SUVH3_CHLRE
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-AUG-2022, entry version 92.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3;
DE EC=2.1.1.367 {ECO:0000269|PubMed:17251191};
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; core chlorophytes; Chlorophyceae;
OC CS clade; 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, CATALYTIC ACTIVITY, 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 'Lys-
CC 9' of histone H3. H3 'Lys-9Me1' (H3K9me1) functions as an epigenetic
CC mark of repressed chromatin. {ECO:0000269|PubMed:17251191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC Evidence={ECO:0000269|PubMed:17251191};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}.
CC Chromosome {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Loss of function mutant (T-DNA insertion)
CC releases the transcriptional silencing of tandem transgenes.
CC {ECO:0000269|PubMed:17251191}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AY702654; AAV84356.1; -; mRNA.
DR RefSeq; XP_001701764.1; XM_001701712.1.
DR AlphaFoldDB; Q5QD03; -.
DR BioGRID; 987255; 1.
DR STRING; 3055.EDP06739; -.
DR EnsemblPlants; PNW86502; PNW86502; CHLRE_02g089200v5.
DR GeneID; 5727449; -.
DR Gramene; PNW86502; PNW86502; CHLRE_02g089200v5.
DR KEGG; cre:CHLRE_02g089200v5; -.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_308463_0_0_1; -.
DR OMA; PVRRFRC; -.
DR OrthoDB; 75825at2759; -.
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:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR Gene3D; 2.170.270.10; -; 2.
DR Gene3D; 2.30.280.10; -; 1.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51015; YDG; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..957
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH3"
FT /id="PRO_0000281047"
FT DOMAIN 73..243
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 319..441
FT /note="Pre-SET"
FT DOMAIN 455..920
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 941..957
FT /note="Post-SET"
FT REGION 182..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
