ID Q7RW47_NEUCR Unreviewed; 1977 AA.
AC Q7RW47;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 3.
DT 08-OCT-2025, entry version 106.
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=NCU03505 {ECO:0000313|EMBL:EAA26571.3};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA26571.3, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA26571.3, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; 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:ARBA00049349};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR EMBL; CM002237; EAA26571.3; -; Genomic_DNA.
DR RefSeq; XP_955807.3; XM_950714.3.
DR SMR; Q7RW47; -.
DR STRING; 367110.Q7RW47; -.
DR PaxDb; 5141-EFNCRP00000002609; -.
DR GeneID; 3871954; -.
DR KEGG; ncr:NCU03505; -.
DR VEuPathDB; FungiDB:NCU03505; -.
DR HOGENOM; CLU_001442_3_0_1; -.
DR InParanoid; Q7RW47; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 1.
DR FunFam; 2.60.120.650:FF:000047; Putative jumonji family transcription factor; 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; IPR055500; DUF7072.
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; PF23258; DUF7072; 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:UP000001805};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 179..220
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 459..622
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 717..840
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..37
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..164
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..666
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..694
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1207
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1295
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1561
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1593
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1647
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1694
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1792
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1955
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1977 AA; 218912 MW; 0314951E1D759B80 CRC64;
MSTQANGATA PDHPVAQDAV AQDLVVAHSS PDAIMTDADP DADPDASTPM GLRSPPESDK
AMNLDEASES ELSDLDDDVA DKLDQDHTFD LDLGSDPLPD PKTGQQQQQP EPSVSHEHEP
ATAATVESAT QIKEEQEGEG KESTSHSQQP DTGAASATTP TSPSEDIGEI LPDRYENNVP
VFKPTLKQFQ DFKLFMEKVD KYGMKSGIIK IIPPEEWRSA LPPLDELVKQ VRVREPIKQE
IMGQNGTYRQ VNILHQRSYN LPQWRQLCDQ SEHQPPARRG ERRANAEKTK PAPRSRAAPP
AANGTTSNKT PTNTNTGRGK RKGRVTRGSA KAATDETDDP PITPVSPPPE DEDKPLASIE
EEDIKDEACE EEESIPRAGR MGFSRQGKPK MQSTSARRKY IRREGSAMID EAAFKDWDYR
MDVSDFTPER CEELERIYWK TLTYAPPLYG ADLPGTLFAE STENWNLNKL PNLLDVLGTK
VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NFLHFGAPKQ WYSISQADAR RFEAAMKNIW
PTDAKACDQF LRHKSFLISP SHLKQHYGIT VNKVVSYPGE FVVTYPYGYH SGYNLGYNCA
EAVNFALDSW LPMGKIAKKC QCAQAQDSVW VDVYEIERKL RGESTEYEVT EDEDEDEDED
SDESDQDTGL PSPPSGLDHR GGKRVRTAGQ KRKREANNRG TEGKAKRSRF RLKAPVEPPC
CLCPNDIPGA EIMPTDDGRK AHRMCALYLP ETYIETVDDQ EIIANVAGID KARLELKCLY
CRSKKGACFQ CSQKKCPRAY HATCAAAAGV FVEEGDVPVI GEDGTEYKEQ AFEFSCRFHR
VKRDRKTEGA ILEDDPVVRK TAEGLKKNDI CQIQYYQGNI FAGVVVENLH EEETLLLDVI
PSGDRIQVEW KWLLVADPSE YRLPKASPNA IPMPTSKKAK QEINAKRPVE EIPRKGDEFS
TGFVWAEFHT GEPDKNKEQV KIDLDKENQV WHYLGPTSTE ARAQYTENPS RKQHNSKSNF
LDTIPKPPPT YPVQVASAPR KSLSATYPTQ QQQTFIASPA SSSALASKQD KPYVYKPRKP
VQPHTQFNVQ YTSHMFMPAP PLPSPSYVPQ QNHPFYQAQL RPNVPQTVHP SQVFSPQPMH
YDGQRRMSQS TQPYPQQQMS PHHFAQHQMP QQMPQHQFQP QQQQQQFQHF QPPQQHYQQQ
PQQNYPQTPV PLPPQAFQFQ QQTCAPLPQQ VQPQQPQQQS PVPLPQQVQT ALPEQQQQQQ
QVHHVQQTPV PVPQVPLQAQ QSTQSSPQQQ QQPQPQDEEA HQPLPPVDQT QPPSPPQPLP
KPRPFKVYKA CQFRKLKLPE KRPGAKKDLP DAFASRRFSF AGIDRIHDLP GIVWPPKNLI
SGRESQCRRG VWAPLSDEGI MPAPMTSSLL KCADDDQRVS QKYEFFQVHN NKDPLKHHSP
YKPAVTELDE TTGKKKLVHA DFTNDYAENF TNFMKNAREA LTRKDISEPS SRPVTSQAHS
RNASSASAQP NDSQFQQNSF TGQPTQHPRV QPQYTYNQHE AGFGESSSSS PFSSHSVPAP
VLFGPAFEQQ SGSHQDMRQQ YQGPWQQQYQ NQGSHNIWMG SPQMVGSPQP QMFSPSPTQQ
GHHHHMPQSQ QQAQNQQPQP QQPAKPQFTK QSHSPIPLPP YVQKMNQAKP SPLSQPPQTN
SRQGSQGASS QSQSQKRRQR KSAQQASEQT ISPTQLSVDT GAGSTPQGQP PKAQQTSNNP
WTNANNVHLQ FPSALNASSQ QPAPATATQR PSQNTSDHTP AEADAGAEQQ ESGGEEEAHD
VEENSYFNEA QGFQTPPLQP QTLSSTDVSP DQNYFPLSAP PPTPLGGIAF GGVGVGGFNP
GSAFNVATLS GGIAGLGALG TLGGLLGGLE SGASGNGTWS GRARGLSRSG DNVFMGSTSA
IEDGEEGELG CGMGGGGGGG GGGSRGGVHG GGNGGTALSR QDVLDKILSN LHRLGTE
//
