SYGB_BUCA5
ID SYGB_BUCA5 Reviewed; 690 AA.
AC B8D8T6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=BUAP5A_133;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=563178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5A;
RX PubMed=19150844; DOI=10.1126/science.1167140;
RA Moran N.A., McLaughlin H.J., Sorek R.;
RT "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT bacteria.";
RL Science 323:379-382(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; CP001161; ACL30508.1; -; Genomic_DNA.
DR RefSeq; WP_009874091.1; NC_011833.1.
DR AlphaFoldDB; B8D8T6; -.
DR SMR; B8D8T6; -.
DR KEGG; bap:BUAP5A_133; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000006904; 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.
FT CHAIN 1..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197170"
SQ SEQUENCE 690 AA; 80803 MW; 2788D93B7B231403 CRC64;
MTKKILLIEI GTEELPARLL SKISLYFYKN FIKELDFHNI SYKNIKYFST PRRLALKIKD
IDITERFVEI KKRGPSIINS YDKDGFLTEA ATRWLKHCGI NINQAIRLKN EKGEWLFYKT
RKKQENIESL IPKITESALK NISIKKSMRW GQDNQKFSRP IRNIVILLDK KVIPGDVFNI
TSKNLLQNHL SSKDSQIKIK DAKDYPKILL EKNNIIADYF IRKEKIIEDI ENIAKKIKGF
IKKNNVLIEE VTALVESPKA LLVNFQEKFL QIPKKILINT IEKKQKCFPI YNSEKKLLPY
FIFISNIQTQ ESEKIIIGNQ RVMHARLSDA EFFFKNDRKV KLESRLLSLK KVLFQNNLGS
LYEKTLRIKL LIKWIAKYSS SDVEDSIRAA LLSKCDLVTD VVCEFPELQG KIGMYYALED
KEKKDVATAL EEQYLPRFSG DKLPCTPIGC GLSIADKMDT LSGMFYIGNI PSSDKDPFAL
RRLAIGIIRI ILEKNIPLNL EDLIKKSLSL YNKKNEDDLI LFDKMIKFFM IRLFHWYEET
GYSAKIIKSV LSCKSIELID IHKKIQAISF FKKLKDSQSI ILSIKRISNI LAKEKEKING
DINKKLMIEK EEIILFNNIE EFDNYTKNLF LEKKYNDILI KIKSFENPIY NFFKKVKIYH
SDSKIRLNRL LLLSKLKKIF FKIADFSYLY