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Histone-lysine N-methyltransferase family member SUVH2 (Cytosine-HMTase 2) (H3-K27-HMTase 2) (H4-K20-HMTase 2) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Protein SET DOMAIN GROUP 3) (Suppressor of variegation 3-9 homolog protein 2) (Su(var)3-9 homolog protein 2)

 SUVH2_ARATH             Reviewed;         651 AA.
O22781;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Histone-lysine N-methyltransferase family member SUVH2;
AltName: Full=Cytosine-HMTase 2;
AltName: Full=H3-K27-HMTase 2;
AltName: Full=H4-K20-HMTase 2;
AltName: Full=Histone H3-K9 methyltransferase 2;
Short=H3-K9-HMTase 2;
AltName: Full=Protein SET DOMAIN GROUP 3;
AltName: Full=Suppressor of variegation 3-9 homolog protein 2;
Short=Su(var)3-9 homolog protein 2;
Name=SUVH2; Synonyms=SDG3, SET3; OrderedLocusNames=At2g33290;
ORFNames=F4P9.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, NOMENCLATURE, AND
TISSUE SPECIFICITY.
PubMed=11691919; DOI=10.1093/nar/29.21.4319;
Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
"The Arabidopsis thaliana genome contains at least 29 active genes
encoding SET domain proteins that can be assigned to four
evolutionarily conserved classes.";
Nucleic Acids Res. 29:4319-4333(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-143; ARG-351;
VAL-385; ARG-411; VAL-584; MET-620; LEU-630 AND GLY-645.
PubMed=15775980; DOI=10.1038/sj.emboj.7600604;
Naumann K., Fischer A., Hofmann I., Krauss V., Phalke S., Irmler K.,
Hause G., Aurich A.-C., Dorn R., Jenuwein T., Reuter G.;
"Pivotal role of AtSUVH2 in heterochromatic histone methylation and
gene silencing in Arabidopsis.";
EMBO J. 24:1418-1429(2005).
[5]
FUNCTION, AND GENE FAMILY.
PubMed=16384625; DOI=10.1016/j.jplph.2005.10.015;
Fischer A., Hofmann I., Naumann K., Reuter G.;
"Heterochromatin proteins and the control of heterochromatic gene
silencing in Arabidopsis.";
J. Plant Physiol. 163:358-368(2006).
[6]
FUNCTION, DNA-BINDING, LACK OF METHYLTRANSFERASE ACTIVITY, AND LACK OF
S-ADENOSYL-L-METHIONINE BINDING.
PubMed=19043555; DOI=10.1371/journal.pgen.1000280;
Johnson L.M., Law J.A., Khattar A., Henderson I.R., Jacobsen S.E.;
"SRA-domain proteins required for DRM2-mediated de novo DNA
methylation.";
PLoS Genet. 4:E1000280-E1000280(2008).
[7]
FUNCTION, AND INTERACTION WITH NRPE1 AND DRD1.
PubMed=24463519; DOI=10.1038/nature12931;
Johnson L.M., Du J., Hale C.J., Bischof S., Feng S., Chodavarapu R.K.,
Zhong X., Marson G., Pellegrini M., Segal D.J., Patel D.J.,
Jacobsen S.E.;
"SRA- and SET-domain-containing proteins link RNA polymerase V
occupancy to DNA methylation.";
Nature 507:124-128(2014).
[8]
INTERACTION WITH MORC1/CRT1; DRD1 AND DMS3, AND SELF-INTERACTION.
STRAIN=cv. Columbia;
PubMed=24465213; DOI=10.1371/journal.pgen.1003948;
Liu Z.-W., Shao C.-R., Zhang C.-J., Zhou J.-X., Zhang S.-W., Li L.,
Chen S., Huang H.-W., Cai T., He X.-J.;
"The SET domain proteins SUVH2 and SUVH9 are required for Pol V
occupancy at RNA-directed DNA methylation loci.";
PLoS Genet. 10:E1003948-E1003948(2014).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27171427; DOI=10.1371/journal.pgen.1006026;
Liu Z.-W., Zhou J.-X., Huang H.-W., Li Y.-Q., Shao C.-R., Li L.,
Cai T., Chen S., He X.-J.;
"Two components of the RNA-Directed DNA methylation pathway associate
with MORC6 and silence loci targeted by MORC6 in Arabidopsis.";
PLoS Genet. 12:E1006026-E1006026(2016).
