ID A0A3Q2UYD6_HAPBU Unreviewed; 1663 AA.
AC A0A3Q2UYD6;
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=KDM5A {ECO:0000313|Ensembl:ENSHBUP00000002920.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000002920.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000002920.1}
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 Ensembl; ENSHBUT00000011261.1; ENSHBUP00000002920.1; ENSHBUG00000004256.1.
DR GeneTree; ENSGT00940000157170; -.
DR Proteomes; UP000264840; 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; cd16873; ARID_KDM5A; 1.
DR CDD; cd15515; PHD1_KDM5A_like; 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); 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; IPR047974; KDM5A_ARID.
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; PF02375; JmjN; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000264840};
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 18..59
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 83..173
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 249..299
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 393..559
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1127..1187
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1553..1607
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1286..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1488..1529
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1663 AA; 189294 MW; F37A9E3E4791EB61 CRC64;
EAGVYFGGHR RFVPPPECPV FEPSWEDFSD PLGFINKIRP IAEKTGICKI RPPQDWQPPF
ACDVRNFRFT PRVQRLNELE ALTRVKLNFL DQIAKFWELQ GSKIRFPHVE RKLLDLYQLS
KIVSSEGGFE TVCKEKLWSK VASRMGYPAG KGTGSLLRSH YERILYPYEL FQTGATLTVS
GAECCLTAFY IIIGRKTTRE NKEPKTLKIF GASPKMVGLE IVSRHLKAQA FAIKMRPRKE
TLEVNFIDLY LCLVCGRGDE EDRLLLCDGC DDSYHTFCLI PPLQDVPKGD WRCPKCVAEE
CSKPREAFGF EQAVREYSLQ SFGEMADHFK SDYFNMPVHM VPTELVEKEF WRLVSSIEED
VIVEYGADIS SKDVGSGFPV RDGKRRLMGD EEEYANSGWN LNNMPVLEQS VLTHINVDIS
GMKVPWLYVG MCFSSFCWHI EDHWSYSINF LHWGEPKTWY GVPASAAEKL EAVMKKLAPE
LFDSQPDLLH QLVTIMNPNV LMEHGVPVYR TNQCAGEFVV TFPRAYHSGF NQGYNFAEAV
NFCTADWLPM GRQCVAHYRR LHRYCVFSHE ELLCKMAADP ESLDVELAAA VYKEMQEMMD
EETKLRQAVQ EMGVLSSELE VFELVPDDER QCYKCKTTCF LSALTCSCSP DRLVCLHHAK
DLCDCPLGDK CLRYRYDLEE FPSMLYGVKT RAQSYDTWAK RVTEALAADQ KNKKDLIELK
VLLEDAEDRK YPENALFRRL REMVKEAETC SSVAQLLLSR KQRHRGPDIS FLKSLFSINF
SNRNRTKLTV DELKAFVEQL YRLPCIISQA RQVKELLENV EDFHERAQVA LSDEMPDSSK
LQALLDLGSG LDVELPELPR LKQELQQARW LDEVRATLAE PHRVTLELMK RLIDSGVGLA
PHHAVEKAMA ELQEILTVSE RWEDKARACL QARPRHSMAT LESIVLEARN IPAYLPNILA
LREALLKAKE WTSKVEAIQN GSSYAYLDQL ESLLARGRSI PVRLDPLAQV ESQVAAARAW
RERTARTFLK KNSTYTLLQV LSPRVDIGVY GNSKSKRKRV KELMEKERGG FDPDTLSDLE
ENHEEVRDPS TVVAAFKAKE QKEVESIHSL RAANLAKMAM ADRIEEVKFC LCRKTASGFM
LQCELCKDWF HGACVPLPKT GSQKKIGVNW QSNSKDSKFL CPLCQRSRRP RLETILSLLV
SLQKLPVRLP EGEALQCLTE RAMSWQDRAR QALATEELSS ALAKLSVLSQ RMVEQAAREK
TEKIINAELQ KAAANPDLQG HIQTFQQSGF SRATSPRPSV DYDDEETDSD EDIRETYGYD
MKVWEASVKP YLFCDEEIPV KSEEVVSHMW LAATPSFCVE HAYSSASKSC VQNLGTPRKQ
PRKTPLVPRS LEPPVLELSP QAKAQLEDLM MLGDLLEVSL DETQHIWRIL QATHPPSEER
FLQVMEPDDS LIEKPLKIKL KDSEKKRKRK LERLGLGGKP KKKKLKINLE KNREMKQLAK
RLAKEEKERK RKEKAAAKAE AIREGMEKRK EKKILDIPSK YDWSGAEDSN DENAVCAAKN
CQRPCKDKVD WVQCDGGCDE WFHQVCVGVS CEMAENEDYI CMDCSRKAAG GGMTVEEVSE
ESVVVLTTSM CGSSVQSVPS SSVIASWSSA SHHQQQQDSQ QGS
//
