GenomeNet

Database: UniProt
Entry: A0A4W2EQK7_BOBOX
LinkDB: A0A4W2EQK7_BOBOX
Original site: A0A4W2EQK7_BOBOX 
ID   A0A4W2EQK7_BOBOX        Unreviewed;      1109 AA.
AC   A0A4W2EQK7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Name=KDM4B {ECO:0000313|Ensembl:ENSBIXP00000039071.1};
OS   Bos indicus x Bos taurus (Hybrid cattle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000039071.1, ECO:0000313|Proteomes:UP000314981};
RN   [1] {ECO:0000313|Proteomes:UP000314981, ECO:0000313|Proteomes:UP000429181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA   Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT   "Haplotype-resolved cattle genomes.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBIXP00000039071.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   -!- 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 JHDM3 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00009711}.
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   Ensembl; ENSBIXT00000032965.1; ENSBIXP00000039071.1; ENSBIXG00000004509.1.
DR   Ensembl; ENSBIXT00005001156.1; ENSBIXP00005008038.1; ENSBIXG00005001510.1.
DR   GeneTree; ENSGT00940000159248; -.
DR   Proteomes; UP000314981; Chromosome 7.
DR   Proteomes; UP000429181; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd15714; ePHD_JMJD2B; 1.
DR   CDD; cd15576; PHD_JMJD2B; 1.
DR   CDD; cd20464; Tudor_JMJD2B_rpt1; 1.
DR   CDD; cd20467; Tudor_JMJD2B_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.10.330.70; -; 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; IPR034732; EPHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR040477; KDM4-like_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047483; Tudor_KDM4B_rpt1.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF30; LYSINE-SPECIFIC DEMETHYLASE 4B; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF18104; Tudor_2; 2.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
DR   PROSITE; PS50966; ZF_SWIM; 1.
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:UP000314981};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00325}.
FT   DOMAIN          15..57
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          146..309
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          814..927
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          874..913
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   REGION          381..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..545
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1109 AA;  124113 MW;  F667ABA9F19AA3FC CRC64;
     MGSEDHGAQN PSCKIMTFRP TMEEFKDFNK YVAYIESQGA HRAGLAKIIP PKEWKPRQTY
     DDIDDVVIPA PIQQVVTGQS GLFTQYNIQK KAMTVGEYRR LANSEKYCTP RHQDFDDLER
     KYWKNLTFVS PIYGADISGS LYDDDVAQWN IGNLRTILDM VERECGTIIE GVNTPYLYFG
     MWKTTFAWHT EDMDLYSINY LHFGEPKSWY AIPPEHGKRL ERLAIGFFPG SSQGCDAFLR
     HKMTLISPII LKKYGIPFSR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY
     GKVATQCTCR KDMVKISMDV FVRILQPERY ELWKQGKDLT VLDHTRPTAL SSPELSTWSA
     SRASLKAKLL RRQISLKENR HWKKTEEERK PSLERKKEQT RRPGLSSHRK RSQPKKPKPD
     DPRSPGEGAA GVALLEEAGG STKEEAAPEA DPEEEEEEAQ LLPQGREAEG SEEDGRGKLR
     LAKAKSDRKK KSYGSLHPHH PLLPPPPSSQ FTEEAPLLDI PGPAPGLEAA EESPLPPPLN
     VVPPKAPGEE PEAKPRPVIP MLYVVPRPGP TGNKGRVSCQ QASEHFAQKG PTWKEQATPM
     ELTGPEEESG ASEGQNPSTF SKLKMEIKKS RRHPLGRPPT RSPLSVVKQE ASSDEESFPF
     SGDEDVGDPE ALRSLMSLQW KNKASNFQAE RKFNVAAALT EPYCAICTLF YPYSQSLQTE
     KEAPQAALGE GSSAIPPSRS GQKTRPLIPE MCFTASGENT EPLPANSYIG DDGTSPLIAC
     AKCCLQVHAS CYGIRPELVN EGWTCSRCTA HAWTAECCLC NLRGGALQMT TDRRWVHVIC
     AIAVPEVRFL NVMERHPVDI SGIPEQRWKL KCVYCRKRMK KVSGACIQCS CEHCSTSFHV
     TCAHAAGVLM EPDDWPYVVS ITCFKHKSGG HSVQVMRAVS LGQVVITKNR NGLYYRCRVI
     GTTTQTFYEV NFDDGSYSDN LYPESITSRD CARLGPPPEG EFVELRWTDG NLYRAKFISS
     VTSHIYQVEF EDGSQLTVKR GDIFTLDEEL PKRVRSRLSV STGAPQESVF SGEEVKKMGF
     CDVFSKERFS LLPGWSSRSA SLGTVFSQS
//
DBGET integrated database retrieval system