SET2_CANAL
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 03-AUG-2022, entry version 119.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:P46995};
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; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; 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., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA 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 aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME 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 allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. {ECO:0000250|UniProtKB:P46995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000250|UniProtKB:P46995, ECO:0000255|PROSITE-
CC ProRule:PRU00901};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {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 methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00901}.
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DR EMBL; CP017624; AOW28002.1; -; Genomic_DNA.
DR RefSeq; XP_714401.1; XM_709308.1.
DR AlphaFoldDB; Q59XV0; -.
DR SMR; Q59XV0; -.
DR STRING; 237561.Q59XV0; -.
DR PRIDE; Q59XV0; -.
DR GeneID; 3643923; -.
DR KEGG; cal:CAALFM_C210250CA; -.
DR CGD; CAL0000174178; SET2.
DR VEuPathDB; FungiDB:C2_10250C_A; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_1_1; -.
DR InParanoid; Q59XV0; -.
DR OMA; CQEKWIA; -.
DR OrthoDB; 453286at2759; -.
DR PRO; PR:Q59XV0; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:EnsemblFungi.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:EnsemblFungi.
DR GO; GO:0016575; P:histone deacetylation; IEA:EnsemblFungi.
DR GO; GO:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IEA:EnsemblFungi.
DR GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; IEA:EnsemblFungi.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IEA:EnsemblFungi.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:1900049; P:regulation of histone exchange; IEA:EnsemblFungi.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.1740.100; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR025788; Set2_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
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 SUPFAM; SSF82199; SSF82199; 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; Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..844
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269782"
FT DOMAIN 84..140
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 142..259
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 266..282
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 558..592
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
