ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q07801


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DYR_CRYNE
Primary accession number Q07801
Secondary accession number Q5KAF0
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: DFR1
Synonyms: DHFR
OrderedLocusNames: CNJ01940
From
Cryptococcus neoformans (Filobasidiella neoformans) [TaxID: 5207] 
Taxonomy Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; Tremellales; Tremellaceae; Filobasidiella; Filobasidiella/Cryptococcus neoformans species complex.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION.
PubMed=8473332 [NCBI, ExPASy, EBI, Israel, Japan]
Sirawaraporn W., Cao M., Santi D.V., Edman J.C.;
"Cloning, expression, and characterization of Cryptococcus neoformans dihydrofolate reductase.";
J. Biol. Chem. 268:8888-8892(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=JEC21;
DOI=10.1126/science.1103773; PubMed=15653466 [NCBI, ExPASy, EBI, Israel, Japan]
Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
"The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans.";
Science 307:1321-1324(2005).
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
S58802; AAB26198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017350; AAW45849.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46049; A46049.
RefSeq XP_567366.1; -.
3D structure databases
HSSP P13922; 1J3K. [HSSP ENTRY / PDB]
ModBase Q07801.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165; Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
Pfam PF00186; DHFR_1; 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).
Genome annotation databases
GeneID 3254250; -.
GenomeReviews AE017350_GR; CNJ01940.
KEGG cne:CNJ01940; -.
Phylogenomic databases
HOGENOM Q07801; -.
Other
ProtoNet Q07801.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   229  229     Dihydrofolate reductase. PRO_0000186375
DOMAIN   11   227  217     DHFR. 
Sequence information
Length: 229 AA [This is the length of the unprocessed precursor] Molecular weight: 25169 Da [This is the MW of the unprocessed precursor] CRC64: 60D9E4FF66C5F198 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQTTAKSSTP SITAVVAATA ENGIGLNGGL PWRLPGEMKY FARVTTGETP SSDPSEQNVV 

        70         80         90        100        110        120 
IMGRKTWESI PSRFRPLKNR RNVVISGKGV DLGTAENSTV YTDIPSALSA LRSTTESGHS 

       130        140        150        160        170        180 
PRIFLIGGAT LYTSSLLPSS VPSLNSSTST SPLPFSRPLI DRILLTRILS PFECDAYLED 

       190        200        210        220 
FAAHTKPDGS KVWKKASIKE FREWIGWDIE EQVEEKGVKY IFEMWVLNQ 

Q07801 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!