ID A0A2K5CYR4_AOTNA Unreviewed; 835 AA.
AC A0A2K5CYR4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:ENSANAP00000013821.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000013821.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000013821.1}
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 -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR AlphaFoldDB; A0A2K5CYR4; -.
DR Ensembl; ENSANAT00000031648.1; ENSANAP00000013821.1; ENSANAG00000024798.1.
DR GeneTree; ENSGT00940000154930; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd15577; PHD_JMJD2C; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
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; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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:UP000233020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 38..80
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 166..332
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 774..835
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 392..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 94375 MW; 0582AFCF3511000A CRC64;
VKHYGRPWKM TEDAASDTDR AIMEVAETES PLNPSCKIMT FRPSMEEFRE FNKYLAYMES
KGAHRAGLAK VIPPKEWKPR QCYDDIDNLL IPAPIQQMVT GQSGLFTQYN IQKKAMTVKE
FRQLANSGKY CTPRYLDYED LERKYWKNLT FVAPIYGADI NGSIYDEGVD EWNIAHLNTV
LDVVEEECGI SIEGVNTPYL YFGMWKTTFA WHTEDMDLYS INYLHFGEPK SWYAIPPEHG
KRLERLAQGF FPSSSQGCDA FLRHKMTLIS PSVLKKYGIP FDKITQEAGE FMITFPYGYH
AGFNHGFNCA ESTNFATVRW IDYGKVAKLC TCRKDMVKIS MDIFVRKFQP DRYQLWKQGK
DIYTIDHTKP TPASTPEVKA WLQRRRKVRK ASRSFQCARS TSKRPKAEEE EEVSAEVSGA
EVPDADSSTD DLKVSEKPQE AAKLRNTEVP SEEEASASSM QADQNLSDHI RLSGSSCLSI
SVTEDIKTED DNTYAYRSVC SKPNEADDSI PLSSGYEKPK KSDSLKLSWP KSPESCSSVA
ESNGVLTEGE ESDVESHGNG LEPGEIPAVP SGERNGFKVP SITEGENKTS KSWRHPLSMP
PARSPMTLVK QQAPSDEELP EVLSIEEEVE ETESWAKPLI HLWQTKSPNF AAEQEYNATV
ARMKPHCAIC TLLMPYHKPD ISNEENDARW ETKLDEVVMS EGKTKPLIPE MCFIYSEENI
EYSPPNAFLE EDGTSLLISC AKCCVRVHAS CYGIPSHEIS DGWLCARCKR NAWTAECCLC
NLRGGALKQT KNNKWAHVMC AVAVPEVRFT NVPERTQIDV GRIPLQRLKL GRLGI
//
