ID   SYGA_SALTY              Reviewed;         303 AA.
AC   Q8ZL95;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   01-MAY-2013, entry version 63.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE            Short=GlyRS;
GN   Name=glyQ; OrderedLocusNames=STM3656;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE006468; AAL22515.1; -; Genomic_DNA.
DR   RefSeq; NP_462556.1; NC_003197.1.
DR   ProteinModelPortal; Q8ZL95; -.
DR   SMR; Q8ZL95; 9-287.
DR   STRING; 99287.STM3656; -.
DR   PaxDb; Q8ZL95; -.
DR   PRIDE; Q8ZL95; -.
DR   EnsemblBacteria; AAL22515; AAL22515; STM3656.
DR   GeneID; 1255180; -.
DR   KEGG; stm:STM3656; -.
DR   PATRIC; 32386141; VBISalEnt20916_3867.
DR   eggNOG; COG0752; -.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; CVILQPY; -.
DR   ProtClustDB; PRK09348; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP.
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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    303       Glycine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_0000072863.
SQ   SEQUENCE   303 AA;  34746 MW;  2D22062909FD4DDC CRC64;
     MQKFDTRTFQ GLILTLQDYW ARQGCTIVQP LDMEVGAGTS HPMTCLRALG PEPMATAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVVIKPS PDNIQELYLG SLKELGMDPT IHDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGLERL AMYIQGVDSV
     YDLVWSDGPL GKTTYGDVFH QNEVEQSTYN FEYADVDFLF TCFEQYEKEA QQLLALENPL
     PLPAYERILK AAHSFNLLDA RKAISVTERQ RYILRIRTLT KAVAEAYYAS REALGFPMCN
     KDK
//