ID   ERT1_LACBS              Reviewed;         548 AA.
AC   B0D0T8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Transcription activator of gluconeogenesis ERT1;
GN   Name=ERT1; ORFNames=LACBIDRAFT_399488;
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX   NCBI_TaxID=486041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686;
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(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; DS547095; EDR11520.1; -; Genomic_DNA.
DR   RefSeq; XP_001877417.1; XM_001877382.1.
DR   AlphaFoldDB; B0D0T8; -.
DR   STRING; 486041.B0D0T8; -.
DR   EnsemblFungi; EDR11520; EDR11520; LACBIDRAFT_399488.
DR   GeneID; 6073497; -.
DR   KEGG; lbc:LACBIDRAFT_399488; -.
DR   HOGENOM; CLU_010748_2_1_1; -.
DR   InParanoid; B0D0T8; -.
DR   OrthoDB; 681770at2759; -.
DR   Proteomes; UP000001194; 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..548
FT                   /note="Transcription activator of gluconeogenesis ERT1"
FT                   /id="PRO_0000406463"
FT   DNA_BIND        88..116
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..222
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  60104 MW;  0C2B89B300C57296 CRC64;
     MSAVYTLASR PPRPLVPPSY VNPAQMQNAQ AGPSTAPSGP KKKSSPTLAT VKRKRTDTPE
     GNSPGSPSPQ PQRKGREGPK KKKANRACFH CQKAHLTCDD SRPCQRCVKR GLASNCTEGH
     RKKAKYLLDE EELEQLKRSK SSAPEIQGNV SAANTADPPS VPIAEPFPQN DSLLTASFDP
     NFSFGSEAAN REYSILSAIL GNPSPPESAS TPPPPPPPPQ SYATWTSDAI DFIGSPRLGT
     ATSSYTSPYG ESMQADTTLS TSPGNAHYLT YPYPQSQRSE DLVDMSYASQ YSSAGQGQPC
     LPANSRPRSP PTVFLHNPSS KDQGSRGLLS PPPSNGSPSS TSSAPSGIAE IVRPQSCGSQ
     LQSINDRVLT PYDYTEGYHF LMKHLPTRFE KNDILRIVRA LAIFRPSLIA LQMPLSLDDE
     VFVEKCFQRS LVELDKLMSF SGTPTVVWRR TGEICLVAPE FCMLTEWPME DLVHQKKYIY
     ELFENQSVVE YWENFASHAF ENTTQSVYSH CVLLKPSGAP VPSTFCFSIR RDLFDLPSIV
     IGQWLPLL