ID A0A091S0Q8_NESNO Unreviewed; 1636 AA.
AC A0A091S0Q8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
DE Flags: Fragment;
GN ORFNames=N333_01422 {ECO:0000313|EMBL:KFQ49197.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ49197.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ49197.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ49197.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK938954; KFQ49197.1; -; Genomic_DNA.
DR Proteomes; UP000053840; Unassembled WGS sequence.
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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KFQ49197.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFQ49197.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 29..119
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 237..287
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 381..547
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1106..1163
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1552..1606
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1272..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1486..1513
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ49197.1"
FT NON_TER 1636
FT /evidence="ECO:0000313|EMBL:KFQ49197.1"
SQ SEQUENCE 1636 AA; 186460 MW; 1347993CD2817550 CRC64;
DWQPPFACEV QSFRFTPRIQ RLNELEAMTR VKLDFLDQLA KFWELQGSNL KIPVVERKIL
DLYGLSKIVA SKGGFEVVTK EKKWSKVASR LGYLPGKGTG SLLKSHYERI LYPYELFQSG
VSLMGIQKPN LDLKEKVEAE DLSSDAQASP KQASRMNVVL KRTRRVKSQA ETGEMSRNTE
LKKLQIFGAG PKMMGLALGA KDKEDEVTRR RKGTRSEAFG MQMRQRKGTL SVNFVDLYVC
LFCGRGNNED KLLLCDGCDD SYHTFCLIPP LPDVPKGDWR CPKCVAEECN KPREAFGFEQ
AVREYTLQSF GEMADNFKSD YFNMPVHMVP TELVEKEFWR LVSSIEEDVI VEYGADISSK
DFGSGFPVKD GRRKLMPEEE DYALSGWNLN NMPILEQSVL AHINADISGM KVPWLYVGMC
FSSFCWHIED HWSYSINYLH WGEPKTWYGV PSHAAEQLED VMKELAPELF ESQPDLLHQL
VTIMNPNVLM EHGVPVYRTN QCAGEFVVTF PRAYHSGFNQ GYNFAEAVNF CTADWLPIGR
QCVSHYRRLG RHCVFSHEEL IFKMAADPEC LDVGLAAMVC KEMTLMIEEE TRLRESVVQM
GVLMSEEEVF ELVPDDERQC TACRTTCFLS ALTCSCNPER LVCLYHPSDL CPCPMQQKCL
RYRYPLEDLP SLLYGVKVRA QSYDTWVSRV TEALSANLNH KKDVIELRVM LEDAEDRKYP
ENDLFRRLRD AVKEAETCAS VAQLLLSKKQ KHSRQSQDSG RTRTKLTMEE LKAFVQQLFS
LPCVISQARQ VKNLLDDVEE FHERAQEAMM DEIPDSSKLQ ELIDMGSGLY VELPELPRLK
QELQQARWLD EVRSTLLDPQ RVTLDVMKKL IDSGVGLAPH HAVEKAMAEL QELLTVSERW
EEKAKVCLQA RPRQSMMALE GIVNEARNIP AYLPNVLALK EALQRARDWT AKVEAIQNGS
NYAYLEQLES LSAKGRPIPV RLDALPQLES QVAAARAWRE RTGRTFLKKN SSYSLLQVLS
PRTDIGVYGS SKNRRKRAKE LMEKEKEKDL DLESLSELED GLEEARDTAA VVAIFKEREQ
KEIEAMHALR AANLAKMTMV DRIEEVKFCI CRKTASGFML QCELCKDWFH SGCVPLPKTS
SQKKGTSWQA KEVKFLCPLC MRSRRPRLET ILSLLVSLQK LPVRLPEGEA LQCLTERAMS
WQDRARQALA TDELSSALAK LSVLSQRMVE QAAREKTEKI ISAELQKAAA NPDLQGHLTS
FQQSAFNRVI GSVSSSPRQT LDYDDEETDS DEDIRETYGY DIKDNISVKS SSSLEPNLFC
DEEIPIKSEE VVTHMWTAPS FCAEHAYSSA SKSCSQGSST PRKQPRKSPL VPRSLEPPVL
ELSPGAKAQL EDLMMVGDLL EVSLDETQHI WRILQATHPP SEDRFLHVME DDSMDEKPLK
MRGRDSSERK RKRKLERAEQ FFGDMKQKSK ELKKLEKPKK KKLKLTMDKT KELNKLAKKL
AKEEERKKKR EKAVVPKMEL AKESTEKKRE KKVLDIPSKY DWSGAEESDD ENAVCAAQNC
QRPCKDKVDW VQCDGGCDEW FHQVCVGVSP EMAENEDYIC INCAKKPMQG PSSPAHAPPP
FLLSYKLPME DLKETS
//
