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Database: UniProt
Entry: A0A094HN12_9PEZI
LinkDB: A0A094HN12_9PEZI
Original site: A0A094HN12_9PEZI 
ID   A0A094HN12_9PEZI        Unreviewed;       850 AA.
AC   A0A094HN12;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V501_02058 {ECO:0000313|EMBL:KFZ16800.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ16800.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ16800.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFZ16800.1}.
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DR   EMBL; JPKD01000737; KFZ16800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HN12; -.
DR   STRING; 1420914.A0A094HN12; -.
DR   HOGENOM; CLU_335591_0_0_1; -.
DR   Proteomes; UP000029315; 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   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   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; 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:UP000029315};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          511..620
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          630..748
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          361..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  95465 MW;  0FBF1D252F083CF6 CRC64;
     MPLTTGEREV IEIPDSPTAH PQFVEISDDE VEVIELLDYQ AKQIKPPRIP PIQPAYVPKG
     DGNPESMKSE LADLYTPHDA PMVSLGMAMH IQSFSSDQGH PAGEESCYDV LDRGLGEISR
     EMEKDQSSMT RHTLEVQSQF QAQPKFTATE NHMASMQSME AHQQGGTCTS PIAIIHHVAK
     KTRPQTFLQG KSIRTPERAV PTYNYYVEID RSRLANNTRL PPEPFVINKN SNSKKEVEAA
     LRKSMISCAK LAKRSRGREK LSSIGVYLPQ IRSAYQECRN YLEKEGLYET FGHKDPNHPS
     YHVEKAFGIP LGSFFDLETH AAKPQKSPTV SLDPLAKTLE RYSRESCLIC SAHQCHIHGR
     FDENDSDVNE SDSSDTTDEE NPSNRSSAMY QPYSMPHTRT QTYYREGNSI ENESEGDSDC
     SEQRRLYHCS AACHLNPSNE ELGNEGNWTE DDHASMQELA ASMRTRKNMR ASCLIAPMLG
     KQCSEVHRHL KKLSNQRIEL DDMVPGEGRR SKKFDWRDLK VEYMHEKRSQ PRPCHHPGQN
     CFVAGEKCTC VSNGICCDKF CTCPQSCDAR YHGCTCTGPC PPKKCTCRLL NRECDPDLCH
     KCSVAESVRT QGPISNTKCH NCEIQRGEGK KVLVGESSIE GIGNGLYLAE PVQTGDFIAE
     YVGEIIDNAE VERRDDFQKR IGNSYIFNLN AEVAIDSMWF GNATRFINHS EVGKNCQAKV
     LLVNSEHRIG FYATESLDAG EELFFDYGKE FKRIEKLKDG VGSSNAERKS AKQQGTEPQE
     SPIENTKGGT GDGADEDDER DDIFEDSPDW LATATKGNRA RDDDEDYIEP GSQQGPKRAR
     PALRNTRGRR
//
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