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SET2_CRYNJ
ID   SET2_CRYNJ              Reviewed;         834 AA.
AC   P0CO28; Q55PX0; Q5KDJ0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=CNG03810;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AE017347; AAW44778.1; -; Genomic_DNA.
DR   RefSeq; XP_572085.1; XM_572085.1.
DR   AlphaFoldDB; P0CO28; -.
DR   SMR; P0CO28; -.
DR   STRING; 5207.AAW44778; -.
DR   PaxDb; P0CO28; -.
DR   EnsemblFungi; AAW44778; AAW44778; CNG03810.
DR   VEuPathDB; FungiDB:CNG03810; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_1_3_1; -.
DR   InParanoid; P0CO28; -.
DR   OMA; CQEKWIA; -.
DR   OrthoDB; 453286at2759; -.
DR   Proteomes; UP000002149; Chromosome 7.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
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:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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   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; 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; Methyltransferase; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..834
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT                   specific"
FT                   /id="PRO_0000269786"
FT   DOMAIN          125..179
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          181..298
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          305..321
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..565
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..793
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..816
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  93485 MW;  6AFF4559E42187A7 CRC64;
     MGDIIEGTKP TLDDLWAGDE DQKPQTPPVS PPRSPSFKHE HKSSFPGSTS PPPASPIGEE
     DLKPRTARAS SSTSKVKSRK ASPEEFKPVL IDDLPTAWDE AHETFEALEK CVYERKDIGL
     SKENDEMMVC ECVYNRHDPD ADPCGPDSDC INRALYIECI AGECRAGKHC HNQQFSKRQY
     ANVDVVLTEK KGYGLRASST IPANTLIYEY IGEVVAEKTF RKRMQQYADE GIRHFYFMML
     QKEEYIDATK KGGIGRFANH SCNPNCEVQK WVVGRRLRMG IFTKRDVIKG EEITFNYNVD
     RYGHDAQTCY CGEPNCVGTI GGKTQTDIGT MNDLFLDALG ITDEVEAMGM KGSKKKKSRQ
     LDEDFVPILR PISAHEVQKV AAAIRQSMEN KKMMSRLLQR IQMTDDGAMH RQLMRMHGFS
     LMYMVLTELA DDNEIVLLAL ESMNKWKLQI RNKIEDSKIE EPVKALSQSG DEKICGLAKQ
     LIEYWSTLEL SYKIPRVSKI ASLDADDEAG TQTIAEANVV SAARRPDAWE NTQEIQIDIA
     PVRPRTLPVS RPRPPPPPPP LPVKKPALNS MSSTDRLKLD AIIAMAEQTV QAQAAAAAVE
     ATASPQAGSS RSGSRPAEDE ERRKRQKRTH MTEEELAEQK ERRLRKLIGA VVVKSMNKYK
     DMMEHDTFKK YARECTDTLV KKEKKRNPSY QDVKHPSLSD DKKAKIKSFT KDYTHKILKH
     LKEKGKLRNP KSSSSLRTNS NDPRQAASSS TNGDTPSIST TPSQGAIQRL RDGELVDDIF
     GADEDMVMDL DEDTPEMQND HPAPPSVPPA TPPLPPVHVE VVDNVSTPTS QWET
 
 
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