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SYL_CAUVC
ID   SYL_CAUVC               Reviewed;         861 AA.
AC   Q9A217;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=CC_3749;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; AE005673; AAK25711.1; -; Genomic_DNA.
DR   PIR; C87714; C87714.
DR   RefSeq; NP_422543.1; NC_002696.2.
DR   RefSeq; WP_010921576.1; NC_002696.2.
DR   AlphaFoldDB; Q9A217; -.
DR   SMR; Q9A217; -.
DR   STRING; 190650.CC_3749; -.
DR   EnsemblBacteria; AAK25711; AAK25711; CC_3749.
DR   KEGG; ccr:CC_3749; -.
DR   PATRIC; fig|190650.5.peg.3751; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   BioCyc; CAULO:CC3749-MON; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151995"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  95536 MW;  C546C7C0BD7DB374 CRC64;
     MARYNPKDTE PKWREAWAKA DVFKTGEIND GRPKYYVLEM FPYPSGRIHM GHVRNYAMGD
     VVARYKRAQG FNVLHPMGWD AFGMPAENAA MERGVHPKGW TYDNIAAMRE QLKSLGISVD
     WSREFATCDP EYYGKQQAWF LRLLKRGLVY RKEASVNWDP VDMTVLANEQ VIDGKGWRSG
     AVVEKRKLTQ WFLRITDYAD ALIDGLKTLD RWPDKVRLMQ ENWIGRSKGL RFKFQFDGEA
     PDGMAEGLEV YTTRPDTLFG ASFVGIAPEH PLAEQLAAAN PQIQTFIADC RKGGTSEAEI
     ESAEKLGYDT GLRVKHPLDP SITLPVWIAN FILMDYGTGA IFACPAHDQR DLDFARKYDL
     PVLPVVLPNG EDPATFTVGK EAYVGPGKIF NSKFLDGLDV EAAKAEAIAR IEAANQGQGA
     TVYRLRDWGV SRQRYWGCPI PVIHCEACGV VPVPEDQLPV ALPDDVTFDK PGNPLLRHPT
     WRHTTCPSCG GKAERETDTL DTFIDSSWYF ARFADTQAAE PVGKDAADHW LPVDQYIGGV
     EHAILHLLYA RFITRALKDE GLLSVEEPFA GLFTQGMVTH EAYKNEAGEW VEPSDVVITT
     EGSTRTAKHA KTGAPIIIGD IEKMSKSKKN VVAPEDIFEA YGVDSARLFV MSDSPPERDV
     QWTNSGVEGS WRFTHRLWNE FDSQPAGDFA HDDSDEAALA LRKAAHKLIG FVTDSIEGFR
     FNSGVARLYE FLNALKAAPA EGASQAVLAA RAEALNILAR LVAPFTPHLA EEAWARMGGE
     GMVVDAPWPK ADPALAADDE RVLPIQINGK RRGEIKVKAG APDDEVTKIA LADPNVMAHL
     EGLTVRKVIV VKDRIVNIVA N
 
 
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