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Database: UniProt/SWISS-PROT
Entry: SUV92_XENTR
LinkDB: SUV92_XENTR
Original site: SUV92_XENTR 
ID   SUV92_XENTR             Reviewed;         406 AA.
AC   Q28CQ7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   25-OCT-2017, entry version 69.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE            EC=2.1.1.43;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE            Short=Su(var)3-9 homolog 2;
GN   Name=suv39h2; ORFNames=TEgg055l20.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ81421.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR926249; CAJ81421.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001016508.1; NM_001016508.1.
DR   UniGene; Str.423; -.
DR   ProteinModelPortal; Q28CQ7; -.
DR   SMR; Q28CQ7; -.
DR   STRING; 8364.ENSXETP00000011888; -.
DR   PaxDb; Q28CQ7; -.
DR   GeneID; 549262; -.
DR   KEGG; xtr:549262; -.
DR   CTD; 79723; -.
DR   Xenbase; XB-GENE-852675; suv39h2.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q28CQ7; -.
DR   KO; K11419; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
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   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00024; CHROMO; 1.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
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; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 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   Complete proteome; Differentiation; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Zinc.
FT   CHAIN         1    406       Histone-lysine N-methyltransferase
FT                                SUV39H2.
FT                                /FTId=PRO_0000281816.
FT   DOMAIN       43    101       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      185    243       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      246    369       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      390    406       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      257    259       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      326    327       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       187    187       Zinc 1. {ECO:0000250}.
FT   METAL       187    187       Zinc 2. {ECO:0000250}.
FT   METAL       189    189       Zinc 1. {ECO:0000250}.
FT   METAL       192    192       Zinc 1. {ECO:0000250}.
FT   METAL       192    192       Zinc 3. {ECO:0000250}.
FT   METAL       197    197       Zinc 1. {ECO:0000250}.
FT   METAL       198    198       Zinc 1. {ECO:0000250}.
FT   METAL       198    198       Zinc 2. {ECO:0000250}.
FT   METAL       225    225       Zinc 2. {ECO:0000250}.
FT   METAL       225    225       Zinc 3. {ECO:0000250}.
FT   METAL       229    229       Zinc 2. {ECO:0000250}.
FT   METAL       231    231       Zinc 3. {ECO:0000250}.
FT   METAL       235    235       Zinc 3. {ECO:0000250}.
FT   METAL       329    329       Zinc 4. {ECO:0000250}.
FT   METAL       394    394       Zinc 4. {ECO:0000250}.
FT   METAL       396    396       Zinc 4. {ECO:0000250}.
FT   METAL       401    401       Zinc 4. {ECO:0000250}.
FT   BINDING     300    300       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   406 AA;  46350 MW;  E8AF03619B8AF75B CRC64;
     MAAARGAWCV PCLASIETLQ ELCRKEMLIC TNIGITRKNL NNYEVEYLCD YRIEKGVEKF
     FVKWKGWPES CNTWEPTRNL KCPTLLKQFY SDLYNYFCAL KPNKKGFLKN SIKSLDPSLS
     DYIVKKAKQR IALRRWEEEL NRKKTHSGTL FVENTVDLEG PPMDFYYIND YKASPGVNTL
     GEAIVGCDCS DCFKGKCCPT EAGVLFAYNE HRQIKIPPGR PIYECNSRCK CGPDCPNRVV
     QKGPPYSLCI FRTDNGRGWG VKTLQKIKKN SFVMEYVGEV ITSEEAERRG QQYDSRGITY
     LFDLDYEADE FTVDAARYGN VSHFVNHSCD PNLQVFNVFI DNLDVRLPRI ALFSTRNIKA
     GEELTFDYQM KGSGDFSTDS IDMSPAKKRV RIACKCGAAT CRGYLN
//
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