ID A0A663F6P0_AQUCH Unreviewed; 1069 AA.
AC A0A663F6P0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN Name=KDM4C {ECO:0000313|Ensembl:ENSACCP00020020169.1};
OS Aquila chrysaetos chrysaetos.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Aquila.
OX NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020020169.1, ECO:0000313|Proteomes:UP000472275};
RN [1] {ECO:0000313|Ensembl:ENSACCP00020020169.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
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 JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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 AlphaFoldDB; A0A663F6P0; -.
DR Ensembl; ENSACCT00020021045.1; ENSACCP00020020169.1; ENSACCG00020013865.1.
DR GeneTree; ENSGT00940000154930; -.
DR InParanoid; A0A663F6P0; -.
DR Proteomes; UP000472275; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15715; ePHD_JMJD2C; 1.
DR CDD; cd20465; Tudor_JMJD2C_rpt1; 1.
DR CDD; cd20468; Tudor_JMJD2C_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
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:UP000472275};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 16..58
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 144..310
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 766..879
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 502..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 121906 MW; A3EF3AA7668CF507 CRC64;
MAAVISDSPP NPSCKIMTFR PSMDEFRDFN KYLAYMESQG AHRAGVAKVI PPKEWKPRKH
YNDIEDLVIP APIQQIVTGH SGLFMQYNIQ KKPMTVKEFK QLANSDRYCT PRYIDYEDLE
RKYWKNLTFV APIYGADING SIYDEGIEEW NIAHLNTILD VVGEECGISI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAVPPEHGKR LERLAQGFFP SSSQGCDAFL
RHKMTLISPS ILKKYGIPFD KVTQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATIRWID
YGKAARLCTC RKDMVSISMD IFVKKFQPDR YQLWKQGKDI YTIDHTKPTP ESTPEVKTWL
QRRKKIKNFP SFQHTRSRSK KLKTPEDKRV SAKVAGAEII ATEAATDGFK VSEEPGKKVR
LVNTGVPSGE EENRSRMQLD QHLLDSVKVA GGIHSDSYLS PVPVLEKTKM EDKDRTDSNH
PLFTFEDSVA CIPASDSCRN EESLKSQNQS VSSIPYHKSE GQASEAENPD KEENVPIEGD
VSDLESCGNS LEHGEVPVVK KDEEDGMETL SSAEVEKKKV SKSWRHPLNK PPARSPITLV
KQQASSDEEL PETILTEEKV QETETWARPL VYLWQTRVPN FNAEKEYNGA CAKKKPYCAI
CTLLMPYYKP DNHDEESPTF GEANSAETLM AENEKTKPLI PEMCFIYSEE NTENYPSNAF
IEEDGTSLLI SCAKCCVRVH ASCYGVPSHE IHTDWLCSRC RTEAWTAECC LCNLRGGALK
QTTDKKWAHV ICAIAIPEVR FGHVTERTPI DTSRIPLQRL KLKCIFCRQR IKKVSGACIQ
CSYGRCPASF HVTCAHAAGV RMEPDDWPYV VYITCFRHKI NQNMRAKAHK KAITVGQTVI
TKHRNTRYYS CRVIRVTSQL FYELMFDDGS FSLDTFPEDI VSRDCLRLGP PAEGEVVQVK
WPDGKLYGAK YLGTNTAHIY QVEFEDGSQI VMKREEIYTL DEELPKRVKA RFSTASDMRF
EDTFYGADTL GEKKRQRVLS SRFTNEYVND PGYRTFLKSS FQKKSQKGL
//
