ID N1Q115_DOTSN Unreviewed; 778 AA.
AC N1Q115;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 02-APR-2025, entry version 41.
DE RecName: Full=2-dehydropantoate 2-reductase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DOTSEDRAFT_67869 {ECO:0000313|EMBL:EME48968.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME48968.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME48968.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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DR EMBL; KB446535; EME48968.1; -; Genomic_DNA.
DR AlphaFoldDB; N1Q115; -.
DR STRING; 675120.N1Q115; -.
DR EnsemblFungi; EME48968; EME48968; DOTSEDRAFT_67869.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OMA; IWVGATN; -.
DR OrthoDB; 5302359at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000424; Meiotically up-regulated gene 72 protein; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016933}.
FT DOMAIN 10..167
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 201..323
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 329..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..406
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..575
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..768
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 84516 MW; 350BD305838F2EC2 CRC64;
MPPSTPRLRI LSVGGNAVSA FLSWRLSATQ ACDVTLVWKN GFENVHQYGI SFRSDKFGNE
RFKPRAVVRS PEDAAGANRA SFDYVLLCVK ALPDVYDLAS VIESVVSPQH TCILVNTTHT
LGIESYLEQR FPTNVVLSLV SGVEITQLGA SEFEHKGSTE LFVGAANKNP SIPASIQQDM
AEALAMTLKS GQVDCEVAAS IRQKQYERMI GPIAFYPASV LYETPVHAEL LEKVGVRSLI
TGLIDEITNL AKAQGCDFPP GFREQTMEKM IIPSDTNSIM YQDFLARRPM EVETYLGSPV
KIAQENGLQI PRIETLYSLL HNINIVNQTK PQGQAPPSPP GQATPRMSSA PMPNGTMHVN
GRGPPPANGP PMRNGMRPPT GTRSSSASAG PPPPGMMRRG PPSMSGYPPP VRMNGYGPRG
HPQQMSRRGS FEGNDLEEFS HVMLYDNMTE GGEDGYDGMQ ASSSGNLALR ERELALRRKE
LELREREFHM RRGGPRMPPP RDTFDEDDED GDDFFDAMAP NGPSPAVDAD KIDMMSVTSR
RTRKAPSASQ LRSNPEMMSN GPVRHSRNPM RRPPKQNRTS AALMADMPGL REQLMNNPLM
GYSSDRFGTV DRMNMGQESR ANSLTAERLN ELQHGGPPPG AYPPHNSFPM NRRGSQSPGN
PLSPGQRPPQ RPSPPNGYGP PAPHRNGRPS PPDMRQPVPR HPPGHGNAVA PQQIEQQTGV
SNLYPPKSGP PNQVRSLTGS ASASAGSGDS NRSAPVDSEP SAHSSSSSLG PRHAIGVR
//
