ID A0A2K0WJS9_GIBNY Unreviewed; 767 AA.
AC A0A2K0WJS9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FNYG_04238 {ECO:0000313|EMBL:PNP82529.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP82529.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP82529.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP82529.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) 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:PNP82529.1}.
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DR EMBL; MTQA01000057; PNP82529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WJS9; -.
DR STRING; 42673.A0A2K0WJS9; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000236664; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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:UP000236664}.
FT DOMAIN 10..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 199..321
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 328..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 83130 MW; B797D9F8C8C17C9B CRC64;
MANSELMSVC SVGGNPVSAF LSWRLQATNA CDVTLVWKSG YEHVAQYGIS FKSPIFGNER
FKPRHVVRNP EDAASARDGP FDYVVLCVKA LPDVYDLASV IDSVVTPQHT CIIVNTTHTL
GVEAALEERF PTNVVLSLVS GAELTQLGQS EFEHKGPADI WIGPANNPNN IPQTIQEDMA
QALAMTLSSG QVECKVSPNI RQQQYERVIG PIAFHPISVI FETPNHASLL EKVGVRDMVS
EVIDELLRLA DANGCKFDPD FKQKTIDEMS KASGESIMWQ DYVARRPMEV ETYLGSPVKL
ARDSNISLPR IETLYSILHN LNLVNRSRPK PGDPNANIIP PASPSAAPVP RMPSQNSHRP
MMNGMPNGNG MPPRQPRPRN SSNFSQGGMR RGPPPMNGGP PNGYGRPPPM NGPGSRQPSR
RGSLEETNLE EFSHLVLYDD IPEGSEPSVN GDPADINLRE RELALRQREM AIREQEMRMR
RGPPPGPPGG PGPRRGPHPM RNSKQVFDED DDDDDDYFDP TANPGPPLID PDNFDMMSVT
SRKNRKAPGP SPGQFRRNPD DMPPPTRGGR FRPNFGRNRS SQVGHSSMTS ENILEDPLMS
CSSDRYGSVD RGAMNAGSRA NSLTASRLDE MQYGPGPGGP PGMNGAYPRR ASQSPGNPYT
PSMRGGSRRG SPPGGYGPGP GMNGRPSPPD GVRQPVPRHP PGHGNSVAPQ QVEQHIGVSA
LHQTKPRNVR SLTGSASASA GSGEFDSEQS ANSSQGSLPP RPPIGVR
//