位置:首页 > 蛋白库 > SET2_CHAGB
SET2_CHAGB
ID   SET2_CHAGB              Reviewed;         894 AA.
AC   Q2H988;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=CHGG_03216;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408030; EAQ91281.1; -; Genomic_DNA.
DR   RefSeq; XP_001229732.1; XM_001229731.1.
DR   AlphaFoldDB; Q2H988; -.
DR   SMR; Q2H988; -.
DR   STRING; 38033.XP_001229732.1; -.
DR   EnsemblFungi; EAQ91281; EAQ91281; CHGG_03216.
DR   GeneID; 4389690; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_0_0_1; -.
DR   InParanoid; Q2H988; -.
DR   OMA; CQEKWIA; -.
DR   OrthoDB; 453286at2759; -.
DR   Proteomes; UP000001056; 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: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   CDD; cd00201; WW; 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   Pfam; PF00397; WW; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 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..894
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT                   specific"
FT                   /id="PRO_0000269784"
FT   DOMAIN          72..126
FT                   /note="AWS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT   DOMAIN          128..245
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          252..268
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DOMAIN          512..544
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..790
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  99098 MW;  4C78E2A758B3ADF5 CRC64;
     MSPDDAKSAA DGTSVPENGT APKLSRKPSQ KLPRGPPPLF DHLPDATADA CDTFQVINDC
     LYGSKNMGSS DHDALDCDCA EEWHDGQNHA CGEDSDCINR ATKIECVSGD CNCGEGCENQ
     RFQRKQYANV SVIKTEKKGF GLRTDADLQA NDFVFEYVGE VINEPTFRNR TVKYDKEGIK
     HFYFMSLTKS EFVDATKKGN LGRFCNHSCN PNCYVDKWVV GDKLRMGIFA TRAIRAGEEL
     VFNYNVDRYG ADPQPCYCGE SNCVGFIGGK TQTERATKLP LATIEALGID DGDSWDTAVA
     KKPRKKKAHE DDEDYVNSVQ PRALDEDGVN KVMATLMQCK EKWIAVKLLS RLQATEDEHL
     RHRVVRMHGY QILKTTLNTF KDDTNVVLQI LDILYQLPRI TKNKISDSKV EGAVEPLASA
     AHEEVALAAK RLLDEWSKLE TAYRIPRKKH DHAGPIPGNS FEEERRNKDR EEPAKPTDPF
     ANIVIPTGPR STIPQRNANF FAGQQRPRKP PTNLPAGWFV NTDKTGRYYF YDATGRTQWQ
     RPLTPAIETP KVSAKAQQDQ KALQSIIDSL TKEPTPRHSA GHTPQRSTTP ATEPKKDKWR
     SLPLEKQMKI YENTHVVDRF HGKLPKEELK KFAREVNKKL VSSDYKNNRV EDPTSIPPKQ
     AKKVRKYAHD FFDRAVAKYT EHEKKKAHNP SKPTSGVPPG DVASSAATPA KDDVTMSDVE
     ADTSPGSSAG RKRKRDGDDE HDDPAESPGA PPSETPSVKR IKEDDAEGEG EPTTIPPPPT
     PPPPPADTPP TEEDRSMREQ EEALMRENEE AQRLEDEAQA EEGGKGSHEW NGRYHRTCAA
     GERAVEWRVG NGWCYGDDGH GRAAATTAAA AATAAAGSAG SLKTTLACFA FAPC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025