ID A0A094JMW2_9PEZI Unreviewed; 1523 AA.
AC A0A094JMW2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
GN ORFNames=V502_08168 {ECO:0000313|EMBL:KFZ10368.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ10368.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ10368.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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:KFZ10368.1}.
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DR EMBL; JPKE01002858; KFZ10368.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094JMW2; -.
DR HOGENOM; CLU_002148_0_0_1; -.
DR OrthoDB; 1786197at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd15482; Sialidase_non-viral; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF00734; CBM_1; 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; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1523
FT /note="Zn(2)-C6 fungal-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001899529"
FT DOMAIN 832..861
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 723..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 163375 MW; D506EFB8EA100424 CRC64;
MRLLVPFSAL VSTVFAAYKW DSVKIGGGGG FTPGIVFSPK TKGLAYARTD IGGLYRLNSD
DSWTALLDIA NDATWNYWGV SAVAADPVDA NTVYISVGTY TNSWDPNNGA ILKSTDKGST
WVKTALPFKL GGNQPGRGMG ERLAVDPNNN KIVYFGAPSG NGLYKSTDSG ASFSKVSSFT
AVGTFREDPT DTSGYQSDIV GVTSVVFDTT SATLNGATST IYVATADVTA SVYVSTDAGA
TWKAVAGQPT GRFPHRVKLS VSEKLLYFTY SNVAGPYDAG DGTVYKYSLS TGAWTNITPA
WQATNSLVFG YGGLALDANN PGTLIVASDN LWWPDAQLFR STDAGASWVT IWDWNANHYT
YDTEKAPWIN ASRTDEKALG WMIASLEIDP FDSDHWLYGT GLSIFGGHDL TKWPAVHVES
LADGFEETSI QSLICPPGGA PLLSGVGDIC GFRHDSITES PAINFINPYY PTTPDLDFAG
QKPLSIVRIG NDGSTAVSQM ALSTDGGKTW NPATVSSTSL CCGKVAYSAD ASSILWATPS
GSYVFVNGVQ SAVGTLPTGS LRIASDKVNA KYFYAADGNS FYVSKDGGLT FAVSVALSNN
GANSIKVHPT VAGDVWFSTS SGMYHSTDFG ASFTKIASVS ASYAIALGKG TGSYPNLYAF
LTTTTSGSNI LALSTDKGVT WTQINDAQHG FGAASANCLA ASWDTVGEVF VGTNGRGIFY
GLPSGGSTPT TTANPTSTAT SKSTTSTTST TSKPVTTTTN PTTTKTSAST TSTPTQVGGT
IPKYGQCGGQ NWTGSGTCIA GTVCQQFPVT MSAVPASGGA SGGTNREPSH LSCERCRRRK
VKCDRTRPCN QCKKAGAECI NAGGEKKRPI SRLYVEALEG QIASLELFIM NLTAASSSER
DVMLANFKET SMEHLPPLPA LAKEIPLAPP LPKGRLMRLK EGSADQFYGE TSFFQINPSE
TDDAEAGFSI MAATPPVQVK PDPQSSPESP LAISPEGNIV EHSFSTPWTP MCQKLMGVFF
DQQYYFHMCM YREYFLRDYK AGGGPYYSDL LLYAICAMGA LASPDETVRD LSAVFSNRAQ
ELLYGSALDS PDLTTLQALL LLGHRDIGRG KSSRGWVFTG MAFRLAQGMG LHLDPSHWNT
PRDTDVEREI SRRAYWAAFI ADKQLSLYFG RPPALYPSES DVHKSNRLIY PPDWDSLLDD
YIKNNTTPTE YEDDLSFVGS FVQQAELCKI VHRMITEVFQ NHNAKADPSI LAASAKGIHV
ALSKWLADLP ARLHWNQWSR GPVAAYILNL HMFFHTVMII LHRPPRHSSL AHLATVTEDL
DICSSSLNSI LQLMKVYSKH YSYSALPVTF IHTCASAASI VLLKRFLSAS PQGVPRNKRD
VQETGTQLEQ ISKVIDSIAE TWDSAKQIQK AISSARETIR LEDEATVGGL VELGTGVDVA
QGVAALGWDE SMRFDWDDPS LQMGPMSVGG DGVKWEEFSG AGMAGEFSEG LGDYVQDYEA
LFGLLGEGGQ PEINFGDLED GLI
//
