ID   SYGA_CAMFF              Reviewed;         285 AA.
AC   A0RPS8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   10-JUN-2026, 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};
GN   OrderedLocusNames=CFF8240_1047;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP +
CC         diphosphate; 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; CP000487; ABK82141.1; -; Genomic_DNA.
DR   RefSeq; WP_002849611.1; NC_008599.1.
DR   AlphaFoldDB; A0RPS8; -.
DR   SMR; A0RPS8; -.
DR   GeneID; 61064874; -.
DR   KEGG; cff:CFF8240_1047; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_7; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.30.930.10:FF:000006; Glycine--tRNA ligase alpha subunit; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 1.20.58.180; Class II aaRS and biotin synthetases, domain 2; 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   NCBIfam; TIGR00388; glyQ; 1.
DR   NCBIfam; NF006827; PRK09348.1; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..285
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000047406"
SQ   SEQUENCE   285 AA;  32820 MW;  57E6E9AB8A9F6EF4 CRC64;
     MTFSEIILTL QTYWHEQGCI IVQPYDMPAG AGTYHQATFL RSLGDKPWNV AYVAPSRRPT
     DGRYGENPNR LGSYYQFQVI MKPSPKNIQE LYLKSLERLG LDINKHDIRF VEDNWESPTL
     GAWGLGWEVW LDGMEVTQFT YFQQVGGIPC ELVSAEVTYG IERLAMYLQD KNNVYDIVWD
     ERDGKIVTYG DVHKQSEYEF SKYNFEIADT AILFKHFEDY GKECKAILEH GLALPAYDYC
     MLAAHTFNVL DARGAISVTQ RQDFILKIRE LAKGCALAYK ESLQK
//