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TRUA1_CLOTE
ID   TRUA1_CLOTE             Reviewed;         245 AA.
AC   Q893H3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=tRNA pseudouridine synthase A 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA-uridine isomerase I 1 {ECO:0000255|HAMAP-Rule:MF_00171};
GN   Name=truA1 {ECO:0000255|HAMAP-Rule:MF_00171}; OrderedLocusNames=CTC_01851;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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}.
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DR   EMBL; AE015927; AAO36369.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q893H3; -.
DR   SMR; Q893H3; -.
DR   STRING; 212717.CTC_01851; -.
DR   EnsemblBacteria; AAO36369; AAO36369; CTC_01851.
DR   KEGG; ctc:CTC_01851; -.
DR   HOGENOM; CLU_014673_0_1_9; -.
DR   OMA; MYIFKIA; -.
DR   Proteomes; UP000001412; 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..245
FT                   /note="tRNA pseudouridine synthase A 1"
FT                   /id="PRO_0000057366"
FT   ACT_SITE        53
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   245 AA;  28264 MW;  DA1884E7384F07D4 CRC64;
     MRNLKMILEY DGTRYKGWQK QKKDVLTIQD KIETVLSKMT GEDIQVIGCG RTDAGVHAEN
     YVANFHTNCD FTVDYMLDYL YEFLPEDIVV KTMKDTSERF HARYNVKSKT YVYRINNNKF
     RSVFNKKYAY HDNEKLNISA MKDAAEFLIG THDFKSFTRL KSNSKSTIRA IKYINITENQ
     GIISIEVNGN GFLLNMVRIV AGALLEVGKE NIKPIDIEKM LNEKKRADAS LILPAKGLCL
     KDIQY
 
 
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