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Database: UniProt
Entry: A0A3B4DR34_PYGNA
LinkDB: A0A3B4DR34_PYGNA
Original site: A0A3B4DR34_PYGNA 
ID   A0A3B4DR34_PYGNA        Unreviewed;      1404 AA.
AC   A0A3B4DR34;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE            EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000025419.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000025419.1}
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(27)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC         Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, 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=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};
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 UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR   RefSeq; XP_017568434.1; XM_017712945.1.
DR   STRING; 42514.ENSPNAP00000025419; -.
DR   Ensembl; ENSPNAT00000007666.1; ENSPNAP00000025419.1; ENSPNAG00000010594.1.
DR   GeneID; 108436446; -.
DR   CTD; 569207; -.
DR   GeneTree; ENSGT00940000166518; -.
DR   OMA; CENNRSH; -.
DR   OrthoDB; 20251at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   Gene3D; 1.20.58.1370; -; 1.
DR   Gene3D; 2.10.110.20; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR046941; KDM6_GATAL_sf.
DR   InterPro; IPR048562; KDM6A_B-like_C-hel.
DR   InterPro; IPR048560; KDM6A_B-like_GATAL.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR14017:SF9; LYSINE-SPECIFIC DEMETHYLASE 6A; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF21322; KDM6_C-hel; 1.
DR   Pfam; PF21326; KDM6_GATAL; 1.
DR   Pfam; PF13432; TPR_16; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS50005; TPR; 3.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          96..129
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          133..166
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          321..354
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1098..1261
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          438..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..839
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..941
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1404 AA;  153466 MW;  A0F5ED88FD571233 CRC64;
     MQSCRVSLAV AACAAARSLG AAGDEEKKMA AGKASETEED FPRLTAQERD SLAGIDSSLF
     GFLRLHEDGA RTKALLLKAV RCYDSLILKA EGKVDPELFC QLGHFNLLLE DYPKALSAYQ
     RYYSLQSDYW KNAAFLYGLG MVYFHYNAFQ WAIKAFQEVL YIDPGFSRAK EIHLRLGLMF
     KVNTDYESSL KHFQLALIDS NHCTLSKAEI QFHIAHLYEI QKRYRAAKEA YESLLKTENL
     PAQVKAATLQ QLGWMHHTVE QLGDRSNKDS YAIQCLQKSL EADPNSGQSW YFLGRCYSSI
     GKVQDAFISY RQSIDKSEAS ADTWCSIGVL YQQQNQPMDA LQAYICAVQL DHSHAAAWMD
     LGTLYESCNQ PQDAIKCYIN ATRSKGCSNT AALTARIKYL QAQLCNLQHT SLQSKSKMLP
     SIEEAWSLPI PAELTSRQGV QNTAQQACKP HPSAGGGLTG AHGSGQSLPP HVSPLGHGEE
     QSSPAKRKRT SSPAKSSAEW GSSPAQQTPS WYLSPQKLQL LEQLRANKAN LKPVQMQRLE
     QLEAQLSAMQ LHQQQMRQNA SGQVRPTLPN GPTAGPSLPV QIHSRGPAVR PPCTAQPLAN
     GPFSASPSSV PRTGPHPSSV GNNHMPGTGT NGDVPYLHPN ALPHNCTSPS DTWKSQHLNS
     TQGLQKGSHW AGPNGDRALS SSASADGGPH NQVGHSSTTH VDPSEPAVNH LSSPTPSSAS
     SPASSSVHTA TSGAPLTKES DHPQGNGSTA ANHHSPSHTP TSTSTSGSPA THSSDNPQLS
     ALLACKESPA TGPRVNHIHP AVTLPAPGSS AASSPASALS TTSPSPRANE LTASLNKPGS
     TTPGPPPAVT VNGSGGGVCS EDSQSPLKAE PPEVCLKPAP PHRPSHSSST VSIYPTSSDI
     LKACRNLGKN GLSSSSILLD KCPPPRLPPP PSPPLPKDKL NPPTPSIYLE NKRDAFFPPL
     HQFCTNPSNP VTVIRGLAGA LKLDLGLFST KTLVEANPEH LVEVRTQLCQ PADENWDTSG
     TRKQWRCESS RSLTTIAKYA QYQAASFQES LREENEKKGQ KELSDSEMSS SENVARRRKG
     PFKQIKFGTN IDVSDEKKWK LQLQELSKLP AFARVVSAGN LLSHVGHTIL GMNTVQLFMK
     VPGCRTPGHQ ENNNFCSVNI NIGPGDCEWF AVPEPYWGVM SEFCEKNNIN FLMGSWWPNL
     EDLYEANVPV YRFIQRPGDL VWLNTGTVHW VQAIGWCNNI SWNVGPLTAH QYKLAVERYE
     WNKLQSVKSA VPMVHLSWNM ARNIKVSDHK LFEMIKFCLL RTLKQCQTVK ESLVASGKET
     IWHGRSRDEP ARYCTICEVE VFNLLFVTSE SYSRKTFVVH CQDCARKGSS DLDGFVVLEQ
     YRMEDLMQVY DQFSLAPPLH SSSS
//
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