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SYGB_AGRFC
ID   SYGB_AGRFC              Reviewed;         717 AA.
AC   A9CK39;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Atu0644;
GN   ORFNames=AGR_C_1144;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
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; AE007869; AAK86451.1; -; Genomic_DNA.
DR   PIR; AF2655; AF2655.
DR   PIR; B97437; B97437.
DR   RefSeq; NP_353666.1; NC_003062.2.
DR   RefSeq; WP_010971033.1; NC_003062.2.
DR   AlphaFoldDB; A9CK39; -.
DR   SMR; A9CK39; -.
DR   STRING; 176299.Atu0644; -.
DR   EnsemblBacteria; AAK86451; AAK86451; Atu0644.
DR   KEGG; atu:Atu0644; -.
DR   PATRIC; fig|176299.10.peg.636; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; A9CK39; -.
DR   BioCyc; AGRO:ATU0644-MON; -.
DR   Proteomes; UP000000813; Chromosome circular.
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; 2.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
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..717
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101261"
SQ   SEQUENCE   717 AA;  78714 MW;  94F26877B8EF0A48 CRC64;
     MPDLLLELRS EEIPARMQRK AAGDLKKLVT DALVERGLTY EGAREYWTPR RLTLDIRGLN
     ARSADVREEK KGPRTDANEK AIEGFLRGAG LNDISEAQVV SDPKKGDFYI AIINKPGRPA
     EEIIAEVMPG IIRSFPWPKS MRSGPASMPK GSSYAGIEGK GSESLRWVRP LQSIVCLFGP
     EHDETQVIPF VIDGIVAGNI TYGHRFHAPG PITVRRFEDY VSNLEKAKVI LDADRRKDII
     LHDAKDLAFA NGLELVEDEG LLEEVSGLVE WPQVLMGTFE EDYLQIPAEI IRLTIKTNQK
     CFVTRNQGAE EGLSNRFILI SNIEASDGGK EIIHGNGKVV RARLSDARHF WNRDQGDLPD
     LETLKDSAAK FDLDLKKPLD QRMAKLDALN VTFHAKLGTQ GERVARIREL AKALAPVVGA
     DGALVDRAVV LAKADLRTEA VGEFPELQGL MGRKYAVLQG ENESVAAAIE DHYKPQGPSD
     RLPADKVAIT VALADKLDTL VGFWAIDEKP TGSKDPFALR RAALGVVRIL LEKNVRLPLL
     SVARDSDLLS FFHDRLKVYL RDLGARYDLI DAVLTPESDD LLMIARRVEA LTAFITGEDG
     RNLLAGAKRA TQLLAAEEKK GTVVADGVSE ELLKLDAEKA LYAAIKTASA DAAKAVEGED
     FRSAMQALST LRAPVDKFFE DVLVNDEDAA IRANRLALLK AIREATGTVA DFSKITG
 
 
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