ID   SYL_ALHEH               Reviewed;         864 AA.
AC   Q0ABN3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Mlg_0400;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000453; ABI55754.1; -; Genomic_DNA.
DR   RefSeq; YP_741244.1; -.
DR   GeneID; 4269978; -.
DR   GenomeReviews; CP000453_GR; Mlg_0400.
DR   KEGG; aeh:Mlg_0400; -.
DR   NMPDR; fig|187272.6.peg.378; -.
DR   HOGENOM; Q0ABN3; -.
DR   OMA; Q0ABN3; MMFASPP.
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    864       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_1000009288.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       621    625       "KMSKS" region.
FT   BINDING     624    624       ATP (By similarity).
SQ   SEQUENCE   864 AA;  96603 MW;  49BADF5A7AD2469E CRC64;
     MDASYQPEQI EAQAQRYWDE QQSFAAREER EGEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMQG RNVLQPMGWD AFGLPAENAA MKHGVPPARW TRENIETMRG QLQRLGFAYD
     WDREFATCDP EYYRWEQWLF TRLYKKGLVY KKTATVNWDP VDQTVLANEQ VVDGRGWRSG
     AVVERRDIPQ WFLRITDYAD ELLEALDELP GWPEQVRAMQ RNWIGRSEGV ELDFAVAGHS
     DTLRVYTTRP DTLYGVTYVG LAPEHPLAAE AAEGNPEMQR FIEDCRKGGV AEADIATMEK
     RGMDTGLKAV HPLTGEQVPI WVANFVLMEY GHGAVMAVPA HDQRDWEFAS KYGLDIRPVV
     HPSAEERADV SEGAFTDDGV LADSGEFSGL PSAEARQAIG EKLEGLGKGE RTVNYRLRDW
     GISRQRYWGA PIPMIQCPAC GDVPVPDEDL PVVLPEDVDV TGGGSPLKDL PAFYQTTCPQ
     CGGEARRETD TFDTFMESSW YYARFACADQ KGAMLDERAD QWLPVDQYIG GIEHAILHLL
     YARFFHKLMR DEGLLQSDEP FRNLLTQGMV IAETYYRERG DGGKDWYNPA EVTVQRDERG
     RPVSAVLEDD GEPVVMGAIE KMSKSKNNGV DPQALIDRYG ADTVRLYTMF AAPPDQSLEW
     SDSAVEGAYR FLRRYYGLVR DHVAAGPVPA LDVASLDDAA RDLRRKVHET IAKASDDVGR
     RYTFNTAIAA VMELCNALGK AAANEPSGAA RAVLQEGLEA ATLILAPIAP HVTHVCWQAL
     GHDEAVIDAR WPAVDESALT RDTIELVVQV NGKLRSRLQL PADADKAAAE AAALADEKVQ
     RFTEGKTVRK VIVVPGKLVN IVAN
//