ID   TRUA_CAUVN              Reviewed;         247 AA.
AC   B8GYF0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CCNA_00280;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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}.
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DR   EMBL; CP001340; ACL93747.1; -; Genomic_DNA.
DR   RefSeq; WP_010918167.1; NC_011916.1.
DR   RefSeq; YP_002515655.1; NC_011916.1.
DR   AlphaFoldDB; B8GYF0; -.
DR   SMR; B8GYF0; -.
DR   EnsemblBacteria; ACL93747; ACL93747; CCNA_00280.
DR   GeneID; 7330733; -.
DR   KEGG; ccs:CCNA_00280; -.
DR   PATRIC; fig|565050.3.peg.277; -.
DR   HOGENOM; CLU_014673_0_2_5; -.
DR   OMA; FLYGMVR; -.
DR   OrthoDB; 1075262at2; -.
DR   PhylomeDB; B8GYF0; -.
DR   Proteomes; UP000001364; 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; cd02570; PseudoU_synth_EcTruA; 1.
DR   Gene3D; 3.30.70.580; -; 1.
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   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   PANTHER; PTHR11142; PTHR11142; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 2.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00071; hisT_truA; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; tRNA processing.
FT   CHAIN           1..247
FT                   /note="tRNA pseudouridine synthase A"
FT                   /id="PRO_1000194537"
FT   ACT_SITE        52
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ   SEQUENCE   247 AA;  27505 MW;  75DEC87412FE1D95 CRC64;
     MPRYRLLVEY DGRPYAGFQA QATLPSVQGA IEAAVKAFCG QEVRIAAAGR TDTGVHATGQ
     VVHVDLDKDW PAQTVFNALN AHLTREAVSI LSAEVAEEGW HARFSANERR YLYRILNRRA
     PPALDKGRVW HMKKDLDHEA MHAAAQHLIG LHDFTTFRDM HCQSKSPVKT LDVARVRRVG
     EEIHLDFEAR SFLHRQVRSM TGTLVEVGAG RWTVDDVKAA LEARDRRECG PVAPADGLYL
     VGVGYGD