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TRUA_METS3
ID   TRUA_METS3              Reviewed;         290 AA.
AC   A5ULI2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Msm_0855;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00171}.
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DR   EMBL; CP000678; ABQ87060.1; -; Genomic_DNA.
DR   RefSeq; WP_011954128.1; NC_009515.1.
DR   AlphaFoldDB; A5ULI2; -.
DR   SMR; A5ULI2; -.
DR   STRING; 420247.Msm_0855; -.
DR   EnsemblBacteria; ABQ87060; ABQ87060; Msm_0855.
DR   GeneID; 5216409; -.
DR   KEGG; msi:Msm_0855; -.
DR   PATRIC; fig|420247.28.peg.852; -.
DR   eggNOG; arCOG04449; Archaea.
DR   HOGENOM; CLU_014673_4_2_2; -.
DR   OMA; FLYGMVR; -.
DR   Proteomes; UP000001992; 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   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; 1.
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; tRNA processing.
FT   CHAIN           1..290
FT                   /note="tRNA pseudouridine synthase A"
FT                   /id="PRO_1000194582"
FT   ACT_SITE        56
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ   SEQUENCE   290 AA;  34124 MW;  D42B53BA8562E93C CRC64;
     MKRTALKIGY IGTNFHGFQR QPDLRTVEEE LIYHLRKLGY IDDLKKSRFR IAGRTDAGVH
     SLGNVISFQS EKEVRVNEIN NSLPDDIQIL AKAPVRFGFK PRYAEMRQYR YVLFRSDLDL
     YKLNEVAEIF KGTHNFTNFT KRFQKTTTRT IDDIKITKAN LNDYHKKEFP NLHDTLSPVF
     VDIYGESFLW NMVRKMMRVF VDVAIGKLSL EKVEELLNPA ENDPRANIKV LDPDYLILMD
     IKYDGVKFVY DDYACERFKR NLVDSLGDLQ RKYAIRESMI KSLEDLERIN
 
 
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