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Database: UniProt
Entry: Q6INA9
LinkDB: Q6INA9
Original site: Q6INA9 
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   01-OCT-2014, entry version 73.
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Associated with non-pericentromeric regions of
CC       chromatin. Excluded from nucleoli and islands of condensed
CC       chromatin (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00906}.
CC   -!- SIMILARITY: Contains 1 MBD (methyl-CpG-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00338}.
CC   -!- SIMILARITY: Contains 1 post-SET domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00155}.
CC   -!- SIMILARITY: Contains 1 pre-SET domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00157}.
CC   -!- SIMILARITY: Contains 1 SET domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SIMILARITY: Contains 2 Tudor domains. {ECO:0000305}.
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DR   EMBL; BC072374; AAH72374.1; -; mRNA.
DR   RefSeq; NP_001085076.2; NM_001091607.1.
DR   UniGene; Xl.54988; -.
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:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR016177; DNA-bd_dom.
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; SSF54171; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Coiled coil; Metal-binding;
KW   Methyltransferase; Nucleus; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00338}.
FT   DOMAIN      753    826       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      829   1244       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1253   1269       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      839    841       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1201   1202       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED        9     63       {ECO:0000255}.
FT   COMPBIAS    508    580       Gln-rich.
FT   METAL       755    755       Zinc 1. {ECO:0000250}.
FT   METAL       755    755       Zinc 2. {ECO:0000250}.
FT   METAL       757    757       Zinc 1. {ECO:0000250}.
FT   METAL       761    761       Zinc 1. {ECO:0000250}.
FT   METAL       761    761       Zinc 3. {ECO:0000250}.
FT   METAL       767    767       Zinc 1. {ECO:0000250}.
FT   METAL       769    769       Zinc 2. {ECO:0000250}.
FT   METAL       807    807       Zinc 2. {ECO:0000250}.
FT   METAL       807    807       Zinc 3. {ECO:0000250}.
FT   METAL       811    811       Zinc 2. {ECO:0000250}.
FT   METAL       813    813       Zinc 3. {ECO:0000250}.
FT   METAL       818    818       Zinc 3. {ECO:0000250}.
FT   METAL      1204   1204       Zinc 4. {ECO:0000250}.
FT   METAL      1257   1257       Zinc 4. {ECO:0000250}.
FT   METAL      1259   1259       Zinc 4. {ECO:0000250}.
FT   METAL      1264   1264       Zinc 4. {ECO:0000250}.
FT   BINDING     877    877       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     879    879       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1198   1198       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
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
//
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