位置:首页 > 蛋白库 > SYL_WOLPP
SYL_WOLPP
ID   SYL_WOLPP               Reviewed;         819 AA.
AC   B3CLT1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=WP0741;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54849.1; -; Genomic_DNA.
DR   RefSeq; WP_012481901.1; NC_010981.1.
DR   AlphaFoldDB; B3CLT1; -.
DR   SMR; B3CLT1; -.
DR   STRING; 570417.WP0741; -.
DR   EnsemblBacteria; CAQ54849; CAQ54849; WP0741.
DR   KEGG; wpi:WP0741; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008814; 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   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.
FT   CHAIN           1..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091378"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  94306 MW;  5D9B6B6366227F7D CRC64;
     MKYDFKNVEK FYQNKWDFSV SKDSKKKKCY VLEMFPYPSG KIHMGHLRNY AIGDVIARYK
     RARGFEVLHP IGWDAFGLPA ENAARDNNIN PAAWTQDNID NMRTQLKSIG LSYNWDRELS
     TCEPDYYKHE QKFFLDFLKH GLAYRKESWV NWDPVDQTVL ANEQVVDGKG WRSGAVVEKR
     KLFQWFLKIT DFAEDLLHCL QSLKNWPEKV KTMQERWIGK SEGATIDFEI FGLNKKLKIF
     TTSPHTLFGA SFLAVGAEHP IVQDLKDKEI RDFIGNMKAK GENDEKIGIY TGLNVKHPFL
     DKELPLYIAN FVLMEYGEGA IFGCPAHDQR DFEFAQKYGL PIIPVVCEES TEILKEPYFG
     DGVMFNSEFL NGLMINEAKK VIIKKLEEKG IGKKTINYRL HDWGISRQRY WGCPIPIIHC
     KDCGIVPVPE KDLPVVLPTD VEFTSGGNPL DKHPTWKFVD CPKCGKQAER ETDTFDTFFE
     SSWYFAAFCS ENKSINKDTC NRFMPVDYYI GGIEHAILHL LYSRFFCRAL TKCGYFDVKE
     PFSTLITQGM VCHITYKDEN GKWLFPEEAK ELIAKGAKIQ VGKVEKMSKS KKNTVDPNFI
     IEKYGADTAR LFVLSDTPPE KDMEWSDDGV EGCFRYINKL WRMVVQLRTV NIHYDNENIV
     GKLLEYRKKI HKLLHGLTDD LENCRLNCVV AKFREMTNLI AEIDVKTGKS LIDEGICILI
     RVIEPLMPHL AENLWQEIGG EGMLYMQPWP KADESLLIDN MVTVAVQING KLRATIKVET
     DLPQEELKKI ATDSVSNKID QSKIRTIYAV PNKVVNIVI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024