ID E4ZGP5_LEPMJ Unreviewed; 1441 AA.
AC E4ZGP5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN ORFNames=LEMA_P065910.1 {ECO:0000313|EMBL:CBX90465.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBX90465.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR EMBL; FP929064; CBX90465.1; -; Genomic_DNA.
DR RefSeq; XP_003833830.1; XM_003833782.1.
DR STRING; 985895.E4ZGP5; -.
DR EnsemblFungi; CBX90465; CBX90465; LEMA_P065910.1.
DR GeneID; 13291945; -.
DR eggNOG; KOG0955; Eukaryota.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_4_3_1; -.
DR InParanoid; E4ZGP5; -.
DR OMA; PWGGFTN; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 68..109
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 349..512
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 606..729
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1441 AA; 159713 MW; 9898567CB1DBF81B CRC64;
MDAPPDIVPS VEEASVAHHH VPAAVALTPP TSEENDKREE RMSSELTDID SDDGEDIEPD
HYFEGGKIPV FKPTMDQFRN FKRFIDKIDK HGMKSGIVKV IPPKEWRDSL PDLSEAVKSI
KVKNPITQEF AGQHGIYTQA NIEKQRSYNL PEWRAVTDEA HHQPPAKRGE RRKAAAEAPS
RTRSTRAQAA PTNADEGSPA PRRGPGRPPR RRQVKKEQAD DDEEEEEEDA SMDVPPTPTS
PGREEKKTTT TRTRTKKEPK QEATPSRTRG RQPKAGVDQK KSVSSRRLNN RGAVADSIDE
AAFGGFDYHL PGLEEFSVER CKELEDNYWK TINYGSPMYG ADMPGSLFDD RTTCWNVAKL
PNLLDVLGTK VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYIHFGAPKQ WYSISQEDAR
RFEAAMKSIW PNDAKHCSQF LRHKTYLISP QRLERDFGIK VNRLVHYEGE FVITYPYGYH
SGYNIGYNCA ESVNFANESW LSYGRIAKKC NCESDSVWVD VNEIERKLRG EPTPEYYEET
DDDDDEEDGA DHLPSPPPSV VGKAKSKSGR KAANNKRKRT KEESKEAPRS KKLKRIRIRI
RIPGRGMPCI LCPNDVEYDD LLPTDNGMKA HRICADYTPE TFIVNKAEGE MVCNVANIGK
DRLELKCNYC RSKRGAVFQC SQKKCTRAFH ATCAVAAGVQ VDLGPMPTFD EEGTEYFYDG
YDFRCRFHRP KKRNNKTVDV DALEKDKFIM AYGKTLKPKD VIQFQYVGGE MYQIYGAQVV
ENRPGEQAVL VDVLPDGDRV EVEWKYILKL HPDESQRPKP SANAKPLPEH LKESDASLDI
TNRTDGVPEM GDPFHDPNSE QKWAEWHTAP EVAQRIAKVD LSKENQLWYY LGKSSTEAKP
QYTENLAKQR NNPKSNFLDT VKPPPPPVPT FHRTAYPATY PLKPAPITVP PRTPVQQQLQ
PSRPYQYRPK EPAMNSWKSP VYNPDTRKNP NSPVAHQPNV SYDHRPPLSP YGQGVFQGYH
SHRPPQSSQQ QQPQPQQYQY HPYVPQQSCS PSNWKAQAAT IDPNLQNGVG QYAHSSQHNK
PLPPYPYSQG LSPSPYSHGP GPQSSASTYS HPTQGTGHGR SSMTNMLSNP SGPPKPPKYA
IIPSTSSIIY AAQSPTEYLA YVMNYPYLRN AYLRRTKTYI SPYSLDGGIA SEWMPKQIQV
PAPNTPGVGI GIKPPGGGGT TMATQQGYYH PHHGPPQTTS SMASVGVSTG ASSGPPAPRP
APQFQSPDAF QREMARSTQP AEAPKWEQML KQLATSAGPG PGLVPTASPS DPSSSSSPSS
APQPKYPPSG PRSGLTYELP RSLSHASVSV GTPTPETTPR EMQRPTPSPI SDDGKSDAAA
AAAVAGSNSA TDATDGADGA PAPASALTQT TAAPIVPAAA GALAPLQQGP HVHGAETWRY
S
//
