SYGB_VIBVY
ID SYGB_VIBVY Reviewed; 693 AA.
AC Q7MQI8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=VV0020;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC92784.1; -; Genomic_DNA.
DR RefSeq; WP_011149060.1; NC_005139.1.
DR AlphaFoldDB; Q7MQI8; -.
DR SMR; Q7MQI8; -.
DR STRING; 672.VV93_v1c00090; -.
DR EnsemblBacteria; BAC92784; BAC92784; BAC92784.
DR KEGG; vvy:VV0020; -.
DR PATRIC; fig|196600.6.peg.73; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT CHAIN 1..693
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072938"
SQ SEQUENCE 693 AA; 76754 MW; FD80CCA3162B6F02 CRC64;
MAKEFLIELG TEELPPTQLR TLAEAFAANF EAELKGAELT HEGVKWYAAP RRLALKVTAL
AEHQADKIVE KRGPAVSAAF DAEGNATKAA QGWARGCGIT VDQAERMITD KGEWLLFKQE
VKGQPTADIV VELAAKALAG LPIAKPMRWG NKTTQFIRPV KTLTMLMGSD LIQGEILGVA
SDRVIRGHRF MGEREFTIES AEQYPAILEE RGKVMADYEM RKAIILADAQ KAAAAIGGIA
DLEDDLVEEV TSLVEWPVVL TAKFEEEFLK VPAEALVYTM KGDQKYFPVY TEDKQLLPNF
IFVSNIESKE PRYVIEGNEK VVRPRLADAE FFFNTDRKSK LIDRLPMLEN AIFQQQLGTI
KDKTDRITEL AGYIAEQIGA DVEKSKRAGL LAKCDLMTSM VFEFTDTQGV MGMHYARHDG
EAEEVALALN EQYMPRFAGD DLPSNGVSAA VAMADKLDTI VGIFGIGQAP KGSDPFALRR
ASLGVLRIIV EYGYNLDLVD LVAKAKSLFA QQDGTSRLTN DNVEQEVIEF MLGRFRAWYQ
DEGFSVDIIQ AVLARRPTKP ADFDQRVKAV SHFRELEAAE ALAAANKRVG NILAKFDGEL
AAEIDLALLQ EDAEKVLAEN VEVMTEALEP AFATGNYQEA LSKLADLREP VDAFFDNVMV
MADDEALKTN RLTLLNNLRN LFLQIADISL LQK