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Database: UniProt
Entry: A0A3Q3W480_MOLML
LinkDB: A0A3Q3W480_MOLML
Original site: A0A3Q3W480_MOLML 
ID   A0A3Q3W480_MOLML        Unreviewed;      1626 AA.
AC   A0A3Q3W480;
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};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000003259.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000003259.1}
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; 94237.ENSMMOP00000003259; -.
DR   Ensembl; ENSMMOT00000003311.1; ENSMMOP00000003259.1; ENSMMOG00000002608.1.
DR   OMA; GFDQVCK; -.
DR   Proteomes; UP000261620; 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:UP000261620};
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          13..54
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          78..168
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          228..278
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          372..538
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1096..1156
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1531..1585
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1255..1280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1466..1507
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1626 AA;  185159 MW;  6C950F24F31F14F2 CRC64;
     MSAFPEFVPP PECPVFEPSW EDFSDPLGFI NKIRPIAEKT GICKIRPPED WQPPFACDVR
     NFRFTPRVQR LNELEALTRV KLNFLDQIAK FWELQGSKIR FPHVERKVLD LYQLSKTVSS
     EGGFETVCKE KRWSKVASRM SYPQGKGTGS LLRSHYERIL YPYELFQSGA TLTVSGTEEN
     KEPKGLKIFG TNPKMVGLEI VSRHLKAQAF AIKMRPRKET LEVNFIDLYL CLVCGRGDEE
     DRLLLCDGCD DSYHTFCLIP PLQDVPKGDW RCPKCVAEEC SKPREAFGFE QAVREYSLQS
     FGEMADQFKS DYFNMPVHMV PTELVEKEFW RLVSSIEEDV IVEYGADISS KDVGSGFPVR
     DGKRRLLGDE EDYANSGWNL NNMPVLEQSV LTHINVDISG MKVPWLYVGM CFSSFCWHIE
     DHWSYSINFL HWGEPKTWYG VPASAAEQLE AVMKKLAPEL FDSQPDLLHQ LVTIMNPNVL
     MEHGVPVYRT NQCAGEFVVT FPRAYHSGFN QGYNFAEAVN FCTADWLPMG RQCVAHYRRL
     HRYCVFSHEE LLCKMAADPE SLDVELAAAV LKEMGEMMEE ETKLRGAVQG LGVLSSEQEV
     FELLPDDERQ CHKCKTTCFL SALTCSCSPD RLVCLHHAAD LCDCPLGNKC LRYRYDLEEF
     PSMLYGVKTR AQSYDTWSKR VTEALAADQK NKKDLIELKV LLEDAEDRKY PEKALFRRLR
     EIVKEAETCS SVAQLLLSRK QRHSRLRSES SCNRTKLTVD ELKAFVDQLY RLPCIISQAR
     QVKELLENVE DFHERAQVAL SDEMPDSSKL QALLDLGSGL DVELPELPRL KQELQQARWL
     DEVRVTLAEP QRFTLELMKR LIDSGVGLAP HHAVEKAMAE LQEILTVSER WEDKARACLQ
     ARPRHSMVTL ESIVLEARNI PAYLPNILAL REALQKAKEW TAKVEAIQSG SSYAYLEQLE
     SLLARGRSIP VRLDPLAQVE SQVAAARAWR ERTARTFLKK NSTYTLLQVL SPRVDIGVYG
     NSKSKRKRVK ELMEKERGGF DPDALSDLED CLEEVRDPST VVAAFKAKEQ KEVESIHSLR
     AANLAKMAMA DRIEEVKFCL CRKTASGFML QCELCKDWFH GACVPLPKTG SQKKLGVGWQ
     SNSKDSKFLC PLCQRSRRPR LETILSLLVS LQKLPVRLPE GEALQCLTER VMSWQDQARQ
     ALATEELSSA LAKLSVLSQR MVEQAAREKT EKIINAELQK AAANPDLQGH IQTFQQSGFS
     RATSPRQSLD YDDEETDSDE DIRETYGYDM KDPGEVKPYL FCDEEIPVKS EEVVSHMWPA
     ATPSFCAEHA YSSASKSCVQ NISTPRKQPR KTPLVPRSLE PPVLELSPQA KAQLEELMML
     GDLLEVSLDE TQHIWRILQA THPPSEERFL QVMEPDDSLM EKPLKIKIKD SEKKRKRKLE
     RAEHHHMVGL ELVLGGKSKK KKLKLNMDKN REMKQLAKRL AKEEKERKRK EKAAAKAEAI
     REGLEKRKEK KILDIPSKYD WSGAEDSNDE NAVCAAKNCQ RPCKDKVDWV QCDGGCDEWF
     HQVCVGVSCE MAENEDYICM DCSRKAAGVS AGGAIKSNQI PLSSLNSYTT KFKPCRGYCF
     PPFVYN
//
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