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Database: UniProt
Entry: Q5QD03
LinkDB: Q5QD03
Original site: Q5QD03 
ID   SUVH3_CHLRE             Reviewed;         957 AA.
AC   Q5QD03;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-SEP-2014, entry version 58.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 3;
DE            Short=H3-K9-HMTase 3;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 3;
DE            Short=Su(var)3-9 homolog protein 3;
GN   Name=SUVH3; Synonyms=SET3;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16100335; DOI=10.1105/tpc.105.034165;
RA   van Dijk K., Marley K.E., Jeong B.-R., Xu J., Hesson J., Cerny R.L.,
RA   Waterborg J.H., Cerutti H.;
RT   "Monomethyl histone H3 lysine 4 as an epigenetic mark for silenced
RT   euchromatin in Chlamydomonas.";
RL   Plant Cell 17:2439-2453(2005).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17251191; DOI=10.1093/nar/gkl1149;
RA   Casas-Mollano J.A., van Dijk K., Eisenhart J., Cerutti H.;
RT   "SET3p monomethylates histone H3 on lysine 9 and is required for the
RT   silencing of tandemly repeated transgenes in Chlamydomonas.";
RL   Nucleic Acids Res. 35:939-950(2007).
CC   -!- FUNCTION: Histone methyltransferase. Monomethylates specifically
CC       'Lys-9' of histone H3. H3 'Lys-9Me1' function as an epigenetic
CC       mark of repressed chromatin.
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).
CC   -!- DISRUPTION PHENOTYPE: Loss of function mutant (T-DNA insertion)
CC       releases the transcriptional silencing of tandem transgenes.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 pre-SET domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SIMILARITY: Contains 1 YDG domain.
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DR   EMBL; AY702654; AAV84356.1; -; mRNA.
DR   RefSeq; XP_001701764.1; XM_001701712.1.
DR   UniGene; Cre.8950; -.
DR   ProteinModelPortal; Q5QD03; -.
DR   BioGrid; 987255; 1.
DR   GeneID; 5727449; -.
DR   KEGG; cre:CHLREDRAFT_6823; -.
DR   eggNOG; COG3440; -.
DR   KO; K11420; -.
DR   GO; GO:0005694; C:chromosome; 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   Gene3D; 2.30.280.10; -; 1.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR003105; SRA_YDG.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    957       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH3.
FT                                /FTId=PRO_0000281047.
FT   DOMAIN       73    243       YDG.
FT   DOMAIN      319    441       Pre-SET.
FT   DOMAIN      455    920       SET.
FT   DOMAIN      941    957       Post-SET.
FT   COMPBIAS    184    218       Gly-rich.
FT   COMPBIAS    560    573       Gln-rich.
FT   COMPBIAS    575    849       Ala-rich.
FT   COMPBIAS    577    657       Gly-rich.
SQ   SEQUENCE   957 AA;  98344 MW;  95933BBEBCFD4489 CRC64;
     MATIQLTDQQ RKVLHEVACT TAAPVLDTAS KDKIKQLLDD YDMRKAAMGS KPGANMVLPG
     QVLGEAGPFL DYGHPPGVAL GDKFKDRGQV MVAGVHGTTV RGIHAPNAGS EHFVRGAYSV
     LMSGVYVDDE DMGEAFWYTG EGGMDGKKQV KDQQMASGSN AALKNNCDTR TPVRVVRGFV
     QEAGGGEGGG GGEGGGGAKK GKGGKGGGKK EKGLVYEGLY LVLECKMEPS KDGPQVCKFL
     MHGLPGHSTV SAKVEYNIFG NAGSAYSLHA RRLAGAGAPA GGKRARKAAQ DEKARELARQ
     WMLSEIRRQY PGPELQLEDV SGGQEAVPIP VINQVNSERL PTDFAYTREY AWAPGVYQLV
     APALRLADEE MLQFSREGDR GGVCGIAFNR HIAALDRRLE QEGRLPQGYE AHLEEQYNAA
     GCLMVTDPCG VHECGDGCSA KACRRNMQLS AGVQLPLEVF MTESKGWGVR CREEVPAGAF
     VCCYVGQLIT DAMAEVRKGV DHYLFDLDFF AHIYAEIAEK GMQAVAEEIP LHKIPPVLSV
     GMIRQAQINA ADAARRLPEQ QPQQQQPQQQ QQQPAAGGAA PGGAAAGEQA AGGAEGGGAY
     GGGGAAAAAT AAGTAPGAGD NMDGVEGPAA QRSGGEEAAA GPGSSGAAGG CGYRLDGMVT
     REGLAQAAHA LAEACDALAR SVADGASTNL GGENILAAIE AAKARAAAAA TTSGGAAAAD
     QHQLEQLDRA AALAAASKAA ADAVKAGDPG AFYLQPIISR DEEKAAERAA AAAAAAAAAA
     GVPPALPSTS DVGNGGTTGS GGGGGAFSNR GPAGCAVGSP RALAARSGME AAAQAAGGAA
     SGPVAGPGAV EDHGEEYAPM LVIDARTTGN VGRFINHSCD GNLTIQAVFA GVYRSTLLYH
     VGLYACRNIP QLEELSYNYG YHKQQQQQQQ AQRGGAAEKQ FVMQCNCGAV GCIGNLM
//
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