ID W9YUX7_9EURO Unreviewed; 455 AA.
AC W9YUX7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=A1O3_01622 {ECO:0000313|EMBL:EXJ93066.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ93066.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ93066.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ93066.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004903}.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000256|RuleBase:RU004474}.
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:EXJ93066.1}.
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DR EMBL; AMGY01000001; EXJ93066.1; -; Genomic_DNA.
DR RefSeq; XP_007729956.1; XM_007731766.1.
DR AlphaFoldDB; W9YUX7; -.
DR STRING; 1182542.W9YUX7; -.
DR GeneID; 19165756; -.
DR eggNOG; KOG1324; Eukaryota.
DR HOGENOM; CLU_043966_2_0_1; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000019478; 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:UniProtKB-UniPathway.
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; IPR017925; DHFR_CS.
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; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT DOMAIN 66..454
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 47999 MW; 106AB0991849BBED CRC64;
MSTIPTPPST TLSAPPSPTE LPSTAFEVTD DSDDADDHET TMQSSAQRII KTTTTTIRPV
TVHPKPIYVI VATSLNPPMG IGQAGGLPWP PIKADMAFFR KATTQVSSTT AAAAPTTSPS
PSTNLPTRTR TLNAVIMGRK TWESIPPKFR PLAGRLNLVI TRSNPRDVGQ QIADDLKSQK
QNADVDWTVC EIPSPARANT RPQISKNTIP TPGTTTTTIV TPSSSSSSSS TQAPILVSSS
IASTLVLLSS PSPIPLPTGG GAEAPSRDTG ISIDKIFCIG GAEIYSQILS LASTSMSTIG
VGKRDKSSGA AVPSTSQRST GTETDTDGET DGEFDVRILQ TQVRRVRCPN IEAGGGDGGP
EVDFECDTFF PDALPADPSI KSAKWKPVPP QRLREWVDGV EVPQCQGQEI PASGDAQGQT
SSSTSLATNT GEDDDAWYDD GKSGVEIRVV GWERR
//
