containing NLR proteins to co-opt their function to suppress immunity [ , , , , ]. AVR-Pik adopts a six-stranded β-sandwich structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22383"
] | [
"AVR-Pik_HID"
] | [
18
] | 1 | [] | [] | [] | 0 | [
"5a6w",
"6fu9",
"6fub",
"6fud",
"6g10",
"6g11",
"6r8k",
"6r8m",
"7a8w",
"7a8x",
"7b1i",
"7bnt",
"7nlj",
"7nmm",
"7qpx",
"7qzd",
"8b2r",
"9imu"
] | 18 | [
"PUB00110005",
"PUB00110006",
"PUB00110007",
"PUB00110008",
"PUB00110009"
] | [
"26304198",
"29988155",
"31535976",
"33647072",
"33548226"
] | [
"Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor.",
"Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen.",
"Protein engineering expands the effector recognition profile of a rice NLR immune receptor.",
"The allel... | [
2015,
2018,
2019,
2021,
2021
] | 5 | [] | [] | 0 | 0 | null | [
"Pyricularia"
] | [
18
] | 1 | [] | [] | 0 | true | Domain | AVR-Pik-like, HMA interaction domain | AVR-Pik-like, HMA interaction domain | AVR-Pik_HID | 7 |
IPR055027 | 55,027 | CRISPR-associated endonuclease Cas9, C-terminal domain | Cas9_C_2 | Domain | 9 | false | false | This domain is found at the C-terminal end of CRISPR-associated endonuclease Cas9 from the gammaproteobacteria Francisella tularensis [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22385"
] | [
"Cas9_C_2"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"5b2o",
"5b2p",
"5b2q",
"9ehf",
"9ehg",
"9ehh",
"9ehr",
"9ehw",
"9ehx",
"9n6t"
] | 10 | [
"PUB00152856"
] | [
"26875867"
] | [
"Structure and Engineering of Francisella novicida Cas9."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Francisella"
] | [
9
] | 1 | [] | [] | 0 | true | Domain | CRISPR-associated endonuclease Cas9, C-terminal domain | CRISPR-associated endonuclease Cas9, C-terminal domain | Cas9_C_2 | 7 |
IPR055028 | 55,028 | Methylated DNA-protein cysteine MeTransferase OGT, N-terminal domain | OGT_N | Domain | 10 | false | false | This entry represents the N-terminal of methylated DNA-protein cysteine methyltransferase (MGMT, also known as 6-O-methylguanine-DNA methyltransferase and MJ1529/OGT) from Methanocaldococcus jannaschii and similar sequences [ ]. This entry corresponds to the ribonuclease-like domain associated with 6-O-methylguanine DN... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22413"
] | [
"OGT_N"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"2g7h"
] | 1 | [
"PUB00040953"
] | [
"16826543"
] | [
"Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Methanocaldococcaceae"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | Methylated DNA-protein cysteine MeTransferase OGT, N-terminal domain | Methylated DNA-protein cysteine MeTransferase OGT, N-terminal domain | OGT_N | 2 |
IPR055029 | 55,029 | EhRGS-RhoGEF, PH domain-like | EhRGS-RhoGEF_PH-like | Domain | 10 | false | false | This entry represents the PH-like domain of a RGS-RhoGEF from Entamoeba histolytica (EhRGS-RhoGEF, ) which, like its mammalian homologues, serves as an EhGalpha1 effector and signals through Rho family GTPases playing important roles in its pathogenesis [ ]. This domain mediates activation of Rho family GTPases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22418"
] | [
"EhRGS-RhoGEF_PH-like"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"4gou"
] | 1 | [
"PUB00153920"
] | [
"23260656"
] | [
"Structural determinants of RGS-RhoGEF signaling critical to Entamoeba histolytica pathogenesis."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Entamoeba"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | EhRGS-RhoGEF, PH domain-like | EhRGS-RhoGEF, PH domain-like | EhRGS-RhoGEF_PH-like | 2 |
IPR055030 | 55,030 | Carbohydrate binding module 74 | Cbm74 | Domain | 15 | false | false | This entry represents a Carbohydrate binding module from Ruminococcus flavefaciens (Cbm74-rfgh5, ) and similar sequences. This domain adopts a β-sandwich fold typical of carbohydrate binding modules (CBMs) ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22579"
] | [
"Cbm74"
] | [
15
] | 1 | [] | [] | [] | 0 | [
"5aos",
"5aot",
"5fu2",
"5fu3",
"5fu4"
] | 5 | [
"PUB00091246"
] | [
"27298375"
] | [
"Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Ruminococcus"
