SET2_ASPOR
ID SET2_ASPOR Reviewed; 965 AA.
AC Q2UTN6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=AO090009000660;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007150; BAE55079.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UTN6; -.
DR SMR; Q2UTN6; -.
DR STRING; 510516.Q2UTN6; -.
DR EnsemblFungi; BAE55079; BAE55079; AO090009000660.
DR HOGENOM; CLU_008492_0_1_1; -.
DR OMA; CQEKWIA; -.
DR Proteomes; UP000006564; Chromosome 1.
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:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 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; IPR035441; TFIIS/LEDGF_dom_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 SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47676; SSF47676; 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..965
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269781"
FT DOMAIN 150..223
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 225..342
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 349..365
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 615..646
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 109182 MW; BAE272D48E1C9069 CRC64;
MSPHDYADRR SESVTDAVTA MNLEPDRATD TPALNGGSTS LKDDTNGVSR SPSAQNMDVA
VKSRSSSQTP VKKEEETSNT ADMEEKVGGD ITVKQEPGQP PKLTRSSSQK VVARPPQLFS
HLRDSTAEAR VSFELMDSCT YANKYMGYTE HAMECDCAEE WVSSVSGNIL SMPISLYALE
PALSKNLACG EDSDCINRAT KIECVGDCGC GPDCQNQRFQ RKEYAQVAVI KTEKKGFGLR
AEADLRPHQF IYEYVGEVIN EGQFRRRMRQ YDEEGIKHFY FMSLSKGEFV DATKRGNLGR
FCNHSCNPNC YVDKWVVGEK LRMGIFAERD IQAGEELVFN YNVDRYGADP QPCYCGEPNC
TGFIGGRTQT ERATKLSNAT IEALGIEDAD GWDTAVAKRP RKKKMGEDDE EYVDSVQPKS
LEENGVTKVM AALMQCQEKW IAVKLLGRIQ RCDDERVRNR VVKMHGYQIL NSQLTMWKDD
FNVVLQILDI LDKFPRLTRN KIIDSKIEVT IQPLTSCGDE RVEKRAATLL QVWSTLEVGY
RIPRMKRDPN ATAQAVNQFE RRETIRDQRR RSKSRSRSRS RSIEAPRGPA AQTRGVYGQR
NPHHHGPRSF RRQFNPLPTG WFAAESNGRT YYYSARGDTT WTRPTKPAPQ PPPPPKESRD
KALQDIIDGI MNAKENTPKE KSGTPGTPQV SKPIPVKKEG QEKWRGYSED KQKKVYENTL
FPHIKYVVDK FKHKLPKEDL KRYAKDVAKK LVNSDFKNNR VEDPTKISEK QQKKVKKYCK
EFFDKAVLKH RAYEQRKYEK QAKGMDSKVE TPQAPSDDEA LDVKMSDDEE DKADEKDTPM
TAEETQGGTK RKREGGIAED SNLGEYISSS KRQRSSTPPP LPPISPGDDP QNMDNAKKIL
RDDIDSRSEN NEFTPPPPPP PPPDDEMPSE SPETDHAIDQ SPSRAEYITD MNKLKSSQPE
IEGKV
