ID A0A2T2NE81_CORCC Unreviewed; 769 AA.
AC A0A2T2NE81;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 18.
DE RecName: Full=ApbA-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BS50DRAFT_637098 {ECO:0000313|EMBL:PSN63737.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN63737.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN63737.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN63737.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
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DR EMBL; KZ678139; PSN63737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2NE81; -.
DR STRING; 1448308.A0A2T2NE81; -.
DR OrthoDB; 5302359at2759; -.
DR Proteomes; UP000240883; 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:UP000240883}.
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 329..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..393
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..560
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..745
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 82388 MW; D316AD6A120B4AA2 CRC64;
MAPAAPRLRI LSVGGNAVSA FLSWRLQATN ACDVTLVWKS GYEGVAQYGI SFKSSLYGNE
RFKPHSVVRT PEEAAHSSKQ PFDYVLLCVK ALPDVYDIAN IIESVVSPQH TCILMNTTHS
LGVESYLEQR FPTNVVLSLV SGAEISQLGA SEFEHKGATD IWVGPANKNA SIPAQIQADM
AEALSMTLAS GQVNSKVAPN IRQQQFERMI GAIAFHPTSV LFETPNHAEL LEKVGVRPLV
TGVIDELLAL ATAHGCTFPA DYRETTIRQM TQPQDNNSTM WMDFEAKRPM EIETYLGSPL
KLSQEANVPV PRIETLYAAL HHINIANRNR PATAPNGGPP QQPPRMSSAP MPRGPGGPMM
NGNGPMKGGP RPGSRAPSVN GGPPMMRRGP PTGQMNGYPP RGMNGAPNGQ RRPSLEGNDL
EEFSHLMLYD NIVDDGAANG GPYETGGVAG NDMALREREL MLRQKELQLR EQELNMRRGP
PGPRRPPPPA SMAGFDEDDD EDDYFDPMAP RGPGPMIDPD NFDMMSVTSR RNRKVPSASQ
IRKNPELAGF GPGPQPGGGR MRNPFGRAGA NKNRTSARMM QDVPGLHDSL MNNPLLGYSS
NRYGDVDRGA MGAQSRANSL TASRIDEMGG PGNYGGAYPS MSRRTSQSPG NPLSPGPRPM
GRPSPPNGFP PNGMPNGMPP NGRPSPPGMR QPVPRHPPGQ GNAVAPQQVE QHAGVSNLYP
PKSRPQVRSL TGSASGSAGS GSSSAQLDSE NSAHSSQSSL GPRPPLGVR
//
