ID A0A1F8A4H4_9EURO Unreviewed; 1088 AA.
AC A0A1F8A4H4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
DE Flags: Fragment;
GN ORFNames=ABOM_004662 {ECO:0000313|EMBL:OGM46616.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM46616.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM46616.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM46616.1}.
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; LYCR01000030; OGM46616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A4H4; -.
DR STRING; 109264.A0A1F8A4H4; -.
DR OrthoDB; 1354898at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR47782:SF15; ZN(2)-C6 FUNGAL-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47782; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..73
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 113..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGM46616.1"
SQ SEQUENCE 1088 AA; 119400 MW; F7DBE6D669AC74DE CRC64;
RCLTPTQGPI GLSSFPAIVV LSSDMESDHR TSPASAPANP RRLQACERCW KRKQKCDRQL
PACTTCVEAD AQCAPRRVPI GPTMEEGSGL SHAAVPNYVE SLKRKRDELD AQFRQQRARR
EREASVPPQP LPNMESTSVG SPGDSNQTPS TAPTSFSERS VQAAMGEIGF LSRNAMAEPR
DESRGFPQEL AMGSMVRAAL VISGEDPSQS RDLCHHRRTF VTMMGPATGI SKEFAAPYLN
RFLDHIGVMF LHIDRNELQG EFDSYFDARR GQPGATKGPN SGTAFLEFRV YMAVAIGMLL
SPEPGSELLA TGLHAAATER FTVIIEQGDC VKTLHCLWSL ALYSMFSSLG GSTWHLVGLA
MKKCISFRLH RELYPDSDTS QEELNSRRSI FWALYVIDRT ISCVMDRPFS IEDEDILVQL
PVYSSTSKTI AEFDFGCHII MHARLMSSVR SSSSRGRLYH YRNLSYWRDS PKSVKDFAPG
DSVLSVSIKQ LTCRALTQIA LLTRGTLSNG GIVGDARAVE HDVVDGCQAY INDAYYYSEQ
GKYAASFVDG FDLFAAGVLV ICLPSLSALA GPPRETAIIS KCTALLTTIG ERFQSLKVLR
KLLLALSSVA AQGAYHDPAL DELPEIISDP MQGLIQDFLR YIEIMAPGIT EPSSSAGPST
TGFKPTVYVL DTFPPKAIEY AKTLFNIIQP QDEEFKNWRQ NARALLVRSS HVTADDIASC
PNLIAIGKHG VGIDKINQDA CAQRDIKILN TPGANARDVA ELVVALALSV ARGIRSITSR
QMLKPVPKET CNGLTLYQKT IGLIGMGNIG RTVAEIFRGG FDANIVAYDA YMPKDVWSHI
PHTRAKSVDE VLSQADVLSI HVPLTTETRD MVSYQQIRAM KPDAILINAA RGGIVNEADL
TKALSEGYLW GAGLDCHEQE PPSHEKYEAL WKNLNVISTP HIGAATSRAQ LAIKYILYLG
LFHISRSWNS PTVPPHTLHI AFETICDKQC FPIRATKGTV RQILSTAWRC YNPGLGDTVR
IHDKHRTEAG MADEYIPLFV HGKSVGTCTS KGLEEETDFG GRPIVDVVGG GDDQVVRAFE
PLEVAPID
//
