ID   SYGB_VIBVU              Reviewed;         693 AA.
AC   Q8DDJ7;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=VV1_0990;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO09480.1; -; Genomic_DNA.
DR   RefSeq; WP_011079027.1; NC_004459.3.
DR   AlphaFoldDB; Q8DDJ7; -.
DR   SMR; Q8DDJ7; -.
DR   EnsemblBacteria; AAO09480; AAO09480; VV1_0990.
DR   KEGG; vvu:VV1_0990; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..693
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072937"
SQ   SEQUENCE   693 AA;  76712 MW;  63F6F4C4455DD83F CRC64;
     MAKEFLIELG TEELPPTQLR TLAEAFAANF EAELKGAELT HEGVKWYAAP RRLALKVTAL
     AEHQADKIVE KRGPAVSAAF DADGNATKAA QGWARGCGIT VDQAERMITD KGEWLLFKQE
     VKGQPTADIV VELAAKALAG LPIAKPMRWG NKTTQFIRPV KTLTMLMGSD LIQGEILGVA
     SDRVIRGHRF MGEREFTIES AEQYPSILEE RGKVMADYEA RKAIILADAQ KAAAAIGGIA
     DLEDDLVEEV TSLVEWPVVL TAKFEEEFLK VPAEALVYTM KGDQKYFPVY TEDKQLLPNF
     IFVSNIESKE PRYVIEGNEK VVRPRLADAE FFFNTDRKSK LIDRLPMLEN AIFQQQLGTI
     KDKTDRITEL AGYIAEQIGA DVEKSKRAGL LAKCDLMTSM VFEFTDTQGV MGMHYARHDG
     EAEEVAVALN EQYMPRFAGD DLPSNGVSSA VAMADKLDTI VGIFGIGQAP KGSDPFALRR
     ASLGVLRIIV EYGYNLDLVD LVAKAKSLFA QQDGTSRLTN DNVEQEVIEF MLGRFRAWYQ
     DEGFSVDIIQ AVLARRPTKP ADFDQRVKAV SHFRELEAAE ALAAANKRVG NILAKFDGEL
     AADIDLALLR EDAEKVLAEN VEVMTEALEP AFATGNYQEA LSKLADLREP VDAFFDNVMV
     MADDEALKTN RLTLLNNLRN LFLQIADISL LQK