ID   A0A2V5I039_9EURO        Unreviewed;       756 AA.
AC   A0A2V5I039;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   SubName: Full=ApbA-domain-containing protein {ECO:0000313|EMBL:PYI30089.1};
GN   ORFNames=BP00DRAFT_477522 {ECO:0000313|EMBL:PYI30089.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI30089.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI30089.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI30089.1,
RC   ECO:0000313|Proteomes:UP000248817};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ825520; PYI30089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5I039; -.
DR   Proteomes; UP000248817; 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;
FT   DOMAIN          10..165
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          198..320
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          324..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..399
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..677
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  81739 MW;  8A6F84E71F9DC791 CRC64;
     MAPPPRLRVL SVGSNAISAF LSWRLQASTS CDVTLVWKSG FEAVSQYGVS FKSKAFGNER
     FKPRHVVRSP EEAASRENAY DYVILCVKAL PDVYDLAAVI ESVVTPQHTC ILLNTTNTLG
     VESHLEQRFP TNVVLSLVSG VEISQIGPSE FEHLNSSNIW VGATNNNSTL PSAMQTDMAA
     ALAMTLNSGQ VDCKVSNNIR QEQFERIIGP IAFYPTSVMF DNGNVTELLQ KVGVRQLVTD
     VIDELIGLAK AHGCSFPSDF PQKTMDAMAA SQSPNTMYQD FQARRPMEIE TYLGSPIKLA
     TELNIRLPRI ETIYAILHHV NTTNLSKPRE SPTPSVQAPP PQPTRMSSAP PPRNGPPMRP
     PPGRSSSAMM MPPPRRGPPM PGMSRPPSTQ PPPASARMPP REPSLEGLEE FSHLVVYDDA
     GEAGPPPRNP NGYPDGHPGP AHSQSTADLS LRERELALRQ RELQLREHEM SMRRGPPRRN
     APSRATFDEE DEDDYFDPMD TSLVPNIDPD NVDMLSITSR RAKKFPSASQ IRKNPELLSN
     GGGGGGGSRS GTFSRYFGGG RKRASDRIMQ EIPGLHDSLL DNPMMAYSSN RYGAVDRNQM
     AAGSRTNSMT TSRMGDYPPH PYPHSRRNSH SPATPYGGPP GPRMGRPATA QDQHFGPPHG
     PPNGGHPSPP GHMRAPVPRY PPGHGNAVGP QQVEQQIGVS NSYPTKGTPK ERSLTGSASA
     SAGSGDSGAS ANLDSENSAH SSQISLGAQQ AAAPVR
//