ID   SYGA_STRPD              Reviewed;         305 AA.
AC   Q1JFJ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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};
GN   OrderedLocusNames=MGAS10270_Spy1504;
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10270;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF34569.1; -; Genomic_DNA.
DR   RefSeq; WP_010922565.1; NZ_CVUH01000010.1.
DR   AlphaFoldDB; Q1JFJ0; -.
DR   SMR; Q1JFJ0; -.
DR   EnsemblBacteria; ABF34569; ABF34569; MGAS10270_Spy1504.
DR   KEGG; sph:MGAS10270_Spy1504; -.
DR   HOGENOM; CLU_057066_1_0_9; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000002436; 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.
FT   CHAIN           1..305
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000047502"
SQ   SEQUENCE   305 AA;  34833 MW;  2103B40E0448C927 CRC64;
     MSKKLTFQEI ILTLQQYWND QGCMLMQAYD NEKGAGTMSP YTFLRAIGPE PWNAAYVEPS
     RRPADGRYGE NPNRLYQHHQ FQVVMKPSPS NIQELYLASL EKLGINPLEH DIRFVEDNWE
     NPSTGSAGLG WEVWLDGMEI TQFTYFQQVG GLATSPVTAE VTYGLERLAS YIQEVDSVYD
     IEWAPGVKYG EIFLQPEYEH SKYSFEISDQ DMLLENFEKF EKEASRALEE GLVHPAYDYV
     LKCSHTFNLL DARGAVSVTE RAGYIARIRN LARVVAKTFV AERKKLGFPL LDEATRAILL
     AEDDE