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Database: UniProt/TrEMBL
Entry: W3XLH5_9PEZI
LinkDB: W3XLH5_9PEZI
Original site: W3XLH5_9PEZI 
ID   W3XLH5_9PEZI            Unreviewed;       335 AA.
AC   W3XLH5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   SubName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 {ECO:0000313|EMBL:ETS86854.1};
GN   ORFNames=PFICI_00682 {ECO:0000313|EMBL:ETS86854.1};
OS   Pestalotiopsis fici W106-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS86854.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00563877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
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DR   EMBL; KI912109; ETS86854.1; -; Genomic_DNA.
DR   RefSeq; XP_007827454.1; XM_007829263.1.
DR   EnsemblFungi; ETS86854; ETS86854; PFICI_00682.
DR   GeneID; 19265695; -.
DR   KEGG; pfy:PFICI_00682; -.
DR   KO; K11419; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030651};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675,
KW   ECO:0000313|EMBL:ETS86854.1};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533,
KW   ECO:0000313|EMBL:ETS86854.1}.
FT   DOMAIN       76    163       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      166    301       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      319    335       Post-SET. {ECO:0000259|PROSITE:PS50868}.
SQ   SEQUENCE   335 AA;  38749 MW;  DD33EE47068E3FB9 CRC64;
     MEEWSKHHFF HHGKPSREAE KRNCHWCQIR RFKTHPEFPV TIINRMDQIV PDPEFRFIDH
     SVFGAGVEPT KDEFRSGCDC EDGMDCQYRD CHCLQEMYDS EDVDEEDGDY GDLTQRKSYA
     YHTHGTKKGH LRSKVLESRE PIYECHDGCS CGPDCPNRVV ERGRQIPLQI FRTPNRGWGV
     RSMVDIKRGQ FIDKYIGEVI TPQEADRRRA RSDIAQRKDV YLFALDKFSD PDSPDERLRG
     PPLEVDGEFM SGPTRFINHS CDPNLRIFAR VGDHADKHIH DLALFAIVDI PKGDELTFDY
     VDGVDDSEND ALDPTKKKDM TVCLCGSSKC RGFLW
//
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