位置:首页 > 蛋白库 > SYL_NITOC
SYL_NITOC
ID   SYL_NITOC               Reviewed;         819 AA.
AC   Q3J7S8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Noc_2665;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/aem.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000127; ABA59118.1; -; Genomic_DNA.
DR   RefSeq; WP_002813910.1; NC_007484.1.
DR   AlphaFoldDB; Q3J7S8; -.
DR   SMR; Q3J7S8; -.
DR   STRING; 323261.Noc_2665; -.
DR   EnsemblBacteria; ABA59118; ABA59118; Noc_2665.
DR   KEGG; noc:Noc_2665; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006838; 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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009381"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  92714 MW;  E35A47C5CB8B559F CRC64;
     MDEHYQAIQI EAEAQAYWEQ HQSFRASEDP SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMRG RNVLQPMGWD AFGLPAENAA IQNRVPPAQW TYENIDHMRR QLKRLGFAYD
     WSRELATCQP DYYRWEQWLF TKLFAKGLVY KKTALVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVERREIPQ WFLKITAYGE ELLTALDGLT GWPEQVRAMQ RNWIGRSEGI EVQFHVEGKE
     ALAVFTTRPD TLMGVTFVSV AAEHPLAREA ATSNPALAAF LEQCQRTATS EAILETLEKE
     GMDTGFKAIH PITGEAVPIW VANFVLMGYG TGAVMAVPAH DQRDYEFAKV YGLPIQQVIA
     PKDDQASCNL EQSAFVEKGL LINSGDFTGL DFDQAFAAIA EHLERGGKGQ RRVNYRLRDW
     GVSRQRYWGA PIPIVHCLHC GAIPVPEEDL PVVLPERVRF DGIRSPLKQL PEFYQTSCPQ
     CGGQAKRETD TFDTFFESSW YYARYCCPDN NATMVDERGD YWLPVDQYIG GIEHAVLHLL
     YARFFHKVMR DMGLVRSDEP FTHLLTQGMV LKDGAKMSKS KGNTVDPQAL IEHYGADTAR
     LFIMFAAPPE QSLEWSESGV EGAHRFLKRL WRIVAAHVEQ DPKAALTLKV KDLNSEQKSF
     RAKVHETIAK ASDDIGRRYT FNTAIAAIME LMNALAKFDD SSPQGQAIRQ EALEAVVLLL
     SPITPHICHR LWQELGHREA IIGVPWPEAD PDALAKESIE LVVQVNGKRR GQITVAVQAP
     REEIEGQAQA EPNVQRFIEG KTVQKVIIVP NRLVNLVVS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024