(data stored in ACNUC30630 zone)

SWISSPROT: TRUB_TROW8

ID   TRUB_TROW8              Reviewed;         383 AA.
AC   Q820Z5;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 89.
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=TW097;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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}.
DR   EMBL; BX251410; CAD66781.1; -; Genomic_DNA.
DR   SMR; Q820Z5; -.
DR   PRIDE; Q820Z5; -.
DR   EnsemblBacteria; CAD66781; CAD66781; TW097.
DR   KEGG; tws:TW097; -.
DR   HOGENOM; HOG000231225; -.
DR   KO; K03177; -.
DR   OMA; KVERSEM; -.
DR   BioCyc; GCF_000196075:G1EE9-96-MONOMER; -.
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   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q820Z5.
DR   SWISS-2DPAGE; Q820Z5.
KW   Isomerase; tRNA processing.
FT   CHAIN           1..383
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121935"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   383 AA;  41740 MW;  0180E4A0A7E246AF CRC64;
     MLGKVERSEM YILFAMTQVL LVDKISGITS HTAVAKIRHL TGVKKIGHCG TLDPAACGLL
     IMGCGTATRL IRYMSNLDKR YIATITLGTQ TTTDDSEGEI IYSAPKPSLD KITLESIGRA
     AEKLSGTIKQ IPSAYSAIKV SGNRAYNLAR QGIIPKLNAR EVRVHWKFLG DFENNQVHVQ
     ITCSSGTYVR ALARDMGKFL GVGGHLSYLK RLSIGPFHLH EIYREINKKE ATMSERTPSG
     NTQGLTDNMA ISDNMAISES DKHDCTEPGI NCTELGIKDT CTALREVHYT QGDTLSFTRL
     TALQALSRIY KPIEVSQKQA DDLSCGRYIS LGIDSNGPVC AVCKENLIAV IQPVSAGLWR
     PETVLSDNRK LNSNAAQDAS GST
//

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