ID A0A3Q2ZY42_KRYMA Unreviewed; 1430 AA.
AC A0A3Q2ZY42;
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 Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000008861.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000008861.1}
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}.
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 Ensembl; ENSKMAT00000008995.1; ENSKMAP00000008861.1; ENSKMAG00000006485.1.
DR GeneTree; ENSGT00940000164196; -.
DR Proteomes; UP000264800; 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; cd16875; ARID_KDM5C_5D; 1.
DR CDD; cd15604; PHD1_KDM5C_5D; 1.
DR CDD; cd15608; PHD2_KDM5C_5D; 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); 1.
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; 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:SF43; LYSINE-SPECIFIC DEMETHYLASE 5C; 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; 1.
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; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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; 1.
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:UP000264800};
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 304..354
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 447..613
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1249..1280
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 268..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 164134 MW; 25BAB5F62DDC0F6E CRC64;
MQPGNRGEFI PPPECPVFEP SWEEFQDPLG YIAKIRPIAE KSGICKVRPP PDWQPPFSVE
LDSFHFTPRI QRLNELEAET RVKLNYLDRI ARFWEIQGSS LKIPHIERRI VDLYSLSKIV
TDEGGFEMVC KERRWARVAQ RLGYPPGKNV GSLLRSHYER IVYPFEMFQS GASLLVFLHT
FLSHVDKEYK PHSIPLRQSV QPSKMSSYGR RANRCQPDPE PTEEDIEKNP ELKKLQIYGA
GPKMMGLGLV ARDKGLRKKG NWVKMEVKKE ELQDENDKDG DNPDGSKMTM RLRRNPNNPQ
CVDSYVCRMC GRGDDDEKLL QCDGCEENYH SYCLLPPLSD TPKCKWRCPK CVAECKKPSE
AFGFEQATRE YTLQSFGEMA DAFKADYFNM PVHMVPPELV EREFWRLVSC IEEDVTVEYG
ADIHSKEFGS GFPMMNGKKK LTKEEEGYAR SGWNLNVMPV LEQSLLCHIN GDISGMKVPW
LYVGMVFSTF CWHIEDHWSY SINYLHWGEP KTWYGVPSVA AEQLEDVMKK LTPELFEFQP
DLLHQLVTIM NPNILMAHGV PVVRTNQCAG EFVITFPRAY HSGFNQGYNF AEAVNFCTAD
WLPAGRHCIE HYRRLRRYCV FSHEELTCKM AASPEKLDLN LAAATHREMF IIVQEERKLR
KNLMERGITE AEREAFELLP DDERQCDKCK TTCFLSALAC SNCPERLVCL YHTQDLCNHP
TEKLYLRYRY TLDELLAMLH RLKVRSESFD SWANRVKEAL EQEEGNKIEM YYLEKLKIEA
AEKKFPDNEL LRKLNSVLKD IMYCQQTSTD AHLFLPTLTY CSAFREGRIT LQELKSMVDK
MQNLPCVINQ LEEDWRKDSP PPEQLQSLLE EGAKLSVVAP ECDLLQGLKE QGHWLEEVRR
TLGTEGGEKH EVTLDVLRNL MEAGCNVPQS GSVETAMAEL QELLTIAERW EEKAQICLEQ
RQKHPLSTLE AIVNEAQLIP VKLPNILALQ SCLVRARAWV TDLEEIQNGE HYPCLDDLEG
LVAIGRDLPV FMEELRQLEL QVASAHSWRD KATKTFLKKS SQHSLLEVLC PCAKRRNKRV
ETELLEDDSD TNTLGLSAQA LRDPAAIVMA FKEGEHQEKE ALLRLQEVNM CKSGLNTSVC
VCAGQTRAPQ LRCHLCKDWF HGGCVPFPSL LPSSGPPISP LCWWDWDTRF LCPQCQRSRR
PRLETILALL VALQRLPVRL PEGEALQCLT ERAITWQGRA KEALETPELQ QALQKLQELK
ETLHYDAEEE EDEKKEAEGN SVIPSFCFWF LLGVGSLLSL LPRLKGQVVE LSPATRVQLQ
ELQLEGDLLE VSLDQTQTLY RVLQAASDPP RETLHTLIQL EEQRRTRRVR PKESKRKRKG
HRGGSGEEAG EKSHDVLQSK KTCPLKLSPS AHLPVETHTE VILSSSWKYF
//
