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UniProtKB/Swiss-Prot entry P36591


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

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Entry information
Entry name DYR_SCHPO
Primary accession number P36591
Secondary accession number O74408
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: dfr1
ORFNames: SPCC1223.08c
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 [MRNA].
DOI=10.1016/0378-1119(94)90052-3; PubMed=8088538 [NCBI, ExPASy, EBI, Israel, Japan]
Bertani L.E., Campbell J.L.;
"The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe.";
Gene 147:131-135(1994).
[2]
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).
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
L13703; AAA57051.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329672; CAA20877.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T43248; T43248.
RefSeq NP_588353.1; -.
3D structure databases
HSSP P16184; 1DYR. [HSSP ENTRY / PDB]
ModBase P36591.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-000273-MON; -.
Organism-specific databases
GeneDB_Spombe SPCC1223.08c; -.
Gene expression databases
ArrayExpress P36591; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from genetic interaction from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR001796; DHFR_reg.
IPR005645; DUF341.
Graphical view of domain structure.
Pfam PF00186; DHFR_1; 1.
PF03959; FSH1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P36591.
Genome annotation databases
GeneID 2539048; -.
KEGG spo:SPCC1223.08c; -.
NMPDR fig|4896.1.peg.691; -.
Other
ProtoNet P36591.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   461  461     Dihydrofolate reductase. PRO_0000186377
DOMAIN   233   447  215     DHFR. 
NP_BIND   275   282  8     ATP (Potential). 
CONFLICT   126   127        QP -> HA (in Ref. 1; AAA57051). 
Sequence information
Length: 461 AA [This is the length of the unprocessed precursor] Molecular weight: 51523 Da [This is the MW of the unprocessed precursor] CRC64: F6A3695F537A03C9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKPLKVLCL HGWIQSGPVF SKKMGSVQKY LSKYAELHFP TGPVVADEEA DPNDEEEKKR 

        70         80         90        100        110        120 
LAALGGEQNG GKFGWFEVED FKNTYGSWDE SLECINQYMQ EKGPFDGLIG FSQGAGIGAM 

       130        140        150        160        170        180 
LAQMLQPGQP PNPYVQHPPF KFVVFVGGFR AEKPEFDHFY NPKLTTPSLH IAGTSDTLVP 

       190        200        210        220        230        240 
LARSKQLVER CENAHVLLHP GQHIVPQQAV YKTGIRDFMF SAPTKEPTKH PRDLTMIVAV 

       250        260        270        280        290        300 
SSPNLGIGKK NSMPWHIKQE MAYFANVTSS TESSGQLEEG KSKIMNVVIM GRSCYDSLPK 

       310        320        330        340        350        360 
KNRPLKDRIN IVITRNSNYN FGLTKKEKMP ENLYAADCID SALDLVAEKY GADSDIQVGK 

       370        380        390        400        410        420 
VFIIGGSFLY GSALYHPLTK NLLFTRIHKE YPCDSFFPFE PAESSDWVRK AHPELEKFVG 

       430        440        450        460 
IPVEEGRLKA ASSNKEEVEI EFELYGKNDD VNVALEKLSI C 

P36591 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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