ID A0A3Q3FKC3_9LABR Unreviewed; 1434 AA.
AC A0A3Q3FKC3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSLBEP00000019493.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000019493.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000019493.1}
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 STRING; 56723.ENSLBEP00000019493; -.
DR Ensembl; ENSLBET00000020549.1; ENSLBEP00000019493.1; ENSLBEG00000014931.1.
DR GeneTree; ENSGT00940000157076; -.
DR InParanoid; A0A3Q3FKC3; -.
DR Proteomes; UP000261660; 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 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; IPR047981; KDM5B_ARID.
DR InterPro; IPR047978; KDM5B_PHD1.
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; 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; 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:UP000261660};
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 80..170
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 275..326
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 420..586
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1144..1192
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1382..1430
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 185..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 162306 MW; 663289FC3397D4B7 CRC64;
MSQPRPDEFK PPPECPVFEP SWEEFKDPFA FINKIRPIAE KTGICKVRPP PGWQPPFACD
VDRLHFVPRI QRLNELEAQT RVKLNFLDQI AKFWDLQGCA LKIPHVERKI LDLYKLNKLV
AEEGGFDIVC RDRRWTKIAM QMGFAPGKAV GSHLRGHYEK TLYPYNLFQS GANLLVKSVE
SVDTKEHKLQ DQAQRQPAQT PEPCPNARRA KRMKCEVGVV DEECQTPDSK MFPAAEKEIP
IPVKQEPVES KEPVIEAEKP KSRYKKYVAP VPPSGSGCVL VCGSGGEEDR LLLCDGCDDS
YHTFCLIPPL QDVPKGDWRC PKCLAQECNK PHEAFGFEQA YRDYSLRAFG QMADAFKSDY
FNMPVHMVPT ELVEKEFWRL VGAIEEDVTV EYGADIASKE FGSGFPIPNG KFKVSPADEK
YLKCGWNLNN LAMMKPSVLT HVTADICGMT LPWLYVGMCF SSFCWHIEDH WSYSINYLHW
GEPKTWYGAP GFAAEQLEEV MRKLAPELFE SQPDLLHQLV TIMNPNTLMA HGVPIYRTNQ
CAGEFVITFP RAYHSGFNQG FNFAEAVNFC TVDWMSMGRQ CVDHYRMLHR YNVFSHDEMV
CNMASKADTL DVVLASSVHK DMVSMIREEK ILREKVKKMG VFLCKEAKYD HLQDDERQCA
KCRTTCYLSA ITCSCNPGVL VCLHHITDLC SCPVTNYTLN YRYTLDDLFP MMNAVKHQAE
LYDDWSALVT ETLEAKLEKK KGLPVFRSLL AASESKLFPD NDLLRRLRMV TKDAEKCASV
AQQLLNGKRQ TRYRCGNGKS CSQLTVEELS SFVRQLYNLS CSLPQAPLLK DLLNRIEDFQ
QHSEKVLADK VPSVAEIQSL LDVSFDFDVE LPELPRLRVR LEQARWLEGV QQASAQPATL
TLETMRRLID QGVGLEPHPL VEKAMARLQE LLTVSEHWED KASSLLKARP PHSIEILSAA
AEKASAIPAY LPNCLLLKDS IRKAQEWLQE AKELQATGCV LMIDSLSDMV LRGQAIQVHL
EPLDRLESLM VEVQEWKESA AATFLPKDST LTLLEVLCPR CEVGNVGSPK RKAKKGKESP
KSNKKKTPRL NTLSDVKKAL SETKDSTSAM ATLEELRVRE MEAYSNLRAA NESKLLPTAD
SMDLKVCVCQ KAPMGAMLQC ELCRDAFHSV CVRDSSDSCE TQPWLCPQCQ RSEKPPMNKV
LSLLASLRRL GVRLPEGDAL HYLVDRTVNW QHQSQLISQS CNLPELEERP GTPPTLTRWA
SAPCLTPEWN RTSHAQTVFY TEQRCIPLQG LSQDLEELMV DGLLLQVSLP EVQSLYHVLL
DRASSQQTNR CMSPPQDESA DCDQHTQFNS QGKNLPLNQT RKRKSDNDVP HTRTAFAPLC
ESILCVCVCL QVDWVQCDGS CNQWFHQVCV GVTAEMAEKE DYICVTCTMN DGHE
//
