(data stored in ACNUC30630 zone)

SWISSPROT: TRUA_TROW8

ID   TRUA_TROW8              Reviewed;         267 AA.
AC   Q820Z2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171};
DE            EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171};
GN   Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; OrderedLocusNames=TW234;
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: Formation of pseudouridine at positions 38, 39 and 40 in the
CC       anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00171}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC         Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00171};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00171}.
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00171}.
DR   EMBL; BX251410; CAD66911.1; -; Genomic_DNA.
DR   RefSeq; WP_011096192.1; NC_004551.1.
DR   SMR; Q820Z2; -.
DR   PRIDE; Q820Z2; -.
DR   EnsemblBacteria; CAD66911; CAD66911; TW234.
DR   KEGG; tws:TW234; -.
DR   HOGENOM; HOG000248674; -.
DR   KO; K06173; -.
DR   OMA; FLYGMVR; -.
DR   BioCyc; GCF_000196075:G1EE9-256-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   Gene3D; 3.30.70.660; -; 1.
DR   HAMAP; MF_00171; TruA; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001406; PsdUridine_synth_TruA.
DR   InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR   InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR   PANTHER; PTHR11142; PTHR11142; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 1.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q820Z2.
DR   SWISS-2DPAGE; Q820Z2.
KW   Isomerase; tRNA processing.
FT   CHAIN           1..267
FT                   /note="tRNA pseudouridine synthase A"
FT                   /id="PRO_0000057480"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   BINDING         114
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ   SEQUENCE   267 AA;  30590 MW;  1787DD2D175F60F8 CRC64;
     MNKTRYRLDV AYDGANFCGW APQPGLRTVG GLILDALRLI CSEPPDIVIA ARTDAGVHAL
     QQVCHVDLIS SPDPVWLLHR LRSLLKSETD LHILSAVKAP VNFHARFSAI GRRYVYRVID
     KRSSWYPQNR YFVYRVNAFL QDYRMRRAAS GLIGLKDFGA FCKPRRMGST VRHLRQFEVI
     RQPDGQIHFF LESDAFCHSM VRNLVGSLIE VGRGALTLQD LFCYTKIAKR TPKIPTLPPH
     ALTLIGIDYP QEHLFECQNR KTRQKRT
//

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