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ACUK_BOTFB
ID   ACUK_BOTFB              Reviewed;         693 AA.
AC   A6SP81;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Transcription activator of gluconeogenesis BC1G_14637;
GN   ORFNames=BC1G_14637;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476989; EDN21044.1; -; Genomic_DNA.
DR   RefSeq; XP_001546882.1; XM_001546832.1.
DR   AlphaFoldDB; A6SP81; -.
DR   SMR; A6SP81; -.
DR   GeneID; 5427344; -.
DR   KEGG; bfu:BCIN_16g00520; -.
DR   VEuPathDB; FungiDB:Bcin16g00520; -.
DR   OMA; VMTTCKL; -.
DR   OrthoDB; 681770at2759; -.
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   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..693
FT                   /note="Transcription activator of gluconeogenesis
FT                   BC1G_14637"
FT                   /id="PRO_0000406436"
FT   DNA_BIND        84..112
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  74939 MW;  DFA800654A5BD103 CRC64;
     MSGETEIDDP EVSDGASEND YSDHEQELDV IGKEGDNQEM AEQKVRPDGE ENGNTVGATA
     TVTKPKFDPK DPLRPRRKKA RRACFACQRA HLTCGDERPC QRCIKRGLAD ACQDGVRKKA
     KYLHDAPPEA LRPVLGPTYN QQVSSNRATA ASTPTEPSPG MGNFFSQPDT SPSYPLFGAN
     QQGQMPPPLQ NRLSFGSNQP SPISPTFHTA GNRPAGMQGI SLPQVSNDSH SAFGGGAFFD
     PSNPALFNFD LEGLNFGNHY GALEFGMLGH MASGSAETPP QDSSAGMPQN VGDLGFSNNS
     AFTNNPPFNQ IYSHDSLPDF AVGLDRPNGG NVFGNNNPHH GLPHAYAIAT SGSQHSPSTD
     ASPAASTMGF ESSPTTTNYP APASHRPAKR QDTKSGPSGK LGPSGILGKR NRDPSSIYDT
     VHEPYSYTTG FHSLTAFIQK RFSPNKTLRI AKSLASIRPS FISCTKTLNR QDLIFMEKCF
     QRTLFEYEDF MLNCCTPTVV CRRTGEIAAA NKEFTLLTGW RKEVLLGNEA NLNTNTGSGG
     PPSSGSSGRG SFTTPRMRPV NLADSNPNGK TQPIFLAELL DDDSVIEFYE DFARLAFGDS
     RGSVTTRYKL LRYQTAKDTS QSPEGDKGKR KDIVGFNGAG IGGMGNRIKE IDANNGIESL
     QQDGKVDCSS CWTIKRDVFD IPMLIVMNFL PCI
 
 
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