ID A0A084QP05_STAC4 Unreviewed; 919 AA.
AC A0A084QP05;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN ORFNames=S40285_04805 {ECO:0000313|EMBL:KFA65690.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA65690.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA65690.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA65690.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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DR EMBL; KL660569; KFA65690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QP05; -.
DR STRING; 1283841.A0A084QP05; -.
DR HOGENOM; CLU_007784_0_0_1; -.
DR InParanoid; A0A084QP05; -.
DR OMA; PHFNPSW; -.
DR OrthoDB; 2322629at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR40626; MIP31509P; 1.
DR PANTHER; PTHR40626:SF25; TRANSCRIPTION FACTOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02070)-RELATED; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 33..60
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 61..91
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 102039 MW; DDFEB69D36308FE1 CRC64;
MLPMQALDGA TAHSVGPLTA DPGEIRQPKP KTLPCKYCSK RFRRVEHVQR HERTHTKEKP
FSCNWDHCGK TFGRRDLLVR HEKLVHLNEG SKENNRPRKL STGAAIHKPS LSEGSVVEDT
IGIRRVTAQP PQSIHQPPPP PPPQYHHSSI NHGPAVPLSQ DPRVPPRGAA CNLDLLSDAA
LASEVNPMQP MMNEMPPQPP SHPTVKGYSD PVGGYSERPR EEAQVMPSGF APQTHSAFED
YNLFLDDFAS PPHFLPPHFE PDQQMNLWSR TPAGLPPRAS SKHQSQFPSR FGSLAPDPRD
SADAGSRLQD DLSRASSLRI SMNDHAVLKN RLEEFSSVLP NDFVFPSRHT LMRFLEGYIN
GFHEHLPFLH LPTLSPVEVA PELLLAMLAV GAQYRFESNR GYALWYAAKA VAMEQIRRRH
SSEVHALLPT AAAYSPHSTR PSPSTTYRHS FASAQSERPV TQDTHREPYV ASALNTPQAR
LETIQGVLLL FAVGLWGAKT ILHDALCLQS NLAMLIREEG LSVETSQNSL TDWDAWIRHE
GATRTKLIAF CFFNFCSTAY NMPPLLLTSE LNLYLPLRSR LWRAESAWQW QDLRQSTPVA
EITVHEAFSR LFGRTNQGLP TQVSSLGNYV LIHALIQHIY LLKQTSLAAG APYDVHRTLK
PDDVDEVTQA LRVWQTSFEH RHQLRTAESG HFTGADSVPG GALAYNATAL LRLAYIRLYT
DIPPSRSLET RDSMLISSAL SSTPLLLRSL RLHRAVFQAI HALSMLVKAG VNYVARTKSS
EWSIQHSLCN FECAILLAKW LLTLASISPS DPPASPEEKN LLEMVRRMLD ETEFAVPVDP
SLAGPSSGSG QMEMGTSDSA KLRQLAGAVV KLWAETFKGS HMFDIVKVMG ASLDGYAELV
QKPRDRSSLG RLAPEAGMG
//