ID A0A218VA13_9PASE Unreviewed; 1071 AA.
AC A0A218VA13;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|EMBL:OWK62766.1};
GN ORFNames=RLOC_00008100 {ECO:0000313|EMBL:OWK62766.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK62766.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK62766.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK62766.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK62766.1}.
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DR EMBL; MUZQ01000022; OWK62766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218VA13; -.
DR STRING; 299123.ENSLSDP00000018935; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Methyltransferase {ECO:0000313|EMBL:OWK62766.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Transferase {ECO:0000313|EMBL:OWK62766.1};
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 767..880
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 493..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 122099 MW; C862DF39C260682D CRC64;
MAAVISDSPP NPSCKIMTFR PSMDEFREFN KYLAHMESQG AHRAGVAKVI PPKEWKPRKH
YDDIEDLVIP APIQQMVTGQ SGLFTQYSIQ KKPMTVKEFK DLANSDKYRT PRYVDYEDLE
RKYWKNLTFV APIYGADING SIYDEGIEEW NIAHLNTILD VVGEDCGIAI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAVPPEHGKR LERLAQGFFP SSSQECHAFL
RHKMTLISPS ILKNHGIPFD KVTQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
YGKAAKLCTC RRDMVSISMD VFVRKFQPER YRLWKQGKDF YTIDHTKPTP ESTPEVNIWL
QRRRKKLNFH KSFQHTRSQS KKLKTPEDKR VSAMVADAKI IVTETATDGF KVSEEPEKKM
RAVNTGLASG EEENSSRMHL HQHLLDHVKV AGSIPSDSVL SPVPVLEKTK MEDEDRIDSS
HFSFSLEDSV ASKTASDRCR KEDSLKSQNQ YVSSIPYSKA DKQTSEAENP DREESVSTED
GIGNLENSGS ILEHGEVPIV KKGEEDRVEI SCSEEAETKK ISKSWHNPLH KPPARSPMTL
VKQQATGDEE LPKTTLIEEK IQESEAWAKP LVYLWQTRPP NFNAEKEYNA ACAKKEPHCA
ICTLLMPYYR SDNQDEESPT FNETNSAEIL MAEDVKTKPL IPEMCFIYSE ENTKNYPSNA
FVEEDGRSLL ILCAKCCVRV HASCYGVPSH EIHNEWLCSR CRIEAWTAEC CLCNLRGGAL
KQTTDKKWAH VICAIAIPEV RFGNVTERTP IDTSRIPLQR LKLKCIFCKQ RVKKISGACI
QCSYGRCPAS FHVTCAHAAG VLMEPNDWPC FVYITCFRHK INQNVRAKVC GKAIAVGQTV
ITKHRNTRYY SCKVIGVTSQ VFYEVMFDDG SFSLNAFPED IVSRDCLRLG PPAEGEAVQV
KWPDGKLYGA KYLGTNTADM YQLEFEDGSQ IVMKREEIYT LDEELPKRVK ARLSTASAMR
FEDTFYGADI ILGEKKRQRV LSSRFKNEYV DDPGYRTFLK SSFQKKCQKG L
//
