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Database: UniProt
Entry: A0A059LE42_9CHLO
LinkDB: A0A059LE42_9CHLO
Original site: A0A059LE42_9CHLO 
ID   A0A059LE42_9CHLO        Unreviewed;       366 AA.
AC   A0A059LE42;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=H632_c3406p0 {ECO:0000313|EMBL:KDD72390.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD72390.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD72390.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD72390.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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   -!- 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:KDD72390.1}.
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DR   EMBL; AYPS01003406; KDD72390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LE42; -.
DR   STRING; 1291522.A0A059LE42; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd10519; SET_EZH; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR045318; EZH1/2-like.
DR   InterPro; IPR041355; Pre-SET_CXC.
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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          114..228
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          235..350
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KDD72390.1"
SQ   SEQUENCE   366 AA;  40577 MW;  2B08F07B58B45292 CRC64;
     RPGLDVSALE ATPLRRRSSD NGDVRDAQPD PGPGSCASPG RRVQQSGEPE WSAAEVELFQ
     QALEVWGPAP CLLAPFVGSR SCCSVHRRLL SLPREVAASP RHARKPKRPT HAKRRHAAVV
     RERLGGPEHE LWNPYQPCAC VGGCHRGTCP CFKSANFCEK FCACNCSECG NRFRGCSCKC
     GAQPGRRCSY KSCPCVAAGR ECDPDLCRDC YPTLHGTHAP GWQCNNFRLR LNQKRRVLVG
     RSVVQGWGAF LDGSAAQGEY LGEYVGELIE HDEADRRGKV YDRDDNSYLF NLNMKHVIDA
     RRCGNNLRFA NHSTNTNCRV NILLVDGDHR VAILASQPLA HGEELFYDYH YEANVAPDWA
     DGKQGK
//
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