ID   SYL_ACAM1               Reviewed;         855 AA.
AC   B0C1R1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
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=AM1_1037;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW26077.1; -; Genomic_DNA.
DR   RefSeq; YP_001515391.1; -.
DR   GeneID; 5679862; -.
DR   GenomeReviews; CP000828_GR; AM1_1037.
DR   KEGG; amr:AM1_1037; -.
DR   OMA; B0C1R1; YYLRFID.
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    855       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_1000074823.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       614    618       "KMSKS" region.
FT   BINDING     617    617       ATP (By similarity).
SQ   SEQUENCE   855 AA;  95949 MW;  6BEA950C874A35F9 CRC64;
     MESRYNPTEI EPKWQASWAK QGLDATPEDT SKPKFYALSM FPYPSGSLHV GHTRNYVITD
     VIARLKRMQG YRVLQPMGWD AFGLPAENAA IARGIHPAEW TYANMAQMKK QLEPLGLSID
     WSREIATCSP DYYRWTQWIF LQFLDMGLAY QKEAAVNWDP VDQTVLANEQ VDNEGRSWRS
     GAKVERKLLR QWFLKITDYA EELLTDLDKL TGWPERVKTM QANWIGKSVG AYLEFPIVGM
     DEKVAVFTTR PDTVYGVTYV VLAPEHPLTP QVTSKAQKKA VDKFIEAVGA ESEMDRTAED
     KPKKGIPTGG KAINPFTGEE IPIWIADYVL YEYGTGAVMG VPAHDTRDFV FAQQNKLPIQ
     TVIVPEGGDA ETPLEAAYTE PGLMVNSGEF DGKVSTEGKQ AIIAKAETKG WGKARVQYRL
     RDWLISRQRY WGVPIPVIHC PNCGAVPVPE ADLPVELPED VEFSAQGGSP LAKLESWVNV
     ACPNCGADAK RETDTMDTFI DSSWYFLRYP DAKNDKAVFD SAKTNDWLPV DQYVGGIEHA
     ILHLLYSRFF TKVMRDRKLL NFDEPFKKLL TQGMVQALTY KNPETGQYIA PINVDADDPK
     DPETGAPLEA FYEKMSKSKY NGVPPEEVTN KYGADTARLF TLFKAPPEKD LEWEGADVEG
     QFRFLNRVWR LVSEHAAQAK GKKAKVNKAK LSKTEKELRR SIHIAIKETS EDLDGDYQFN
     TAVSELMKLS NALSDSKEKA SPVYAEGVET LLLLLTPFAP HISEELWENL GHSESILGQT
     WPQVDEEALV ADEITLVIQI MGKTRGTIQV PAGSSREDLE QLARESEVAQ RYIAGKEVKK
     VIVVPGKLVN FVVPK
//