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Entry: TYSY_SCHPO
LinkDB: TYSY_SCHPO
Original site: TYSY_SCHPO 
ID   TYSY_SCHPO              Reviewed;         625 AA.
AC   Q9UTI7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   26-NOV-2014, entry version 90.
DE   RecName: Full=Probable thymidylate synthase;
DE            Short=TS;
DE            Short=TSase;
DE            EC=2.1.1.45;
GN   ORFNames=SPAC15E1.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAB52423.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Required for both nuclear and mitochondrial DNA
CC       synthesis. {ECO:0000250|UniProtKB:P06785}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP =
CC       dihydrofolate + dTMP. {ECO:0000250|UniProtKB:P06785}.
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC       oligomeric flavin containing Cys decarboxylase) superfamily.
CC       {ECO:0000255}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thymidylate
CC       synthase family. {ECO:0000255}.
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DR   EMBL; CU329670; CAB52423.1; -; Genomic_DNA.
DR   PIR; T37719; T37719.
DR   RefSeq; NP_594305.1; NM_001019728.2.
DR   ProteinModelPortal; Q9UTI7; -.
DR   SMR; Q9UTI7; 327-625.
DR   BioGrid; 279249; 3.
DR   MINT; MINT-4710571; -.
DR   STRING; 4896.SPAC15E1.04-1; -.
DR   MaxQB; Q9UTI7; -.
DR   EnsemblFungi; SPAC15E1.04.1; SPAC15E1.04.1:pep; SPAC15E1.04.
DR   GeneID; 2542801; -.
DR   KEGG; spo:SPAC15E1.04; -.
DR   PomBase; SPAC15E1.04; -.
DR   eggNOG; COG0452; -.
DR   InParanoid; Q9UTI7; -.
DR   KO; K01598; -.
DR   OMA; ITHIELR; -.
DR   OrthoDB; EOG7X6M9G; -.
DR   PhylomeDB; Q9UTI7; -.
DR   Reactome; REACT_188629; G1/S-Specific Transcription.
DR   Reactome; REACT_227862; Pyrimidine biosynthesis.
DR   Reactome; REACT_229963; E2F mediated regulation of DNA replication.
DR   UniPathway; UPA00575; -.
DR   NextBio; 20803844; -.
DR   PRO; PR:Q9UTI7; -.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:PomBase.
DR   GO; GO:0004799; F:thymidylate synthase activity; ISS:PomBase.
DR   GO; GO:0006231; P:dTMP biosynthetic process; ISS:PomBase.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.572.10; -; 1.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   InterPro; IPR020940; Thymidylate_synthase_AS.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   SUPFAM; SSF55831; SSF55831; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   Nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    625       Probable thymidylate synthase.
FT                                /FTId=PRO_0000310825.
FT   COMPBIAS    229    255       Asp-rich. {ECO:0000255}.
FT   ACT_SITE    497    497       {ECO:0000250|UniProtKB:P13100}.
SQ   SEQUENCE   625 AA;  69893 MW;  B3BC6034BF26F61E CRC64;
     MSQPLHARFA TRAVKNPMIL EKERQLTDSK YHILVAATGS VAAIKLTLIV KSLLTYKGVD
     VQVVLTDPAR NFVEKEDLTA LGVNVYNNAD DWKNWDGLEC PITHIELRRW AHLLLIAPLS
     ANTMAKMANG LCDNLLTSLI RAWAPLKPIL LAPAMNTLMW TNPITQEHLS AISRIYKNSE
     FIMPIEKVLA CGDIGMGGMA EWRNIVGRVA DKLQLEQKSV LPNAVKNIDG QDDDSSEQTA
     AFEEYDDDDD DDVDDNEQSN SMIETSANAD ITPKASLLPS TTESSISKDH ETSQAPLGSE
     SVDTQASENV TTKPEPPVPF TSSEYRNTEE EQYLNLIRYI LENGQSRPDR TGTGTRSVFA
     PPQLRFSLRN NTLPLLTTKR VFLRGVLEEL LWFIHGDTNA NHLSEKGIHI WDGNGSREFL
     DSRGLTDRKV GDLGPIYGFQ WRHFGAQYVD CDTDYTNKGV DQLAQVISTL KLNPYDRRII
     LSAWNPLAIP EMALPPCHIF CQFYVSEPCK PGGKPQLSSM MYQRSADMGL GVPFNIASYS
     LLTHMIAHMC GYEAAEFVHV MGDCHIYNDH LEALQTQLER VPKAFPKLFF KRDAKDIGSI
     DSFSVDDFAV EGYNPYGPIK MKMSV
//
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