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