ID A0A1M2VYF3_TRAPU Unreviewed; 1931 AA.
AC A0A1M2VYF3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=TRAPUB_10890 {ECO:0000313|EMBL:OJT12566.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT12566.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT12566.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT12566.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJT12566.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNAD01000476; OJT12566.1; -; Genomic_DNA.
DR STRING; 154538.A0A1M2VYF3; -.
DR OMA; KERNWHF; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000184267; 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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; 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; 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:OJT12566.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW Transferase {ECO:0000313|EMBL:OJT12566.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 158..199
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 223..314
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 615..781
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1704
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1931 AA; 216102 MW; 31A01D25B3307855 CRC64;
MHGSPSPRGA SARRGRSPRT HPTSPAPSSL PPDFSAKAPA TFTSCLSIAV EGAIPIERPD
PTAPPQDVPA PSVSADSKRA PRKSKTDALA ALHTHAQTTL GEESLNDTIN DEAGIRIQLR
DGPPLSVPQM LDLSSVKTAD ARPTTPKTGP RPFGLTDCPT FHPTPEQWKD PMAYIASISD
AGKRYGMCKI VPPAGWNMPF VTDTERFRFK TRLQRLNSIE ASSRAKVNFL EQLYRFHKQQ
GNPRVSVPTI NHKPLDLWLL RKEVHKLGGY DAVTKDKKWA DLGRLLGYTG IPGLATQLRN
SFSRVILPYE QFCDRVRSSP ALSPNKARDP QLKTHVNIQS AGSIPRPSTP DSAAGDESPP
SSPLTATSSP LSEPPDEGDH KDANGVKSES SRPRRSARHV SQEHGTRARR ASTANDTGQL
AFAKTASQDN KSPQELHCEI CLKKDQGEKM LICDGCDCGA SRLQAVYAKR FVTSLDLGFH
MFCLDPPLLN IPRGQWFCHT CLFGTGGDFG FDEGEEHSLS SFQARDLEFR RLWFLSHPPQ
SVTANGGQSS SSAHANDPYA NRFGNMVVTE DDVEKEFWRL VQSQNETVEV EYGADVHSTT
HGSGMPTLET HPLDPYSKDP WNLNNIPILP QSLLRYIKSD ISGMTVPWTY VGMIFSTFCW
HNEDHYTYSI NYMHWGETKT WYSIPGCDAE KFEAAIRKEA PDLFEAQPDL LFQLVTLMNP
QRLKEAGVDV YACNQRAGEF TVTFPKAYHA GFNHGLNFNE AVNFALPDWL PLGLDCVKRY
QEHRKMPVFS HDELLITITQ QSQSIQTALW LNDSLQEMTD REMDARTRAR ARQMNEVLEE
TDRGDDQYQC SVCKVFCYLS QITCTCTSKI ACIDHVDQLC KCPPVNHVLR KRFSDTELQD
IQARVSERAA VPTVWRGKLK RLLDDSPRPP LKGLRNLFTE GERIQFPLAE LNSLRKCVNK
ANEWLEAANG ILIRKPTRKR TRKSRGRSST ADPGLSTGIG EEIIDKPDRT LEDLYALLSE
VENLGFDAPE IAQLRTIAGE AEDTRRKARA LLDAKMLPRE REFFVRECEH LILHAQTLNV
LVEEIVEVEK IVLREQLVKE LEEALDDDNL TLEDVRQLMA RAHACNLPAE NSYMQRLEAL
LRAGSNWEEK AKALLDKQQR TLEDLEEFVK PRRSGMPVDP DLLERILDLR KKGKDLEKQA
KIWLLSEPGV PKPKVQEVVR LVTEHDKDFE IPAVEDLKRT VDFAQDLEAR CEAVMRGIYN
PQDEPDVFHT MLQWRKYAKE HLTMFSLPNF ETLDKQLTTH YRWLEGLPWW CRQHQESHGQ
PILDDVVEST RPEDDLPPND EYFTCICTTP VRPPAHGTVS DAVQCDHCFA RFHGICAANG
GSCPFCDHHH WNGTIHKERN WHFFFLPQLL LQAPDVTKNY SEEWKQLEII VHRVDRLCSV
IGQFLSFAAQ PTNQRADYMP QVRHYMRKLY KIQFNVASNP DANFGLDLAG LHRILAGQPI
PVRMKKRRRP KFVFGQDVDK DWNDGTRCIC RGRTNYLLNF AKVECEVCNK FYHGGCVFYP
PDGANNRFMC PLCCVRKNRV YPYSEVRVKH VDTKEADVFV DTKEMLDTFS KDIIYMRLPP
PYTQTLFVEL IRFTPGQPDN VAANGSTPSA PPRNGAGPPN HQAPMTLANG SSANPRAMHP
HPHPHPHPHS HSHPHAHLAH PAHPHAHHGP VSTPPASAGP YEAPPHGPHG PGQAIPPPPW
AATSRWSSAA AAAAPPSART MPSMPPGSEQ LRSPLSTPPQ GARKRKYPDD MPPGAPDERL
APAPMIRSPK RLHSSQTTPP MPRANPGMSP SLAMMLAQAP GDPRSPTRQP SGSTPYSRGP
PGMVPPSPVA VGRGPGPEDG MPSPSGSHHS VRKVKVGYPG GGPPNSRGEE DRGWRPPPPH
DNRSPPGPPR H
//
