ID A0A2S6C3A4_9PEZI Unreviewed; 762 AA.
AC A0A2S6C3A4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=CBER1_01128 {ECO:0000313|EMBL:PPJ54193.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54193.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ54193.1}.
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DR EMBL; PNEN01000570; PPJ54193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6C3A4; -.
DR STRING; 357750.A0A2S6C3A4; -.
DR OrthoDB; 124870at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR037869; Spp1/CFP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46174; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 363..414
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 81787 MW; 1D11F6A4BFEA67E1 CRC64;
MASLASLLNP ENRPLSPVQP TLAHDPARPS TQASTTAHEA AQALASLSTS PPPTQWSGSS
MQDGASLERK RSWERRASAQ LPVPGDLTRK PTSPTLEQFH AASRSPDHRR LSAASPQPSN
IVLPPIQDFA PPKTAATDPL QRQPHSPPAS GALMAASEDQ SASPGAPNDA HSSATVESPS
TNNSAAVPSI MSRPQGTSSA AMDSTSTFQS TSPDDTRPGL EIDSHAQKAV TTLKYEHTQQ
HAKSPLRESS IPVPSTEDPT KDEAAAAAAS RKRPAPTKKK GTASTVKKEK APPAKKRKLE
TKRADTPSSR ASKSAAGKVA SAKGTPINSS PAPSTRSYSV DPQEELDDDD DDVDDEGRSQ
DGDLYCICRK PDSGEFMIGC DGTCDDWFHG KCVGVAERDK NLIDKYICPA CTKAGVGQTT
WKRICRRSDC RRPAKAGKTK SGSHSSKYCS EECGVLYFRE MAGKSRGAGD SASRRAARRK
GSLDTSDRHD EDLGARGGAL AAGEVKALLN ASNTVDEFRK LGDGVLSPPA TPEADEAKDA
PQYTESEARD LARIESEKEH ARQRHALLKD RMKFVTLAKQ AASRVATEKE LKPKEYCGYD
PRIEWSEDQF QEWRSSKAGQ QAFDTDLLVT GQGPDGDDMV DEELSVPEIC DRKKCARHME
WAKLAVDDLR FETSDNGDRM RSLDREEHDI KDRVARRTKS GGGNNGGTVE VHASGPAEKP
VENGAAVDAD HKSAGDLEAV VETSTEVVPT VEAGDQMDID VS
//
