ID W9XGA1_9EURO Unreviewed; 482 AA.
AC W9XGA1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=A1O5_00858 {ECO:0000313|EMBL:EXJ76350.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ76350.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ76350.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ76350.1,
RC ECO:0000313|Proteomes:UP000019471};
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 Cladophialophora psammophila CBS 110553.";
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:EXJ76350.1}.
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DR EMBL; AMGX01000001; EXJ76350.1; -; Genomic_DNA.
DR RefSeq; XP_007739667.1; XM_007741477.1.
DR AlphaFoldDB; W9XGA1; -.
DR STRING; 1182543.W9XGA1; -.
DR GeneID; 19185594; -.
DR eggNOG; KOG1324; Eukaryota.
DR HOGENOM; CLU_043966_2_0_1; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000019471; 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:UP000019471}.
FT DOMAIN 68..481
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 51354 MW; 35A60C3FCD81B623 CRC64;
MSVPTPLTTT LSAPPSPTEL PTSASTLLPP NLDDNNEEEP ERMLSPSAKR IIKITTTIVT
PIFMRPKPIY IVVATSLNPP MGIGHQGKLP WLPIRADMAF FKNVTSDVPG DAKAGSRLES
SASSSSSSAA GPTGLRTLNA VVMGRKTWES IPPKFRPLGG RLNVIITRSD SEELGWKILQ
ELKSPASKGM DAASQWELHV LPSSSSSAKT NAKIKSSSTS KSSANQRRRS STILVPPAST
FTLSKHASIS PILISASLPS TLSLLSSQTP IHIPPATATT APTSAPGSGR DPSLSLSIHK
IFCIGGGEIY RQVLSLSSTS PHTPTTPAGS ETGTDTEGET SADGGGGGGG GEQHFEVRIL
QTQIRRMPSS TTASGDKRGH GDFECDTFFP DLLPSPHLGV KSAKWKHVSP SKVQEWIGGE
LELPQHLGRR KQSAVEAITR QGDRSGDEDE EELTPLDSSG KEMWMKDEKA GVEIRVVGWE
RR
//
