ID W9XEW2_9EURO Unreviewed; 1048 AA.
AC W9XEW2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O5_00372 {ECO:0000313|EMBL:EXJ75865.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ75865.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ75865.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ75865.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) 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:EXJ75865.1}.
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DR EMBL; AMGX01000001; EXJ75865.1; -; Genomic_DNA.
DR RefSeq; XP_007739182.1; XM_007740992.1.
DR AlphaFoldDB; W9XEW2; -.
DR STRING; 1182543.W9XEW2; -.
DR GeneID; 19185109; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_003620_0_0_1; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000019471; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 617..729
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 744..862
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..158
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1048
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 118423 MW; E7B12BCBA5C311AB CRC64;
MTISARNTSS ETTKQTTLQK GQSSSESDSD DSSEDEISDS SNPDPDQEPP LRLVFRPQPS
QNSDAEQEAP TEKQSQKSRV IEVEKDESVE EDGGAEGSSA VSGEDEDDDC ISVSSDSSVE
SIEKATFRPS VKSFTNLLKR IRQQLREYQQ TNVLADLRQA TIDARKYSGP KLDPSLPYPF
KTLTEERRRG WDPDAEENKD VEVIPAPQKW DHTGSIILPK AKSIGRVNSS FLAPNVRIAT
HRAYDDEDED DPDSSIKYEE FELRYKTDFQ GMEQQRLCQE LIYLWEPWVE ELLKRLRIQK
SDVLYFFTQD HFEPDRQIEF KCCEGSRTAW RTEQKSVCNT CKLADPQSRQ SYLGEGFKRL
PRPDDRSLVF AGLAARAFHK MTGSSLWHIA LGSTIQPRNM DSEAATTQDP GFCLICFRHQ
CPDHGSYEEP PDDDEGPETS RAFINDDESD RNVRKFVSLP RAKRDVENKS HICGIFCVES
STNLRQILGR QLNGNISGES RPPENYIRPI LADDHLCSSS CFWDVTNRRD ITVSEVEFRP
FVSESQKISV EKLMGFYLYN KRGPCLISRV IKEVSCMMIF NHIIFAIFRV KHPPNPCPIA
TNTSPTRGGS SQMARGKKKP AQIIDVSRSS DLEKREPFFP CSHEGPCINN PACSCATSKV
HCERFCGCDE SCKRRFRGCT CKAGGNKICF EDNRCECWKI NRECDPHLCG RCGVLEVLDS
FNKYRDDIRK GRCRNNRIQL GVPANTTRAP SQVQGYGLYA LTNIPSGDFI GEYVGEIISK
TEGDRRGALY HLRNQEYLFA LNATQEIDAS NHGNKMRYMN NSLKEENVNV EPKSLWCNGQ
ARIGLFARRR VNAGEELLWT YGYSEEHVKN FWEPGEKPAS DRALLPYSAE RVTRTTGTDK
LAKATGDNAR EDRSSQSRVL RQQLKRRRED GQSTGAGSGA DEEAAHSSTN GSTGGPADEA
TQDPPIEDAE DSDYEARGHV SDDGDLGEDE RDVESDLDGS RKRRTKVQQR NRTSNNGAGE
RWRTSGAKDK RGRERARNHK HGKRKAEF
//
