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Database: UniProt/TrEMBL
Entry: B6HGS4_PENRW
LinkDB: B6HGS4_PENRW
Original site: B6HGS4_PENRW 
ID   B6HGS4_PENRW            Unreviewed;       688 AA.
AC   B6HGS4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028};
DE            EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE   AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN   ORFNames=Pc20g01100 {ECO:0000313|EMBL:CAP85439.1}, PCH_Pc20g01100
GN   {ECO:0000313|EMBL:CAP85439.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85439.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85439.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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:0000256|ARBA:ARBA00000317};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AM920435; CAP85439.1; -; Genomic_DNA.
DR   RefSeq; XP_002562671.1; XM_002562625.1.
DR   AlphaFoldDB; B6HGS4; -.
DR   STRING; 500485.B6HGS4; -.
DR   GeneID; 8312247; -.
DR   KEGG; pcs:Pc20g01100; -.
DR   VEuPathDB; FungiDB:PCH_Pc20g01100; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_0_1_1; -.
DR   OMA; CQEKWIA; -.
DR   OrthoDB; 950362at2759; -.
DR   BioCyc; PCHR:PC20G01100-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19172; SET_SETD2; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.170.270.10; SET 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; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR001202; WW_dom.
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; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 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.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023015};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          121..176
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          178..295
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          302..318
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          560..591
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77791 MW;  E8A379D195EB55C6 CRC64;
     MSAHDYADSE EPAKMERDSP VNGNHLKNGD SRTSSRSPLP PKKESSPNSD APDPMKENIG
     EIVLKQEPGQ PPKLSRSSSQ KVASRPPPLY THLPDSTQDA LATFEQIPGC IYANKYMGYT
     EHAMECDCAE EWDPKIGRNI ACGEDSDCIN RATKIECAGE CGCGPDCQNQ RFQKRQFAPV
     SVIKTEKKGF GLRAEKNLDP GELIYEYVGE VVGEQQFRKR MRQYDEEGIK HFYFMSLNKG
     EFVDATKRGN LGRFCNHSCN PNCYVDKWVV GEKLRMGIFA ERAVQAGEEL VFNYNVDRYG
     ADPQPCYCGE PMCTGFIGGR TQTERATKLS NATIEALGID EADGWDTVVA KRPKKKKMEE
     DDEEYVDSVQ PKSLDEDGVT KVMAALVQCQ EKWIAVKLLG RIQRCDDERV RNRVVRMHGY
     QILNSQLAQW KEDQNVVLQI LNILDGFPRL TRNKIQDSKI ETNIRPLTTC DDERVPKKAV
     ALLESWAGLE VAYRIPRMKR GKDAKQAINQ FERRETGQEQ RQRSLTRSPS PVYDAPRGPA
     QQRRDRGPQR SRQPNRRGPR PLPEGWYTAE AEGRVYYYSA SGKTTWERPT LPATPATPAP
     GQPAKNQQNL ALQSIIDGIM NTQEDTPSEN RTATPVTPQP SADQPERRHK DGEKWRKLPL
     EKQKRIYENT VTFPAYQARG GSVQTQDP
//
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