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Database: UniProt/SWISS-PROT
Entry: SET2_EMENI
LinkDB: SET2_EMENI
Original site: SET2_EMENI 
ID   SET2_EMENI              Reviewed;         980 AA.
AC   Q5ASA5; C8V9K8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   28-MAR-2018, entry version 97.
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; ORFNames=AN8825;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000162; EAA60113.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77940.1; -; Genomic_DNA.
DR   RefSeq; XP_682094.1; XM_677002.1.
DR   ProteinModelPortal; Q5ASA5; -.
DR   SMR; Q5ASA5; -.
DR   STRING; 162425.CADANIAP00006232; -.
DR   EnsemblFungi; CADANIAT00006232; CADANIAP00006232; CADANIAG00006232.
DR   EnsemblFungi; EAA60113; EAA60113; AN8825.2.
DR   GeneID; 2868338; -.
DR   KEGG; ani:AN8825.2; -.
DR   HOGENOM; HOG000172130; -.
DR   InParanoid; Q5ASA5; -.
DR   KO; K11423; -.
DR   OMA; CYVDKWV; -.
DR   OrthoDB; EOG092C3T9B; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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   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; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 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.
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    980       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 specific.
FT                                /FTId=PRO_0000269788.
FT   DOMAIN      167    239       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      241    358       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      365    381       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN      630    661       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   COMPBIAS    662    670       Poly-Pro.
FT   COMPBIAS    726    818       Lys-rich.
FT   COMPBIAS    890    942       Pro-rich.
SQ   SEQUENCE   980 AA;  109885 MW;  EC1707F11CA27E61 CRC64;
     MSTHDNADRQ SEFVADAVTA MKLEQSENNT DAPILNGGGA AMKPDSKAAS PEPLIKDERA
     SSTFMKSRSS SRTPSSRTPL KKEHSDSEDI QEKRGDDASG TEKVGGGISV KMEPGQPPKL
     ARSSSQKVVP RPPQLFLDLP DSTEEAQKTF EVIETCQYAN KYMGYTEHAM ECDCAEEWVL
     VVVLAPSPSF RVPSQNPASS TNRACGEDSD CINRATKIEC MGDCGCGPDC QNQRFQRREY
     ANVAVIKTEK KGYGLRAEED LRPHQFIFEY VGEVINEGPF HRRMRQYDAE GIKHFYFMSL
     SKGEFVDATK KGNLGRFCNH SCNPNCYVDK WVVGEKLRMG IFAERHIQAG EELVFNYNVD
     RYGADPQPCY CGEPNCTGFI GGKTQTERAT KLSNATIEAL GIEDADGWDT AVAKRPRKKK
     MGEEDEEYVD SVQPKSLDES GVTKVMAALM QCKEKWIAVK LLGRIQRCDD ERVRNRVVKM
     HGYQILNSQL AMWKDDFNVV LQILDILDKF PRLTRNKIID SKIESTIQPL TSCGDERVEQ
     KATVLLQLWS TLEIGYRIPR MKRDPNAATP TVSQFHRRDD ISDERQQRPR SRSRSRSIEA
     PRGPAAQKRG GQGPRNQHHQ GPRTFRRRFD PLPQGWFAAE SNGRTYYYSA RGDTTWTRPT
     KPAPQPPPPP KESRDKALQS IIDGIMNAKE QTPKEKSGTP TTPQPSKPTP EGKDRQEKWR
     SYSEEKQKKL YENTLYPHIK YVVDKFKHKL PKDDLKRYAK DVAKKLVNSD FKNNRVTDPT
     KIDDKQQKKV KKFCKEFFDK AVAKHQAHEK RKAEKLAKEG SSDNKLATPV GGQSEGDGTP
     DVKMSDDEGS TGREGTGSLK RKRDELSVGN TNTPDDTPTS STKRQRSSTP PPPPPPAMNT
     NDNNNDNDDM SVRSDEPDAD ADADEVVLVG NPTPPPPPPP PPQEDMRIPD ADAETNGHNF
     EGYGEMNRSH QAQIGIEGNV
//
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