(data stored in ACNUC1104 zone)

SWISSPROT: TRUA_BURCC

ID   TRUA_BURCC              Reviewed;         270 AA.
AC   B1K370;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
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};
GN   OrderedLocusNames=Bcenmc03_3572;
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in
CC       the anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00171}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA uridine(38-40) = tRNA pseudouridine(38-40);
CC         Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-
CC         COMP:10087, 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
CC       family. {ECO:0000255|HAMAP-Rule:MF_00171}.
DR   EMBL; CP000959; ACA92724.1; -; Genomic_DNA.
DR   SMR; B1K370; -.
DR   EnsemblBacteria; ACA92724; ACA92724; Bcenmc03_3572.
DR   KEGG; bcm:Bcenmc03_3572; -.
DR   HOGENOM; HOG000248672; -.
DR   KO; K06173; -.
DR   OMA; FLYGMVR; -.
DR   Proteomes; UP000002169; Chromosome 2.
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; 2.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00071; hisT_truA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1K370.
DR   SWISS-2DPAGE; B1K370.
KW   Complete proteome; Isomerase; tRNA processing.
FT   CHAIN         1    270       tRNA pseudouridine synthase A.
FT                                /FTId=PRO_1000097725.
FT   ACT_SITE     51     51       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00171}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00171}.
SQ   SEQUENCE   270 AA;  30166 MW;  3ED1BB44AFEC243C CRC64;
     MRIALGIQYD GAAFCGWQAQ PHGKTVQDRL EHALAEFARV PLHTTVAGRT DTGVHGLGQV
     VHFDTDLERE VFSWVRGTNA FLPSTVSVQW AKPMPDTFHA RFSAFERTYY YALYVHPVRS
     PMLAGRAGWI HTPLDDDAMR AAAAHLIGEH DFSSFRSSEC QSKTPVKHLY QIDVRRAGHF
     IHFRFRANAF LHHMVRNLMG CLVAVGRGRY PADWLADVLA GRDRNLAAPT FMADGLYLAH
     VGYPAEFAVP PAQLGSVPWS SVWADLDPQT
//

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