ID A0A078KEC2_9GAMM Unreviewed; 295 AA.
AC A0A078KEC2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN ECO:0000313|EMBL:CDZ16508.1};
GN ORFNames=CEM_249 {ECO:0000313|EMBL:CDZ16508.1};
OS Candidatus Evansia muelleri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Evansia.
OX NCBI_TaxID=1495769 {ECO:0000313|EMBL:CDZ16508.1, ECO:0000313|Proteomes:UP000032420};
RN [1] {ECO:0000313|Proteomes:UP000032420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Santos-Garcia D.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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DR EMBL; LM655252; CDZ16508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KEC2; -.
DR STRING; 1495769.CEM_249; -.
DR KEGG; eme:CEM_249; -.
DR PATRIC; fig|1495769.3.peg.230; -.
DR HOGENOM; CLU_057066_1_0_6; -.
DR OrthoDB; 9802183at2; -.
DR Proteomes; UP000032420; 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 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 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00254};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00254};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Reference proteome {ECO:0000313|Proteomes:UP000032420}.
SQ SEQUENCE 295 AA; 34949 MW; 71E7292C1D843A53 CRC64;
MFLYKKLITF QQIILNLKKY WSEQGCIIIE PLDLEVGAGT FHPATFLKAI DPKSKIWNAA
YLQSCRRPSD SRYAKTPNRI QHYYQFQVIM KPSPENLQEL YINSLYNLGI NPNIHDIRFV
KDNWKSPVLG AWGLGWEIWI NGMEVTQFTY LQQVGGIECN PIIGELTYGI ERLAMYLQNV
NDIYEIIWYF TLDGNQITYG NIYLQNEIDQ SNYNLKYTNS KFLYNNFDYH ENMCLQLIKF
NLIYPAYEQI IKASHIFNII DAKKSISITE RQRYILRIRT MSCNLAKKYY NLRLK
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