(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 110.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE            EC=2.1.1.-;
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 methylates histone H3 to form
CC       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(+) + N(6)-
CC         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; Evidence={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}.
DR   EMBL; AE016818; AAS52557.2; -; Genomic_DNA.
DR   RefSeq; NP_984733.2; NM_210087.2.
DR   SMR; Q757Y8; -.
DR   STRING; 33169.AAS52557; -.
DR   EnsemblFungi; AAS52557; AAS52557; AGOS_AEL128C.
DR   GeneID; 4620920; -.
DR   KEGG; ago:AGOS_AEL128C; -.
DR   HOGENOM; HOG000248214; -.
DR   InParanoid; Q757Y8; -.
DR   KO; K23700; -.
DR   OMA; NHACGED; -.
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-dependent 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   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; 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   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;
DR   PRODOM; Q757Y8.
DR   SWISS-2DPAGE; Q757Y8.
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   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
//

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