ID   SYGA_STRGC              Reviewed;         305 AA.
AC   A8AVS4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=SGO_0568;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10626.1; -; Genomic_DNA.
DR   RefSeq; WP_002911276.1; NC_009785.1.
DR   AlphaFoldDB; A8AVS4; -.
DR   SMR; A8AVS4; -.
DR   STRING; 467705.SGO_0568; -.
DR   EnsemblBacteria; ABV10626; ABV10626; SGO_0568.
DR   GeneID; 48424018; -.
DR   KEGG; sgo:SGO_0568; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_9; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000001131; 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..305
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000078537"
SQ   SEQUENCE   305 AA;  35020 MW;  C5B95A5F95B5C13C CRC64;
     MSKKLTFQEI ILTLQQFWND QGCMLMQAYD NEKGAGTMSP YTFLRAIGPE PWNAAYVEPS
     RRPADGRYGE NPNRLYQHHQ FQVVMKPSPS NIQELYLQSL ELLGINPLEH DIRFVEDNWE
     NPSTGSAGLG WEVWLDGMEI TQFTYFQQVG GLPTQPVTAE VTYGLERLAS YIQEVDSVYD
     IEWADGVKYG EIFTHPEYEH SKYSFEVSDQ DLLLGNFERF EAEAKRCLDE HLVHPAYDYV
     LKCSHTFNLL DARGAVSVTE RAGYIARIRN LARVVAKTFV AERKRLGYPL LDAETREKLL
     AEEGE