ID A0A3B5AEQ2_9TELE Unreviewed; 1545 AA.
AC A0A3B5AEQ2;
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:ENSSPAP00000018866.1};
GN Synonyms=LOC103354421 {ECO:0000313|RefSeq:XP_008276011.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000018866.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000018866.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008276011.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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 RefSeq; XP_008276011.1; XM_008277789.1.
DR STRING; 144197.ENSSPAP00000018866; -.
DR Ensembl; ENSSPAT00000019152.1; ENSSPAP00000018866.1; ENSSPAG00000014172.1.
DR GeneID; 103354421; -.
DR CTD; 415256; -.
DR GeneTree; ENSGT00940000157076; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; 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 Reference proteome {ECO:0000313|Proteomes:UP000694891};
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 320..370
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 464..630
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1188..1236
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1485..1539
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 215..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 175555 MW; D665E165EC736119 CRC64;
MSQPRPDEFE PPPECPVFEP SWEEFQDPFT FINKIRPIAE KTGICKVRPP PGWQPPFACD
VDRLHFVPRI QRLNELEAQT RVKLNFLDQI AKFWDLQGCA LKIPHVERKI LDLYKLNKLV
ADEGGFDIVC QDRRWTKIAL QMGFAPGKAV GSHLRGHYER ILYPYNLFQN GANLLAPDPA
SKLMRLEADP ELEKFVQKPV QPVEIAAVKE SLDTKEHKLQ DQAQRQPVQT PDTCPSARRA
KRMKYEAICV KTEPGELGEN KPNLRRRMGS FVAKPEPEKE IPIPVKQEPV EFKEPIIEPD
KFKSRYKKMI PPVPPSPVDL VVCLVCGSGG DEDRLLLCDG CDDSYHTFCL IPPLHDVPKG
DWRCPKCLAQ ECNKPHEAFG FEQAYRDYSL RAFGQMADAF KSDYFNMPVH MVPTELVEKE
FWRLVGAIEE DVTVEYGADI ASKEFGSGFP IPNGKFKVSP ADEKYLKCGW NLNNLAMMNP
SVLTHVTADI CGMTLPWLYV GMCFSSFCWH IEDHWSYSIN YLHWGEPKTW YGAPGFAAEQ
LEEVMKKLAP ELFDSQPDLL HQLVTIMNPN TLMAHGVPIY RTNQCAGEFV ITFPRAYHSG
FNQGFNFAEA VNFCTVDWMP LGRQCVDHYR MLHRYNVFSH DEMVCNMASK AETLNVVLAS
AVHKDMVFMI QEEKELREKV KKMGVLHCKE AKYDHLQDDE RQCAKCRTTC YLSAVTCPCN
PGVLVCLYHI NDLCSCHSSN YTLNYRYTLD DLFPMMTAVK QRAELYDEWA SRVTETLEAK
LEKKKGLPVF RTLLSESESR LFPDNDLLRR LRLVTQDAEK CSSVAQQLLN GKRQTRYRCG
SGKSRSQLTV EELSSFVRQL YNLSCSLPQA PMLKELLNRI EDFQQHSEKV LADEVPSVAE
IQSLLDVSFD FDVDLPELPQ LRVRLEQARW LEGVQQASAQ PATLTLETMR RLIDQGVGLA
PHPSVEKAMA RLQEQLTMSE HWEDKASSLL KASPPHSIET LSAAAEKASG IPAYLPNCLL
LKDTIRKARE WLQEAEELQA TGCIPLVDSL SDMVLRGQAI QVHLEPLDRL ETFMVEVQQW
KESAATTFLP KDSTLTLLEV LCPRCEVGNI GSPKRKIKKG KESPKSNKKK MPRLNTLSDV
EKALSETKDS TSAMATLEEL RAREMEAFSN LRAANESKLL PTADCMDLTV CFCQKAPMGA
MLQCELCRDA FHSVCVRDPS DSHETQPWLC PQCQRSEKPP LSKVLSLLAS LRHTGVRLPE
GDALHYLVER TINWQQRAQE MTQACNLPEL EERPGTPPTL TRWVSGTDDT HNNTQAPCLT
PEWNRTSHAQ TVFYTEQRCI PLQGLSQELE ELMVEGLLLQ VSLPEVQSLY HILLDRASSQ
HSDICMSPSQ EESADKHMQF NSQGTNLPLN QDGAKTMRET VMGSEKKAKR HLEREGLDAE
RRGKDKKHSH KRQKMNKKNP QRRSASTSSS PRSDFSQSDD SDEEMAVCPA ERCQLPEGDE
VNWVQCDGSC NQWFHQVCVG VTAEMAEKED YICVTCTLND GHMRK
//
