ID A0A0A2VYT5_BEABA Unreviewed; 786 AA.
AC A0A0A2VYT5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Meiotically up-regulated72 protein {ECO:0000313|EMBL:KGQ05914.1};
GN ORFNames=BBAD15_g8817 {ECO:0000313|EMBL:KGQ05914.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05914.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05914.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05914.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ05914.1}.
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DR EMBL; ANFO01000904; KGQ05914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VYT5; -.
DR STRING; 1245745.A0A0A2VYT5; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR Proteomes; UP000030106; 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:UP000030106}.
FT DOMAIN 10..191
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 224..347
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 363..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 85243 MW; 7EAC7C35AE7AD4B0 CRC64;
MSDVELMQVC SVGGNPVSAF LSWRLQATNA CDVTLVWKSG FEHVSQYGIS FKYVALTSGA
PGRQPLAHHH VANNPFRSPV FGNERFKPRH VVRNPEDAST VRDGPFDYVV LCVKALPDVY
DLAAVIDSVV TPQHTCILIN TTHTLGVEAA IEDRYPTNVV LSLVSGAELT QLGPSEFEHK
GSTSVWVGPV NQQSNIPKAI QEDMAQALAM TLSTGQVDCK VSPNIRQQQY ERVIGPIAFH
PVSVLFETPN QSVLLDKIGV KDMVTGIIDE LLLLAEANGC KFDLDFKQRV MDDMTKTNLP
ESIMWQDYVA RRPMEIETYL GSPIKLAHQA KIPVPRIETL YAIMHNLNVV NRNRPKTGDV
AGAIPPGSPT VGQPPRMPSQ NGHRPMMGGM PNGNGMPPRQ VRPRNSSNFG PPGPMRRGPP
PMNGGPNGMG RPPPHMNGGS RAPSRRGSMD GNDLEEFSHL VLYDDIPEGH EQDFADGGDV
ALRDREMQLR QREMALKDQE TRMRRGPPPP GPPGPRRGPH PMRHSTQMFD DDDDDDFFDP
PMGPSMPAID ADNFDMMSVT SRKNRKASGP PPAQIRRNPE FDAPPPSRGS RFRPSFGRNR
SSQISSIPMM TDNILDDPLM SCSSNRYGTV DRGTMNGGSR ANSLTASRLD ELQYGQAPGG
PPGMNYGRRA SQSPGNPYSP SMRGGSGRPS PPNGYGPPMN GRPSPPEGVR QPIPRYPPGQ
GNAVAPQQVE QHIGVSALHP SKTRNVRSLT GSASASAGSG ELDSGNSARS SQASLPPARP
AVTSVH
//