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Database: UniProt/TrEMBL
Entry: K1WEA6_MARBU
LinkDB: K1WEA6_MARBU
Original site: K1WEA6_MARBU 
ID   K1WEA6_MARBU            Unreviewed;       335 AA.
AC   K1WEA6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   SubName: Full=SET domain-containing protein {ECO:0000313|EMBL:EKD15740.1};
GN   ORFNames=MBM_05751 {ECO:0000313|EMBL:EKD15740.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina
OS   leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15740.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15740.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15740.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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; JH921440; EKD15740.1; -; Genomic_DNA.
DR   RefSeq; XP_007293640.1; XM_007293578.1.
DR   EnsemblFungi; EKD15740; EKD15740; MBM_05751.
DR   GeneID; 18761686; -.
DR   KEGG; mbe:MBM_05751; -.
DR   InParanoid; K1WEA6; -.
DR   KO; K11419; -.
DR   OrthoDB; EOG092C2EWO; -.
DR   Proteomes; UP000006753; 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; 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:UP000006753};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533}.
FT   DOMAIN       86    162       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      165    300       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      319    335       Post-SET. {ECO:0000259|PROSITE:PS50868}.
SQ   SEQUENCE   335 AA;  38235 MW;  04F508D41A3F9DEC CRC64;
     MTSPQHPMEF RHKCHFLYHG RADPKLAHQE EKCHYCQFGK FNSHKLHPIS IIFQDNTKLV
     IPKDFVFIEK SIPVEGVRFA EDEYLNGCEC ESDAQCMGSM CDPCLGDVDR VPKGGKPGAY
     HVSGDKKGCL RGWMLESRLP IYECHEKCTC SDKCPNRVVG RGRKVALQIF PTSGRGWGVK
     STEDIKRGQF VGEYVGEIIT PAEANRRRQA ATDRKKKDIY LFALDKFQDR ESYDQRLRGE
     PYEIDGEFKS GPTRFINHSC EPNLRIFAVV TAHANKPFHQ LCFFAAKDIP RETELTFDYT
     DGVTDARMDV EEAIAQDKEL TKCLCGTPSC RGYLW
//
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