ID   SYLC_SCHPO              Reviewed;        1111 AA.
AC   Q10490;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Putative leucyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase;
DE            Short=LeuRS;
GN   ORFNames=SPAC26F1.13c;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 739-1110.
RC   STRAIN=PR745;
RX   MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(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; CU329670; CAA97370.1; -; Genomic_DNA.
DR   EMBL; D89170; BAA13832.1; -; mRNA.
DR   PIR; T38407; T38407.
DR   PIR; T42535; T42535.
DR   RefSeq; NP_594882.1; -.
DR   GeneID; 2542670; -.
DR   KEGG; spo:SPAC26F1.13c; -.
DR   NMPDR; fig|4896.1.peg.4852; -.
DR   GeneDB_Spombe; SPAC26F1.13c; -.
DR   OMA; Q10490; HVTGTPI.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002950-MON; -.
DR   BRENDA; 6.1.1.4; 653.
DR   ArrayExpress; Q10490; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
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; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN         1   1111       Putative leucyl-tRNA synthetase,
FT                                cytoplasmic.
FT                                /FTId=PRO_0000152154.
FT   MOTIF        74     84       "HIGH" region.
FT   MOTIF       737    741       "KMSKS" region.
FT   BINDING     740    740       ATP (By similarity).
FT   MOD_RES     460    460       Phosphoserine.
SQ   SEQUENCE   1111 AA;  126452 MW;  88D654634F0415A9 CRC64;
     MATTEPSVEQ LETKTAKLKL ENTTKRDTLI ELEKKYQQKW QEEKAFEVDA PLEDVPIDEL
     RKKYPKFFGN MPYPYMNGAL HLGHAFTLSK VEFTTAFERL NGKRVLFPMG FHCTGMPICA
     SADRLSREIE MFGPSFDVPE EKEEEVEVEV KTPNAREDVT KHSGKKSKAA AKTAAVKYQF
     QIMESLGVPR TEIHKFADAK YWLSYFPPLC QRDCTEFGLG IDWRRSFITT DVNPYYDSFV
     RWQVNHLHDS GKIKFGERYT VYSIKDGQPC MDHDRKSGEG VGPQEYTGIK MEVLEFPEAA
     RKALQSIDLS NKKVCMIAAT LRPETMYGQT NCYVGPNITY GIYESNVPNE LFICTRRAAN
     NMAYQKLSKE RGVVSELGTI KGQDLIGALV NAPLSVHKQV YVLPMETVLA TKGTGVVTSV
     PSDSPDDFAT LTELRKKAEF YHLNPEWMKY EAVPIIRTPS YGDMCAEFLC KKLKIQSPKD
     VKQLAQAKEL AYKECFYQGT MIIGKYSGEK VETAKPKVRK ELIDQGLAFV YNEPEGQVIS
     RSGDDCIVAL CDQWFLDYGE ASWKAVTEKA LDRLNTFSPE VRNGFLKTLD WLSQWACARS
     YGLGTRLPWD PQFLVESLTD STIYMAYYTI CHLLHSDVYG KVPGALNIKP EQMTPEVWDH
     VFRQAPKPKN TSISDEALAR LCREFQYFYP FDIRASGKDL VPNHLTFCLY THTAIFDEKY
     WPKGIRANGH LLMNGEKMSK STGNFMTLHE ATKKFGADAT RLALADAGDT VDDANFEEAL
     ANSAILRLYT QEAWCKEMME NLDNLRTGPY NFHDKVFENE INQLIESSRE AFSATLFKAA
     LKSCFYDLQN ARDWYREVTA DRKMHRDLVC RWIETQVLLL ATFAPHWSEH IWLTTLKKPQ
     SIHVSGRFPQ VSSPVNTALS NSLLYIRTLS RVIREAEAAQ LKRQKKGKGM LFDPSKPKRL
     TVFVAEKFPE WQAQYVALLQ KYYNESENKF DDKAIISSVD KKEMKRAMPF IQQFKQSVIN
     RGEHVSANSI FSRELGFNEL EVLREVKPYL VRNVGIQELR IVLLQKPADK SSAAIGLVES
     GSDAGATVEI APNFANTVPG QPTFLFENVS A
//