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SYGB_COLP3
ID   SYGB_COLP3              Reviewed;         688 AA.
AC   Q48AS2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=CPS_0006;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ27379.1; -; Genomic_DNA.
DR   RefSeq; WP_011040896.1; NC_003910.7.
DR   AlphaFoldDB; Q48AS2; -.
DR   SMR; Q48AS2; -.
DR   STRING; 167879.CPS_0006; -.
DR   EnsemblBacteria; AAZ27379; AAZ27379; CPS_0006.
DR   KEGG; cps:CPS_0006; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000547; 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_1000006354"
SQ   SEQUENCE   688 AA;  76524 MW;  85360A7AB56EB311 CRC64;
     MTTETLLIEL GTEELPPKSL KTLATAFYDN IKGQLDSHNL SYSDIKWFAT PRRFAVQVFD
     LVEKQDDKIV EKRGPAVNVA FDDAGNASKA AQGWARSNGI EVDQAERLVT GKGEWLLHRA
     TVSGKAVVEL IPDMVTTALN KLPIAKPMRW GAERTQFIRP VQTLTMLFGS DIIAGEALGV
     SSSNQVQGHR FHHEGLVTIN HANDYQAELA KAYVEVDFNE RQNKIVAQIK QVANDIDAVA
     LIDEELLNEV TALVEWPVTL VGTFDEDFLN VPAEPLIYSM KDHQKYFPVT DKNGQLVNKF
     IFVTNIESKD PNTIIFGNEK VIRPRLADAE FFFKTDKKQS LESRLKSLES VLFQKQLGTL
     KAKSERIASL SQFIAEQLNE NAQDAYRAGL LSKTDLMSDM VLEFPQVQGT MGKYYALHDG
     ENENIAQALE DQYRPRFAGD SLPEANIGCA VAISDKIDSL VGIFGINQAP KGDKDPFALR
     RAAIGSIRII IEKQLDLDLS TLINKSIELF GDKLVNENTA TDVLEFIMGR FRAFYQEQGI
     SVDVIQAVLA KKPSAPLDFE KRIKAVTFFG ELPEAATLAA ANKRVGNILA KFDGELYQSF
     NTDLATEQAE RDLADIYRDI SLKVAPLMAD KNYQAALSEL AQLKAPIDTF FDGVMVMSDD
     EAVKINRLTL LNQIRNSFFA IADISVLQ
 
 
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