ID TRUB_METBF Reviewed; 338 AA. AC Q46GC3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 18-JUN-2025, entry version 126. DE RecName: Full=Probable tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01081}; DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01081}; GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01081}; GN OrderedLocusNames=Mbar_A0082; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). CC -!- FUNCTION: Could be responsible for synthesis of pseudouridine from CC uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_01081}. CC -!- CATALYTIC ACTIVITY: CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA; CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102, CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01081}; CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01081}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000099; AAZ69069.1; -; Genomic_DNA. DR AlphaFoldDB; Q46GC3; -. DR SMR; Q46GC3; -. DR STRING; 269797.Mbar_A0082; -. DR PaxDb; 269797-Mbar_A0082; -. DR KEGG; mba:Mbar_A0082; -. DR eggNOG; arCOG00987; Archaea. DR HOGENOM; CLU_032087_3_0_2; -. DR OrthoDB; 35866at2157; -. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0160148; F:tRNA pseudouridine(55) synthase activity; IEA:UniProtKB-EC. DR GO; GO:0000495; P:box H/ACA sno(s)RNA 3'-end processing; IEA:TreeGrafter. DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:TreeGrafter. DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IEA:TreeGrafter. DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IEA:TreeGrafter. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule. DR CDD; cd02572; PseudoU_synth_hDyskerin; 1. DR CDD; cd21148; PUA_Cbf5; 1. DR FunFam; 3.30.2350.10:FF:000001; H/ACA ribonucleoprotein complex subunit CBF5; 1. DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1. DR Gene3D; 2.30.130.10; PUA domain; 1. DR HAMAP; MF_01081; TruB_arch; 1. DR InterPro; IPR012960; Dyskerin-like. DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR036974; PUA_sf. DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam. DR InterPro; IPR026326; TruB_arch. DR InterPro; IPR032819; TruB_C. DR NCBIfam; TIGR00425; CBF5; 1. DR NCBIfam; NF003280; PRK04270.1; 1. DR PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1. DR PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1. DR Pfam; PF08068; DKCLD; 1. DR Pfam; PF01472; PUA; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SMART; SM01136; DKCLD; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF55120; Pseudouridine synthase; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Isomerase; tRNA processing. FT CHAIN 1..338 FT /note="Probable tRNA pseudouridine synthase B" FT /id="PRO_1000084721" FT DOMAIN 245..320 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01081" FT ACT_SITE 78 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01081" SQ SEQUENCE 338 AA; 36888 MW; A346867FC9192D06 CRC64; MSPAGKLPSE AERILVRKSG AWTNPSYGSY PEKRPILEYI EKGVVNIDKP KGPTSHEVAA WVKAILGVST AGHAGSLDPK VTGLLPTLLG KATKAVPALR LSGKEYVCLL KLHKEMPQKL VRKVCEEFTG PIYQMPPIKS AVKRVIRIRT IYYLEVLEIE GSFVLFRVGC EAGTYIRKLC HDIGLALGCG GHMQELRRTK AGPFTEETLV TLQDLKDAYV LWKEDGDESE IRRVIMPMET AVSHLPKIIL RDSAVDAICS GAALAVPGIT SLDANLKKGE LIALFTLKGE LVALAKAEMS TEELLKASTG LAATSVRIMM EIGTYPKGWT KKEYGVES //