ID A0A2S6C0N5_9PEZI Unreviewed; 1290 AA.
AC A0A2S6C0N5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_00984 {ECO:0000313|EMBL:PPJ53297.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ53297.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ53297.1}.
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DR EMBL; PNEN01000579; PPJ53297.1; -; Genomic_DNA.
DR STRING; 357750.A0A2S6C0N5; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000237631; 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; 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; 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:UP000237631};
KW Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT DOMAIN 863..984
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 999..1116
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 142354 MW; 98BBFFCCC984FB28 CRC64;
MAAVVDLCSS SDEDDHAPQR IYSSKHPSQN TAARPVPKPV APMKPCLNNK PLSHTHRDRD
STLRDPKPSA RLHSATIQKA RPEDVRHAKD NKISSSAGTF PSGSSLSAHA GHTTPSGFQV
PQFPGSFRSP QRTDSRVLAD SQQRAPKRPY DDDRALPTAS QPQKKRKTAS LSQSSVNTPP
SNAASGSVTV HNRSSTGTAR SDPIDLTGGD EGIKPRNVLS PRHASRKNME SSPLPAQATR
NAPAKAVKDK SPASTRAPTA ATSSARPASP LKPSGIAASL ETLSRDIFTS KAKPVSSPKK
SEPSRTQLGQ PFASNRAPES SGQRERRSTV PETPPLSADA SESRTSSPAK NPRSGEAGLP
SSLANQKVQS IHTELESSRE KRDTERPPRT ATRSKHNEEG TDTRRLNGVG SPRASGISSP
GKLREQPQSA HVIGERGTAQ PTNEMLARAG RRLSGEEKAS QERDTKAQAK RDREPDTAVK
TPKASTVAEP NGQRPTVSTV VAAPHTNSAR VTSNIPQVHG IEKLVGQYIE EMRDDNEHWT
RLELQRARAK FPPRLRESTE ASSVFKKLTP LPLRPLAKKG VPAGCAKFTI ELHTSTSRSP
KASYVVERTN YSTSGTVDVP RYSHYVSIRQ NQLAHNVTTL QHWPYFGDDF DMDEAYSLRR
EFNIDVDERE RKLLRLGQAE NFGPYAEDLI HSIGCEWSDV LTFLLQVAPA VGESDDARKA
LRDRALLASE DCTRNEDRWK KVLTKLPRAD PAKVGKAAVL CDHFQRMAKF SFWHIVRRTA
FVRELVMRSE DHENDDQLTC RVCMRYRCPF HGAIEGQPND QYGSDPDNPV VETDIILPQA
VNFRRRVEFP STIDSEPATI DKRRTLEYWE KGPFGNLKWK ADDRGPFFPC HHPGISCSDA
RCNCYNERIA CEKTCSCGPG CKRKWKGCAC QSSTRANPKA KLVCWDDDRC VCFQKSRECD
PDLCGPCGVA NVLDPVHRHD DRILEGRCRM ASIQRGLAKH TILGDSGVHG LGLYACENMA
RGDFAGEYKG ETITKPEAER RGAVYFHQKL SYLFSLNNAQ EVDSTYFGCK TRFINHVGGT
LANLSPRIIM VNTVFRIGMF ANRLIKAGEE LLFDYGPSFP KDQLGIESAK STLAVKSAPR
VRNAGLVRDN FYDVSLTKDQ DGNIRATKKA TDTGNSDEDE NQSDTSPRRY RLPQRSRSAM
HARRVGASVV PGRPRKAAMA PNEEASESDD EFAAEGAALK DQGDNEDVRM DAQHRLSMYN
LLENNGAEDE DFEPEEDSES EMDLANSDGN
//
