ID A0A094CEK6_9PEZI Unreviewed; 1628 AA.
AC A0A094CEK6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Zn(2)-C6 fungal-type domain-containing protein {ECO:0000259|PROSITE:PS50048};
GN ORFNames=V494_00732 {ECO:0000313|EMBL:KFY45845.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY45845.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY45845.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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 multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:KFY45845.1}.
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; JPJW01000225; KFY45845.1; -; Genomic_DNA.
DR STRING; 1420907.A0A094CEK6; -.
DR HOGENOM; CLU_003342_0_0_1; -.
DR OrthoDB; 2720737at2759; -.
DR Proteomes; UP000029288; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion 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:0016491; F:oxidoreductase activity; 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:0006811; P:monoatomic ion transport; IEA:InterPro.
DR CDD; cd13851; CuRO_1_Fet3p; 1.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR CDD; cd13899; CuRO_3_Fet3p; 1.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
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:UP000029288};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1628
FT /note="Zn(2)-C6 fungal-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001899232"
FT REPEAT 704..736
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 738..770
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 772..804
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 805..837
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1012..1043
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 961..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1628 AA; 181252 MW; 8F6D2ED882FD6B77 CRC64;
MFYSWRQLSA LPALLVALPA LVQAATVTYD FNITWVTANP DGQFDRPTIG INGAWPLPII
TANVNDTIIV NVENQLGNQT TTLHFHGLYM NGTTHMDGPM QVSQCGIPDG HKFTYNFTIT
QPGTYWYHSH AKGQYPDGLR APLIIHDPES PYKDEYDEEY VLSVSDWYHD QMQDLIPIFM
NRANPTGAEP VPDSALFNDT QDLKVKMTPG KTYLFRVVNI GAFAGQYIWF EGHNMTIVEV
DGVYTEKAEA ELIYLSAAQR CSFLITAKNE SSTNYAFVGS MDTSLFDAFS PDLDYNVTGW
LTYDEKAAFP PAALLDDFDN EYDDFTLVPY DKQELYTNPD QSIALEVVMD NLDDGANYAF
FNNITYTSPK VPTLYTVLSA GEHATNPAIY GEYSHPFVLA KDEVIEIIIN NNDPGKHPFH
LHGHAFQAVW RADEEEGYFN TTENPTTESE LPATPVRRDT FVVRPNGNIV LRFKADNPGV
WLFHCHIEWH VDSGLIATMV EAPAEMQKSL TIPADHLRVC DASKTPIKGN AAGNTMDLLD
LSGQNQPPNP LPEGFTAKGI IAMTFSVLAA ILGVAVISWY GLADMGAAEM ENERRRITAV
GGGYQLDQDS LYIFFLARMI PPPNSPPLND PSLDEHLSFI VIDKLRLTSS ATVYRATLAR
FTGRNNPDLC PNTSPFMLGC TTWARSDSSN FLEEGADIQA KDSSSLTPLS WAAQKGHKSI
VKLLMEKGAE VDTKDTKYGL TPLSWAALSG HGTVVELLME KGADVVAEDR DFGQTPLFWA
LENGHEAVVK LLLEKGAKVD TKTYSGWTLL LFAKDNGDEA VVKLLMQKGA EVEAEDTEMA
GRRYPGRHGA GAHNGAQPCV SVNGEAGYKG RPEHPIDVIG IQTSDSLETG AKTRGVHQEP
NTFHNSSIRN MKPSVDVVAR SSLSPQSRST YCERWYREIR IQAASDSLEN VSLRTIRPLV
GDSSASASDP SQPTIESTSS DHRLIHYDDK GREPARLPSK RRRVPESITR NACLNCKKGR
AKCDGNKPCS RCTTRAEMTP CVYEIHIKHA KEELMKQIHE LRAKNNLNER VIKALQSGDK
APDILRALSS GDSLESIVQS LGSQPVEEQD HVSPEGSPTS IVGGSEHEPR TQIRSGFAWT
IVTHESTVLD HLFQLYFAWV HPISTLFSEA HFVQSYKGQN SRHCSSQLVN AMCALACHLH
TQSEESELDS DQLGIQFSEA FLTGFDPDDK SITSIQAAAV MFLVELGRGF GLRGSSYLRL
ATESIAELSA SSNEELPCVL KKTVQGIRCL NVEWAQVTFQ FPSVLGFRAV EDTHDEEAYL
DDSPWHFYRY EDDQCPLWPG LLATTSREKM KLIDIIKDVS VIIYSPLSNF ITARHVLEQY
GRFIAWRTAL PPTLGNAETS IQALPHILSL LILYDYSVVQ LLCPLLDLED VSPQLVEVVW
THAEHALLLL ERHYRLHYTC RYQPALQMFA VLNICHVIAR FFPAKPPNDS DIKDGSEAVT
IGLEALQESN IGFPAAGALK ELLRRSAAAC SLRLPRSLDY LITQQRDACP TYSYHDFIDV
CTRPSCHQPL WAVCEKFDSK FAEDWYSQSQ ELGHRLAHPI QQPPRELQGE PDRGVQHLMQ
VWSLLNTN
//
