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Database: UniProt
Entry: X0B0V6_FUSOX
LinkDB: X0B0V6_FUSOX
Original site: X0B0V6_FUSOX 
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
//
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