ID   SYL_ALCBS               Reviewed;         815 AA.
AC   Q0VN53;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Leucyl-tRNA synthetase;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase;
DE            Short=LeuRS;
GN   Name=leuS; OrderedLocusNames=ABO_1947;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM286690; CAL17395.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_693667.1; -.
DR   GeneID; 4211542; -.
DR   GenomeReviews; AM286690_GR; ABO_1947.
DR   KEGG; abo:ABO_1947; -.
DR   NMPDR; fig|393595.12.peg.1948; -.
DR   HOGENOM; Q0VN53; -.
DR   BioCyc; ABOR393595:ABO_1947-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00049; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-synth_Ia_bac/mito.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF7; Leu_tRNAsyn_1a; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    815       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_0000334726.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       574    578       "KMSKS" region.
FT   BINDING     577    577       ATP (By similarity).
SQ   SEQUENCE   815 AA;  91315 MW;  4B1E6B8ECD966DBA CRC64;
     MDVQYRPDQI EAQAQQYWDD NQSFKVTEDA SKEKFYCLSM FPYPSGRLHM GHVRNYSIGD
     VVSRYQRMLG KNVLQPMGWD AFGLPAENAA IKNKVAPAKW TFENIDYMRG QLQRLGFGYD
     WGRELATCTP EYYRWEQWFF TKLYEKGLVY RKMSTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEQKEIPQ WFIKITDYAD ELLNDLDQLD GWPEQVKTMQ RNWIGRSEGV ELDFPIEGEE
     SLRVYTTRPD TLMGVSYVAV AAGHPLAQKA AAANHEVADF IKECQNTKTA EADMATMEKK
     GIYTGLTATH PISGEAVPVW IANFVLMGYG TGAVMAVPAH DQRDFEFAQK YGLPINQVIE
     PANGEPIDLA LEAFTGKGTL IHSGEFDGLS SAEAFNAIAN WLSERSLGEK KVNYRLRDWG
     VSRQRYWGTP IPMVETEDGT LHPTPEDQLP VALPTDVEMD GVTSPIKADP EWAKTTFNGQ
     PALRETDTFD TFMESSWYYA RYCSPQSDTA MLDPAATNYW LPVDQYIGGI EHAILHLLYS
     RFFHKLLRDT GLVNCDEPFK QLLCQGMVLK DGAKMSKSKG NTVDPQQMIE EYGADTVRLF
     MMFAAPPEQS LEWNDAGVEG AFRFIKRLWR LVAEHVEAGN TGTLDVNALD DAGKALRRKT
     HETIQKVSDD YGRRNTFNTA IAAVMELINE VSKFDAATDN ALAVKQEALE AAVLLLAPII
     PHAGHSLWQA LGHDEAVIDA SWPSVDESAL VKDSIELVVQ VNGKVRAKLN VPANADKASV
     ESLAMDEPNV KKFTEGKTVR KVIVVPGKLV NIVAN
//