NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
MISCELLANEOUS: The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
SIMILARITY: Belongs to the dihydrofolate reductase family.
SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.

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

Z80215; CAB02272.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T19778; T19778.

NP_492364.1; -.

3D structure databases

HSSP

P13922; 1J3K. [HSSP ENTRY / PDB]

ModBase

Q93341.

Organism-specific databases

WormBase

WBGene00007974; C36B1.7.

WormPep

C36B1.7; CE05374. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

Q93341; -.

Ontologies

GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
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).

BLOCKS

Q93341.

Genome annotation databases

Ensembl

C36B1.7; Caenorhabditis elegans. [Contig view]

GeneID

172681; -.

KEGG

cel:C36B1.7; -.

NMPDR

fig|6239.3.peg.2297; -.

Other

ProtoNet

Q93341.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 189`	`189`	`Putative dihydrofolate reductase.`	`PRO_0000186372`
`DOMAIN`	`3 185`	`183`	`DHFR.`

Sequence information

Length: 189 AA [This is the length of the unprocessed precursor]

Molecular weight: 21602 Da [This is the MW of the unprocessed precursor]

CRC64: C1642558E097725F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKMNLIVAM DAEGGIGKNG VLPWRIKKDM QYFASVTKNV SDQSKRNAVL MGRKCWESIP 

        70         80         90        100        110        120 
VTRRPLAGRL NIVLSRQLPA QKSDDYIVVN SLEAAMKLLS EPPFVDSIET IWNIGGAEIY 

       130        140        150        160        170        180 
DLALRENLVD EIHLTRIFKN FEADVHLKSL DFSKMEKVQN AEVSSENSEI FEENGLKFEF 


CKWKVVENH

Q93341 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools