ID A8P2R1_COPC7 Unreviewed; 1235 AA.
AC A8P2R1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 56.
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=CC1G_12335 {ECO:0000313|EMBL:EAU83432.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU83432.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU83432.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU83432.2}.
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DR EMBL; AACS02000013; EAU83432.2; -; Genomic_DNA.
DR RefSeq; XP_001838385.2; XM_001838333.2.
DR AlphaFoldDB; A8P2R1; -.
DR STRING; 240176.A8P2R1; -.
DR GeneID; 6014969; -.
DR KEGG; cci:CC1G_12335; -.
DR VEuPathDB; FungiDB:CC1G_12335; -.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_1_0_1; -.
DR InParanoid; A8P2R1; -.
DR OMA; WNLKCTA; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000001861; 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; 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; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 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:UP000001861};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 60..101
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 316..482
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 625..765
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 134722 MW; BB1FDA8038995435 CRC64;
MAYSSRASSL TPCPSPSPEP PVVQPDHFYG SEGIQLPPSP NSDGKTWLDP DDDPTASRGI
PVFKPTMEEF EDFEAYMDKI NCWGLKSGIV KVIPPKEWSE SLPDIKPQLR EVKIRSPIEQ
VMLGSGGLFR QQNMEKRRIM SVREWAELCS KDEYRAPAKQ DIGLQSRAER MAIPRGSRRT
ARKKESVPPE AKSDKNYTEA SRLSSVPSPP PSEAGDTPAS GSAKREQSVD KSQPKPKGKR
VAQTREARQA NLAERALRDN EFIDTFDPHT DWLPPNTTAD DYTPEYCQKL ERHYWRNCGL
GKSAWYGADT QGTLYTDETK VWNVGRLPSA LSRLLPASDQ GLPGVNTPYL YFGMWRATFA
WHVEDMDLYS INYIHFGAPK FWYAVPQARA NTLEHAMRNY FPKDTSQCPQ FLRHKSFLAS
PTLLAKSSCR PNHLVQHAGE FVITYPRGYH AGFNLGFNCA ESVNFALECW IEMGRVAKAC
KCVSDSVRID VDQLLQDRAE EAMKAVAQME MEMEQNGGEL FQMPKPKRKR KERSGFSPVK
EETCDGVIPT LKIPLKRKPE EVVESPKTKK IKIKPTTTTV SQLSPSKVAN GVASTSKSAT
STGPSSQPKI SVKLKLGPKP AEPEEFPCCL CISTDRTGLL RVQGPPLNRK DAIEAAGNPK
VWMAHEHCAS IIPETWVDET ALPDGSTEKV VLGIDAIVKD RWNLKCSACT RTRPKVHGAP
VQCTKGKCPK AFHVSCAREG SAHGIIFSVL KEVEKEVVLF ETNPSNAFPV PMQVDGATSS
FGEDEGRVLK VVKKLVCEIL CPQHNPALAA QKKASKQEKI KAELLLLPSM SRIKIRVSSG
VFEVSLIRVI EETGSVEVLW DRGITREFKW GSVIFGSTDG PVLQRPVDDN PSPPVKDERS
VSVAAPSTSA PVQTYPSTTA ATTTSSAAAS RVGTPSVGNG GAASEPSTSN PPAAVVTQPT
TSSQYPFGSQ VVPTSATPYW SVYAPQQIPY GHPQLTAGSS AYPYTGYYRD AYGVPQPNYP
PTQTYHRPAA YNVGGYHGTG VQDSRLQWQR PYEGPGSQQQ QRAQHQQSHY RQPVAVFHIP
VAPNPNSQTG SNVTPAPSSS ASQTSSSDLP SSSSSGHSNG SPQQGVTTAT QVQTSEQTQV
GATTVAQSST SGPSTSSGCQ SSVQDGQSSQ SGKSPSDQPS GAHSQTTQQG YPDLSTLAKL
PPEELTEMLQ NNPDLRNYIM STLKMSAPVD GQVAA
//
