ID   SYLM_SCHPO              Reviewed;         874 AA.
AC   Q09828;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Putative leucyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase;
DE            Short=LeuRS;
DE   Flags: Precursor;
GN   ORFNames=SPAC4G8.09;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CU329670; CAA91210.1; -; Genomic_DNA.
DR   PIR; T38854; S62486.
DR   RefSeq; NP_593069.1; -.
DR   GeneID; 2543476; -.
DR   KEGG; spo:SPAC4G8.09; -.
DR   NMPDR; fig|4896.1.peg.3039; -.
DR   GeneDB_Spombe; SPAC4G8.09; -.
DR   OMA; Q09828; MMFASPP.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000784-MON; -.
DR   BRENDA; 6.1.1.4; 653.
DR   ArrayExpress; Q09828; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Transit peptide.
FT   TRANSIT       1     21       Mitochondrion (By similarity).
FT   CHAIN        22    874       Putative leucyl-tRNA synthetase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000035811.
FT   MOTIF        67     77       "HIGH" region.
FT   MOTIF       628    632       "KMSKS" region.
FT   BINDING     631    631       ATP (By similarity).
SQ   SEQUENCE   874 AA;  100886 MW;  0F9550E7E720AFC6 CRC64;
     MLKSVGTNGR KVPKIASLCN FLKFNKNIHS NPDFLAIAEN WKSYWKSHYP FVKNDKGKKK
     YILSMFPYPS GLLHIGHVRV YTISDILSRY YRMKGYKVIH PMGWDAFGLP AENAAIENGI
     SASSWTYENI KKMKEQTYHM NIYFDWDREI STCNPDYYKW SQYLFLQMFH KGLAYQAEAT
     VNWDPVDCTV LANEQVDSHG RSWRSGAIVE KKNLRQWFLK ISDYSDQLLD DLETLPKWPD
     KVKKMQRNWI GRTTGFEISF PLLNDKETLT VFTTKPETII DVSFIALSKN HKLVLLESQK
     DPSLAEHLRN ESLLDKGYQL PCFAKNPVTG KALPIFYAPY VLDCYGTGAV MGAPIHDRRD
     FEFAKRNNII FSKESCIGSY FTNEGKELLN HHDSSNLMDI KQKMLQQKIV SYLEEKKLAK
     RVKNYRLKDW LISRQRFWGT PIPMVHCETC GAVPVPESEL PVKLPDLDKI YEKGTSPLSN
     LETWMKTTCP KCHGPATRET DTMDTFVDSS WYYFRFLDSK NSELPVGLAS ASSLMPVDIY
     IGGVEHSILH LLYSRFFSKF MKDIGLWNGD KYLNEPFTQL ITQGMVHGLT YTTMSDERIL
     NPKEVQKIGD EYFLISNPKE KVQLSYQKMS KSKHNGVDPI RTIQKYGSDI IRAYIIFSAP
     VEGVLLWNEN AIMGTKRWLT KIWNCVHQLL EREKKMSDAM RQTKLTIVDD HNSRKLESQY
     NEFISQCSAH YENVFSLNLV ISDAMKLTNN IADALKNNKV NIGTIKASLE VLVKCIAPII
     PCFSSECWLL LGHNSSVYSN WPISKNKKEN MEEPVTIPVQ INGKVRFKIE MPKLNDENEI
     LNFVLETNDG KRWLSNKKVL KSFVKQKIIS LVTD
//