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Database: UniProt/SWISS-PROT
Entry: SUV92_CHICK
LinkDB: SUV92_CHICK
Original site: SUV92_CHICK 
ID   SUV92_CHICK             Reviewed;         407 AA.
AC   Q5F3W5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-OCT-2017, entry version 96.
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=RCJMB04_5f7;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
DR   EMBL; AJ851535; CAH65169.1; -; mRNA.
DR   RefSeq; NP_001026541.1; NM_001031370.2.
DR   UniGene; Gga.13450; -.
DR   ProteinModelPortal; Q5F3W5; -.
DR   SMR; Q5F3W5; -.
DR   STRING; 9031.ENSGALP00000028525; -.
DR   PaxDb; Q5F3W5; -.
DR   Ensembl; ENSGALT00000029187; ENSGALP00000028525; ENSGALG00000013920.
DR   GeneID; 426314; -.
DR   KEGG; gga:426314; -.
DR   CTD; 79723; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q5F3W5; -.
DR   KO; K11419; -.
DR   OMA; AWCVPCL; -.
DR   OrthoDB; EOG091G0Y4N; -.
DR   PhylomeDB; Q5F3W5; -.
DR   TreeFam; TF106452; -.
DR   PRO; PR:Q5F3W5; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000013920; -.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IEA:Ensembl.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
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; 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    407       Histone-lysine N-methyltransferase
FT                                SUV39H2.
FT                                /FTId=PRO_0000281815.
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      391    407       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       395    395       Zinc 4. {ECO:0000250}.
FT   METAL       397    397       Zinc 4. {ECO:0000250}.
FT   METAL       402    402       Zinc 4. {ECO:0000250}.
FT   BINDING     300    300       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   407 AA;  46659 MW;  430C980EB03AC627 CRC64;
     MEGWRGAWYV PCLASHETLQ ELCRKENLRC KSIGITNKSL KSYEVEYLCD YKVEEGKEYY
     LVKWKGWPES SNTWEPQKNL KCPKLLENFL SDKDEYLSRM KEGRALKVRN SVKALKPAVA
     DYIVKKAKQR IALQRWKEEL NRKKNHKGMI LVENTVDLEG PPIDFYYINE YKPAPGINVI
     NGITTGCECS DCPAEKCCPK EAGFILAYNK QKKLKIQPGL PIYECNSFCR CGPDCPNRIV
     QKGTQYSLCI FRTNNGRGWG VKTLQKIKTN SFVMEYVGEV ITSEEAERRG QFYDNQGNTY
     LFDLDYDSDE FTVDAARYGN VSHFVNHSCD PNLQVFNVFI DNLDLRLPRI ALFSTRTIKA
     GEELTFDYQM KGSIDLTSDS ADGLSSSRKR IRTVCKCGAV CCRGYLN
//
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