ID   SYGA_SHEON              Reviewed;         301 AA.
AC   Q8EKS5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=SO_0015;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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}.
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DR   EMBL; AE014299; AAN53102.1; -; Genomic_DNA.
DR   RefSeq; NP_715657.1; NC_004347.2.
DR   RefSeq; WP_011070431.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EKS5; -.
DR   SMR; Q8EKS5; -.
DR   STRING; 211586.SO_0015; -.
DR   PaxDb; Q8EKS5; -.
DR   GeneID; 58509999; -.
DR   GeneID; 67441599; -.
DR   KEGG; son:SO_0015; -.
DR   PATRIC; fig|211586.12.peg.15; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_6; -.
DR   OMA; SYYQFQV; -.
DR   OrthoDB; 676868at2; -.
DR   PhylomeDB; Q8EKS5; -.
DR   BioCyc; SONE211586:G1GMP-15-MON; -.
DR   Proteomes; UP000008186; Chromosome.
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   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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   SUPFAM; SSF55681; SSF55681; 1.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000072864"
SQ   SEQUENCE   301 AA;  34478 MW;  F61F1D27CBA4902C CRC64;
     MTTKHDVKTF QGFILTLQEY WAQQGCAIVQ PLDMEVGAGT FHPQTFLRSL GPEPMSSAYV
     QPSRRPTDGR YGENPNRLQH YYQFQVVLKP SPDNIQELYL GSLQALGIDT QIHDIRFVED
     NWESPTLGAW GLGWEVWLNG MEVTQFTYFQ QVGGLECSPV TGEITYGLER LAMYIQGVDS
     VYDLVWTDGP MGRITYGDVF HQNEVEQSTY NFEHADVDFM FALFDQCEKM CQHLLSLEKP
     LPLPAYEQVM KASHAFNLLD ARHAISVTER QRYILRVRTM AKAVAESYYQ AREALGFPMC
     K