ID A0A0Q3PUG5_AMAAE Unreviewed; 1170 AA.
AC A0A0Q3PUG5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=AAES_32639 {ECO:0000313|EMBL:KQL08872.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL08872.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL08872.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL08872.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KQL08872.1}.
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DR EMBL; LMAW01000570; KQL08872.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3PUG5; -.
DR Proteomes; UP000051836; 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 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 Methyltransferase {ECO:0000313|EMBL:KQL08872.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transferase {ECO:0000313|EMBL:KQL08872.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 116..158
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 244..410
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 866..979
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 555..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 133683 MW; CB0DC2E0EB954AFA CRC64;
MGMAAGTELR KRNRQVSEKH VWYSRLWAAV LGRGGREEAF RRIRQLPRVL ECIQYRGQSG
HHLANEMVPK SIFGRKIVSS LVWFKARKFW FPAAGLKGTA MSAVVSDSPP NPSCKIMTFR
PSMDEFREFN KYLVYMESQG AHRAGVAKVI PPKEWKPRKH YDDIEDLVIP APIQQMVTGQ
SGLFTQYNIQ KKPMTVKEFK QLANSTKYCA PRYVDYEDLE RKYWRNLTFV APIYGADING
SIYDEGIEEW NIAHLNTILD VVEEECGISI EGVNTPYLYF GMWKTTFAWH TEDMDLYSIN
YLHFGEPKSW YAVPPEHGKR LERLAQGFFP SSSHGCDAFL RHKMTLISPS ILKKYGIPFD
KVTQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATFRWID YGKAAKLCTC RRDMVKISMD
VFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ESTPEVNTWL QRRKKIKKFP KSFPHTKSRS
KKLKTPEDKR VSAMVAGAEI TGTEAATDGF KVSEEPGEKV RLVNAEVPSG GKDDSSRMQL
NQHLLDHVKV AGSIHSDSFS RPVPVXEKTK REDENRTDSS HPLAFEVSVA CMPASDSYKE
EESLTSQNQS VSPIPCHKSE GQASEAENPD EEENVFIDDD VSKLESCGSM LEHGEVPVVK
NDEKDGMETS SSVEVERVKI SKSWRHPLNK PPTRSPMTLV KQQTTSDEEL PETTLIEDKV
QETELWARPL VYLWQTGVPN FNAEKEYNAA CAKKEPHCAI CTLLMPYYRP DNHDEESPAF
REANSAETLM AENKKTKPLI PEMCFIYSEE NTENYPSNAF IEEDGTSLLI CCAKCCVRVH
ASCYGVPSHE IRNEWLCSRC RKEAWTAECC LCNLRGGALK QTTDNKWAHV ICAVAIPEVR
FGNVTXRTAI DTSRIPLQRL KLKCVLCRQR IKKISGACIQ CSYGRCPASF HVTCAHAAGV
LMEPDDWPYV VYITCFRHKI NQNVRAKACE KGIRVGQTVI TKHRNTRYYS CRVIRVTSQL
FYEVVFDDGS FSLDTFPEDI VSRDCLRLGP PAEGEVVQVK WPDGKLYGAK YVGTNTTYMY
QVEFEDGSQI VMKREEIYTL DEELPKRVKA RFSTASDMRF EDTFYGADII LGEKKRQRVL
SSRFRNEYVD DPGYRTFLKS SFXKESRKGL
//
