(data stored in SCRATCH3701 zone)

SWISSPROT: SYGA_VIBVY

ID   SYGA_VIBVY              Reviewed;         305 AA.
AC   Q7MQI7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254}; OrderedLocusNames=VV0021;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
DR   EMBL; BA000037; BAC92785.1; -; Genomic_DNA.
DR   RefSeq; WP_011079026.1; NC_005139.1.
DR   SMR; Q7MQI7; -.
DR   STRING; 672.VV93_v1c00100; -.
DR   EnsemblBacteria; BAC92785; BAC92785; BAC92785.
DR   GeneID; 2622769; -.
DR   KEGG; vvy:VV0021; -.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; SYYQFQV; -.
DR   OrthoDB; 676868at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MQI7.
DR   SWISS-2DPAGE; Q7MQI7.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072881"
SQ   SEQUENCE   305 AA;  35006 MW;  0C2A3596729013C8 CRC64;
     MQKYDIKTFQ GMILALQDYW AQNGCTIVQP LDMEVGAGTS HPMTCLRALG PEPMSTAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVALKPS PDNIQELYLG SLEVLGIDPL VHDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGIERL AMYIQEVDSV
     YDLTWNIAPD GSKVTYGDIF HQNEVEQSTY NFEHADVDFL FSFFEQCEKE CQQLLELEKP
     LPLPAYERIL KAAHAFNLLD ARKAISVTER QRYILRIRNL TKSVAEAYYA SREALGFPMC
     KKEQA
//

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