SYGB_SULSY
ID SYGB_SULSY Reviewed; 678 AA.
AC B2V9P9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=SYO3AOP1_1053;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001080; ACD66672.1; -; Genomic_DNA.
DR RefSeq; WP_012459740.1; NC_010730.1.
DR AlphaFoldDB; B2V9P9; -.
DR SMR; B2V9P9; -.
DR STRING; 436114.SYO3AOP1_1053; -.
DR EnsemblBacteria; ACD66672; ACD66672; SYO3AOP1_1053.
DR KEGG; sul:SYO3AOP1_1053; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_0; -.
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..678
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101362"
SQ SEQUENCE 678 AA; 78884 MW; 65A29045FDBBCB5E CRC64;
MKSYLLEIGC EELPPKAILT YKEFLKEYAH QTFKDFFIYN SPENIKIYAT PRRLAVLIKN
LKKKQDNQKI TLIGPPYKVA VDSEGKFTKA ALSFAEKNNI PLEKLEKITT EKGEYLGATI
EKEGESLELF IKHKIPQLFN QFPQLKSMKW NNSDYRFPRP IRWIVSLLDD KVIEFEVASV
KTDRFTHLHR FMTKPIGRGE RKDINHANDY EEITKLGYII ANFEDRKHSI KTQYEGFARQ
LNASIIEDDE LIDEITCLTE FPVGIVGDFS PEYLTLPKEV IITVCKHHQR YLNFEKDGKL
IPKFLAFSNN AVKDRDIVKN GYEKVLRARL EDALFFYKED LKKKLDDNIE KLKGIQFHEK
LGSMYDKVLR NLELALKLAD LTGYKDAEKI KRAVMLSKAD LLTEMVKEFD ELQGIMGMYY
SQKQGEEEEI SKSIYEHYLP KTAEDNIPET NLGTLLALAD KLDTVISFIK IGELPKPSAD
PFGIRRNAIG IVRLLVEKEI DLDLRKVIDD ESILDFILSR LESYLQSKGY KTDIINAVLS
LKDGNIYRNY LKVKALSQLR NLPDYENVIM VFKRVGNIIP EDFKFSNVDV NLLVSQPEKE
LYKKFIEIKD KFKRFIENKD YDKALGLLLE LKPYIDRFFD NVMIMVEDEK LKNNRLSLLK
EINDLFRNIA DFTKLIGG