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Database: UniProt/SWISS-PROT
Entry: SET2_YARLI
LinkDB: SET2_YARLI
Original site: SET2_YARLI 
ID   SET2_YARLI              Reviewed;         768 AA.
AC   Q6C5G5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   23-MAY-2018, entry version 103.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain-containing protein 2;
GN   Name=set-2; OrderedLocusNames=YALI0E18260g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Histone methyltransferase that methylates histone H3 to
CC       form H3K36me. Involved in transcription elongation as well as in
CC       transcription repression (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00901}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- DOMAIN: The AWS and SET domains are necessary for transcription
CC       repression. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00901}.
DR   EMBL; CR382131; CAG79692.1; -; Genomic_DNA.
DR   RefSeq; XP_504097.1; XM_504097.1.
DR   ProteinModelPortal; Q6C5G5; -.
DR   SMR; Q6C5G5; -.
DR   STRING; 4952.XP_504097.1; -.
DR   PRIDE; Q6C5G5; -.
DR   EnsemblFungi; CAG79692; CAG79692; YALI0_E18260g.
DR   GeneID; 2911710; -.
DR   KEGG; yli:YALI0E18260g; -.
DR   HOGENOM; HOG000248214; -.
DR   InParanoid; Q6C5G5; -.
DR   KO; K11423; -.
DR   OMA; CYVDKWV; -.
DR   OrthoDB; EOG092C3T9B; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IEA:InterPro.
DR   GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.10.1740.100; -; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR025788; Hist-Lys_N-MeTrfase_SET2_fun.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013257; SRI.
DR   InterPro; IPR038190; SRI_sf.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF47676; SSF47676; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Chromosome; Complete proteome; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    768       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 specific.
FT                                /FTId=PRO_0000269794.
FT   DOMAIN       45     90       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN       92    209       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      216    232       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN      501    534       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
SQ   SEQUENCE   768 AA;  85679 MW;  B7919C3B79F9D6F5 CRC64;
     MSGNNSPINA QLFPDARDVT KDALQTFVEL PECTYMKGLG SSQQAEVMAC DCKPGPTACD
     EDSGCINRLT SIECVRCCKG CQNKRFQGKK YASVDVISTE KKGFGLRATK DIAAGEFVYE
     YVGEVIDEPT FKERTAIYTT QGVKHFYFMM LQKGEFIDAT AKGGLGRFCN HSCAPNGHVE
     KWVVGKRLRM GIFASRHIQR GEEVTFDYNV DRYGAEAQAC YCGEKNCVGF LGGKTQTESA
     SKVSGTLTAA LGLTSRDINA ILRGKKSAED LRPRDLTVQD VSKVMASLMM NQEAWQVNLM
     LQRIALCTDT SVQAAVMKMH GYQIFAQILT ATWGDNPLGL DDSDRVNVTL MLLRVLQKWP
     RITKNKISSS QIENVVKSLT SNDNSDIATI AQELLSEWAN LKMAFRIPRR KIDPDGDEHS
     VSRGTSEEVT KESSKSEEPN DVEVVKVNKK ADNNGNGVTD SPSTRSESPF TFIPTPYSNK
     TAPKGPKKAV KQPASPMVPP RSLPKGWQFA NDPQGKVYYY NLELNIQQWD FPKASRASSP
     STPKGPKGPK GPRGNRRDER RDNSETREPL SLQSQRESDL QRIIEQARLQ EVKNNSEPAP
     SASAKPVNAQ AHRLTKLLAK VVPNQVSKYD VDRERAKKCS KDIVQILVDK ELKRPEPMTE
     ISDEKAKKIK EFVKGYMGKV VKRLEEKEGG AKDFGRGRQG NRRDSERQSD RRGRQGQSDR
     DHSDNHGRKR KGEENQPYEA GPMYDDESAE TSTETVKKPK VDMEIDLE
//
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