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 06-MAR-2013, entry version 50.
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 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 HSSP; Q8X225; 1PEG.
DR ProteinModelPortal; Q5QD03; -.
DR GeneID; 5727449; -.
DR KEGG; cre:CHLREDRAFT_6823; -.
DR eggNOG; COG3440; -.
DR ProtClustDB; CLSN2923752; -.
DR BioCyc; CHLAMY:CHLREDRAFT_6823-MONOMER; -.
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:EC.
DR GO; GO:0034968; P:histone lysine methylation; IEA:GOC.
DR Gene3D; 2.30.280.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR003105; SRA_YDG.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF02182; YDG_SRA; 1.
DR SMART; SM00317; SET; 1.
DR PROSITE; PS50868; POST_SET; FALSE_NEG.
DR PROSITE; PS50867; PRE_SET; FALSE_NEG.
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 454 924 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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