ID A0A074WVY9_9PEZI Unreviewed; 789 AA.
AC A0A074WVY9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=ApbA-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M436DRAFT_45571 {ECO:0000313|EMBL:KEQ73912.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73912.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ73912.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73912.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584708; KEQ73912.1; -; Genomic_DNA.
DR RefSeq; XP_013428057.1; XM_013572603.1.
DR AlphaFoldDB; A0A074WVY9; -.
DR STRING; 1043004.A0A074WVY9; -.
DR GeneID; 25410359; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000027730; 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:UP000027730}.
FT DOMAIN 10..167
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 329..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 84856 MW; 8E7BC310CF0672B2 CRC64;
MAPTVPRLRI LSVGGNAVSA FMSWRLSATN ACDVTLVWKN GFENVSQYGL SFKSATFGNE
RFKPRQVVRT PEEAAKSSRA PYDYVLLCVK ALPDVYDIAS IIESVVAPQH TCILINTTHS
LGVESYLEQR FPTNVVLSLV AGAELSQIGA SEFEHKGSAE IWVGPANKNP SIPASIQSDM
AEALAMTLSS GQVDCKVSTN IRQQQYERMI GPITFHPASV LFETPNHAEL LEKTGARAMI
TGIIDELLVL AQTQGCVFPE NFHEQTMEAM IQPTATPSTM YQDFTARRPL EIETFLGAPI
KLAQDMGVSV PRIETLYALL HNANTLNQSR PPPAAAISPP NPAQTPRVGS GPNMGPGPNQ
RGPMNGPMNG PMNGAMPGHP GRPGMMRPGS RAPSMTGGPP PQMRRGPSMN NGFGPSMRMN
GNGHRGPPQQ PTRRPSLEDN ELEEFSHLML YDNLPEGALP EGAIPNGAGP GGEMGMRERE
FALRQRELAL REQEFSMRRR MPPPPASHAG GFDDDDEDGE DYFDPMAAGR NVPMIDPDNF
DMMSVTSKRA RKAPPPSANQ LRNNPEMGGH QMRGGGGGRG MFGRPKVQNR TSARLMSEIP
NLHDNLMGNP LLGYSSDRYG GVDRHNLGQE SRTNSLTAER LNELSRGGPP GQGPYPGPMP
PQMGRRASNS PGHPLGPPRG PPGQRPYPPN GQNGYPPHMN GRPSPPGAMG SPMQRPMGQQ
GQVPQHVEQQ NGVSHLYPPK SGPQERSLTG SASASAGSGD SNHSVPLDSD PSAHSSSSSL
GPRPPQGFR
//