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Database: UniProt
Entry: G4RBS2_PELHB
LinkDB: G4RBS2_PELHB
Original site: G4RBS2_PELHB 
ID   G4RBS2_PELHB            Unreviewed;       308 AA.
AC   G4RBS2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=KKY_544 {ECO:0000313|EMBL:AEQ50585.1};
OS   Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS   B2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Devosiaceae; Pelagibacterium.
OX   NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ50585.1, ECO:0000313|Proteomes:UP000008850};
RN   [1] {ECO:0000313|EMBL:AEQ50585.1, ECO:0000313|Proteomes:UP000008850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC   {ECO:0000313|Proteomes:UP000008850};
RX   PubMed=22156395; DOI=10.1128/JB.06343-11;
RA   Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA   Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT   "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL   J. Bacteriol. 194:197-198(2012).
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; CP003075; AEQ50585.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4RBS2; -.
DR   STRING; 1082931.KKY_544; -.
DR   KEGG; phl:KKY_544; -.
DR   PATRIC; fig|1082931.4.peg.540; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_5; -.
DR   Proteomes; UP000008850; 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   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:UP000008850}.
SQ   SEQUENCE   308 AA;  34761 MW;  273CB45423C2C5C4 CRC64;
     MTDALAPHMD PRNSFQGLIL TLQRFWADQG CVILQPYDMQ MGAGTFHTAT TLRALGPKPW
     NAAYVQPSRR PTDGRYGENP NRLQHYYQFQ VILKPSPANI QELYLQSLAA IGLDAKLHDI
     RFVEDDWESP TLGAWGLGWE CWCDGMEVSQ FTYFQQVAGF ECSPVPGEIT YGLERLAMYV
     QGVENVYDLN FNGREGDQKV TYGEVFLQNE QEFSKYNFEA ADTEMLFRHF RDAENECRAI
     LAKGKDGERQ TMAVPAYEQV IKASHTFNLL DARGVISVTE RQSYILRIRE LAKACGAAWL
     QTAGGGAA
//
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