ID   SYGB_THESQ              Reviewed;         672 AA.
AC   B1L9T5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=TRQ2_0731;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC   unclassified Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-2008) 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:0000255|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR   EMBL; CP000969; ACB09083.1; -; Genomic_DNA.
DR   RefSeq; WP_012310708.1; NC_010483.1.
DR   AlphaFoldDB; B1L9T5; -.
DR   SMR; B1L9T5; -.
DR   EnsemblBacteria; ACB09083; ACB09083; TRQ2_0731.
DR   KEGG; trq:TRQ2_0731; -.
DR   HOGENOM; CLU_007220_2_2_0; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001687; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00211; glyS; 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..672
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101365"
SQ   SEQUENCE   672 AA;  78064 MW;  519934275781D437 CRC64;
     MRTALLEVGL EELPASEFHS ILRQLEEKSA ELLKAYRISS GSVEVFVGSR RFGVILNNLP
     ERQEDFTEEK KGPPLNIAYD ENGKPTRALE GFLRNNNASL ENVVHREGYV YLSRVVEGKP
     VEEVLPDLFR DLVLGLNFRK PMRWGSGEHE YVRPVHWIVA MVDGRVLDLE IFGLRSSRIS
     YGKRYHAGSI EIPDPERYYE SLKKGFVISS HLERKKFVLE QIDEFEKRSG MKIERDEELI
     EEIVAITEYP RIVVGQFDRK YLELPEEIIV TAVKHHQRSF IAHKETLTNI FVAFQDGPQP
     PENVVKGYER VINARLEDAR YYFQKDLETS LEKMNEKLKE IVFQEKLGTL YDKVERIKKI
     SQRLCEDLKL PEMFTQKVLE AASICKADIA SKVVYEFPEL QGVMGRIYAL REGINEEIAT
     AIEDHYSEEP QTVIGSILGI ADRIDTIVGN FAIGNVPTSS KDPYGLKSKA DTIFRIIRKN
     EWDISLEELL TFASSLVKYH LSEELETFFA GRFYQFLINE LGISFDVARA VNHLWKKPLR
     GILSAEALQE ISEKPEFQDL FVGFERVHNI TKNHDSTKFD GALFEKEEEK KLMNKFYEVK
     EKVLKALERL NYREALQYLI ELKPYIDEYF DNVFVMVKRD DLRVNRLSFL KNIDELFMMV
     GDMTYLVKRS QV