ID A0A093P8W1_PYGAD Unreviewed; 1637 AA.
AC A0A093P8W1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=AS28_09096 {ECO:0000313|EMBL:KFW73388.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW73388.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW73388.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW73388.1};
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; KL225530; KFW73388.1; -; Genomic_DNA.
DR STRING; 9238.A0A093P8W1; -.
DR Proteomes; UP000054081; 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:KFW73388.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFW73388.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 30..120
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 238..288
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 382..548
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..1293
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 COILED 1486..1513
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW73388.1"
FT NON_TER 1637
FT /evidence="ECO:0000313|EMBL:KFW73388.1"
SQ SEQUENCE 1637 AA; 186511 MW; 2F78E2AC2940616E CRC64;
QDWQPPFACE VQSFRFTPRI QRLNELEAMT RVKLDFLDQL AKFWELQGSN LKIPVVERKI
LDLYALSKIV ANKGGFEVVT KEKKWSKVAS RLGYLPGKGT GSLLKSHYER ILYPYELFQS
GVSLMGIQKP NLDLKEKVEA EDLSSDAQAS PKQASRMNVV LKRTRRVKSQ AEAGEMSRNT
ELKKLQIFGA GPKMMGLALG AKDKEDEVTR RRKGTRSEAF GMQMRQRKGT LSVNFVDLYV
CLFCGRGNNE DKLLLCDGCD DSYHTFCLIP PLPDVPKGDW RCPKCVAEEC NKPREAFGFE
QAVREYTLQS FGEMADNFKS DYFNMPVHMV PTELVEKEFW RLVSSIEEDV IVEYGADISS
KDFGSGFPVK DGRRKLMPEE EDYALSGWNL NNMPILEQSV LAHINADISG MKVPWLYVGM
CFSSFCWHIE DHWSYSINYL HWGEPKTWYG VPSHAAEQLE DVMKELAPEL FESQPDLLHQ
LVTIMNPNVL MEHGVPVYRT NQCAGEFVVT FPRAYHSGFN QGYNFAEAVN FCTADWLPIG
RQCVSHYRRL GRHCVFSHEE LIFKMAADPE CLDVGLAAMV CKEMTLMIEE ETRLRESVVQ
MGVLMSEEEV FELVPDDERQ CTACRTTCFL SALTCSCNPE RLVCLYHPSD LCPCPMQKKC
LRYRYPLEDL PSLLYGVKVR AQSYDTWVSR VTEALSANLN HKKDVIELRV MLEDAEDRKY
PENDLFRRLR DAVKEAETCA SVAQLLLSKK QKHRQSQDSG RTRTKLTMEE LKAFVQQLFS
LPCVISQARQ VKNLLDDVEE FHERAQEAMM DEIPDSSKLQ ELIDMGSGLY VELPELPRLK
QELQQARWLD EVRSTLLDPQ RVTLDVMKKL IDSGVGLAPH HAVEKAMAEL QELLTVSERW
EEKAKVCLQA RPRQSMMALE GIVNEAKNIP AYLPNVLALK EALQRARDWT AKVEAIQNGS
NYAYLEQLES LSAKGRPIPV RLDALPQLES QVAAARAWRE RTGRTFLKKN SSYSLLQVLS
PRTDIGVYGS SKNRRKRAKE LMEKEKEKDL DLESLSELED GLEEARDTAA VVAIFKEREQ
KEIEAMHALR AANLAKMTMV DRIEEVKFCI CRKTASGFML QCELCKDWFH SGCVPLPKTS
SQKKGSSWQA KEVKFLCPLC MRSRRPRLET ILSLLVSLQK LPVRLPEGEA LQCLTERAMS
WQDRARQALA TDELSSALAK LSVLSQRMVE QAAREKTEKI ISAELQKAAA NPDLQGHLTS
FQQSAFNRVI GSVSSSPRQT LDYDDEETDS DEDIRETYGY DIKDNASVKS SSSLEPNLFC
DEEIPIKSEE VVTHMWTAPS FCAEHAYSSA SKSCSQGSST PRKQPRKSPL VPRSLEPPVL
ELSPGAKAQL EDLMMVGDLL EVSLDETQHI WRILQATHPP SEDRFLHVME DDSMDEKPLK
MRGRDSSERK RKRKLERAEQ FFGDMKQKSK ELKKLEKPKK KKLKLTMDKT KELNKLAKKL
AKEEERKKKR EKAVVTKVEL AKESTEKKRE KKVLDIPSKY DWSGAEESDD ENAVCAAQNC
QRPCKDKVDW VQCDGGCDEW FHQICVGVSP EMAENEDYIC INCAKKPMQG PSSPAHAPPP
PFLLSYKLPM EDLKETS
//
