SYGB_MAGSA
ID SYGB_MAGSA Reviewed; 688 AA.
AC Q2W3X1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=amb2650;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE51454.1; -; Genomic_DNA.
DR RefSeq; WP_011385030.1; NC_007626.1.
DR AlphaFoldDB; Q2W3X1; -.
DR SMR; Q2W3X1; -.
DR STRING; 342108.amb2650; -.
DR EnsemblBacteria; BAE51454; BAE51454; amb2650.
DR KEGG; mag:amb2650; -.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000007058; Chromosome.
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_1000101299"
SQ SEQUENCE 688 AA; 74505 MW; F3F23C8A1C756247 CRC64;
MAEFLLEIFS EEIPARMQAR AADDLRGMVS DGLAKNGITF DAARSYVTPR RLVLVIEGLP
LAGPDVSEEK RGPRVSSPAQ AMEGFLKSTG MTVEQLEQRD TGKGVFYFAV INRKGRPTAE
VLREVTEGAM ATFPWPKSQR WGANSIRWVR PIQSILALFD GSIVPVAFGP ATAGDMTAGH
RFLAPEPFRV KDFADYLSKL RHAKVMLDPV ERRHAILAGA EGLAAAEGLQ LKADDGLLAE
VTGLVEWPVP LVGSIDDKFM DVPAEVLITS MRAHQKYFSL LKADGSLAPR FIVISNMETD
DGGKAVVAGN QRVLRARLSD AKFFWDTDRK QRLEARLPKL AERTFYASLG TVADKVDRIS
ALAGNIAGMI GADRAVAERA ARLAKADLST ELVGEFPELQ GLMGRYYALN DGETPEVADA
IAAHYSPQGP GDSCPTAPVS VAVALADKID SLVGFFAINE KPTGSKDPFA LRRAALGIIR
LVLENGLRLP LSQVIFLASG HYKANLVNSP GEVANDLLNF FADRLAVALK EKGVRHDLIT
AIFSLGGEDD LVRLLKRVEA LGAFLDSDDG ANLLIAYRRA ANIVRIEEKK DGTIFSGYAD
IQLLRQDEEK ALEHALSDVG QAVSNALVTE DFAAAMAALA RLRRPVDAFF DKVTVNADEA
PLRVNRLKLL AMIGSAMGRL ADFSKVEG