SYGB_XYLFM
ID SYGB_XYLFM Reviewed; 722 AA.
AC B0U7B2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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};
GN OrderedLocusNames=Xfasm12_1013;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA11978.1; -; Genomic_DNA.
DR RefSeq; WP_004085462.1; NC_010513.1.
DR AlphaFoldDB; B0U7B2; -.
DR SMR; B0U7B2; -.
DR PRIDE; B0U7B2; -.
DR KEGG; xfm:Xfasm12_1013; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
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..722
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101373"
SQ SEQUENCE 722 AA; 80181 MW; 93801C029356A52D CRC64;
MTELKPLLIE LGTEELPVNA LPSLSRAFFE GVLAGLERRG IVIDHGEAKS LSTPRRLAVL
LTAVAVEQPK QYRELFGPYL NTAFDTEGKP TKALEGFAAK CGVNWRTLER IRDTKGERFV
HRVVVPGERT DALLPGILTE AIAGMPIPKP MRWGAHEYLF ARPVHWLVML FGQDVVEAEI
MGVKAGRISR GHRFLYDKPV SLSDPQNYID VLQAAYVLVD PAARRARIVA EIEAVARQVG
GVARITEDNV AQVVNLVEWP SAVLCSFERV FLEVPQEALI QTMEVNQKFF PVLDSLGKLT
EKFIGIANIE SNDVAEVAKG YERVIRPRFS DAKFFFNEDL KQGLKAMGER LRTVTYHAKL
GTLADKVARV LVLAEAIAPQ IGVDPLLARR VALLSKNDLQ SRMVNEFPEL QGVAGHHYAL
ISGELPEVAM AIEDAYRPRF SGDEIARSPL GKVLGLAERL DTLACGFAVG MKPTGNKDPF
GLRRNALGLA RTIIESRFDL DLKVLLDQAS DWVAFATTIE QERHAQESVK QSKKEAAVKH
SLPQVSDEKS ARIEELYDFI VERLRGYYAD KGIPTTHFNA VAELKPVSLY DFHRRLDAIG
RFAALPEAEA LAVANKRIRN ILRKAEIKIP ASVDATLFDQ PAESGLLVAL EGVITDTRSA
LDCKNYVSVL TCLARLRPPI DEFFDKVMVN DENLMLRANR LALLQRLGEY LCCVAAIEHL
SN