ID A0A3B3V7T9_9TELE Unreviewed; 1420 AA.
AC A0A3B3V7T9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=KDM5B {ECO:0000313|Ensembl:ENSPLAP00000021840.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000021840.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000021840.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; ENSPLAT00000009953.1; ENSPLAP00000021840.1; ENSPLAG00000006021.1.
DR GeneTree; ENSGT00940000157076; -.
DR Proteomes; UP000261500; Unplaced.
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; cd16874; ARID_KDM5B; 1.
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; 1.
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; IPR047981; KDM5B_ARID.
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 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 9..50
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 74..164
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 247..297
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 391..557
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1115..1163
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1360..1414
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1039..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1336
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 160723 MW; E7344DBDCBDBB0F3 CRC64;
MAFKPPPECP VFEPSWEEFR DPYAFINKIR PIAERTGICK VRPPPDWQPP FACDVDKLHF
VPRIQRLNEL EAQTRVKLNF LDQIAKFWDL QGCTLKIPHV ERKILDLYKL NKLVADEGGF
DIVCQDRRWT KIAVQMGFSP GKAVGSHLRG HYERILYPYN LFQNGANLLC VQKPDQLAEA
MSVDEPKLQE AVQRAPAPLP DVCPSARRAK RMKIEVRVAA ASLFTAGSKN SFTFPVDISA
FVSQVDLVVC LVCGSGGDED RLLLCDGCDD SYHTFCLIPP LHDVPKGDWR CPKCLAQECS
KPHEAFGFEQ AHRDYSLRAF GQMADAFKSD YFNMPVHMVP MELVEKEFWR LVGAIEEDVT
VEYGADIASK EFGSGFPIPN GKFKVSPADE KYLKCGWNLN NLAMMNPSVL THVTADICGM
TLPWLYVGMC FSSFCWHIED HWSYSINYLH WGEPKTWYGA PGFAAEQLEK VMKKLAPELF
ESQPDLLHQL VTIMNPNTLM AHGVPIYRTN QCAGEFVITF PRAYHSGFNQ GFNFAEAVNF
CTVDWMPLGR QCVDHYRLLH RYNVFSHDEM VCNMATKAET LNVVLASAVH KDMALMIKEE
QELRDKVKKM GVVNCKEAKY DHLQDDERQC AKCRTTCYLS AITCPCSPGV LVCLYHINSL
CSCHVSNYTL NYRYTMDDLF PMMNAVKQRA ELYDEWASRV TQTLEAKLEK KKGLPVFRSL
LTESETRLFP DNDLLRRLRL VTQDAEKCAS VAQQLLNGKK QTRYRCGSGK SRSQLTVEEL
SSFVRQLYNL CCSLPQAPQL KELLNRIEDF QQHSEKVLME ESPSVAEIQS LLDVSFDFDV
DLPELPQLRE RLEQARWLEA VQLASAQPNT LTLEAMRRLI DQGVGLAPHP SVEKAMARLQ
EQLTLSEHWE EKASSLLKAR PPHSIETLSA AAEKASVIPA HLPNCLLLKD TIRKAREWLQ
EAEERQASGC VLVADSLSDM LLRGQAIQVQ LEPLDRLESL MADVQKWKES AAATFLLKDS
TLTLLEVLCP RFEAGAVGSP KRKAKKGKES LKNNKKKPTR LNSLSDVEKA LSETQDSTSA
MATLEELRVR EMETFFSLRA ANESKLLPTA DCMDLKVCFC QKAPMGAMLQ CELCRDAFHS
VCVRDPAESR ETQPWLCPHC QRSEKPPLSK VLSLLASLHD VGVRLPEGDA LNYLVERTLN
WQQRTQQILQ TCNLPELEER PETPPTLTHW VSGCDNTHNN TQAPCLTPEW NRTSHAQTVF
YTEQRCIPLQ GPCSPSPGFK SEARDATTDA MTDAMTASER KAKRRLERDG LPDAESRGKD
KKHSHKRQKV NKKKLQRRPA STSSSPRSDF SQSDDSDEEM AVCPAESCLL PEGDEVNWVQ
CDGRCNQWFH QVCVGVTAET AEKEDYVCVA CSLSDRQTRK
//
