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Database: UniProt
Entry: A0A452C8M7_BALAS
LinkDB: A0A452C8M7_BALAS
Original site: A0A452C8M7_BALAS 
ID   A0A452C8M7_BALAS        Unreviewed;      1607 AA.
AC   A0A452C8M7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=KDM5A {ECO:0000313|RefSeq:XP_028019330.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028019330.1};
RN   [1] {ECO:0000313|RefSeq:XP_028019330.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028019330.1};
RG   RefSeq;
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00006801}.
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DR   RefSeq; XP_028019330.1; XM_028163529.1.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd16873; ARID_KDM5A; 1.
DR   CDD; cd15602; PHD1_KDM5A; 1.
DR   CDD; cd15606; PHD2_KDM5A; 1.
DR   CDD; cd15686; PHD3_KDM5A; 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; IPR048615; KDM5_C-hel.
DR   InterPro; IPR047974; KDM5A_ARID.
DR   InterPro; IPR047973; KDM5A_PHD1.
DR   InterPro; IPR047970; KDM5A_PHD2.
DR   InterPro; IPR047972; KDM5A_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:SF17; LYSINE-SPECIFIC DEMETHYLASE 5A; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF21323; KDM5_C-hel; 1.
DR   Pfam; PF00628; PHD; 2.
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; 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; 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:UP000261681};
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          2..92
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          211..261
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          355..521
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1079..1136
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1524..1578
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1248..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1607 AA;  182424 MW;  0FCE92E1EA482858 CRC64;
     MTRVRLDFLD QLAKFWELQG STLKIPVVER KILDLYALSK IVASKGGFEM VTKEKKWSKV
     GSRLGYLPGK GTGSLLKSHY ERILYPYELF QSGVSLMGVQ MPNLDLKEKV EPEVLGTDVQ
     TPPEPGTRVN ILPKRTRRVK SQSESGEVNR NTELKKLRIF GAGPKVVGLA MGVKDKEDEV
     SRRRKVTNRS DAFNMQMRQR KGTLSVNFVD LYVCMFCGRG NNEDKLLLCD GCDDSYHTFC
     LIPPLPDVPK GDWRCPKCVA EECNKPREAF GFEQAVREYT LQSFGEMADN FKSDYFNMPV
     HMVPTELVEK EFWRLVSSIE EDVIVEYGAD ISSKDFGSGF PVKDGRRKML PEEEEYALSG
     WNLNNMPVLE QSVLAHISVD ISGMKVPWLY VGMCFSSFCW HIEDHWSYSI NYLHWGEPKT
     WYGVPSHAAE QLEEVMRELA PELFESQPDL LHQLVTIMNP NVLMEHGVPV YRTNQCAGEF
     VVTFPRAYHS GFNQGYNFAE AVNFCTADWL PIGRQCVSHY RRLRRHCVFS HEELIFKMAA
     DPECLDVGLA AMVCKELTLL TEEETRLRES VMQMGVLVSQ EEVFELVPDD ERQCAACRTT
     CFLSALTCAC NPERLVCLYH PTDLCPCPMQ KKCLRYRYPL EDLPSLLYGV KVRAQSYDTW
     VSRVTEALSA NFNHKKDLIE LRVMLEDAED RKYPENDLFR KLRDAVKEAE TCASVAQLLL
     SKKQKHRQSP DSGRTRTKLT VEELKAFVQQ LFSLPCVISQ ARQVKNLLDD VEEFHERAQE
     AMMDETPDSS KLQMLIDMGS GLYVELPELA RLKQELQQAR WLDEVRLTLS DPQQVTLDVM
     KKLIDSGVGL APHHAVEKAM AELQELLTVS ERWEEKAKVC LQARPRHSVA SLESIVNEAK
     NIPAFLPNVL SLKEALQKAR EWTTKVEAIQ SGSNYAYLEQ LESLSAKGRP LPVRLDALPQ
     VESQVAAARA WRERTGRTFL KKNSSHTLLQ VLSPRTDIGI YGSGKNRRKK VKELIEKEKE
     KDLDLEPLSD LEEGLEETRD TATVVAVFKE REQKEIEAMH SLRAANLAKM TMVDRIEEVK
     FCICRKTASG FMLQCELCKD WFHNSCVPLP KSSSQKKGSS WQAKEVKFLC PLCMRSRRPR
     LETILSLLVS LQKLPVRLPE GEALQCLTER AMSWQDRARQ ALATGELSSA LAKLSVLSQR
     MVEQAAREKT EKIISAELQK AAANPDLQGH LPSFQQSAFN RVASSVSSSP RQTVDYDDEE
     TDSDADIREA YGYDTKDTAS VKSSSSLEPS LFCDEEIPIK SEEVVTHMWT APSFCAEHAY
     SSASKSCSQG SSTPRKQPRX XXXXXXXXXX VLELSPGAKA QLEELMMVGD LLEVSLDETQ
     HIWRILQATH PPSEDRFLHI MEDDSMEEKP LKIKGRDSSE KKRKRKLEKV EQLFGEGKQK
     SKELKKMDKP KKKKLKLSAE KSKELNKLAK KLAKEEERKK KKEKAAAAKV ELVKESSEKK
     REKKVLDIPS KYDWSGAEES DDENAVCAAQ NCQRPCKDKV DWVQCDGGCD EWFHQVCVGV
     SPEMAENEDY ICTNCAKKQG PDSPGPAPPP SFIMSYKLPV EDLKETS
//
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