ACUK_ASPNC
ID ACUK_ASPNC Reviewed; 686 AA.
AC A2QFG8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Transcription activator of gluconeogenesis acuK;
GN Name=acuK; ORFNames=AN7468;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC utilization. Activator of gluconeogenetic genes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270040; CAK48879.1; -; Genomic_DNA.
DR RefSeq; XP_001400579.1; XM_001400542.2.
DR AlphaFoldDB; A2QFG8; -.
DR SMR; A2QFG8; -.
DR PaxDb; A2QFG8; -.
DR EnsemblFungi; CAK48879; CAK48879; An02g14490.
DR GeneID; 4979989; -.
DR KEGG; ang:ANI_1_1998024; -.
DR VEuPathDB; FungiDB:An02g14490; -.
DR HOGENOM; CLU_010748_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Gluconeogenesis; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..686
FT /note="Transcription activator of gluconeogenesis acuK"
FT /id="PRO_0000406433"
FT DNA_BIND 71..99
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 73793 MW; BD6E9362737D5F81 CRC64;
MNAEPKEQDS PAPSAERTEA SQEISAAGAQ ADKPKTEANG DGTANGASAN GQKPNPKDPS
RPRRKKARRA CFACQRAHLT CGDERPCQRC IKRGLQDACH DGVRKKAKYL HDAPDGALMP
GIGGTFYNNP MRNSLPLSRN GANAVNATGQ QSAGANFYPT PQSTTYVYQE NTINQGSFPS
QSPVSPTFNL KATPTARTNS LSSVNPQPPS TSVSGPPGQG QNPFAGPFFD PSDPALFNFD
LSSMNFENRY GALEFGMLGH MATGAGDSPS DSATQRGSMG RSGSAQYAST PITGAPGFGE
SPGNQQPFMF GDPLLNEWPS GQAPGQPHLP GVYPQSGQGS AIPGHLSKAD APHAFAIESG
PASFNSPGAT TSPQMTTGLE ETPFHSAVAS KSNGLAPHGQ RPMITTPSLK HQNLQVGVRR
RQRNPSAIYD SVKEPYAYTS RFHGLTAFIQ RRFPPQKTLQ IAKALASIRP SFIATTKTLN
RDDLIFMEKC FQRTLWEYED FINACGTPTI VCRRTGEIAA VGKEFSILTG WKKDVLLGKE
PNLNVNTGGS SMPNSGASSR SFTPRSTVDN TPGRPQPVFL AELLDDDSVV QFYEDFARLA
FGDSRGSVMT TCKLLKYKTK EDMEGAAAED SQRWNNHLRK GGIASEAGMN QLGFKDGKVE
CAYCWTVKRD VFDIPMLIVM NFLPCI
