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Database: UniProt
Entry: Q6NRE8
LinkDB: Q6NRE8
Original site: Q6NRE8 
ID   SUV91_XENLA             Reviewed;         421 AA.
AC   Q6NRE8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 79.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE            EC=2.1.1.43;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 1;
DE            Short=Su(var)3-9 homolog 1;
GN   Name=suv39h1;
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin (By similarity).
CC       {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:PRU00912}.
DR   EMBL; BC070805; AAH70805.1; -; mRNA.
DR   RefSeq; NP_001084892.1; NM_001091423.1.
DR   UniGene; Xl.46583; -.
DR   ProteinModelPortal; Q6NRE8; -.
DR   SMR; Q6NRE8; -.
DR   BioGrid; 101309; 1.
DR   GeneID; 431943; -.
DR   KEGG; xla:431943; -.
DR   CTD; 431943; -.
DR   Xenbase; XB-GENE-6049313; suv39h1.
DR   HOVERGEN; HBG055621; -.
DR   KO; K11419; -.
DR   OrthoDB; 753093at2759; -.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   CDD; cd00024; CHROMO; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009343; SUV39_SET; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Centromere; Chromatin regulator; Chromosome;
KW   Differentiation; Metal-binding; Methyltransferase; Nucleus; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN         1    421       Histone-lysine N-methyltransferase
FT                                SUV39H1.
FT                                /FTId=PRO_0000281812.
FT   DOMAIN       46    104       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      189    249       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      252    375       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      405    421       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      263    265       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      332    333       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       191    191       Zinc 1. {ECO:0000250}.
FT   METAL       191    191       Zinc 2. {ECO:0000250}.
FT   METAL       193    193       Zinc 1. {ECO:0000250}.
FT   METAL       196    196       Zinc 1. {ECO:0000250}.
FT   METAL       196    196       Zinc 3. {ECO:0000250}.
FT   METAL       203    203       Zinc 1. {ECO:0000250}.
FT   METAL       204    204       Zinc 1. {ECO:0000250}.
FT   METAL       204    204       Zinc 2. {ECO:0000250}.
FT   METAL       231    231       Zinc 2. {ECO:0000250}.
FT   METAL       231    231       Zinc 3. {ECO:0000250}.
FT   METAL       235    235       Zinc 2. {ECO:0000250}.
FT   METAL       237    237       Zinc 3. {ECO:0000250}.
FT   METAL       241    241       Zinc 3. {ECO:0000250}.
FT   METAL       335    335       Zinc 4. {ECO:0000250}.
FT   METAL       409    409       Zinc 4. {ECO:0000250}.
FT   METAL       411    411       Zinc 4. {ECO:0000250}.
FT   METAL       416    416       Zinc 4. {ECO:0000250}.
FT   BINDING     306    306       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   421 AA;  48581 MW;  776BD7633D03C069 CRC64;
     MAENSNGALG CVVRCLSSES ELQELCREEQ LCCAELGVTR KNLSDFEVEY LWNYKKVQDQ
     ELYLVKWKYY PDSESTWEPR HHLKCNNLLK QFHLDLEREL LRRAKAAGTK KTAVRCPRRL
     DQSLSHYLVL KAKQRKRLRQ WAQQLNAKRS HLGLILVENE VDLEGPPRDF VYINEYRVGE
     GVTINRISAG CKCRDCFSDE GGCCPGAFQH KKAYNNEGQV KVKPGFPIYE CNSCCRCGPS
     CPNRVVQKGI QYKFCIFRTS DGRGWGVRTL EKIRKNSFVM EYVGEIITSE EAERRGQIYD
     RQGTTYLFDL DYVEDVYTVD AARYGNISHF VNHSCKPNLQ VYNVFIDNLD ERLPRIAFFA
     TRTIRTGEEL TFDYNMQVDP VDVESSKMDS NFGIAGLPAS PKKRVRVECK CGVSSCRKYL
     F
//
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