ID   ACUK_AJECN              Reviewed;         776 AA.
AC   A6R213;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Transcription activator of gluconeogenesis HCAG_03671;
GN   ORFNames=HCAG_03671;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476657; EDN07140.1; -; Genomic_DNA.
DR   RefSeq; XP_001541573.1; XM_001541523.1.
DR   AlphaFoldDB; A6R213; -.
DR   STRING; 339724.A6R213; -.
DR   EnsemblFungi; EDN07140; EDN07140; HCAG_03671.
DR   GeneID; 5447923; -.
DR   KEGG; aje:HCAG_03671; -.
DR   VEuPathDB; FungiDB:HCAG_03671; -.
DR   HOGENOM; CLU_010748_1_0_1; -.
DR   OMA; VMTTCKL; -.
DR   OrthoDB; 681770at2759; -.
DR   Proteomes; UP000009297; 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; -; 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..776
FT                   /note="Transcription activator of gluconeogenesis
FT                   HCAG_03671"
FT                   /id="PRO_0000406425"
FT   DNA_BIND        77..105
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  82947 MW;  96B29880BC6DE8AA CRC64;
     MTASTQNGSP TPPPAAPTAT NQESKNMTAN PADASESQSP ANEKGGGTAE NGQKHTSTAA
     NAKDPLRPRR KKAKRACFAC QRAHLTCGDE RPCQRCIKRG LQDACHDGVR KKAKYLHDAP
     NEALMPGIRR NFYNQANATR TNASQQQNGP NSNSNKDSRQ NVAANFYSPQ SASNFDVYTQ
     AKSQQGQGHI PPTVMQDTSI NPSAFQAPSP TSTPNFDLSS NPPNRNLSSA MTQTPSSASN
     QTQDPFGAAF FDPSHPALFN FDIASMNFGN RYGALEFGML GHMATGAGDT PPSDSATQRG
     SIGRSSGTFT AQNFGDSTNT QPPFLFGDPV LNDWNPSGQS QTNPRNNNIY NQNTVAGQMG
     EQHPNAFAIE SAPMNFASPG STESPQMTTM NQFDEANAKF SSRTALMHQT NPHQPPPIST
     PGLKHQGFQV GVKRRYRSPS SIYESVKEPY SYTSGFHNLT AFIQRRFSPQ KTLQIAKALA
     SIRPSFIATT KTLNQDDLIF MEKCFQRTLW EYEDFINACG TPTIVCRRTG EIAAVGKEFS
     ILTGWKKEVL LGKEPNLNVN TGGSSPRGSG TFTPRNGNGV DPHSGMSASG GGGGRTQPVF
     LAELLDDDSV IEFYEDFAKL AFGDSRGSVM TTCKLLKYKT KEDSAALFQG REAQQGGPDG
     KGGGGGGGDV ATTAATTSTS TSNGANSSGH ANANRNNTNP NNSSPPSSSS AAAAGPLHGA
     QLSPKQTWGK RGIAGEAGMN QLGFRDGKVE CSYCWTVKRD VFDIPMLIVM NFLPCI