ID W2MCN7_PHYPR Unreviewed; 1856 AA.
AC W2MCN7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=L914_18740 {ECO:0000313|EMBL:ETM34101.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM34101.1};
RN [1] {ECO:0000313|EMBL:ETM34101.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM34101.1};
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 IAC_01/95.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI695835; ETM34101.1; -; Genomic_DNA.
DR EnsemblProtists; ETM34101; ETM34101; L914_18740.
DR VEuPathDB; FungiDB:PPTG_05573; -.
DR Proteomes; UP000054532; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15560; PHD2_3_BPTF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013637; Lys_sp_deMease-like_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; PTHR46723; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR46723:SF1; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1134..1183
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 679..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1237..1264
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 687..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1814
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1856 AA; 203173 MW; 4F7F97E6C0A25915 CRC64;
MTLALQHLHR FDYNTTDAAC SLYARHSIEL PKSTTGVNQS VSKPTPAEEA KKWLLAFYRC
MRCTEIDGKM LEQMCELHEK AKASGDVIPA TEAGVLSRLV TRILTWREQC ESVSKEKVDR
ARLLQLLHQA EYMQIVLPEK EAVVSRLQAF DTALTQLKEA LEHSSKRHQS KRVELNELIG
LFEAVMAPQL IFPEESNFRE TVDEVKELKA TIDKMLAEDK VSLPLIRDVL AKIELVPVNF
EQEVEQFQTK MQSAQTWLAK ARKCMPNRRP TRRAGGADPK KMDLETIRAL VDDAPCENSS
EMFEMQDLLE CADVWAVKVK EAIDGGADVT LEQLKELLEE AKDIPVVMDE QKFLEAEIDA
REWCTTAASK LASRTSIEEM EDLLTQAKTI RERIYPKKQS RWKPQVERDI NAAMDQSRKW
INELRDNLGV AAFDKLFASL SSYFPSSHSS RSSSSTASID RSKKKTMDAI SKLVEKSQAL
AIDVSSYTTP LNDLLLKGVE AQAEASAILM SIGCLSGTIA NNLDESSMEI DSMPRELGDL
AQASALLEKI DSFPFTFEEG LSLASIVEGE KEWAARVREC IPPRQSRKKR LANDSFTTEQ
LHELLNESKR LRFLFRDELR ILSKELHDLT AWRAKAQEVI NGEVSVSVAS VVERLQSFDL
MIYEKLQKAK KKLHIGDVSP AAADNESTES RDVDMSSTPF NDESKEVKKE EESEFSAMEV
DAAGSSDYVA PMEVSEQNSK PDSKPEVVSP GDKLTSAEAG VQAEAAADTK PTNANGVAAV
SMPALEIHAD AIMTHVRIES GCMQKSIAKK EEDDPDDSKT SWMAKNGRDL LEPVLAMAEE
SFETVNSLDL KEAEARQTVE ELVLAGEKGD ITENITDESV RVLDGWKQQL LQVQKESDVL
SVEAPEQKVI ALIISLLEWL QGSRSLFYDE ILPLQDLVAK GDNITESLEE IKTLDVVKPV
TLATLERMLW PLSYLKTHEK VVLEWTERVH KCIADKHARV NELQALLDNG SGLLLEQGAF
KIVMDEAKKA RVWLSKLKKR LRALITKGVG RMSMSAARSL VEEGEDIAID MPVFDFLKEH
LEIASDWESR VLASGIESGQ ARVANLLALL NEYECARLVI DLDMHRDVLK SATERYCICR
QPFDGLMIGC DHCDDWFHDS CIGMSKEKAE KVEHYTCPSC TILQELGSML QHAKATEKQS
NMWDMQEYAR AFEKHQASAL RKVKREEKTV ERTDMLLFSC NNQMNQLRAR IDDIERAKAC
LSIKSVAGSG ALGQQQALNQ AQVKPSTVQP SATMSMPEAA PVKAETSTIT NVAAPTSSVG
TNALLLAAAA SASSSSVSTA TSSAAAASTL AGINATALNR PQYPSILIPP MRAVNNILKS
APKVELVTKP VTTTSEGGAA SANGVKSSSD LANSSSTSTT STVPSTVSAS TSSTPQPTAA
VSTTSTTTAA SAMTTTATSK PTSSTAATTP ASTSGVHQVP TPQLLNPMAA TLMGSTERLA
ALVVAGGVEQ QLAKMKSEHV DASKQVLELQ SSLRLSRERL ANAQQSLREL SDVFHARHRM
LPYAQAWVRQ AVTLLNTTAN LSRANIDFST FLPRGFATAL SEMEHPPAPA SSTTAESESV
GIDKLFPGVD MYARLLRTVS WSQVVVSLLQ ERPSRCELSD AIAYALEYGL WEDKKTVAPL
RSLIGRVDAW VSRAHKCITK SASKTQQLSR LKVLMNEYSK LPLTYAKTAE PLDVYVKLLT
GGGVKSKIKD EGEALTTEAA EAAAVKALDE AMVGLSPSVT SAAIASGTSA TKKQAPRKRK
AYTRKDKAPV RSTKKAKKPQ GASAVASSAP SSTNSATKVT AQPTTRAAQA GSSAST
//
