ID A0A0W8DVL6_PHYNI Unreviewed; 842 AA.
AC A0A0W8DVL6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=[histone H3]-dimethyl-L-lysine(36) demethylase {ECO:0000256|ARBA:ARBA00013246};
DE EC=1.14.11.27 {ECO:0000256|ARBA:ARBA00013246};
GN ORFNames=AM587_10002864 {ECO:0000313|EMBL:KUG00289.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG00289.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUG00289.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000256|ARBA:ARBA00001574};
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 -!- 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:KUG00289.1}.
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DR EMBL; LNFO01000724; KUG00289.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8DVL6; -.
DR EnsemblProtists; KUG00289; KUG00289; AM587_10002864.
DR OMA; SCHRCGN; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23123:SF21; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 1; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF00628; PHD; 1.
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.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KUG00289.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000313|EMBL:KUG00289.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 112..166
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 763..808
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 651..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 91282 MW; 287562E2740FA56D CRC64;
MALLWQFAIT SAKYTHPPVT IAAANAGAGQ GDETYCHLYS ECHHRLAVVI GACNTPIAVS
GPSPLYSSTD SPPLTAPLWV NSKLQFAAHS AICQLARTSV KMLPPPSAQH NAMLCVVCGQ
DVDPRAPAFL IECHFCGRWL HGTCVQVSEQ DALLVAKFAC TKCQQHGHEG VKYQPVNNDP
FDADAVTFSP LPVHLGGYAS SSSPVQLRHK KSSPSFRRVL GAAIYARSGV HLVPCQDFQP
SFLQRNALEE PVLIAANSHR AAGLDVPFPV LDATSTADLL TSNRVVRTID VATQTRQQLT
ASAWQTKANQ ENTAQLANAE FQLQQTPMQM KVAAPLAVTQ VDWSGLVVSN NENSSGNAVN
TNVFGAFLAS NAYLDFAIAP GGQCTWLSVS SGELWVYLIP PTSNNFEAYR DWKNDPDFAT
AFLAERVDKC IKCVVSTGST LLVPAGWMFA RFAGGVQSCS LFHGFFACTS AMDAQLSVVL
LEMQHDALAQ YWSETTAGWL SVDANVQLWT AVCYYVRQLL MINNGMNAQV SDLDRRALQR
ALPRLREWSA LPASLKSVSG ITWTPSSQRE AQAIVGRLEQ ALAATCLPTH SLDDLQPTSG
LGNDSKLPPI SPNEATYIYS AASVPDSMSG SPWVATSTGF DSTNAPMGTM WSNFDPTHHH
HQQDHLVIST QNQPYSNSDP SFQQHSPNQN LPGYGSSDYG YLPGMAGSER YIEAGSHDLG
LEGLSSIAAS GQLGAPMATS FQQPRVDSNG NYVDMLMRXR ASCHRCGNLR KKNVRCPVCP
HIFCAKCAEK MVEEHGEHIF EGGCPVCKEL CCCGKNRTTR CTRKFHCYKK CPSTKRPASG
SN
//
