ID A0A100IEA9_ASPNG Unreviewed; 1179 AA.
AC A0A100IEA9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=PHD finger domain protein {ECO:0000313|EMBL:GAQ39662.1};
GN ORFNames=ABL_03253 {ECO:0000313|EMBL:GAQ39662.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ39662.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ39662.1}.
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DR EMBL; BCMY01000004; GAQ39662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IEA9; -.
DR PaxDb; 5061-CADANGAP00005461; -.
DR VEuPathDB; FungiDB:An07g03000; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1104909; -.
DR VEuPathDB; FungiDB:ATCC64974_45310; -.
DR VEuPathDB; FungiDB:M747DRAFT_373384; -.
DR OMA; NTSKWSH; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 420..470
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 474..592
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 131846 MW; F95B56A0A4F243F9 CRC64;
MAPLSWPKSH RSPSRPSRSQ TRVTLKPPSS SDSSVTNEGP PLKKRKYVPG GPGGGGRYIE
LEVKDTPKPK PSPAVRRNSS NSRGRNGPVP LPESAPQPQP VQLPPPPPPP PVPTTPPSAR
LRREKSQNRG RFGSSTAAAL ALQQGDGYKP REERGWEEFH PDLDIDAKFA VFDAEEVDRP
PPTSSIAHIL SPNGLDKTNE KDPIAELIRA HTNGSSPTPI KRRPGRPPRR PEAILNALGI
THQQKNVPPP GPNPRERLTL PKPSFRIRDP FTFYDQPGVG QQNYVDRTMA SVGYQESDLF
LRHDRRLIRM TEGAQEDDLD PANPVTSEGE VNAAVGRVEY DMDEQDEKWL EEYNAKRRED
QLEPIKPAVF EITMTKIEKE WHVLEKRIPK PNPKPPQTQR PRSSSAAAVN GETAPGEEQD
SKCAICDDGD CENSNAIVFC DGCDLAVHQE CYGVPFIPEG QWLCRKCQLI GRGSVNCIFC
PNTEGAFKQT TSSKWSHLLC AIWIPEVSIG NPSLMEPITD VEKVPRSRWK LHCYICRQRM
GASIQCSNKN CFVAFHVTCA RRAQLYLKMK SGHGTPAVMD SHLLKAFCDK HVPPEWRREH
GTDVATAEAI EYYRTTMQGR RWGDSQAAAL SLEPTHPLGC DHGDEDGHRM HTPRITLTVG
GNKRKRPTVP KTIWKLPSGA PVIPQVVLNS VVASLQRFGV RQRKQYAEDA CKYWTLKREA
RRGAALLKRL QLQLETFSSM EMTRRDYVAM GVPGSKRLQR RIEFGERLYH DLDRLRMLCD
EVKNREREKL KDVETLKSIV DTVYFPIFPL LWPIFEKAQV LDGKGIFRQG LASIRTKLQE
RFYPSVATFS ADLAHVFTTE IGVQPAGDTA ELQMQISGRA PELSLEQREK RKLAKRIIKA
IQPSLEDAIR KESELNRKPF EQELKELDLM LENSVMSRRG SEVDAPETVN DEQASAVPNG
TEQKVEEMDV LAKSEPEDSA GVADVPGNTA TTAEPSAAES QPAEASTEPQ VQQDTNMEDA
PADMQDTEPQ SADVAPTVVQ PTIENQPSVP DQNGNLEKES VEPSKPPVET QNGPLTPPPS
FKGDQQYPLA QGGIQWYMQP FDPIGTTIHE ERWTGRDVMR GMSEELSELD EEELKDLVED
EELEGQMVNG SNEAANGGDA PTQQSVKVHR TRRRWRGFR
//
