SYGB_VIBA3
ID SYGB_VIBA3 Reviewed; 688 AA.
AC B7VGK6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=VS_0032;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) 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; FM954972; CAV17089.1; -; Genomic_DNA.
DR RefSeq; WP_012602954.1; NC_011753.2.
DR AlphaFoldDB; B7VGK6; -.
DR SMR; B7VGK6; -.
DR STRING; 575788.VS_0032; -.
DR EnsemblBacteria; CAV17089; CAV17089; VS_0032.
DR KEGG; vsp:VS_0032; -.
DR PATRIC; fig|575788.5.peg.1446; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000009100; 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; Reference proteome.
FT CHAIN 1..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197226"
SQ SEQUENCE 688 AA; 75785 MW; AE343A7BBC09DB24 CRC64;
MAKNFLIELG TEELPPTALR SLAEAFASNF EAGLKTAELS HEGIKWYAAP RRLALKVTAL
AEGQADKVVE KRGPAISVAF DAEGNATKAA QGWARGNGIT VEQADRLKTD KGEWLLFKQE
VAGKPVQELV MDIAAKALAG LPIPKAMRWG NSDIQFIRPV KTLTVLLGDE LVEGKILGVA
SARTIRGHRF MGEQEFTIDS ADQYPAILEE RGKVMADYDA RKAIILADAK KAADAVGGIA
DLEDDLVEEV TSLVEWPVVL TAKFEQVFLK VPSEALVYTM KGDQKYFPVY DADKNLLPNF
IFVSNIESKE PRHVIEGNEK VVRPRLADAE FFFNTDRKRP LIDRLAELDQ AIFQKQLGTI
KDKTDRITEL AGYIAEQIDA DVEKSKRAGL LAKCDLMTSM VFEFTDTQGV MGMHYATHDG
EDEQVALALY EQYMPRFAGD TLPSTGISSA VAMADKLDTI VGIFGIGQAP KGSDPFALRR
ASLGVLRIIV ENGYNLDLTD LIGKAKELLG DKLTNENVEA DVIDFMLGRF RAWYQDAGFS
VDIIQAVLAR RPTKPADFDQ RVKAVSHFRE LEAAEALAAA NKRVGNILAK FDGELPAEID
LALLQEDAEK ALAENVEVMT EALEPAFATG NYQEALSKLA DLREPVDAFF DNVMVMADDE
ALKKNRLTLL NNLRNLFLQI ADISLLQK