ID G4YWW5_PHYSP Unreviewed; 1778 AA.
AC G4YWW5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN ORFNames=PHYSODRAFT_344723 {ECO:0000313|EMBL:EGZ24463.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ24463.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ24463.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ24463.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR EMBL; JH159152; EGZ24463.1; -; Genomic_DNA.
DR RefSeq; XP_009519751.1; XM_009521456.1.
DR STRING; 1094619.G4YWW5; -.
DR EnsemblProtists; EGZ24463; EGZ24463; PHYSODRAFT_344723.
DR GeneID; 20648660; -.
DR KEGG; psoj:PHYSODRAFT_344723; -.
DR InParanoid; G4YWW5; -.
DR OMA; MASGKMM; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
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; IPR048615; KDM5_C-hel.
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; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640};
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 382..432
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 588..754
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1447..1516
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 177..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1763
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1778 AA; 200775 MW; 8C2DC3577ED4B9DC CRC64;
MDWDPNATDT DGYICPPCPV FYPTAEEFQQ PLKYISSIRH IGMQAGICKI VPPKGWRPPF
AINEKTFRFR TRVQQLNCIE GHSRAEGQFV EALRLFLYQR GEPMKELPRA DGQLVNLHLL
YKTVVALGGF EAVCASDRWE QVVRRVGRTK AASEPSEELC QTYKTHYQTM LLAYEKQQQG
KQENNNNNSS SSDTTEAKVK VKVEEVHATP SAASASGDTK ATPSSKPHSI SGRKRSAATL
TTREEDDTEE DGRLRVKRTL FSEGEHTSSE ENDAPTKTEK RQNDQTRKVR TRDLEPEALK
PSETRNVRLG APEILAGQKF YRFFPDAGAV LAEVKRVFGG KKPHVAVRYL EDGSNDDIEL
STMEILIANG WDANAAELAY NSEICQVCLR GDCWDKMLLC DGCNSGQHLF CLDNPLKEVP
TGDWYCKECV EDAMDPDKKK DNPKFGFDMG AEISMVDYKE RADAWKRGYF SLSSDTNPDE
AISDRDLEKE YWRLLSIPMH EQRLEVQYGS DVDTGANGSG FPRLDLYMKN LRTVSKRWKN
LTTKAKSEYM LQLSKFFSHG LREGLASAAG GENVNADAAK SLEELVQRYA QDDWNLNNMP
KLPGSVLQHL DEDIKGVMVP WLYAGMCFST FCWHVEDHNF YSTSYLHCGA PKTWYGIPCA
SAEHFERTMK ELTPELFGSQ PDLHMQLVTM FSPKTLREHG VPVYRATHRP NEFIVTFPSA
YHAGFNNGFN CAEAVNFATV DWLPWGAKSL RKYREFRKLP VFCHEALVCT LAETLVDGSS
FDFEHTESSL LPAVEQLLHD YREFEQRVND SDSKTRVVKR ELMVEFEKHQ YRVVSAGVAD
PEASSTTLMR RSMVARACTR PSKMGTTNPT RGNRGGKMRM KMETADATMR PSRMVLWAGR
SGKNEGLRCV TCKQYCYLQA VVCTRCRPPQ SSNGGPTVGC LEHYPTMCKC GDPENFVYLY
RYEASRLEEM INSLRGRLEG AQAWSRDCDA ALRPLNKVHV TKPTVEDLKR LLSRGKSCDG
ADRGRLDALE LAIADTERWD SHAQRLLGFL RQEDGSVYLN VTQFESLLQS SEKMIVEPAG
LSQIREVVRE WHAAHAAAVD MLRSTIDVQR NEAASKVHLR TSPSDALSVV RSMSAPNVLL
HDNVRHGMLT TSISELGSRL RAMKESSSGG SLLSQLAGAQ RYLEVLCKVN VLSASIVERA
QGRTAMSAPT QEQVHRVLGE VHDLHLVDPN TIANTEALCK LLTITQTEAM EVDAALRDRS
KSTEELEALL RRAKSLPIPP ARVQELEERL EKCRLWEQRA HQILSVVSGS AAAPNFKSMM
ERPSVDQVET FYAQADSHFV PSTSLLRRQV HSRLQDCRRW CDAVHALFLR PSNSHLPLGQ
FLQSALDKVQ QQLSRSVDQA LRAHSRLHCV CQQVLSERAQ LVTCQRCRCY FHPQCVPELL
PQRAKEAFLC ASCRPPQRKR ASHGNAPIFC VCRGPEHAPM ICCDFCDEWY HSTCVDLSPR
ELDGIEAFRC PRCSRRQNLY YLDKKLLRRE CLGRRPALAR VENVLAQMQA QLVACPPGAH
ELMAYVHAVK GVENHANNFV RDFALRPFSP AAYSTLDYVR TQEAAVVQLM ERVTSLEVGL
ETAQLQLGAV HWCLRACQLV LGPNSHAPRY AYLAALLQDV KSQEPGFVFP REEYRMMQLT
IAERVSKAAQ WMRAAKTLEV EEWNVEKARR LQREAEELSA YLELPAAELQ LVQNIVVGRM
HQAVGAVAVE EEEEEEEATY DEEPDSPSAV AWKKQARW
//
