ID SETB1_XENLA Reviewed; 1269 AA.
AC Q6INA9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 06-MAR-2013, entry version 65.
DE RecName: Full=Histone-lysine N-methyltransferase SETDB1;
DE EC=2.1.1.43;
DE AltName: Full=SET domain bifurcated 1;
GN Name=setdb1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically
CC trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation
CC represents a specific tag for epigenetic transcriptional
CC repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to
CC methylated histones. Mainly functions in euchromatin regions,
CC thereby playing a central role in the silencing of euchromatic
CC genes. H3 'Lys-9' trimethylation is coordinated with DNA
CC methylation (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC similarity). Note=Associated with non-pericentromeric regions of
CC chromatin. Excluded from nucleoli and islands of condensed
CC chromatin (By similarity).
CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC family. Suvar3-9 subfamily.
CC -!- SIMILARITY: Contains 1 MBD (methyl-CpG-binding) domain.
CC -!- SIMILARITY: Contains 1 post-SET domain.
CC -!- SIMILARITY: Contains 1 pre-SET domain.
CC -!- SIMILARITY: Contains 1 SET domain.
CC -!- SIMILARITY: Contains 2 Tudor domains.
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DR EMBL; BC072374; AAH72374.1; -; mRNA.
DR RefSeq; NP_001085076.2; NM_001091607.1.
DR UniGene; Xl.54988; -.
DR HSSP; Q8X225; 1PEG.
DR ProteinModelPortal; Q6INA9; -.
DR SMR; Q6INA9; 190-391.
DR GeneID; 432147; -.
DR KEGG; xla:432147; -.
DR CTD; 9869; -.
DR Xenbase; XB-GENE-866480; setdb1.
DR HOVERGEN; HBG061013; -.
DR KO; K11421; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR016177; DNA-bd_integrase-typ.
DR InterPro; IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR003606; Pre-SET_Zn-bd_sub.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF54171; DNA-binding_integrase-type; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50304; TUDOR; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Coiled coil; Methyltransferase;
KW Nucleus; Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1 1269 Histone-lysine N-methyltransferase
FT SETDB1.
FT /FTId=PRO_0000281821.
FT DOMAIN 250 312 Tudor 1.
FT DOMAIN 340 395 Tudor 2.
FT DOMAIN 620 691 MBD.
FT DOMAIN 753 826 Pre-SET.
FT DOMAIN 828 1248 SET.
FT DOMAIN 1253 1269 Post-SET.
FT COILED 9 63 Potential.
FT COMPBIAS 508 580 Gln-rich.
SQ SEQUENCE 1269 AA; 141777 MW; 6241910CB4266FAC CRC64;
MELEQMVVKE LGISMDDLRE LIDRELEKIE FVKQRKAQLL EMEQLVKQKE AEVDHVDKLF
DNATRAVDDC ETLVKSLYDQ IGMTYKESSS EDEGSSKPTE VIEIPDEDDD DVMSVGSGEA
VSKIPKEKHL LREAMAAMKR SRQDVQSIVE AIQKKSDGPQ TRFSSHPSSP TSSVGGSNQA
SASNDMSKDG DLVVGMRILG KKRTKTWHKG TLISIQCVGT GKKFKVKFDN KGKSLLSGNH
IAYDYHPPPE NLTVGSRVVA KYKDGNQVWL YAGIVAEPPS SKNKMRYLIF FDDGYASYVT
HAELYPVCRP WSKSWEDIED VSCRDFIQEY VNAYPNRPMV LLKSGQLIKT EWEGTWWKSK
VEEVDGSLVK ILFLDDKRCE WIYRGSTRLE PMFSMKTSNA STQEKQQAGQ QRTRPNVGAI
RSKGPVVQFT HDLTGNEPEH NPAAPPSPQS MPSPQLIDTD SDSQQAQSKK QVAKKSTSFR
PGSAGSGQSS PIPTESVPQP PAAPRPFQSN QSVQPVQSIQ PIQPIHNIQT IQTIQGIQTI
QAIQPIQSIQ TLQPIQTIQP LQTIQTLQGN RIVTSIQQFQ IIRTENIPAE STYKAPKEKL
FYLPHVCNYT CLSRIRPLSH RGKNPLLVPL LYDFRRMTAR RRVNRKMGFH VIYKSPCGLS
LRTMPEIERY LFETQCKMLF LEMFCLDPYV LVDRKFQPQK PFYYIPDITY GKEDVMLSCV
NEIDRTPPPQ VAYSKERIPG KGVFINTGAD YLVGCDCTDG CRDKSKCACH QLTIQATACT
PGAQSNPMAG YQHKRLEECL PTGVYECNKR CKCSANMCNN RLVQHGLQVR LQLFKTQNKG
WGIRGLDDIA KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA
KSSSDSSGVD LKEDHEENSG SEDQEESNDS SDDNFGKNED ITTSSVWRSY ATRRTTRGQK
ENGTSETASK DSRTRDETTD CKLPEETSKN KVASWLSSNT MADSVMDSDS RSSLKMGEAL
ETDKPKESEE ASKYPRFAEG NRAYGYNPTP TKKDGVRRPV TKTALHQIKR QSSSAQPTEE
VLTLSSSSDS EVGSGTNGSK KPAAQATAND SDDIQTISSG SDEEEEKKNV AASAGPVKRQ
VAVKSTRGFA LKSTHGITVK SNMASGEGGP GRRNTRQFFD GEESCYIIDA KLEGNLGRYL
NHSCSPNLFV QNVFVDTHDL RFPWVAFFAS KRIRAGTELT WDYNYEVGSV EGKKLLCCCG
STECRGRLL
//
