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SYGB_RALSO
ID   SYGB_RALSO              Reviewed;         697 AA.
AC   Q8Y213;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=RSc0524;
GN   ORFNames=RS04944;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646052; CAD14052.1; -; Genomic_DNA.
DR   RefSeq; WP_011000483.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y213; -.
DR   SMR; Q8Y213; -.
DR   STRING; 267608.RSc0524; -.
DR   EnsemblBacteria; CAD14052; CAD14052; RSc0524.
DR   GeneID; 60500035; -.
DR   KEGG; rso:RSc0524; -.
DR   PATRIC; fig|267608.8.peg.546; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001436; 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   SMART; SM00836; DALR_1; 1.
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..697
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072921"
SQ   SEQUENCE   697 AA;  75257 MW;  15A133DAD177EBDE CRC64;
     MSTLLIELLT EELPPKALAR LGEAFAQSLF DGLSAQGLLE EGAQVEGFAT PRRLAASITG
     VRRAAPDREL REKVLPVNIA FDAEGKPTAP LTKKLAALAK SIGADTIAPE SLERAPDGKA
     ESLFHRYTAR GAVLADGLQA ALSQTIAGLP IPKVMIYQRP NGDNVQFVRP AHRLIALLDD
     EIIPAGVLGL QSGNVTLGHR FLSAGEIIIP HATAYASTLK SQGKVIAGYA ERKEAIRAEL
     LKAAGADTVV MPEALLDEVN ALVEWPVVYP CHFEEQFLAV PQECLILTMQ TNQKYFALTD
     AQGHLRNRFL IVSNLATETP QAIIEGNERV VRPRLADARF FFEHDKKKPL ADRVPQLARV
     VYHNKIGTQL ERVSRLQAIA GQLAEKLGAE VAHASRAALL AKADLLTDMV GEFPELQGTM
     GTYYARHDGE AEDVALACSE HYQPRFAGDA LPGTATGTVV ALADKLETLV GIWGIGLAPT
     GEKDPFALRR HALGILRMLI EKPLALGIAE VLEAAAASFE GIAAVKPDLA AITDFLYDRL
     RGYLKDKGYS TNEVEAVVSQ RPQRLDDIVA RLEAVRAFAA LPQAEALAAA NKRITNILKK
     TDITIGSVQP QLLREDAERA LHQAVATSEP HVHDAFARGD FTTALKTLAS LREAVDSFFD
     GVMVMADDTA LRDNRLALLG ELHGLMNRVA DISKLAA
 
 
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