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Database: UniProt
Entry: A0A2U3WNG9_ODORO
LinkDB: A0A2U3WNG9_ODORO
Original site: A0A2U3WNG9_ODORO 
ID   A0A2U3WNG9_ODORO        Unreviewed;       738 AA.
AC   A0A2U3WNG9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN   Name=EZH1 {ECO:0000313|RefSeq:XP_004410618.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004410618.1};
RN   [1] {ECO:0000313|RefSeq:XP_004410618.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-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_004410618.1; XM_004410561.2.
DR   AlphaFoldDB; A0A2U3WNG9; -.
DR   GeneID; 101379551; -.
DR   CTD; 2145; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000245340; Unplaced.
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   CDD; cd00167; SANT; 1.
DR   CDD; cd19217; SET_EZH1; 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; IPR044438; EZH1_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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EZH1; 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   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340};
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          495..597
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          604..719
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          179..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  84355 MW;  1B99C62D1D008569 CRC64;
     MDMPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQL MKPCTIESIF PGFASQHMLM RSLNTVALVP IMYSWSPLQQ NFMVEDETVL
     CNIPYMGDEV KEEDETFIEE LINNYDGKVH GEEEMIPGSV LISDAVFLEL VDALNQYSDE
     EEEGHNDTSD GKQDDSKEDL PVTRKRKRHA LEGNKKSSKK QFPNDMIFSA IASMFPENGV
     PDDMKERYRE LTEMSDPNAL PPQCTPNIDG PNAKSVQREQ SLHSFHTLFC RRCFKYDCFL
     HPFHATPNVY KRKNKEIKIE PEPCGTDCFL LLEGAKEYAM LHNPRSKCSG RRRRRHHMVS
     ASCSNTSASA VAETKEGDSD RDTGNDWASS SSEANSRCQT PTKQKASPAP PQLCVVEAPS
     EPVEWTGAEE SLFRVFHGTY FNNFCSIARL LGTKTCKQVF QFAVKESLIL KLPTDELMNP
     SQKKKRKHRL WAAHCRKIQL KKDNSSTQVY NYQPCDHPDR PCDSTCPCIM TQNFCEKFCQ
     CNPDCQNRFP GCRCKTQCNT KQCPCYLAVR ECDPDLCLTC GASEHWDCKV VSCKNCSIQR
     GLKKHLLLAP SDVAGWGTFI KESVQKNEFI SEYCGELISQ DEADRRGKVY DKYMSSFLFN
     LNNDFVVDAT RKGNKIRFAN HSVNPNCYAK VVMVNGDHRI GIFAKRAIQA GEELFFDYRY
     SQADALKYVG IERETDVL
//
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