ID   SYCC_SCHPO              Reviewed;         754 AA.
AC   Q09860;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Probable cysteinyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase;
DE            Short=CysRS;
GN   ORFNames=SPAC29E6.06c, SPAC30.10c;
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-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; Z66525; CAA91428.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB66469.1; -; Genomic_DNA.
DR   PIR; T38507; S62512.
DR   RefSeq; NP_594564.1; -.
DR   HSSP; P21888; 1LI5.
DR   GeneID; 2542721; -.
DR   KEGG; spo:SPAC29E6.06c; -.
DR   NMPDR; fig|4896.1.peg.4534; -.
DR   GeneDB_Spombe; SPAC29E6.06c; -.
DR   OMA; Q09860; IERIARW.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002660-MON; -.
DR   BRENDA; 6.1.1.16; 653.
DR   ArrayExpress; Q09860; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR015804; Cys-tRNA-synt_Ia_C.
DR   InterPro; IPR015803; Cys-tRNA-synt_Ia_N.
DR   InterPro; IPR002308; Cys-tRNA-synth_1a.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR10890; Cys_tRNA-synt_1a; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR00435; cysS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    754       Probable cysteinyl-tRNA synthetase,
FT                                cytoplasmic.
FT                                /FTId=PRO_0000159552.
FT   MOTIF        48     58       "HIGH" region.
FT   MOTIF       408    412       "KMSKS" region.
FT   METAL        46     46       Zinc (By similarity).
FT   METAL       350    350       Zinc (By similarity).
FT   METAL       375    375       Zinc (By similarity).
FT   METAL       379    379       Zinc (By similarity).
FT   BINDING     411    411       ATP (By similarity).
SQ   SEQUENCE   754 AA;  85555 MW;  985E0301CC105358 CRC64;
     MSTRNPAQSH WGVPKGQRTE LYVYNTLTHS KVPFVSNGSN LTWYCCGPTV YDASHMGHAR
     NYVTTDILRR ILQSYFGYNI TFVQNVTDID DKIILRARQQ YLFEEYKKQQ GTNKSHSEAR
     EKVTEAWFAY AKKNLPEPPS SMSEWPQWLA SHDIPTLAIN NPKLPMHVDA LKSALDALQV
     SEASEIISLD GFWPKVQDVL VPLLDAELGS TVTDPAIFRK LAAYWEDDFN KDMANLNVLP
     PTAVTRVSEY VPEIVDFVQR IIDRGYAYPV TDGSVYFDTE AFEKGGHFYA KLEPWNKGNR
     ELIAEGEGSL AALTGKKRPG DFALWKASKP GEPSWDSPWS KGRPGWHIEC SVMASALLGS
     NIDIHSGGID LAFPHHDNEL AQSEAYFDCP QWVNYFFHAG HLHIEGQKMS KSLKNFITIK
     EILKKFTPRQ LRLAFLLQQW NTQLDFKETL LAYVLNIEQA LENFFRTVRA LMNETEGVSA
     NGGHVPEKFD KLEIELLEKF QQTQQNTHLA LCDSFNTPLV MQHIDNLVTQ ANIYIREVGQ
     QPCSRLLGQI ASWITSMLQI FGLDENGHPN AVGWSSSKGS SSENTDAMPY IRAVSSFRDR
     VRELCIAKAS SQEILKACDI FRDYDMAALG VSFNDRPQGS ALVKLVDAEE LIAAREQKLE
     EERAKQAKKA QAKAEQEKKQ VERVMKGKTS PSEMFKMFKE YLSFDEAGLP TKMRGEDGSE
     IDVPKSRKKK LQKEYAQQEK LHKEYLSYIE SNKS
//