ID ACUK_NEOFI Reviewed; 683 AA. AC A1DG01; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Transcription activator of gluconeogenesis acuK; GN Name=acuK; ORFNames=AN7468; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181; 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}. 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; DS027696; EAW18308.1; -; Genomic_DNA. DR RefSeq; XP_001260205.1; XM_001260204.1. DR AlphaFoldDB; A1DG01; -. DR SMR; A1DG01; -. DR STRING; 331117.A1DG01; -. DR EnsemblFungi; EAW18308; EAW18308; NFIA_082550. DR GeneID; 4586762; -. DR KEGG; nfi:NFIA_082550; -. DR VEuPathDB; FungiDB:NFIA_082550; -. DR eggNOG; ENOG502R1M5; Eukaryota. DR HOGENOM; CLU_010748_1_0_1; -. DR OMA; VMTTCKL; -. DR OrthoDB; 5483783at2759; -. DR Proteomes; UP000006702; 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..683 FT /note="Transcription activator of gluconeogenesis acuK" FT /id="PRO_0000406442" FT DNA_BIND 65..93 FT /note="Zn(2)-C6 fungal-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 131..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 354..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 537..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..221 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 262..290 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..328 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..568 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 683 AA; 74236 MW; 1DD243D44C14C210 CRC64; MKTEDNGSAP ALAGDHGGVD QDTPDAGDRT EQAKHKTNGT TEKAPKSSNA KDPSRPRRKK ARRACFACQR AHLTCGDERP CQRCIKRGLQ DACHDGVRKK AKYLHDAPDG ALMPGVGGNF YNNAMRNNLP LSRNGATTVN TTSQQNSGSS YYPTPQSNSY NVYQDTPLTQ NSFPSQSPVS PTFNMKTTPT ARSNSLSSSV NQQPPNTTVS GATQSQNPFA GPFFDPSDPA LFNFDLSSMN FENRYGALEF GMLGHMATGA GDSPTDSATQ RGSMGRSGST QYSTTPITGA PGFGESPGNQ QPFMFGNDPL LNEWPNSQAP NQGHLNVSGV YPQGGMMHMA KSDAPHAFAI ESGPASFSSP SATTSPHINS GYDESSLSNT VVNKSNGLTA NGQRPAITTP SLKHQSLQFG VKRRQRNPST VYESVKEPYA YTNRFHNLTA FIQRRFSPQK TLQIAKALAS IRPSFIATTK TLNRDDLIFM EKCFQRTLWE YEDFINACGT PTIVCRRTGE IAAVGKEFSI LTGWKKDVLL GKEPNLNVNT GGSSAPGSGT TSRGSFTPRS STLENATPGR PQPVFLAELL DDDSVVEFYE DFARLAFGDS RGSVMTTCKL LKYKTKEDME LAQSDDNQRW NNHLRKGGIA GEAGMNQLGF KDGKVECAYC WTVKRDVFDI PMLIVMNVSC QCF //