ID W2I573_PHYPR Unreviewed; 1710 AA.
AC W2I573;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=[Histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=L916_17510 {ECO:0000313|EMBL:ETL29275.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL29275.1};
RN [1] {ECO:0000313|EMBL:ETL29275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL29275.1};
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 CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; KI675504; ETL29275.1; -; Genomic_DNA.
DR EnsemblProtists; ETL29275; ETL29275; L916_17510.
DR VEuPathDB; FungiDB:PPTG_16707; -.
DR Proteomes; UP000053864; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 2.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 18..59
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 83..179
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 357..407
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 563..729
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1404..1471
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 183..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 193832 MW; 4B08596FF616D498 CRC64;
MDWDPTNNDT DGYICPPCPV FYPTAEEFQH PLKYISSIRH IGMQAGICKI VPPSGWRPPF
AINEKTFRFR TRVQQLNCIE GHSRAEGQFV EALRLFLYQR GQPMKELPRA DGQLVNLHLL
YKTVVSLGGF DAVCSSSRWE QVVRRVGRTK AASEPSPDLC GLYKTHYETT LLAYEQEQQA
KSSGSTVEAK IQATPSTTNA SGDTKATPSS KPRTLSGRKR PAFIKHEETE EERRVKRTLF
SDGEHTSSDE NDTPKSEIRP KEKTTQHNLE PEALKPLETR KMRLGAPEIR AGQKFYRFFP
DAGAVLAEVK RVFGGKKPHV AVKYLEDGSN DDIELSTMEI LIANGWDARA AELAFNSEIC
QACLRGDCWD RMLLCDGCNS GQHIFCLDNP LDKVPTGDWY CKECVDDAMD PDKRKENPKF
GFDMGAEISM VDYKQRADAW KRDYFSLSSD INPDEAISDR ELEAEYWRLL SIPIHEQRLE
VQYGSDVDTG ANGSAFPRTD LYMKNLRTVN KRWKNLTTKA KSDYVRQLSE FFSHGLRDGL
AVKTEGDNCN VDAAQSLEEL LQRYAQDDWN LNNMPKLPGS VLQYLDEDIK GIMVPWLYAG
MCFSTFCWHV EDHNFYSTSY LHCGAPKTWY GIPSASAEHF ERTMKELTPE LFGSQPDLHM
QLVTMFSPKT LREHGVPVYR ATHRPNEFIV TFPSAYHAGF NNGFNCAEAV NFATLDWLSW
GAKSLIKYRK FRKLPVFCHE ALVCTLAETL ADSDSIDFEN TRSSLLPAVE QLLRDYQEFQ
RRVDSSEMRV EKRERMAEYE KHGAVIAADP EASSTSSMRR SMVARACNKP SKIGGNRGSK
MRMKMETSET SMRPTRMVLW AGRSGKHEGL RCVTCKQYCY LQAVVCTRCR PPQGSNGGPT
VGCLEHYPTM CKCRDPANFL YLYRFEASRL EEMITSLRRR LDSVQDWNEE CDTVMQAFRE
CSSQYKPTIV DLKHLLSRGK ASGGADRRRL DSLEFRIQNA ENWNSRADRL LLSVKQSRTA
QSLVDFESLL MEADKLLVKP SAMDKLRDVV TEWRAVRAEA VKLLNTVQRI VNDEIRNNSR
PRSSSADTSL VVQSMGAPNV LLHDNVHFGR LCTAIKTVSD RLRAKKESSA DGSFLSQLAR
GQRYLEVLCK VNVLAATIVD RTQGGTVMGT PTQGQVERVL GEVQGLRLSN PNSIANAGAL
QQLVAATEAV ATEIEQALRD DSKSSEELEV LLRRAVAVPI PPLNTQSLKD RLEKCRVWER
KAHQILAVAG SSYKALIERP SVEDVERFYA QADAHFVSSS SILRRQVHSR LQDCRRWYDA
VHALFLRPSN SHLSLSQFLQ TALDKVQHQH SQNASQALQV HSRLHCVCQQ VLNERAQVVS
CQQCQQYFHP QCVPELMPQR SKDAFVCASC RPRKRTSSPE APIFCLCRGV EQAPMICCDF
CDEWYHASCV DLSPLGLDNI DAFRCPRCAR RQNLYYMDKK LLRRECLGRR PALSRVESFL
VQMQTQLIAC PPGAHELIAY IHAVKTVQSD VTAFVRTFAS REFSAAAYAT EQYVQRQEGA
VIRLMERVTN LEVGLETSQV QLGAVHWCLR ACQLVLGPSD RAPRYAHLVA LLQDVKSQEP
GFAFPRQEYR LMQLTIAERV NKAAQWLRAA KSLEVEEWNV EKAQRLLRIA EELSAYLQLP
PTELQLVQRI IDGGVASGEG HVAWKKQRHW
//