ID I3JXM2_ORENI Unreviewed; 1038 AA.
AC I3JXM2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Lysine-specific demethylase 2B {ECO:0000313|Ensembl:ENSONIP00000013617.2};
GN Name=KDM2B {ECO:0000313|Ensembl:ENSONIP00000013617.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000013617.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000013617.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR AlphaFoldDB; I3JXM2; -.
DR Ensembl; ENSONIT00000013627.2; ENSONIP00000013617.2; ENSONIG00000013875.2.
DR GeneTree; ENSGT00940000154717; -.
DR HOGENOM; CLU_003540_0_2_1; -.
DR Proteomes; UP000005207; Linkage group LG7.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd21785; CTD_KDM2B; 1.
DR CDD; cd22180; F-box_FBXL10; 1.
DR CDD; cd15644; PHD_KDM2B; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
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; PTHR23123:SF10; LYSINE-SPECIFIC DEMETHYLASE 2B; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 4.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 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:UP000005207};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 137..304
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 514..560
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 567..633
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 118652 MW; C62EA24314EC0D1D CRC64;
SRSISRTMYD ENEDLSDVEE IVNIRGFSVE EKVLSDSYSA DFVRVMEGKD FTYEYVQREG
LRIPLIFKEK DQLGIRMPDP EFTVSEIKGL VGSRRSVDVM DVSTQKGSEM SMAQFVRYYE
TPEEERDKLF NVISLEFSHT KLENLIKRPT VDQVDWVDNM WPPGLKQSQT EATNIISEMK
YPKVQRYCLM SVKGCYTDFH VDFGGTSVWY HVFKGQKVFW LVPPTPYNLA LYEDWVLSGK
QSDVFLGDRA DGCQRVELQQ GYTFFIPSGW IHAVYTPVDT LVFGGNILHS FNIPMQLTIY
EIENRTKVHS KFRFPFYYEI CWYVLERYLH CLTKRSYLSQ EIRKESMGED EQGEKLERVP
QDGPCTPDNG KAQHLKAVLS IDSEDSCNPS SASLDFPKTP SDSPNSEPQN KWIHLTEFEL
NGLRTLIEKL ESLPENRKCI PMGIENPQAL LDDLKVVLKE HTNDDPKLAI TGYPVVYWPK
KTIKPRPPNR PKPKMAASPA SAVKLSASRG TSGARRRRTR CRKCEACLRT ECGECHFCKD
MKKFGGPGRM KQSCIMRQCI APVLPHTAVC LVCGEAGKED TVEDEEEKFN LMLMECSICN
EIVHPNCLKI KDSNGVVNDE LPNCWECPKC NHAGKTGKVS ISMDFILSVF ELPLKTEDSL
TNQNQRPVKS EPESEVDEQK PRWPLNNGSS DLGDWLRHRG REMNGTPRGY SPLGWNRNAP
IAPICPRPLP CRSPPKCIQM ERHVIRPPPI SPPPDRLPLN DGEAHVMQRE TWMMVFGHLS
HRDLCVCMRV CRTWNRWCCD KRLWKHINLN RCKSITPLML SGIIRRQPVA LDLSWTNISK
KQLSWLINRL PGLRVLLLSG CSWVAVSALC TSSCPLLRTL DVQWVEGLKD AQMRDLLSPP
TDNRPGQLDN RSKLRNVEDL RLAGLDITDT SLRLIIRYMP LLSKLDLSYC NHVTDQSVNI
LTAAGTTTRD SLTDINLSVC NRVTDQSLTY FKRCGSICHI DLRYCKQVTK EGCDQFIAEM
SVSVQFELIE DKLLQKIS
//
