SET2_ASHGO
ID SET2_ASHGO Reviewed; 684 AA.
AC Q757Y8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
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=AEL128C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 531.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016818; AAS52557.2; -; Genomic_DNA.
DR RefSeq; NP_984733.2; NM_210087.2.
DR AlphaFoldDB; Q757Y8; -.
DR SMR; Q757Y8; -.
DR STRING; 33169.AAS52557; -.
DR PRIDE; Q757Y8; -.
DR EnsemblFungi; AAS52557; AAS52557; AGOS_AEL128C.
DR GeneID; 4620920; -.
DR KEGG; ago:AGOS_AEL128C; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_1_1; -.
DR InParanoid; Q757Y8; -.
DR OMA; CQEKWIA; -.
DR Proteomes; UP000000591; Chromosome V.
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:0006353; P:DNA-templated transcription, termination; IEA:EnsemblFungi.
DR GO; GO:0016575; P:histone deacetylation; IEA:EnsemblFungi.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; IEA:EnsemblFungi.
DR GO; GO:0097198; P:histone H3-K36 trimethylation; IEA:EnsemblFungi.
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 GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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; 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; PF18507; WW_1; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 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.
PE 3: Inferred from homology;
KW Chromosome; Coiled coil; Methyltransferase; Nucleus; Reference proteome;
KW Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..684
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269779"
FT DOMAIN 53..108
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 110..227
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 234..250
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 452..484
FT /note="WW"
FT REGION 479..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 518..594
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 79779 MW; 78DDBE28F4078577 CRC64;
MSRSSSPSVS LPLPSSATLF LDREDKTEEA LGTFIELEQC TYTHKRLGDS RSNEFMECDC
FEDYKDEQNH ACDENSDCIN RLTLIECVND LCTSCGDDCQ NQRFQKKEYA DIAVFQTEKK
GYGVRAERDI EANEFIYEYI GEVISEADFR DRMVDYDMRG FKHFYFMMLQ AGEFIDATER
GCLARFCNHS CNPNAYVSKW DVAGKLKMGI FAHRKILKGE EITFDYNVDR YGATAQPCYC
DEPNCIGFLG GKTQTDAASL LPQNYADALG VRPSVEKKWV KMRKALGEEI DKSGSSNINI
EFVESLELEP CVQYSDVNKV MSVLLQIDDK FICSKLLERI LLTSDETMRY QIIKLHGYKC
FSKLLGLFET DENTQHRILQ YLSDLPKTTK NGIVSSQIDK KVESLLQKEA LKEDASALLE
RWNTYETYQR IAKKDFTKTS NGLNKVTDFR RVRLPLGWEI IHENGRPMYY NAQRQIKRVD
PPSDTHLQRP ARTTPPQRYN GGFYDRTTKR PLDPESFEKR KRQRLEWEQQ ELAKKKQEEV
RHLKEKLEVE KQKKSELEQI IEDANKQQEQ QRLERLQKEK ETAERRERRR QTHSASRIEH
KWNKFFAQIV PNLIKSYATS MDRARIKECA RDIVKILSSK ELKKDATKVP PAEVTKEKRK
KVNEFCKSYM DKLLAKMHEK AVSK
