TRUB_WOLPP
ID TRUB_WOLPP Reviewed; 353 AA.
AC B3CM19;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080};
DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080};
GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01080}; OrderedLocusNames=WP0829;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}.
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_01080};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}.
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DR EMBL; AM999887; CAQ54937.1; -; Genomic_DNA.
DR RefSeq; WP_007302236.1; NC_010981.1.
DR AlphaFoldDB; B3CM19; -.
DR SMR; B3CM19; -.
DR STRING; 570417.WP0829; -.
DR PRIDE; B3CM19; -.
DR EnsemblBacteria; CAQ54937; CAQ54937; WP0829.
DR KEGG; wpi:WP0829; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_032087_0_3_5; -.
DR OrthoDB; 1166299at2; -.
DR Proteomes; UP000008814; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd02573; PseudoU_synth_EcTruB; 1.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 3: Inferred from homology;
KW Isomerase; tRNA processing.
FT CHAIN 1..353
FT /note="tRNA pseudouridine synthase B"
FT /id="PRO_1000149836"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ SEQUENCE 353 AA; 39052 MW; 5C2759D942D843E0 CRC64;
MVNGWLNLDK PTGMSSAQAV TQIKRIFGIK KAGHLGTLDP LASGILPIAL GEATKTIPYL
SCDLKAYNFT IKWGKQTTTD DLGGDIIRTS DIKPEYNQIN CAIKDFIGEI TQTPPQFSAV
KIKGARAYKL ARSGQKVNIK PRQVKIHELK MIFLDTINNI ADFSMICGSG VYVRSIARDL
GIELNCFGHI TQLRRTMVGD FKEDESVTIE QLTKKNTTTY SPQCLTLDTN TYKSCNGQKI
LGAYVKNNVR DEIGLIPVLD TGMTSEGGMT EDDGGNTKGF IIPIESALKS MFKVEISLEE
AEKIRKGQEI ILNNLRNLKN YDIFCTIVGN VPIAICSFTH GYVKPIRVFN ILK
