SYGB_DESVV
ID SYGB_DESVV Reviewed; 696 AA.
AC A1VCW9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Dvul_1266;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM28285.1; -; Genomic_DNA.
DR RefSeq; WP_011792161.1; NC_008751.1.
DR AlphaFoldDB; A1VCW9; -.
DR SMR; A1VCW9; -.
DR EnsemblBacteria; ABM28285; ABM28285; Dvul_1266.
DR KEGG; dvl:Dvul_1266; -.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000009173; 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 HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 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..696
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197182"
SQ SEQUENCE 696 AA; 75359 MW; 39ACE7DD3EFF4D43 CRC64;
MSQFVLEIGT EELPARFLPA LERELAERFT RALADAGIEC DPVCVMSTPR RAVVRMDAVN
PVQSESEEVV TGPPARIAFT PEGGLTKAAE GFARTQGVEV ADIFRLTTDK GEYIAVRKHM
GGARSIDLLR DICPAIIGAL PFPKRMRWGS GDFTYARPMR WLLALFDESV VDFEVGGVRS
GNITYGHRIH GAGPLTVAHA GDYERVIREQ GGVTPVGEER RNAVVTGGNT LATAAGGKVI
WKDSLLDEVQ GLVEHPVPCL GNIDPSFLEL PREVLLTSME SHQKSFGVED AEGRLMPHFL
TVLNLTPLDG DLVRKGWERV LRARLEDARF FWKTDLASSF DAWLASLDNV IFLGPLGSMG
DKTRRLEQLC AWLASEVGFD DATAAARAGR LSKGDLVSGM VGEFDTLQGI MGGIYARRMG
EAEAVAAAIA EQYLPAGPDS PVPSSMCGAL LSIADKADTL AGCFGLGMIP TGAADPYALR
RCVLGIARII LEHGLQLDVR GLFAKAFALY GERAWKLAPE DALVKLDEFF MARLRNLFIA
NGYETLLVEA VLAAGCDDVR SAGARLEALA AFSRRDDFAS AVLTFKRAAN IIRKQGGDSD
VALDGAWKAD LLVEDAERHL AASLEAMFPR FDGLWAEGDY PALFGLLGEL RPVVDGFFEG
VMVMSDDAAL RTNRLNLLQA LVGRLSRLAD FGALQM
