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Database: UniProt
Entry: A0A0C4E363_MAGP6
LinkDB: A0A0C4E363_MAGP6
Original site: A0A0C4E363_MAGP6 
ID   A0A0C4E363_MAGP6        Unreviewed;       259 AA.
AC   A0A0C4E363;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00018886};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   ORFNames=MAPG_06855 {ECO:0000313|EMBL:KLU87864.1};
OS   Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS   fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_06855T0, ECO:0000313|Proteomes:UP000011715};
RN   [1] {ECO:0000313|Proteomes:UP000011715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KLU87864.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU87864.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KLU87864.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU87864.1};
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Magnaporthe poae ATCC 64411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblFungi:MAPG_06855T0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_06855T0};
RX   PubMed=26416668; DOI=10.1534/g3.115.020057;
RA   Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA   Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA   Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA   Ma L.-J., Dean R.A.;
RT   "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT   family of fungi.";
RL   G3 (Bethesda) 5:2539-2545(2015).
RN   [5] {ECO:0000313|EnsemblFungi:MAPG_06855T0}
RP   IDENTIFICATION.
RC   STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_06855T0};
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   EMBL; ADBL01001650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL876970; KLU87864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4E363; -.
DR   STRING; 644358.A0A0C4E363; -.
DR   EnsemblFungi; MAPG_06855T0; MAPG_06855T0; MAPG_06855.
DR   VEuPathDB; FungiDB:MAPG_06855; -.
DR   eggNOG; KOG1324; Eukaryota.
DR   OMA; QYEFQMW; -.
DR   OrthoDB; 1118873at2759; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000011715; 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:UP000011715}.
FT   DOMAIN          30..253
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  27633 MW;  85E7DEC16298A9D2 CRC64;
     MAASTDAGAE TAATTNPDAP PPVSSAAAMD LTLIVAATRT MGIGRAGTLP WTGLKREMAY
     FARVTKRAPP TSPPGAINAV VMGRKTWDSI PPRFRPLRGR LNVVLSRSFT AAAPAAATGE
     EEGQSSSSSP VVHARSLPEA LEYLARRRGE QTQTHRAPPP LARVFVMGGA QIYDAALALR
     DPAVGTVRRV LLTSVLTDFE LGEDDGAGAE ADEGFGPWRR ASKEQLDAWT GETVPEGVQE
     ENGTSYEFQM WEREVEETA
//
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