ID A0A8H5HVP5_9AGAR Unreviewed; 413 AA.
AC A0A8H5HVP5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=D9757_002966 {ECO:0000313|EMBL:KAF5390347.1};
OS Collybiopsis confluens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis.
OX NCBI_TaxID=2823264 {ECO:0000313|EMBL:KAF5390347.1, ECO:0000313|Proteomes:UP000518752};
RN [1] {ECO:0000313|EMBL:KAF5390347.1, ECO:0000313|Proteomes:UP000518752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 406.79 {ECO:0000313|EMBL:KAF5390347.1,
RC ECO:0000313|Proteomes:UP000518752};
RX PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT mushroom-forming fungi.";
RL ISME J. 14:2046-2059(2020).
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:KAF5390347.1}.
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DR EMBL; JAACJN010000016; KAF5390347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H5HVP5; -.
DR OrthoDB; 414698at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000518752; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046452; P:dihydrofolate metabolic process; IEA:TreeGrafter.
DR GO; GO:0046655; P:folic acid metabolic process; IEA:TreeGrafter.
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; 2.60.40.790; -; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR Pfam; PF05002; SGS; 1.
DR PRINTS; PR00070; DHFR.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
DR PROSITE; PS51048; SGS; 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:UP000518752}.
FT DOMAIN 1..85
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 99..196
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
FT DOMAIN 210..411
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 86..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 46338 MW; 8766003BD8E7BC46 CRC64;
MSIRHEYYEN DERTTLSIFD RGADPDKISL AFEPRKVTYT HGDKTLILEP LKGQINPDAC
DYTVGKVKVE VRLVKIAQGR WGGLIGDSPD PLANSASTTA PTPKGQRKNW DSVTTEILSS
EKERTIEDDP NVGGDSAVNP FFQKLFADAD DDTKRAMMKS YQESGGTTLS TNWEEVQKGR
VDVKPPEGQE WRKCSNQLPV SSPSATQMSR LTLIVAATRT NGIGENGRLP WHVPQEMAYF
ARVTSKAPPG QQNAVIMGRH TWESIPDKYR PLKDRVNVVL SRKSGLQFDD SVQVHRDLAS
AMDQLRSLTE PPIHRMFLIG GAMLYSASLQ LPRTSPVAYV DRVLLTRIIT PPFDHCDVFM
PDFLGEWIGS KDFNGWKQAT AEEMDEWCGF AVPQGVQQDN GVEYEFQLWV RDT
//
