ID   SYGB_TRIEI              Reviewed;         719 AA.
AC   Q10WA6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Tery_4481;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG53468.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q10WA6; -.
DR   SMR; Q10WA6; -.
DR   STRING; 203124.Tery_4481; -.
DR   EnsemblBacteria; ABG53468; ABG53468; Tery_4481.
DR   KEGG; ter:Tery_4481; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_3; -.
DR   OMA; LPIPKRM; -.
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   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
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..719
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101368"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  81063 MW;  FF0F1414D7250DD6 CRC64;
     MIVTFLLEIG TEELPANFVY EAIQQWQELI PMTLKEAFLT NDSVNVYATP RRLAVVIDAL
     PTKQPDREEE IKGPPAKAAF KDGKPTKAAE GFSKKQGVQL NDLQICTTEK GDFVFVNKKI
     QGKPTAAILT ELIPKWIDKL EGKRFMRWAD GELKFPRPIR WLVALLDDEI LPINLDNGSQ
     KITSDRFSYG HRVLHPKLIE ISQAKNYVEV LKKAYIEVDY KQRKSKIEQQ IKTAAEEIKG
     KAEISEELLA EVTNLVEWPT VVIGKFDEEF LILPGEVTTT VMETHQRYFP VFKSTKTFKD
     MELLPYFITI SNGDPEKSEI IAIGNERVIK ARLADGQFFY KTDLAKPLES YLPELETVTF
     QAKLGSMREK VKRIVSIAKL IAGQLQITQE ESKNIERAAL LCKADLVTQM VYEFPELQGV
     MGEKYARAAG ETEAVATAIF EHYLPRGAGD ILPKTISGQV ISLADRLDTL VSIFGLGMLP
     TGSADPFALR RAANGVVNIS WSANLPLNLH QLLEEIATNF FKTYSQTNSD LLAQLSNFLL
     QRIKTILLEE KNIDYDLVNA VLGDNDAEYK ERGLKDLLDV RNRAIFLQNI RQNGMLGKIY
     ETINRSTRLA AQGELDKIQL KPLKVIDSKL FKSESELAFY NALVELVPQT EISQKTRNYQ
     QLVDALLKIA PTVSNFFDGP DSVLVIDPDP KIKKNRLNLL GLLRNNARVL ADFGQIVKN