ID W9KYH6_FUSOX Unreviewed; 1335 AA.
AC W9KYH6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=FOZG_00416 {ECO:0000313|EMBL:EWZ49506.1};
OS Fusarium oxysporum Fo47.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660027 {ECO:0000313|EMBL:EWZ49506.1};
RN [1] {ECO:0000313|EMBL:EWZ49506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo47 {ECO:0000313|EMBL:EWZ49506.1};
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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum Fo47.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EWZ49506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fo47 {ECO:0000313|EMBL:EWZ49506.1};
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 Fo47.";
RL Submitted (JUN-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; JH717896; EWZ49506.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOZG_00416; -.
DR HOGENOM; CLU_001442_4_0_1; -.
DR Proteomes; UP000030766; 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 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..100
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..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1335
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..599
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 150040 MW; 6F21724B191AF087 CRC64;
MSESTSTLID AGIAVAATPH SHDTVVTTAP VDTNTKNPTT AQPGATFLHS PPDSNNTAKS
DGSDSESELS DLEDEPILSD PPQPVSSGEN 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 EEDDEDEQGG
MPTPPSGSGV KFRLAGRKRK RAPGEKGGKV KKIRLRLKSK AEPPCCLCPN DTPSADLLLT
DDGRRAHRLC AHYLPETYTE TIDGQETVVN VSEIHKDRFE LKCLYCRSKQ GACFQCSQKR
CARAYHATCA AAAGVFVEEE EIPVFGEDGT EYKEQAFEFS CRYHRTKRDR KLDGDALETD
SRVRTAALKL QPGETCQLQY FKGDIFAGVV VENRHDEQTL LIDILPNGDR LEVEWKWLLV
PDPADYRLPK ASAKAIPMPA SQKAKEKLKT KRLHDGKPQK DDPFVEGCTW AEFNSHPVGN
KEQVKIDFCK PDQIWYYLPK TSTEARAQFT EDPSNPRHNP RGNFLSTVPK PVKPPRPVPA
YPPRQAYQPA APYPAARLDK PYMYKPRTPA SNNYPAMGNF TTQRFTPAAP SPVPVQQQPG
NYRYPYAQPT LSGQQAAPAY SAQKFEARQS PAYTPPGSTP RVQSSANALP HYQQNQWHGR
YTSALPAPTP SHPGVAHPYP QPYQAPAPAN HHQAQQARVA LQADVSIFQK YPFFQVNHNR
DSTKYRTPYA AWGGFTNGYE GNFRAHIMAN KDAYLNGTIK DNRFQSSQNF GAYQPLHHHP
PAHGHHASPE SQLRISQQPN LKQVPTPSPG TGTPSFSQFP RPAIKQQYLP PMPVQTHAPT
QAQVQAPMQP QVQPQAQPQK STPKPQQRPP QKPPQKAEEK PQQKSPQTAQ PPNQSSKPKI
GTIFKEYKVS TWNSR
//
