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Database: UniProt
Entry: A0A395IGM9_9HELO
LinkDB: A0A395IGM9_9HELO
Original site: A0A395IGM9_9HELO 
ID   A0A395IGM9_9HELO        Unreviewed;       559 AA.
AC   A0A395IGM9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DID88_006926 {ECO:0000313|EMBL:RAL59321.1};
OS   Monilinia fructigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Monilinia.
OX   NCBI_TaxID=38457 {ECO:0000313|EMBL:RAL59321.1, ECO:0000313|Proteomes:UP000249056};
RN   [1] {ECO:0000313|EMBL:RAL59321.1, ECO:0000313|Proteomes:UP000249056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mfrg269 {ECO:0000313|EMBL:RAL59321.1,
RC   ECO:0000313|Proteomes:UP000249056};
RA   Landi L., De Miccolis Angelini R.M., Pollastro S., Abate D., Faretra F.,
RA   Romanazzi G.;
RT   "Genome Sequence of the Brown Rot Fungal Pathogen Monilinia fructigena.";
RL   Submitted (JUN-2018) 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:RAL59321.1}.
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DR   EMBL; QKRW01000055; RAL59321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395IGM9; -.
DR   Proteomes; UP000249056; 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   Reference proteome {ECO:0000313|Proteomes:UP000249056};
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          277..327
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          331..450
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62018 MW;  E355119B01D6D46B CRC64;
     MATPSRFGSS SQAAAAVAQN DGYKPREERG WEEFHPDLDI NQEMMCFSQE AVEGISSSRP
     PTPAGASQTA DGITNGTPGQ ATTNGENGTR GGKRRPGRPP KNPEAFYAAR AAANLGITLN
     VGTPKTPKTP KNMHVANTNA KEKLTLPQPS FRLTNTLKKF DTPEFDQYVD KSMANVGYQE
     SDEFIRPEQD TLGRVEYDMD EADDKWLQQY NEKRKSEGVD EVPRHIFEVT LTKIEKDWHN
     LERTIPKPNP KPPQTHRPRS SSAAAVNGEA PTGEEQDSKC AICDDGDCEN TNAIVFCDGC
     DLAVHQECYG VPFIPEGQWM CRKCQLIGRS TPTCIFCPNT DGAFKQTNAS KWSHLLCAMW
     IPEVSLGNTT FMEPVMEVEK VPKSRWKLNC YICNQNMGAC VQCGNKACFT AFHVTCARRA
     RLFLKMKNNH GTLAVLDGHA VLKAFCDKHS PQDHSRENDT VLATAEARRF YKKTMRGRVW
     ADSNEAAGML AAAHRRAGRY PEATDLNGGR GPFMQYNQDI QSEEPIKGLW KLPSGAPIIP
     KVIFNSVEAS LQRYKSSQA
//
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