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UniProtKB/Swiss-Prot entry Q8WZJ7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name C1TC_SCHPO
Primary accession number Q8WZJ7
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 34)
Name and origin of the protein
Protein name C-1-tetrahydrofolate synthase, cytoplasmic
Synonym C1-THF synthase
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Formyltetrahydrofolate synthetase
     (EC 6.3.4.3)
Gene name
ORFNames: SPBC839.16
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329671; CAB46709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40723; T40723.
RefSeq NP_595256.1; -.
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase Q8WZJ7.
Organism-specific databases
GeneDB_Spombe SPBC839.16; -.
Gene expression databases
ArrayExpress Q8WZJ7; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR000559; Fmtethyd_synth.
IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01268; FTHFS; 1.
PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00721; FTHFS_1; 1.
PS00722; FTHFS_2; 1.
BLOCKS Q8WZJ7.
Genome annotation databases
GeneID 2541217; -.
KEGG spo:SPBC839.16; -.
NMPDR fig|4896.1.peg.1122; -.
Other
ProtoNet Q8WZJ7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   937  937     C-1-tetrahydrofolate synthase, cytoplasmic. PRO_0000315626
NP_BIND   168   170  3     NADP (By similarity). 
NP_BIND   374   381  8     ATP (By similarity). 
REGION   1   309  309     Methylenetetrahydrofolate dehydrogenase and cyclohydrolase. 
REGION   50    54  5     Substrate binding (By similarity). 
REGION   97    99  3     Substrate binding (By similarity). 
REGION   268   272  5     Substrate binding (By similarity). 
REGION   310   937  628     Formyltetrahydrofolate synthetase. 
BINDING   193   193        NADP (By similarity). 
Sequence information
Length: 937 AA [This is the length of the unprocessed precursor] Molecular weight: 101203 Da [This is the MW of the unprocessed precursor] CRC64: 70FF8700FD023C90 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALLLEGTSL ARKVREELRE QISSIKSVDP YFNVSLKIIQ VGGREDSNVY VRMKTRAANE 

        70         80         90        100        110        120 
AGISCEHVNF PEDITEYDLL LAIKGFNEDP TVHGIIVQLP LPAHINEQII TEAVAPEKDV 

       130        140        150        160        170        180 
DGFCETNLGK LTKREGQPLF TACTPKGIMC ILKHYGINVQ GKHAVVIGRS NIVGRPMSIL 

       190        200        210        220        230        240 
LEKANATVTL CHSKTESIAD IVRTADIVVA AIGIPHFVKA DWLKKGVVAI DVGINSIPDA 

       250        260        270        280        290        300 
TKKSGYRLTG DIDFENAKEV ASAITPVPGS VGPMTVAMLL QNVVESAVRF RKMSRKRKPT 

       310        320        330        340        350        360 
LLPLKLQTPV PSDIEIARSQ TPKNIGDLAS EIGIAKSELE FYGSHKAKVN LEILQRLAHR 

       370        380        390        400        410        420 
RDGHYVVVTG ITPTPFGEGK STLTAGLVQA LSNLDKLAIA CVRQPSQGPT FGIKGGAAGG 

       430        440        450        460        470        480 
GYSQFIPMEE FNLHLTGDIH AITAATNLLA AAIDTRMFHE NTQSDAALYK RLTLVKGNKR 

       490        500        510        520        530        540 
EFAPVMFRRL KKLGIDKTNP EELTEEEQRK FARLDIEPST ISWNRTLDVN DRFLRKITIG 

       550        560        570        580        590        600 
ENPTEKGFTR QTGFDLSVAS ECMSVLALAT DLKDMRERLG RMVVASNKSG EPVTADDLGV 

       610        620        630        640        650        660 
GGALTVLLKD AIKPTLMQTL EGTPALVHAG PFANISIGAS SILADRIALK LAGTEVDEDA 

       670        680        690        700        710        720 
KKEAGYVVTE AGFASDIGME KFFNIKCRTS GLKPDAIVIV ATVQALKLHG GGPPVGPGKP 

       730        740        750        760        770        780 
IPEVYKREDV DLVRKGCANL AKHISNARKY GLPVVVAINK FSSDSPNEIS AIREEALAAG 

       790        800        810        820        830        840 
ATDAVDSNHW AEGGKGALGV ARALINACEN VDSEFRLLYD VHEPIEKKIE IIAKEMYGAD 

       850        860        870        880        890        900 
GIELSPLAKE RLETFTKQGY NNLPICIAKT QYSLSHDPDL KGAPTNFTVP IRDMRLSAGA 

       910        920        930 
GFIYPLAAAI STIPGLPTKP AYYNIDIAEN GDIVGLS 

Q8WZJ7 in FASTA format

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