(data stored in SCRATCH3701 zone)

SWISSPROT: TRUB_RICTY

ID   TRUB_RICTY              Reviewed;         292 AA.
AC   Q68WN3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=RT0487;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03959.1; -; Genomic_DNA.
DR   RefSeq; WP_011190941.1; NC_006142.1.
DR   STRING; 257363.RT0487; -.
DR   EnsemblBacteria; AAU03959; AAU03959; RT0487.
DR   KEGG; rty:RT0487; -.
DR   eggNOG; ENOG4105D0T; Bacteria.
DR   eggNOG; COG0130; LUCA.
DR   HOGENOM; HOG000231225; -.
DR   KO; K03177; -.
DR   OMA; ELQFIRW; -.
DR   OrthoDB; 1166299at2; -.
DR   BioCyc; RTYP257363:G1G0L-495-MONOMER; -.
DR   Proteomes; UP000000604; 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;
DR   PRODOM; Q68WN3.
DR   SWISS-2DPAGE; Q68WN3.
KW   Isomerase; tRNA processing.
FT   CHAIN           1..292
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121896"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   292 AA;  32722 MW;  6AC32A7441B7B804 CRC64;
     MSNYWLNFYK PKGISSAKLV NIVKKIIGKT KIGHAGTLDV EAEGILPLAV GEATKLIQLL
     IDAKKTYIFS VKFGAQTDNG DYTGKVIASK NYIPSQEEAY AVCSKFIGNI KQIPPMFSAI
     KVNGIRAYKL AREGKVVELK PRNVTIYDLK CLNFDKEKAI ATYYTECSKG TYIRTLTEDL
     ALSLQSLGFV IELRRTQVGI FKEENAIHIK ASDAITKNFI DKKSIKIEAI LDDILVLDAT
     DDQAQKIKYG QKCVFDYEED VNFLWVRYNG TLLAIGSLNK SCFNSLRVFN LL
//

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