ID A0A2P8A1H7_9PEZI Unreviewed; 1578 AA.
AC A0A2P8A1H7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B9Z65_3425 {ECO:0000313|EMBL:PSK54306.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK54306.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK54306.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK54306.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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:PSK54306.1}.
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DR EMBL; NHZQ01000083; PSK54306.1; -; Genomic_DNA.
DR STRING; 40998.A0A2P8A1H7; -.
DR Proteomes; UP000243723; 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:UP000243723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1095..1204
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 1219..1340
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1578 AA; 173050 MW; 02121A068088A4FC CRC64;
MSLNSHSAPI VISDDDDRSP ARQFLKKTSS THGSPFPFIG SLAASNPIIP TLPDDEAQLP
PQSSHLSNGT RTSTTKSSTA RDSAGRSHLS NGARLSTSKS STAEDSPRPS NVSKGSRPNT
DKSSAGKQSA WPSTSLNGAS SSDSKSFTED SPRPSTSSKG TRPSTSKSSA VGGNTSRFNG
QIDATGTNSH ADATGVDSQT DTPRQGQKRH RPDGVYREAI GDLRAKKRLK GSNSTLDLHA
DRPSVESPTD GSDSALSIET QAFKAGISPS LQARINANHK TTAHLVSHVR GKSNGLPKSA
LLGPTSRFSD SSSSSPKPTS NRSSLPSSGT SKRQMEGPSS KHATERKPVD HNNAAMSHKD
KHADPSLALL SKEKHTTPLL PPFGGTAGLA SSSGLTSRLD RPQSVIKAAL VSAAGASSPM
GNGISESSTP KQQDRVRNGF AAAKNSNSPI ARPANKSLPD HRSQNGSLVS SDSQPSPLHH
QIRDLQSQKS KAYTGPNGPE NTEFDRILKS VSSIQDRNQS RRKETSSSSI GNKRITYKGT
THDTGKSRRN DSEASTLAGA KDEALSTNIA RSTKDHSARH IAHIEKIGNA ANVADSPLLL
DTNGRKGAHS VISFGPAPAT LSPHSTSTQG EAGARESSME PARSLQLRTE AVQMRTPESS
RAVTPKKALT DVTNNNNSTK SPSARAPIVE MPPPDLPNST ISRLIANKSD VEEVLDRCFN
TLAEEQKYTV KNALTKARSL RTALENSDFL AKQPRRVFDE EILDRCYVNG MIGAKTISPF
ASMKPMHKAA NGKPDSTFNC ITVETLEPGA KRIKGPSYVL GCQPTRWTDT AKTTPAYTQC
TAVKKNVAAP NQKVLHSYPY FGENVDDKVY EALHSRYDVD ARQRERKVAD GQQSRRLMTH
THQWLEQIGC SERNVLFYLL NRNTSADQKN VYTDRERSCK HDFNREADHW TSVFKKVSDP
APSPEKVQLA AWACTVFLAK TKLSLWQIVR KSHIASPDED ETSKEGTSIL DKTQQLACRI
CHEHDCPYHI DFMENSDFED DTASLASVEA LDVDWPPEYN FKRHVTIAQP LSERPDSRDE
IVVAGRPASR DKNAYKRLLE QVIETSNHDR NRYYPCYHPG KSCADEECKC YRDGVLCEKA
CGCSSTCERK FQGCSCASGN RKTCYQDDRC DCFRLHRECD ADLCKDCGAD IVLDPENRHD
DSIRPRHCQN VNMQLGIPKR TILGRSRIHG FGVYAGERIK RHDFVGEYSG EIVLEGERNR
RGEVYDIQKM SYLFILTSDQ EIDSHHVGNK MRFVNHASTT GKNGACNLRP EIVICNMTPR
IGMYATRDIE TGEELFFNYG DHYMQLLRDA NAATADDRDA VVASGRGGKE KVGKRGRKKK
VAQMRRKKNT DLTIGFAEPE YEDLEVEVAG EGVRSKKVTP RWKGKGKAGA PVGEWEPPGE
RPLRVREMAS KSAAGSRLGS SAEDEEGNGE EVAESEDEVV GGEIEAEKEV DESPIKVGRR
GSKKRLTEEV EESDFEMGED EDDDLPRRRS SVRSGKRTTY ALDDEDEDED ERPRKKYVAP
IINGKKKRGR PKKSMLED
//
