ID A0A074YBZ6_AURPU Unreviewed; 791 AA.
AC A0A074YBZ6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 02-APR-2025, entry version 28.
DE RecName: Full=ApbA-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M438DRAFT_335171 {ECO:0000313|EMBL:KEQ84386.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ84386.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ84386.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ84386.1,
RC ECO:0000313|Proteomes:UP000030706};
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; KL584982; KEQ84386.1; -; Genomic_DNA.
DR RefSeq; XP_029760573.1; XM_029903780.1.
DR AlphaFoldDB; A0A074YBZ6; -.
DR STRING; 1043002.A0A074YBZ6; -.
DR GeneID; 40746086; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 301968at147541; -.
DR Proteomes; UP000030706; 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:UP000030706}.
FT DOMAIN 15..172
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 205..327
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 332..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..373
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..388
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..520
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..577
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..732
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..761
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..783
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 85218 MW; 50CC0F4D77EFA0DF CRC64;
MAADQARQEQ QLTNILVVGG NAVSAFMSWR LSATNACDVT LVWKNGFENV SQYGLSFKSA
TFGNERFKPR QVVRTPEEAA KTSRAPYDYV LLCVKALPDV YDIASIIESV VAPQHTCILI
NTTHSLGVES YLEQRFPTNV VLSLVAGAEL SQLGPSEFEH KGTAEIWVGP ANKNPSIPAS
IQSDMAEALA MTLSSGQVDC KVSTNIRQQQ YERMIGPIAF HPASVLFETS NHAELLEKTG
ARAMISGIID EILLLAKSQG CDFPENFREQ TMEAMIQPTA TPSTMYQDFT ARRPLEIETF
LGAPIKLAQD VGVPVPRIET LYALLHNANT LNQSRPPPSA AIAPQPTPAQ TPRMGPGPMG
PGPNQRGPMN GPMPGHPGRP GMMRPGSRAP SMTGGPPPQM RRGPSMNNGF GPQMRMNGNG
HRGPPQQQTR RPSLEGNELE EFSHLMLYDN LPEGALPEGA IPEGAGPGGE MGLRERELAL
RQRELSLREQ EFHMRRRMPP PPASHAGGYE EDDEDGEDFF DPMAAGRNVP VIDPDNFDMM
SVTSKRTRKA PSANQLRNNP EMGGPQMRGG GGGGRGMFGR PKVQNRTSAR LMSEIPGLHE
NLMGNPLLGY SSDRYGGVDR HNLGQESRTN SLTAERLNEL SRGGPPGQGP YPGPMPPPMG
RRASNSPGHP LGPPMGPPRG PPGQQRPYPP NGQNGYPPHM NGRPSPPGVM GSPMQQRPPT
QQGQVPQHVE QQNGVSHLYP PKSGPQERSL TGSASASAGS GDSNHSVPLD SDPSAHSSSS
SLGPRPPHGF R
//
