ID   SET2_ASPFU              Reviewed;         966 AA.
AC   Q4WTT2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
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; ORFNames=AFUA_5G06000;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000003; EAL91994.1; -; Genomic_DNA.
DR   RefSeq; XP_754032.1; XM_748939.1.
DR   AlphaFoldDB; Q4WTT2; -.
DR   SMR; Q4WTT2; -.
DR   STRING; 330879.Q4WTT2; -.
DR   EnsemblFungi; EAL91994; EAL91994; AFUA_5G06000.
DR   GeneID; 3511090; -.
DR   KEGG; afm:AFUA_5G06000; -.
DR   VEuPathDB; FungiDB:Afu5g06000; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_0_1_1; -.
DR   InParanoid; Q4WTT2; -.
DR   OMA; AQSQPCY; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd19172; SET_SETD2; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 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; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF08711; Med26; 1.
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; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   SUPFAM; SSF51045; WW domain; 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; Methyltransferase; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..966
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT                   specific"
FT                   /id="PRO_0000269780"
FT   DOMAIN          157..212
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          214..331
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          338..354
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DOMAIN          603..634
FT                   /note="WW"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..855
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..878
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  107882 MW;  8BFCB1445A56D0C1 CRC64;
     MSSHDNADSP SSSVANAVTA MKIEQHDGAA DMLLSNGGDA VLKRDSNGLS EHAVTAKDYP
     GMNDLASSTV KSRTSSLTPI KTENGDSTAK EEKVGGDITV KMEPGQPPKL SRSSSQKVVA
     QPPQLFLHLP DSTAEAQSTF EVMETCTYAN KYMGYTEHAM ECDCAEEWEP SLSRNLACGE
     DSDCINRATK IECVGDCSCG AECQNQRFQR KEYANVAVIK TEKKGFGLRA ETDLRPHQFI
     FEYVGEVINE AQFRRRMRQY DEEGIKHFYF MSLSRGEFVD ATKKGNLGRF CNHSCNPNCY
     VDKWVVGEKL RMGIFAERAI QAGEELVFNY NVDRYGADPQ PCYCGEPNCT GFIGGKTQTD
     RATKLSNATI EALGIEDADS WDTVVAKRPR KKKMGEDDEE YVDSVQPKSL DENGVTKVMA
     ALMQCKEKWI AVKLLRRIER CDDDRVRHRV VKMHGYQILN SQLTLWKDDF NVVLQILNIL
     DGFPRLTRNK IIDSKIESTV QPLTTCGDER VEKKAAALLQ HWATLEVGYR IPRMKRDPNA
     VASVSQFGRR EHTTDEQKRS QSRSRSRSPS LDAPRGPANP GRKSNGPRNS QHHGARQFRR
     QFNPLPPGWF AAESHGRTYY YCARGDVTWT RPIHAAPEAE VPGQQAKNKA LQGIIDNILN
     AKENTPKEKT VTPGTPQASR ETASLNEGQE RWRSYSEEKQ KKLYENTLFP HIKYVVDKFK
     HKLPKEDLKR YAKDVAKKLV NSDFKNNRVE DPTKISEKQQ KKVKAFCKEF FDKAVAKHRA
     YEQRKAEKQA KGGNSKADDM ISGHNTVEDD VKLSDGEAEK VEENDNSMSS DPQGILKRKR
     EDEMDIGEGA AEEAMKRQKS STPIPPPPPP PPPLGDEEQP TPNGTGEDDF LAENGVSMLH
     SPGSAPTPPP PPPLSTEHSD NDEMGQSPSM SNHLLEQKSF PAPLGEEYEA DSGKLSSNRI
     GIEGQV
//