ID A0A139IWC9_9PEZI Unreviewed; 1166 AA.
AC A0A139IWC9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_8763 {ECO:0000313|EMBL:KXT19051.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT19051.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT19051.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT19051.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT19051.1}.
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DR EMBL; LFZO01000001; KXT19051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IWC9; -.
DR STRING; 113226.A0A139IWC9; -.
DR Proteomes; UP000073492; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
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 423..473
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 477..593
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 890..937
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 69..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 130032 MW; 9D7F5EAACAA2C683 CRC64;
MAAPALSPRR ANRTPRALAS IEPATEPPQK KRRFLPGGPG GGGRYIDEDG NEMTRAEAVA
AGLVSTAPRP RRREPRDPVA SAARQRAPRE KDNHDDNDTP TTTRSAMQTR PRRERPERYA
PPPTTPRPRY SNAAAAAAAS QASDGYKPRE ERAWEEFHPE LDLAAGLSLF SADEVDGRTS
KNDPKIQKLR LNGSNSVNGD VDMKDADAED GLSPARRKPG RPPRRPESML SGLGSPPAPR
IMPLPTHNPK ERLNLPKPSY RQYNHFLQYE DSQKENKVNY VDRTMAGVGY QETDRFDLPP
HVLIRLSENQ HVEDEADVSL RLESDGPAER HQGHPPVGRV EYDMDEQDVA WLEDVNEQRK
AEGVDAIKPA ILEITLTQIE KEYHALEKRI PKPQPRHAQT HRPRSSSQAA VNGDPNPPGD
EPDSKCSICD DGDCENANAI IFCDGCDLAV HQECYGVPFI PEGQWFCRKC KEIGRGTPTC
IFCPNVDGAF KQTSTLRWSH LLCAIWIPEV TIANMTFMEP IQDVDKVPKP RWKLSCYICE
QKMGACIQCG NKTCYRAFHV TCARRAKLFL KMKSQNQGSI DTTSLKAFCD RHVPADWRRT
HDTENAIQEA RRWYKHTMRD RKWADSQATA LELGAPPPPD GGFSAEAPSA EDTIAVTKRR
NKKDPKMHWR LPSGAPVVPA VVYSTVETSL TRFTIRRRKE FVEKACRYWT LKREARRGAA
LLKRLQLQME SFSSMEVTRR NFAGMGSAGG PRLQRRIDFA EMLQKDMGYL KDLTAEVKSR
ELLRLQEIEL LRELVDTVYF PVPPMLWPIL NRAQKLDEKT HAYRPGLDML GQRLRERYYT
SVSDFSRDLT KVFSDAFAAK NGEAAAGADI ETIHTQLNEI RPGTAEHMKL TQEQKDLKRL
AKRIIKAIKE PLEEATKKEA ELRGRELEEE LRKLDAMGIF ATATVNGEED VEATRKRRSG
SDASAIAGAE EQIQTNGDID MPDADADQHT DETVIHLNVA GREDTVPVPN KKNTPASKAA
SYASSVVDQT SEASKKKPTE PLSPPISRSS SAPNGSASGE SSNAEPHDVF AEGGVPWYLQ
PFDPVGTTIH EERYTGREVL RAMSEELSDM DEDALTELAG AEGAPRTKSA CNSGGSVNGP
LASASGFKKA ASTNKKKRPK RSHWSR
//
