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Database: UniProt
Entry: A0A4Q4U4V3_9PEZI
LinkDB: A0A4Q4U4V3_9PEZI
Original site: A0A4Q4U4V3_9PEZI 
ID   A0A4Q4U4V3_9PEZI        Unreviewed;       760 AA.
AC   A0A4Q4U4V3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   02-APR-2025, entry version 18.
DE   RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DL766_009607 {ECO:0000313|EMBL:RYP14672.1};
OS   Monosporascus sp. MC13-8B.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX   NCBI_TaxID=2211646 {ECO:0000313|EMBL:RYP14672.1, ECO:0000313|Proteomes:UP000292509};
RN   [1] {ECO:0000313|EMBL:RYP14672.1, ECO:0000313|Proteomes:UP000292509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC13-8B {ECO:0000313|EMBL:RYP14672.1,
RC   ECO:0000313|Proteomes:UP000292509};
RA   Robinson A.J., Natvig D.O.;
RT   "Complete Genomes of Monosporascus.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RYP14672.1}.
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DR   EMBL; QJNW01000640; RYP14672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4U4V3; -.
DR   STRING; 2211646.A0A4Q4U4V3; -.
DR   OrthoDB; 5302359at2759; -.
DR   Proteomes; UP000292509; 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:UP000292509}.
FT   DOMAIN          10..167
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          200..323
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          331..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..355
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..571
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..733
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  82087 MW;  4DE3F65F2AD95396 CRC64;
     MAPGTPRLKI LSVGGNAVSA FLSWRLQATN ACDVTLVWKS GFEAVYQYGI SFKSVPFGNE
     RFKPRHVVRT PEEAAKSREG AFDYVILCIK ALPDVYDLAA VIDAVVTPQH TCILVNTTHT
     LGVEAAIEER FPTNVVLSLV SKAEITQLGT SEFEHSGSTE VWVGPANRSS DIPLSIQEDM
     AQALAMTLST GRVDCKVSSN IRQQQFERVI GPIAFHPASV IFDTPSHSAL LEKTGVRQLV
     SDVIDELISL ATTQGCTLPA DFRQRTIDEQ TRHSDSPSIM WQDYVARRPM EVETFLGSPI
     KLAQSSGIKL PRIETLYAIF HNINIVNQSR PKEVIAQPPP PASPTSLSPM PRMSSVPPPR
     TVSNGVPNGN GMARGPRPRN SSNFSGPPPG MRRPPPPTNG GPPTGYRPSA NGAPNGYPPA
     RQASRRGSMD EHDLGEFSHL VLYDDSADTG DNGYPADTSD IALRERELQL RQRELALKEQ
     EMRMRRPGPA PRRRGPPPRT GGYYDEEDEE DDYFDVNAGP VTPMIDPDNF DMMSVTSRKN
     RSKAPASHSD IRSNPEGPAA RGGRWRPGFG RNRSSQIMAS AVPGLHDNIL DDPLLGYSSN
     RYGDVDRGQL HQQGSRANSL TASHLHELSN GPGMSGPYPR RASQSPGTPY TPSIRGGNGR
     PSPPNGMGGP GPNGRPSPPD GMRQPIPRYP PGHGNSVAPQ QVEQRVGVST LQSPKPKPMR
     SLTGSASASA GSGDSTHLDS EPSAYSSQSS LGPRPPIGVR
//
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