ID X0B0V6_FUSOX Unreviewed; 1354 AA.
AC X0B0V6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=FOMG_00410 {ECO:0000313|EMBL:EXK46752.1};
OS Fusarium oxysporum f. sp. melonis 26406.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK46752.1};
RN [1] {ECO:0000313|EMBL:EXK46752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK46752.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum melonis.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK46752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK46752.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., 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 "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT 26406.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH659329; EXK46752.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOMG_00410; -.
DR HOGENOM; CLU_001442_4_0_1; -.
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:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 118..159
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 396..559
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 642..765
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 152153 MW; BD4559D20179A28C CRC64;
MSESTSTSID AGIAVAATPH SHDTVVTTPP VDTNTKNPTT AQPGATFLHS PPDSNNTAKS
DGSDSESELS DLEDEPILSD PPQPVSSSDN VNSDDKKEDA DEDIDIGEVL PDSWSGAVPI
FKPTMHQFKD FKRFMEAVDS YGMKSGIIKV IPPQEWKDAL PKLDDLVKQV KVREPIKQDI
MGSNGTYRQV NILHGRSYNL PQWRQLCDQS EHQPPARRGE RRANAEKPKT RTRAATATVA
KPADPSTPKK RGRGRPAKRG GRGKRLKQEQ ADDNEDRPMT PVSPKPEVAE TEDKPVESVE
KDPGEEVEED YEPTVGRMGG LRQARTKTQT VSARRKYSRR EGSAMIDEAA FKDWDYKMDI
SEYTPERCEE LERAYWKTLT YAPPLYGADL MGTLFDESTE QWNLNKLPNL LDVLGEKVPG
VNTAYLYLGM WKATFAWHLE DVDLYSINYL HFGAPKQWYS ISQADARRFE AAMKNIWPTD
AKACDQFLRH KGFLISPQHL KSHYNITVNK CVSYPGEFVV TYPYGYHSGY NLGYNCAEAV
NFALDSWLDI GKIAKKCECA EAQDSVWINV YDIERKLRGE ETEYEETEDD EEDDEDEQGD
MPTPPSGSGV KFRLAGRKRK RAPGEKGGKV KKIRLRLKSK AEPPCCLCPN DTPSADLLLT
DDGRKAHRLC AHYLPETYTE TIDGQETVVN VSEIHKDRFE LKCLYCRSKQ GACFQCSQKR
CARAYHATCA AAAGVFVEEE EIPVFGEDGT EYKEQAFEFS CRYHRTKRDR KLDGDALETD
SRVRTAASKL QPGETCQLQY FKGDIFAGVV VENRHDEQTL LIDILPNGYA RIYQKLDVVK
SKLTACSDRL EVEWKWLLVP DPADYRLPKA SAKAIPMPAS QKAKEKLKTK RLHDGKPQKD
DPFVEGCTWA EFNSHPVGNK EQVKIDFCKP DQIWYYLPKT STEARAQFTE DPSNPRHNPR
GNFLSTVPKP VKPPRPVPAY PPRQAYQPAA PYPAARLDKP YMYKPRTPAS NNYPAMGNFT
TQRFTPAAPS PVPVQQQPGN YRYPYAQPTL SGQQAAPAYS AQKFEVRQSP AYTPPGSTPR
VQSSANALPH YQQNQWHGRY TSALPAPTPS HPGVAHPYPQ PYQAPAPANH HQAPQARVAL
QADVSIFQKY PFFQVNHNRD STKYRTPYAA WGGFTNGYEG NFRAHIMANK DAYLNGTIKD
NRFQSSQNFG AYQPLHHHPP AHGHHASPGS QLRISQQPNL KQVPTPSPGT GTPSFSQFPR
PAIKQQYLPP MPVQTHAPTQ AQVQAPMQPQ VQPQAQPQKS TPKPQQRPPQ KPPQKAEEKP
QQKSPQTAQP PNQSSKPKIG TIFKEYKVST WNSR
//