ID B2W2M6_PYRTR Unreviewed; 1291 AA.
AC B2W2M6;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=PTRG_03674 {ECO:0000313|EMBL:EDU46512.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU46512.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU46512.1; -; Genomic_DNA.
DR RefSeq; XP_001934007.1; XM_001933972.1.
DR STRING; 426418.B2W2M6; -.
DR EnsemblFungi; EDU46512; EDU46512; PTRG_03674.
DR GeneID; 6341905; -.
DR eggNOG; KOG0955; Eukaryota.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_4_3_1; -.
DR InParanoid; B2W2M6; -.
DR OMA; NQERVNR; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
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:UP000001471};
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 339..502
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 594..717
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 155..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..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 238..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 144823 MW; B5F4E1108657F5F2 CRC64;
MEAPIDVVPS VEAPAATHDD STTKAALTPP TSEDNDKRFE RMSSELSDID SDDGEDIEPD
HYFEGGKIPV FKPTMEQFHN FKRFIDKIDK YGMKSGIVKV IPPPEWRETL PDLTEAVKSI
KVKNPITQEF VGQHGIYTQA NIEKLRSYNL PEWRAVTDEP HHQPPAKRGE RRKAAAEAPS
RTRSTRAQAA PANDEASPAS RRSGRQSRRR QVKKEVEEDD DEDGSIDVPP TPTSPGKEEK
KTSTRRAKKE PRDATPVRSR GRQPKTVDEK KSVSSRRLNN RGAVADHIDE AAFEDFDYRL
PGLEEYTVER CKELEDNYWK TINYGQPMYG ADMPGSLFDE RTTSWNVAKL PNLLDVLGTK
VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYIHFGAPKQ WYSISQEDAR RFEAAMKTIW
PNDAKHCSQF LRHKTYLISP QRLERDFNIK VNRLVHYEGE FVITYPYGYH SGYNIGYNCA
ESVNFANESW LSYGRIAKKC LCESDSVWVD VNEIERKLRG EPTPEYYEET DDEEDEDDGA
DRLPSPPASV VGKAKPRARK PAAKRKRGKE DPKETPRPKK LKRIRIRIRI PGRGMPCILC
PNDVEYDDLL PTDNGMKAHR ICADYTPETY IVSKADVETV CNVANIGKDR LELKCNYCRS
KRGAVFQCSQ KKCTRAFHAT CAVAAGVQVD LGPMPTFDEE GTEYFYDGYD FRCRFHRPKK
RNNKTVDVEA LEKDKYVLAY GKTLKPKDVI QFQYVGGEMY QIYGAQVVEN RPGEQAVLVD
VLPDGDRVEV EWKYILKLHP DESQRPKPSA NAKPLPEHLK ETDASLDITN RTDGVPEMGD
PFHDPNSVQK WAEWYTAPDV VQKMAKVDLA KEDRLWYYLG KPSTEARPQY TEDPAKQRNN
PKSNFLDTVK PPPPPVPTFH RASYPATYPI KPAPIAVPSR TTIQLSDGRP YTYKPKDTVI
TSFRSPVYNP DTRKNPNSPV AHQPNVSYDH RMPAGPYGQQ YHGYHSQRTP QPQPQQFQCH
PYVPPQSYST ASWKAQPATS GPLLSGIDKY AQPSNATLPP YPYGQSPRQV PASPYSPTPG
SSAASPYGPP GRQNQAPNGR TSISSMSSNP TGPPKPPILD GGIAPEWMPK PPVPRASTTP
TAIAPRPIAP SGVTSGYYGP RPAGPPAPRP AAQFQTPDAF QREMARTTQT PEAPKWEQML
KQLATSAAPH APQPRYPLSG PRSSMSYDLP RSMQASPSQT PPGPPPKEPQ RPTPSPISDD
GKEGGEKNPV LPPLQPAPSG VHGAETWRYS S
//
