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Database: UniProt
Entry: Q59XV0
LinkDB: Q59XV0
Original site: Q59XV0 
ID   SET2_CANAL              Reviewed;         844 AA.
AC   Q59XV0; A0A1D8PIP1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   10-APR-2019, 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=SET2; OrderedLocusNames=CAALFM_C210250CA;
GN   ORFNames=CaO19.1755, CaO19.9324;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={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; CP017624; AOW28002.1; -; Genomic_DNA.
DR   RefSeq; XP_714401.1; XM_709308.1.
DR   ProteinModelPortal; Q59XV0; -.
DR   SMR; Q59XV0; -.
DR   STRING; 5476.C4YKT8; -.
DR   PRIDE; Q59XV0; -.
DR   GeneID; 3643923; -.
DR   KEGG; cal:CAALFM_C210250CA; -.
DR   CGD; CAL0000174178; SET2.
DR   EuPathDB; FungiDB:C2_10250C_A; -.
DR   InParanoid; Q59XV0; -.
DR   KO; K11423; -.
DR   OMA; NHACGED; -.
DR   OrthoDB; 453286at2759; -.
DR   PRO; PR:Q59XV0; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF17907; AWS; 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; 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; PS01159; WW_DOMAIN_1; 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    844       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 specific.
FT                                /FTId=PRO_0000269782.
FT   DOMAIN       84    140       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      142    259       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      266    282       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN      558    592       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
SQ   SEQUENCE   844 AA;  95327 MW;  0E913A5CA46BA55F CRC64;
     MSNNNFQESS NNTSSPSKRS TPMLFLDAEN KTQEALTTFE LLNACTYQNK YVGSANVTTT
     ATTSTKTSNS TSTKSHQQQH RRKLEYMTCD CEEEWDSELQ MNLACGPDSN CINRITCVEC
     VNRNCLCGDD CQNQRFQNRQ YSKVKVIQTE LKGYGLIAEQ DIEENQFIYE YIGEVIDEIS
     FRQRMIEYDL RHLKHFYFMM LSNDSFIDAT EKGSLGRFIN HSCNPNAFVD KWHVGDRLRM
     GIFAKRKISR GEEITFDYNV DRYGAQSQPC YCGEPNCIKF MGGKTQTDAA LLLPQMIAEA
     LGVTPRQEKA WLKENKSIRN QQQNDESNIN EEFVNSIEIE PIENQDGVTK VMSALMKTQH
     PLIIKKLIER IFLSNDQDDI NVMFVRFHGY KTISTILQDL LVAKNSGKES ETTDNNDIDN
     STGDDDQDKD ELIIKILKIL VSWPAVTKNK IASANLEEVV KDIQTNNENS NNNDEINQLC
     TSLLDRWSKL EMAYRIPKQE SVPTNNAAAA ATTTATATGT TTSASPFERI SSHTPEVGGT
     NTPSSTSQQQ QQQNSRDAGL PENWRSAFDK NTGGYYYYNL VTKETTWERP LGSLPLGPKP
     PSGPGLKGRI NKYNEIDLAK REELRIQKEK EMKFIEMQNR DRKLKELIEM SKKSMNNIGG
     SSGTTITAAT INGLSDNGGN NNGNITGIYG DDKHSKHHHH HHDKHLKNGP RNTSTSSSSG
     NNVEKIWKRI FAKYIPNIIK KYESEIGRDN VKGCAKELVN ILTQSEIKHG NSLPSSSSSN
     GYSMELSDKK LKKIKEYSHG YMDKFLIKFN NSKKHKSTMG SKGSDNHKRK HNGDGDNGVK
     RSKV
//
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