] | [
15
] | 1 | [] | [] | 0 | true | Domain | Carbohydrate binding module 74 | Carbohydrate binding module 74 | Cbm74 | 5 |
IPR055031 | 55,031 | Colicin S4, translocation domain | Csa_translocation_dom | Domain | 16 | false | false | This entry represents the N-terminal translocation domain of Colicin S4 from Escherichia coli (Csa, ), a polypeptide toxin produced and active against E.coli. This protein consists of four distinct domains, this domain, two receptor-binding domains and the C-terminal pore-forming domain ( ). This domain shows an antipa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22512"
] | [
"Csa_translocation_dom"
] | [
16
] | 1 | [] | [] | [] | 0 | [
"3few"
] | 1 | [
"PUB00051950"
] | [
"19056731"
] | [
"Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
16
] | 1 | [] | [] | 0 | true | Domain | Colicin S4, translocation domain | Colicin S4, translocation domain | Csa_translocation_dom | 1 |
IPR055032 | 55,032 | Class 2 C-terminal docking domain | Class_2_docking_dom | Domain | 4 | false | false | This short domain is found at the C-terminal end of the polyketide synthase module CurG from the cyanobacteria Moorena producens ( ). It consists of two α-helices connected by a sharp bend ( ) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22488"
] | [
"Class_2_docking_dom"
] | [
4
] | 1 | [] | [] | [] | 0 | [
"4myy"
] | 1 | [
"PUB00153871"
] | [
"24183970"
] | [
"Cyanobacterial polyketide synthase docking domains: a tool for engineering natural product biosynthesis."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Cyanophyceae"
] | [
4
] | 1 | [] | [] | 0 | true | Domain | Class 2 C-terminal docking domain | Class 2 C-terminal docking domain | Class_2_docking_dom | 7 |
IPR055034 | 55,034 | Mu Gam/Sipho_Gp157-like domain of the TOTE conflict systems | Mu_Gam-Sipho_Gp157-TOTE | Domain | 22 | false | false | This entry represents a DNA/RNA hybrid duplex binding domain found in the TOTE (TPR, OB, TBP, Effector) conflict systems [ ]. This domain occasionally displaces the more widely observed TOTE-TPR domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22709"
] | [
"Mu_Gam-Sipho_Gp157-TOTE"
] | [
22
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153788"
] | [
"35609893"
] | [
"Discovering Biological Conflict Systems Through Genome Analysis: Evolutionary Principles and Biochemical Novelty."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanogaster sp."
] | [
21,
1
] | 2 | [] | [] | 0 | true | Domain | Mu Gam/Sipho_Gp157-like domain of the TOTE conflict systems | Mu Gam/Sipho_Gp157-like domain of the TOTE conflict systems | Mu_Gam-Sipho_Gp157-TOTE | 7 |
IPR055035 | 55,035 | DNA transposase THAP9, C-terminal domain | THAP9_C | Domain | 3,244 | false | false | This domain is found at the C-terminal of human DNA transposase THAP9 and similar proteins mainly from vertebrates. This domain is predicted to be mainly formed by α-helices. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22824"
] | [
"THAP9_C"
] | [
3244
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
3244
] | 1 | [
"Danio rerio",
"Homo sapiens"
] | [
1,
1
] | 2 | true | Domain | DNA transposase THAP9, C-terminal domain | DNA transposase THAP9, C-terminal domain | THAP9_C | 6 |
IPR055036 | 55,036 | Short NACHT-associated C-terminal domain, family 5 | SNaCT5 | Domain | 59 | false | false | The SNaCT domains are a rapidly evolving, monophyletic assemblage of domains found C-terminal to the NACHT module in several bacterial NACHT conflict systems. They contain a well-conserved aspartate near the N-terminal of the domain. SNaCT domains are thought to occlude the NTP-binding region, potentially until they in... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF22711"
] | [
"SNaCT5"
] | [
59
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154095"
] | [
"37160116"
] | [
"Bacterial NLR-related proteins protect against phage."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Clostridium phage CDMH1"
] | [
58,
1
] | 2 | [] | [] | 0 | true | Domain | Short NACHT-associated C-terminal domain, family 5 | Short NACHT-associated C-terminal domain, family 5 | SNaCT5 | 6 |
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