ID I1RD69_GIBZE Unreviewed; 1510 AA.
AC I1RD69; A0A098D5I0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 Name=FG01558.1 {ECO:0000313|EnsemblFungi:CEF73705};
GN ORFNames=FGRAMPH1_01T03799 {ECO:0000313|EMBL:CEF73705.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF73705.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF73705, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF73705};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF73705, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF73705};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF73705.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF73705.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF73705}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF73705};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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; HG970332; CEF73705.1; -; Genomic_DNA.
DR RefSeq; XP_011317370.1; XM_011319068.1.
DR STRING; 229533.I1RD69; -.
DR EnsemblFungi; CEF73705; CEF73705; FGRRES_01558.
DR GeneID; 23548992; -.
DR KEGG; fgr:FGSG_01558; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G03799; -.
DR eggNOG; KOG0958; Eukaryota.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_001442_4_2_1; -.
DR InParanoid; I1RD69; -.
DR OrthoDB; 48111at2759; -.
DR PHI-base; PHI:1620; -.
DR Proteomes; UP000070720; Chromosome 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; 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:UP000070720};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 119..160
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 396..559
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 647..770
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 16..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..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..602
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1510 AA; 168546 MW; 99FC029F0D0187BA CRC64;
MSESTSKSID AGAVAANANV SALDSRDPVV ATAPADSNPN NTATAKTDPA FLHSPPDSNN
TAKSDGSDSE LSDLEDEPIF SDPLQPADPG DKTTSDEDKS KPSDDDIGEV LPDHWSGAVP
IFKPTMHQFR DFKRFMEAVD SYGMKSGIIK IIPPQEWKDD LPKLDDLVKQ VRVREPIKQE
IMGSNGTYRQ VNILHGRSYN LPQWRQLCDQ SEHQPPARRG ERRANAEKPK PRTRAAAPAP
KPVDPSVPKK RGRGRPAKRG GRGRRANPEP AEDAEDRPMT PVSPKPDAAE VEDKPVESVE
LDPGEEVEDD YEPRVGRMGI SRPAKTKTQT VSARRKYSRR EGSAMIDEAA FKDWDYKMDT
SEYTPERCEE LERAYWKTLT YAPPLYGADL MGTLFDETTE EWNLNKLPNL LDVLGTKVPG
VNTAYLYLGM WKATFAWHLE DVDLYSINFL HFGAPKQWYS ISQADARRFE AAMKNIWPTE
AKSCDQFLRH KGFLISPQHL KSHYNITVNK VVSYPGEFVV TYPYGYHSGY NLGYNCAEAV
NFALDSWLEI GKIAKKCECA QAQDSVWVNV YEIERKLRGE ETEYEETEEE EEDEEDDDDE
QSGMPTPPSA SGVKFKESRR KRKRGPGDKS GKVKVKKIRL RLRAKAEPPC CLCPNDTPSA
ELLPTDDGRK AHRLCAHYLP ETYIETIDNQ ETVVNVSEIH RDRLDLKCLY CRSKRGACFQ
CSQKKCARAY HATCAAAAGV FVEEEEVPVF GEDGTEYKEQ AFEFSCRFHR TKRDKKLDGE
LLETDARIQT AASKVQSGET CQFQYHKGDI FAGVVIENRA NEQILLVDIL PNGDRLEVQW
KWLLVPDAAD YRLPKASANA IPMPSSQKAK EKLKTKRLHD GKPQKDDPFV EGYTWAEFQL
HPASNKEQVS IDFSKPNQIW HYLPKTSTDA RAQFTEDLAK QRHNPQGNFL STVPKPVKPA
RPPRQVPAYA QQQPYQHATP YNAGRMERPY VYKPRIPAES NMPAMGSFTT QRFVPAASLP
TPHQHHPAQY PSYAQPAPPG HQPPHPPYSA QRFEVRSSPA YTPPGSTPRI HSPMNAPAHP
QHTQWPGVAS VSHPPPVLAP AAGAIHPHHG AHQAPYQAPA PYQQAHPAQQ QNHQMKASWQ
VHPSIYQKYP FFQVNYNRDS SKYRTPYATW RGFTNGYEGN MRAHIMANQD AFLRGQPSSH
NYSAHGSTYQ RPSAVPPQAP SSSQMPPSGH EFRQQTFVNG VPAPSPMLTH QTSGQFPRPA
LKPQYMPPIQ AQAQEHPQQR QQPQPNAQQG PQEATQTPNQ NSKVKTATVF KPYKIPPKQS
PVPLPANYLA AMTPTSTSNT AAATAGQSAL QQPLNKGSPV EPKSARKVQG TQHSPSVTHN
PGRQPLGAKI SETPIPVPRL PGFMPASTSR EQAAPPQKRV PEQDRSSQRL PVHQGGPVTP
VATQEQMASS ARDGKLALTN TKPGNMSQTV SAEQAIPFQP HDFPDVPGSE SMKFLDNILK
NVRTLARRDE
//
