ID A0A3Q3RSB5_9TELE Unreviewed; 1471 AA.
AC A0A3Q3RSB5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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 Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000008610.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000008610.2}
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; 205130.ENSMAMP00000008610; -.
DR Ensembl; ENSMAMT00000008837.2; ENSMAMP00000008610.2; ENSMAMG00000005781.2.
DR GeneTree; ENSGT00940000157076; -.
DR Proteomes; UP000261640; 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:UP000261640};
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 34..75
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 99..189
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 274..324
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 418..584
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1151..1199
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1412..1466
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1331..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1471 AA; 167156 MW; 92E98987280A5D71 CRC64;
MQVAVCYAAC HALPPADATM TQPQLNEFIP PPECPVFEPS WEEFADPFAY INKIRPIAEK
TGICKIRPPP EWQPPFACDV DRLKFTPRIQ RLNELEAQTR VKLNFLDQIA KFWELQGCTL
KIPHVERKIL DLYQLNKLVN EEGGFDAVCK DRRWTKISVK MGFAPGKAIG SHLRAHYERI
LYPYNLFQTG SNLPKATLTN DTKDKEYTPH DLPQRQSVQP QETCSIARRA KRMKSEVSLV
KAEPGEFCKT RPNLRRRMGT YVSYQKNCFT QVDHYMCLVC GSGSSEDRLL LCDGCDDSYH
IFCLIPPLHD VPKGDWRCPK CLAQECGKPP VAFGFEQAGR SYTLQAFGDM ADSFKSDYFN
MPVHMVPTEL VEKEFWRLVS TIEEDVTVEY GADIASKEFG SGFPVRNSHF QVSPEDEHYL
TSGWNLNNMP VLDASVLTHV TADICGMKLP WLYVGMCFSS FCWHIEDHWS YSINYLHWGE
PKTWYGAPGY AAEHLEAVMK KLAPELFESQ PDLLHQLVTI MNPNTLMNNG VPIYRTNQCA
GEFVITFPRA YHSGFNQGFN FAEAVNFCTM DWLPIGRNCV KHYRQLSRYC VFSHDEMICN
MACKADTMDV DLASAIHKDM TTMIQEEEEL RQKTKKMGVV QSRQVDYEVL PDEERQCCKC
WTTCYLSGIT CACSPQKTVC LYHTQNLCSC PQSNLTLHYK FTLDELYSMM VSIKLRAESY
KDWVRSVEEI LENKGNKKRE NEKNLHSLVE QAETKVFSHT SLLDQLRTVT SEADKVAVVA
QQLLNGKRQT RYRSGGGKSQ NQNELTVEEL RGFVRQLDSL PCNIRQAPLL KDLLTRVDDF
QQRSERLLSD ESPSPLELQD LLDVSLGLDV ELPQLPLLRE RLEQARWLEA VHQASGRPDS
LCLDTMRRLI DQGVGLAPHS SVERAMARLQ ELLTVSEQWE ERVLSLMEAR PYHSLDTLDA
ALQEVENIPA YLPNCLQLKD VVTKAKKWLH EAEALQVKYT CTYLGGRIPV LESLSELVLR
ADGIPVKLDP LSRLEALIND VQMWKESAAK TFLLKNSPFS LLEVLCPKCD IGAGYQKSRS
KKIKEAPQIS KKSSTKLESV CDVERALSES KDSASAMVTL AEVRQREMEI LLALRASNES
KFLPGENCYA LSVCVCQKAP SGAMVQCELC RDIFHCGCVE TTVDLEYGQA WLCPLCQQSR
KPPLDKVLPL LASLQRIRVR LPEGDALRFL IERTVRWQHR VQQACTEGVL EKVSKMVSAS
KVVPRISSHL SQEINGSSFY TEHQSVPLQG LGPELEELMV EGFLLQVTLP ETEQLYRYLL
YKLAPLPSHS TPCGGNTEQD QQSPRGSPEH NKVTQHLKQW LLRKESSDSQ HSEKAKKCRK
KSKKSKERSE ESQSSPTHSV SDPAPSDSEE DYSLCAAPWC REPEGDEVNW VQCDGSCNQW
FHQICVGLSA ERAEKEDYIC ISCSQKSLTL I
//
