TRUA_AYWBP
ID TRUA_AYWBP Reviewed; 243 AA.
AC Q2NIY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=AYWB_493;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65610.1; -; Genomic_DNA.
DR RefSeq; WP_011412773.1; NC_007716.1.
DR AlphaFoldDB; Q2NIY3; -.
DR SMR; Q2NIY3; -.
DR STRING; 322098.AYWB_493; -.
DR EnsemblBacteria; ABC65610; ABC65610; AYWB_493.
DR KEGG; ayw:AYWB_493; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_1_14; -.
DR OMA; FLYGMVR; -.
DR OrthoDB; 1075262at2; -.
DR PhylomeDB; Q2NIY3; -.
DR Proteomes; UP000001934; 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; tRNA processing.
FT CHAIN 1..243
FT /note="tRNA pseudouridine synthase A"
FT /id="PRO_1000017038"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00171"
SQ SEQUENCE 243 AA; 28419 MW; 5BBF5CE60D1D1558 CRC64;
MQHFFYKLIL SYDGTFYCGY QKQPQKKTVQ QTFEKALKKM THQNIPTFAA SRTDKGVHSQ
GQTLHFQTTF SLKPKHFQKT LNYLLPPDIR VRQMHFATPN FHARYSAKSK IYQYVFSKKP
LNAFNHHFQI FADKFDFVKI TKALKFIEGT HNFFAFTSET QPKNFSKTIF QASLKETVHK
YILVFHGNGF LKYMIRFLVG SLIEIGKNKF SLEQFQAMLL GNKTKKATLL APAKALVLKK
IFY
