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Database: UniProt
Entry: A0A2U4B8A5_TURTR
LinkDB: A0A2U4B8A5_TURTR
Original site: A0A2U4B8A5_TURTR 
ID   A0A2U4B8A5_TURTR        Unreviewed;       742 AA.
AC   A0A2U4B8A5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH2 {ECO:0000256|ARBA:ARBA00024111};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN   Name=EZH2 {ECO:0000313|RefSeq:XP_019789458.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019789458.1};
RN   [1] {ECO:0000313|RefSeq:XP_019789458.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019789458.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC         COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC         Evidence={ECO:0000256|ARBA:ARBA00000090};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_019789458.1; XM_019933899.2.
DR   AlphaFoldDB; A0A2U4B8A5; -.
DR   GeneID; 101327512; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000245320; Chromosome 9.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd19218; SET_EZH2; 1.
DR   Gene3D; 1.20.58.1880; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR045318; EZH1/2-like.
DR   InterPro; IPR048358; EZH1/2_MCSS.
DR   InterPro; IPR021654; EZH1/EZH2.
DR   InterPro; IPR044439; EZH2_SET.
DR   InterPro; IPR041343; PRC2_HTH_1.
DR   InterPro; IPR041355; Pre-SET_CXC.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   PANTHER; PTHR45747:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE EZH2; 1.
DR   Pfam; PF21358; Ezh2_MCSS; 1.
DR   Pfam; PF11616; EZH2_WD-Binding; 1.
DR   Pfam; PF18118; PRC2_HTH_1; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00717; SANT; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          499..601
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          608..723
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          171..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..186
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  84841 MW;  E60E2A6967904F08 CRC64;
     MGQTGKKSEK GPVCWRKRVK SEYMRLRQLK RFRRADEVKS MFSSNRQKIL ERTEILNQEW
     KQRRIQPVHI LTSCSVTSDL DFPTQVIPLK TLNAVASVPI MYSWSPLQQN FMVEDETVLH
     NIPYMGDEVL DQDGTFIEEL IKNYDGKVHG DRECGFINDE IFVELVNALG QYNDDDDDDD
     GDDPDEREEK QKDLEENRED KESRPPRKFP SDKIFEAISS MFPDKGTAEE LKEKYKELTE
     QQLPGALPPE CTPNIDGPNA KSVQREQSLH SFHTLFCRRC FKYDCFLHRK CSYSFHATPN
     TYKRKNTETA LDNKPCGPQC YQHLEGAKEF AAALTAERIK TPPKRPGGRR RGRLPNNSSR
     PGTPTTNVLE SKDTDSDREA GTETGGEGND KEEEEKKDET SSSSEANSRC QTPIKMKPNA
     EPPENVEWSG AEASMFRVLI GTYYDNFCAI ARLIGTKTCR QVYEFRVKES SVIAPAPAED
     VDTPPRKKKR KHRLWAAHCR KIQLKKDGSS NHVYNYQPCD HPRQPCDSSC PCVIAQNFCE
     KFCQCSSECQ NRFPGCRCKA QCNTKQCPCY LAVRECDPDL CLTCGAADHW DSKNVSCKNC
     SIQRGSKKHL LLAPSDVAGW GIFIKDPVQK NEFISEYCGE IISQDEADRR GKVYDKYMCS
     FLFNLNNDFV VDATRKGNKI RFANHSVNPN CYAKVMMVNG DHRIGIFAKR AIQTGEELFF
     DYRYSQADAL KYVGIEREME IP
//
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