ID A0A3B4WMY6_SERLL Unreviewed; 1458 AA.
AC A0A3B4WMY6;
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};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000006064.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000006064.1}
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 STRING; 1841481.ENSSLDP00000006064; -.
DR Ensembl; ENSSLDT00000006272.1; ENSSLDP00000006064.1; ENSSLDG00000004789.1.
DR GeneTree; ENSGT00940000157076; -.
DR Proteomes; UP000261360; 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); 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; 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 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 272..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 416..582
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1141..1189
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1398..1452
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1062..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 165761 MW; 1B81DC96799A1B7F CRC64;
MSQPQLNEFI PPPECPVFEP SWEEFADPFA YINKIRPIAE KTGICKVRPP PEWQPPFACD
VDRLKFMPRI QRLNELEAQT RVKLNFLDQI AKFWELQGCT LKIPHVERKI LDLYQLNKLV
NDEGGFDAVC RDRRWTKISV KMGFAPGKAI GSHLRAHYER ILYPYNLFQT GANLPKATLT
NDTKDKEYTP HDLPQRQSVQ PQETCSIARR AKRMRSEVSL IFRGCVKTEP GEVCENRPNL
RRRMGTFVAK PEPGKNKDRT VLTIVLCTQV DQYMCLVCGS GSAEDRLLLC DGCDDSYHIF
CLIPPLHDVP KGDWRCPKCL AQECGKPPVA FGFEQAGRSY TLQAFGDMAD SFKSDYFNMP
VHMVPTELVE KEFWRLVSTI EEDVTVEYGA DIASKEFGSG FPVMNSHFEV SPEDKHYLSS
GWNLNNMPVL DASVLTHVTA DICGMKLPWL YVGMCFSSFC WHIEDHWSYS INYLHWGEPK
TWYGAPGYAA EHLESVMKKL APELFESQPD LLHQLVTIMN PNTLMNNGVP IYRTNQCAGE
FVITFPRAYH SGFNQGFNFA EAVNFCTMDW MPIGRKCVDH YRQLSRYCVF SHDEMVCNMA
CKADTMDVDL ASAVQKEMTI MVQEEEKLRE KINKMGVVQS QQVDYEVLPD EERQCSKCRT
TCYLSGITCA CSPGKMVCLY HTQDLCSCPH SNLTLHYKFT LDELYPMMAS VKLRAESYKD
WLCNVQEILE NRGNKKKGLE ELHSLVEQAE TKAFPQTGLV DQLRTVTSEA DKVGVMAQQL
LNGKRQTRYR SGGGKSQNQN ELTVEELRSF VRQLDNLPCT IRQAPLLKDL LTRVDDFRQR
SEHLLSDESP SPLELQDLLD VSLGLDVELP QLPLLRERLE QARWLEAVQQ ASSWPDSLCL
DTMRRLIDQG VGLAPHNSVE RAMARLQELL TVSEQWEERV LSLIEARPYH SLETLDAALQ
EVENIPAYLP NCLQLKDFVT KAKKWLHEAE ALQLGGRIPV LDSLSELVLR AEGIPVRLEP
LSRLEALISD VQAWKESAAK TFLLKNSPFS LLEVLCPRCD VGTGHQKSRS KKTRESPQMN
KKSSTKLESL CDVERALCES RDSASAMTTL AEVHQREMEI LLVLRASNES KLLPAENCCA
LSVCVCQKAP SGAMVQCELC REVFHCGCVE TTSDLEYGQA WLCPLCQRSR KPPLDKVLPL
LASLQRIRVR LPEGDALRFL IERTVRWQHR VQQASPVCST PGSVLKAFPT LHLHITLHSF
CLFYPLTSII FVTGLGPELD ELMVEGFLLQ VTLPETEQLY RYLLYKLAPL PSHSAPCGNN
TEQDQQSQRG SPQHNKVMIT LKTKRRKESS DSQHSDNAKK CRKKKSKKSK ERSEETKRTC
SPTHTVSDPA PSDSEEDYSL CAAPWCREPE GDEVNWVQCD GSCNQWFHQI CVGLSAERAE
KEDYICISCT QPDYKKGE
//
