ID A0A2G8SUJ2_9APHY Unreviewed; 1998 AA.
AC A0A2G8SUJ2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN ORFNames=GSI_01143 {ECO:0000313|EMBL:PIL37449.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL37449.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL37449.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL37449.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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:PIL37449.1}.
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DR EMBL; AYKW01000001; PIL37449.1; -; Genomic_DNA.
DR STRING; 1077348.A0A2G8SUJ2; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 247..288
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 312..403
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 526..576
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 687..853
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1772
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1998 AA; 223320 MW; 428D8F62E869FCAD CRC64;
MASQTGVRRR GGGRRLVGGG GEGEGAVGGV VYVAMSPAIR RRQDRRWELD SAKAEVPTWK
VSGLKDRSSG RNRGEHSLAA VSSFLSFSTA AMHGSPSPRG GPARRGRSPR TNADSPAPPA
LPPDFSVRSP ATFTSCLTIA VEGAIPIERP EPAPVAPDAA TSDSNSRRAP RKSKTDALAA
LHTHAQSNAG EEALADAMTE DGGIRIQLRD GPPLPVPATL DLSSVKTPHT RPSGPKAAPR
LFGLTDCPTF YPTPEEFKDP MAYIASISDT GKKYGVCKIV PPPGWNMPFV TDTERFRFKT
RLQRLNSIEA SSRAKVNFLE QLYRFHKQQG NPRVSVPTIN HKPLDLWSLR KEVHKLGGFD
AVTRDKKWAD LGRLLGYTGI PGLATQMRNS YNRVILPYEQ FCERVRNSPA LSPSKPRDPG
LKTHTNIQTS TTLPQLSTAE SAADDDSPPS SPLTATSSPL SEPPDESDMK ETNGVKSDAS
RPRRSTRNTT QDLLPLARTS RTSTGNDALV AGQMDPDAPK KKLPSELHCE ICLKKDQGER
MLICDGCDCG FHMFCLDPPL ANIPRGQWFC HNCLFGTGGD FGFDEGEEHS LSSFQARDRE
FRRLWFLSHP PQSGMFNGTD SSSSARVGDP YANRFGNMVV TEDDVETEFW RLVQTPTETV
EVEYGADVHS TTHGSGMPSL ETHPLDPYSK DPWNLNNIPI LPQSLLRYIK SDISGMTVPW
TYVGMIFSTF CWHNEDHYTY SINYMHWGET KTWYSIPGSA AEKFEAAIKK EAPDLFEAQP
DLLFQLVTLM NPQRLREAGV DVYACNQRAG EFVVTFPKAF HAGFNHGLNF NEAVNFALPD
WLPLGLDCVR RYQEHRKMPV FSHDELLITI TQQTNSIQTA LWLNDCLQEM TDREMDARTR
ARSLQMGEVL EETDRADDQY QCAICKVFLY LSQITCPCTT RVVCIDHVDL LCKCPPANHV
LRKRFNDIEL QDIQARVSEQ AAIPTIWRNK LKKLLDESPS PHLKSLKAIF AEGERIQFPL
AELNSLRKCV SKANEWLEAA NTIIARKPAR KRTRKSRGRS STATVDGLSS DVAEEVIEKP
DRTLDDLYGL LDEVANLGFD APEIGQLRQI AREAEEIRGN AKDLLARERS ARDREGFVHE
CRRLIVHSAT LNVLVDEIVE VDKIVLREQL LKDLVVELED ENLSLEDIRQ LKARADACNL
PMDNLQMQRL YGLYKSGMAW EDKAKRLLEK KDRSLDELEE FMQPRRNGLP FDPEILERIA
ELRKKGREYE KQAKIWLLAD ARAEKPKVQD VVKLVADAQR DFVIPAVQDL QRTVAWAQDL
EGRSEAVLNA SYSGIDDKDI FETMGTWRDY AKKHLTMFSL TNFQKLETQL ELHHRWIQSL
PWYCAQHKDT HGQPILDDVV ESTRPEDDLP PTDEYFTCIC TTPVRPPAMG QVSDAVQCDH
CFARFHGVCA ANGGSCPFCD HHHWNGTIHK ERSWHFCYLP TIMMHAPDIS KCYSEEWKQL
EIIVHRVDRL CGVIGQFLSF LNQPANQRVE YIPQVRHYMR KLYKIQFAVS PNPEVSFGLE
LASLHRVLAG QPAPTRMKKR RRPKFTFGQD QDKDWLDGTR CICRGRTNYL LNYPTVECEL
CGKLYHGGCV FFPVEGGRGA RFMCPLCCVR KNRVYPYSEV RVKHVENPEQ DLFVDTKEML
DTFSKDIIYM RLPPPYTQTL FVELLRFTPG QPDNIAANGA SISAPPTRPM SMSGPSNPAP
MPVTNGSSAH PRSMHPPHSH HSHSHSHSQS HSQSHSHSHS MSAPPPAGPS YDNGRPPSHV
PPPPPWALTL TSRWSSAAAA AAPPGPSRPA PPPQSPAEQM RSPIGGMQTP PLASRKRKYP
EEVAPPHGPP PPDDRLAPAP LIRSPKRHHS TTVSPPQPSA APRSSQGMSP SLAMMLSPTP
SADMRSPTRQ QPPPPLPTYV HAHSRSIPPS PGRSGPTEDP NSHHRGQKVK AIYPGQSSAP
PRVDEERWSP SLPPPPRH
//
