ID   S8A5C1_DACHA            Unreviewed;       234 AA.
AC   S8A5C1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   ORFNames=H072_8029 {ECO:0000313|EMBL:EPS38225.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38225.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS38225.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38225.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS38225.1}.
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DR   EMBL; AQGS01000575; EPS38225.1; -; Genomic_DNA.
DR   RefSeq; XP_011113754.1; XM_011115452.1.
DR   AlphaFoldDB; S8A5C1; -.
DR   STRING; 1284197.S8A5C1; -.
DR   eggNOG; KOG1324; Eukaryota.
DR   HOGENOM; CLU_043966_2_1_1; -.
DR   OMA; QYEFQMW; -.
DR   OrthoDB; 1118873at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR   CDD; cd00209; DHFR; 1.
DR   Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR001796; DHFR_dom.
DR   PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT   DOMAIN          4..231
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   234 AA;  25937 MW;  1CA5DB3A502275CD CRC64;
     MSTPITLVVA TTPAPTLAIG KSLTNNMPWP RLPSEMSYFA RVTRRVPPPP PNSPHKYANA
     VIMGRKTWES LPPKYRPLPG RINVVVSRDH ASSLGTSKGL GGGEFWVGNI EEGVKLLKQK
     FPSKPPPQDM TEGSLELHQI FIIGGSQIYK LAMELPKDNE AYPTRILHTT ILSPDYGSEE
     GVDVVFPPID EEQWKRGDVD RLVDVTGEER AVVEGVKNEE GVQFEFGLWE RVPA
//