GenomeNet

Database: UniProt
Entry: V9EGY5_PHYPR
LinkDB: V9EGY5_PHYPR
Original site: V9EGY5_PHYPR 
ID   V9EGY5_PHYPR            Unreviewed;       893 AA.
AC   V9EGY5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   13-SEP-2023, entry version 46.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F443_15815 {ECO:0000313|EMBL:ETI38409.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI38409.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI38409.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI38409.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) 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:ETI38409.1}.
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DR   EMBL; ANIZ01002767; ETI38409.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9EGY5; -.
DR   EnsemblProtists; ETI38409; ETI38409; F443_15815.
DR   eggNOG; ENOG502RBQ1; Eukaryota.
DR   HOGENOM; CLU_344713_0_0_1; -.
DR   OrthoDB; 55195at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15568; PHD5_NSD; 1.
DR   CDD; cd15543; PHD_RSF1; 1.
DR   CDD; cd20143; PWWP_AtATX3-like; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR000313; PWWP_dom.
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; PTHR24102; PHD FINGER PROTEIN; 1.
DR   PANTHER; PTHR24102:SF28; PHD-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50812; PWWP; 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:UP000018721};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          36..97
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          146..199
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          204..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          796..851
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        241..255
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  100355 MW;  F08A41E8C73835BF CRC64;
     MAKERISSEE LAQRKEEYYE LLATSDSSLQ DVLNQRGGLI LARVGRYQPW PARFSEPGEF
     AKMARYRAKK GQACVYFFGS RNYGWVSKSS IQPFPEDLST LTASNKYNQQ HIQEALDEAK
     LVMDVTDETG KRFFDRIMER REEAVDLPCE RCNRVDDHYS LLILCDGKNC KREYHMNCLS
     PPLVSVPPGE WFCPDCEKER EKEREKELQK RAKAEAMDSQ DSVATTVNGL DSTLPLAKTL
     SSKKTKKHKH ISRDGIVKRR LSSVSPDRPG GPVKKPRGHR SSSREVSPPP RKDSTMPKKL
     DGRKKKPSQL SISSSRAQLL SDPDSGTADD EQRSEEKCLI CGFGGELIVC EFVGCTKVYH
     QFCLGAYPFP KNEDATWHCP RHTCALTGEK ETCEDGEKLT TKLKHPSPRK LSVKNMLWKC
     NQCPLAILDG ALPQLPQGQV LSKKSRTFLC SNCYLNAPSK VQLSKRLEKI WSTIATNRQG
     MPFCGPLLCG VEPVDGQSNE SRTQLDLFKV LARIRRLEYE DSATFSRDID EVVANALDLI
     ANRSYPLMEA AKTLKIIRNE QFGIHQQKLN FLDSKIRRVL ADRESGRDNE DDLAIKRWPL
     RWRQECGPFE DKYYPRLEAK SLDEWTALVS AAPLYASADE FDGRSLVGAY MSDEMSASED
     PPQGHFGSTR SRSPSLGSAN ELSDPPAATR TESGLTLSEG TDVMIALGDL SKPGTGIQKR
     RFGGEQTKEL DSMDAREFFL SPSTSEMQHM FDQQSTLLRS ALEAHSTLQR SWLISQQDML
     GLGGTGGFSV GEGRLAAELR LANKNLRQRL RNKDKLVDQL TSDHMALRAE VINLQRELSQ
     SKSHARELED RIAVVQGALE GRIVPHPENQ DPVTNGDATA TPDRNTDEEH LFE
//
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