ID H2UAB7_TAKRU Unreviewed; 1393 AA.
AC H2UAB7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 64.
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 Name=LOC101069859 {ECO:0000313|Ensembl:ENSTRUP00000033884.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000033884.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000033884.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000033884.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR Ensembl; ENSTRUT00000034010.3; ENSTRUP00000033884.3; ENSTRUG00000013308.3.
DR GeneTree; ENSGT00940000157076; -.
DR Proteomes; UP000005226; Chromosome 19.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15603; PHD1_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
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; IPR047978; KDM5B_PHD1.
DR InterPro; IPR047979; KDM5B_PHD3.
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:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 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; 3.
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; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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 15..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 83..173
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 260..310
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 404..570
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1125..1173
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1333..1387
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1281..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1393 AA; 157850 MW; 4F9F5FD66C7784BC CRC64;
MTQPQLNEFI PPPECPVFEP SWEEFADPFA YIKKIRPIAE KTGICKIRPP PDWQPPFACD
VDRLKFTPRI QRLNELEYSF LNFNSGLNFL DQIAKFWELQ GCTLKIPHVE RKILDLYQLN
RLVNEEGGFD AVCRERRWTK ISVKLGFAPG KAVGSHLRAH YERILYPYNL FQTGDNLVIN
SKATLTNDTK DKEYTPHDLP QRQSVQPQET CSIARRAKRM RSERSFIKSE PGEICTTRNS
VRRRMGYSVK PEYGKSKVDQ YMCLVCGCGT AEDRLLLCDG CDDSYHTFCL IPPLHDVPKG
DWRCPKCLAQ ECGKPAVAFG FEQAGRSYTL QTFGDMADSF KSDYFNMPVH MVPTELVEKE
FWRLVSTIDE DVTVEYGADI ASKEFGSGFP VKNSHFQVAP EDEHYLTSGW NLNNMPVLDG
SVLTYITADI CGMKLPWLYV GMCFSAFCWH IEDHWSYSIN YLHWGEPKTW YGAPAYAAEQ
LESVMRNLAP ELFESQPDLL HQLVTIMNPN TLMNNGVPIY RTNQCAGEFV ITFPRAYHSG
FNQGFNFAEA VNFCTMDWIP VGRSCVSHYR ELSRYCVFSH DEMVCNMASK ANTMDVDLAA
VVQKEMTVIV EQEDKLREMI KKMGVVQSRQ VDSEALPDEE QQCCKCRTTC FLSGISCACT
PRKMACLYHS QHLCSCPHGN LTLNYKFTLD ELYSMKASVT QRAESYKIWL INVQEILENK
GSLEELHSLV EQAETSAFPK ISLVDQLRTA TAEADKVAVM AQQLLNGKRQ TRYRSGGGKS
QNQNDLTAEE LRSFVQQLDN LPCNIRQGPL LKDLLTRVDD FQQRSERLLS DESPSPVELQ
DLLDMSLGLD VELPQLPLLR ERLEQARWLD AVQQASSRPE SLCLDTMRRL IDQGVGLAPH
SSVERAMARL QELLTVSEQW EERALSLLES RPHNSMETLE AALQEVENIP AYLPNCLQLQ
DVIDKAKNWL QEAEALQLGG RIPVLDSLSE LVLRAEGIPV RLDPLSRLEA LVCDIQSWKE
SAGKTFLLKN SPLSLLEVLC PRCDIGAAPQ KSRCKKTKDA AQSGKKSPTL LDSLCDVERA
LSESKDSASA MATLTEVHQR ELELLLALRA SNESKLLSSE NYCTLSVCVC QKAPSGAMVQ
CELCRDVFHS GCVTMTSEAA YGQAWLCPYC QRSKKPPLDK VLPLLASLQR IRVRLPEGDA
LRFLIERTVR WQHRVQVSLG TSLHLFPFLF LFLNCLYFIS GLGPELEELM VEGFLLQVTL
PETEQLYKYL LYKLAPLPPS SAPSGKNKEQ DQPSSRGSPH KKKSKEKSED NRRTCSAQQM
VPEPPPSDSE EDYSLCAAPW CREPEGDEVN WVQCDGSCNQ WFHQVCVGLS AERAEKEDYI
CISCTQPDYD RGE
//
