ID A0A3E2HGH8_SCYLI Unreviewed; 1181 AA.
AC A0A3E2HGH8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g4144 {ECO:0000313|EMBL:RFU32161.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU32161.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU32161.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU32161.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU32161.1}.
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DR EMBL; NCSJ02000060; RFU32161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HGH8; -.
DR STRING; 5539.A0A3E2HGH8; -.
DR OMA; ARTHTAC; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) 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; cd19120; AKR_AKR3C2-3; 1.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044494; AKR3C2/3.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR PANTHER; PTHR11732:SF531; NADPH-DEPENDENT ALPHA-KETO AMIDE REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 13..40
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 41..68
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 82..112
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 256..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU32161.1"
FT NON_TER 1181
FT /evidence="ECO:0000313|EMBL:RFU32161.1"
SQ SEQUENCE 1181 AA; 133276 MW; DE1CC9B3B737078A CRC64;
MEQGRKKPSQ ILYTCSDCHR QYQAKETLQR HRKNHSRRAE YVCEICAATF FRRDLLLRHF
RIHEADNVSE GLFRDRQRSR RACDRCARLK VKCSSISLPC SNCRQHNSVC TFSGHSHQAL
NRKASQATNQ PTEIPKLAEA SDQGEATTKV LEGADIQLGL ESPRLQLDDH NLSSIDEIDM
YARGSHNLPE LGSSSLVAMW TPELAWPWLH EDLFLQADPI AGAEFMEAED FNITAYSSEP
TAVVQENFLE SQILGTSDAQ PSRECNRNES HHHNAPSSPT GLDIRPLEGN NPSSLESNPR
TTVEHEVLST GTLQQKEATP PGNGGLISRK RARNATANET TKSHPTKIQL QQEVVSKLVE
FACNFSSTTP DPTTFKKFRY NICDEIKHAF GLDQQDTVPS SGNDLLDHFV ALYLQHFYPL
WPLFRKQDLV FDRISPILYI TLTAIGSIYA GDEAAAYGFA THESIRQKII VAPLQSQLPE
EIYVPLCQSL LLIQASALYF GRRQAFSVAQ QLGSIIVAHA RKMNLFNDGF CVFPTPEESI
SRSHEEVLSD WIRAETRKRL AFGILRAEAF ISHLLNSRAL ISYEEFNITL PCSSDIWENR
EEDLPDLLPG EFELLLFGLQ HSVWQFSHDR DIMPRLIQNF RSDFLTNPQN DMFSSWSYSV
QSWDPSQVAR DPLTASDIGE SDNTDLLDYS SRRMRDLHAD YYRCLAALRK WKRSFSAACI
RTDILGIRNS LLASRLLYHL SFIRLNADVQ KFHLLNHQFV KSPVAPELVS SVYEWASSHD
AKVALEHSCA VWSLISRELK REWHLRAGFN ILTHITLYHA ASVVWVYAGT HPLPDGAALD
MIEPPSKSSN VDLLIRSSNL SKLMSEFSLR VAAENLSSHI NSTAMAQPNL SIPSRKLSDS
VSIPVISYGT GTAWFKKSGI EDVDRKLIES IKTAVSLGYS HLDCAEAYNT EVELGIAIRE
SGVARENLFI TTKVQNGIDD IPSALSRSLE KLGLDYVDLY LIHTPYFAQS DATKLQHAWK
EMEAMQRSGK AKQIGVSNFL KGHIESILEI ATIPPALNQI ELHPYLPRHE FVAYLHSKNI
VISAFGTQTP IIRTKGGPLD DFLSTLGAKY SVGPGEILLR WSIDQNFIPI TTSSQESRLR
DYLKVLTFQL TPEEITEISR IGDGKHYRAF WTKQFQESDR S
//
