ID   ACUK_ASPCL              Reviewed;         698 AA.
AC   A1C602;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Transcription activator of gluconeogenesis acuK;
GN   Name=acuK; ORFNames=AN7468;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027045; EAW13823.1; -; Genomic_DNA.
DR   RefSeq; XP_001275249.1; XM_001275248.1.
DR   AlphaFoldDB; A1C602; -.
DR   SMR; A1C602; -.
DR   STRING; 344612.A1C602; -.
DR   EnsemblFungi; EAW13823; EAW13823; ACLA_068510.
DR   GeneID; 4707944; -.
DR   KEGG; act:ACLA_068510; -.
DR   VEuPathDB; FungiDB:ACLA_068510; -.
DR   eggNOG; ENOG502R1M5; Eukaryota.
DR   HOGENOM; CLU_010748_1_0_1; -.
DR   OMA; VMTTCKL; -.
DR   OrthoDB; 5483783at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR47659:SF1; TRANSCRIPTION ACTIVATOR OF GLUCONEOGENESIS ERT1; 1.
DR   PANTHER; PTHR47659; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 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..698
FT                   /note="Transcription activator of gluconeogenesis acuK"
FT                   /id="PRO_0000406430"
FT   DNA_BIND        69..97
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  75805 MW;  1AEE9421BEAC6485 CRC64;
     MNVEAKESSV APAGDHGGAV QDPADVRDRL ELLKNKANGE TNGATPNGTK STNAKDPSRP
     RRKKARRACF ACQRAHLTCG DERPCQRCIK RGLQDACHDG VRKKAKYLHD APDGALMPGV
     GGNFYNHPMR HNMPLSSNGA NAVNATSQQN SGASFYPTPQ SNPYNVYQES TLSQNSFPSQ
     SPVSPTFNMK NTATARSNSL SSSVNQPQSN PAASGPPSQS QNPFAGPFFD PSDPALFNFD
     LSSMNFENRY GALEFGMLGH MATGAGDSPS ESATQRGSIG RSGSAQFATT PITGNPGFGE
     SPGNQQPFMF GNDPLLNEWP NNHPPGQGHM NVGGVYPQNS MMAGHLSKAD APHAFAIESG
     PASFSSPSAT TSPHVNGGYD ENALSNAVAH KPNGLPTNGQ RPAITTPRLK HQSLQLGVKR
     RHRNPSTVYE SVKEPYAYTN RFHNLTAFIQ RRFSSQKTLQ IAKALASIRP SFIATTKTLN
     RDDLIFMEKC FQRTLWEYED FINACGTPTI VCRRTGEIAA VGKEFSILTG WKKDVLLGKE
     PNLNVNTGGT SIPQSGTSSR GSFTPRISTL EQANPARPQP VFLAELLDDD SVVDFYEDFA
     RLAFGDSRGS VMTTCKLLKY KTKEDMELAQ SDDNQRWNNH LRKGGIAGEA GMNQLGFKDG
     KVECAYCWTV KRDVFDIPML IVMNYLIPSD GFKSSIPF
//