-!- FUNCTION: Histone methyltransferase family member that plays a
central role in gene silencing (PubMed:15775980, PubMed:16384625,
PubMed:19043555, PubMed:24463519, PubMed:27171427). Together with
MORC6 and SUVH9, regulates the silencing of some transposable
elements (TEs) (PubMed:27171427). According to PubMed:15775980, it
is required for normal methylation of 'Lys-9' and 'Lys-27' of
histone H3, 'Lys-20' of H4, and cytosine, but PubMed:19043555 see
no significant effect on histone methylation when the gene is
mutated. According to PubMed:19043555, the protein does not bind
S-adenosyl-L-methionine and lacks methyltransferase activity.
Instead, it may function downstream of DRM2 in RNA-directed DNA
methylation, binding to methylated DNA and recruiting DNA-directed
RNA polymerase V to chromatin (PubMed:24463519, PubMed:27171427).
{ECO:0000269|PubMed:15775980, ECO:0000269|PubMed:16384625,
ECO:0000269|PubMed:19043555, ECO:0000269|PubMed:24463519,
ECO:0000269|PubMed:27171427}.
-!- SUBUNIT: Self-interacts (PubMed:24465213). Interacts with DNA-
directed RNA polymerase V subunit NRPE1 and with DRD1 and DMS3
(PubMed:24463519, PubMed:24465213). Binds to MORC1/CRT1
(PubMed:24465213). {ECO:0000269|PubMed:24463519,
ECO:0000269|PubMed:24465213}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
Note=Associates with centromeric constitutive heterochromatin.
-!- TISSUE SPECIFICITY: Expressed at low levels in leaves stems and
flowers. {ECO:0000269|PubMed:11691919}.
-!- DOMAIN: Although both SET and pre-SET domains are present, the
absence of the post-SET domain may explain the lack of
methyltransferase activity. Besides, the Cys residues in the SET
domain that normally bind a zinc ion are not conserved.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Impaired gene silencing due to
decondensation of chromocenters leading to the derepression of
DNA-methylated genes and transposable elements (TEs).
{ECO:0000269|PubMed:27171427}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00908}.
-----------------------------------------------------------------------
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EMBL; AF344445; AAK28967.1; -; mRNA.
EMBL; AC002332; AAB80647.1; -; Genomic_DNA.
EMBL; CP002685; AEC08810.1; -; Genomic_DNA.
EMBL; CP002685; ANM61886.1; -; Genomic_DNA.
EMBL; CP002685; ANM61887.1; -; Genomic_DNA.
EMBL; CP002685; ANM61888.1; -; Genomic_DNA.
PIR; F84743; F84743.
RefSeq; NP_001318341.1; NM_001336444.1.
RefSeq; NP_001324077.1; NM_001336445.1.
RefSeq; NP_001324078.1; NM_001336446.1.
RefSeq; NP_180887.1; NM_128889.3.
UniGene; At.12115; -.
ProteinModelPortal; O22781; -.
SMR; O22781; -.
BioGrid; 3239; 1.
DIP; DIP-62059N; -.
IntAct; O22781; 37.
STRING; 3702.AT2G33290.1; -.
PaxDb; O22781; -.
EnsemblPlants; AT2G33290.1; AT2G33290.1; AT2G33290.
EnsemblPlants; AT2G33290.2; AT2G33290.2; AT2G33290.
EnsemblPlants; AT2G33290.3; AT2G33290.3; AT2G33290.
EnsemblPlants; AT2G33290.4; AT2G33290.4; AT2G33290.
GeneID; 817892; -.
Gramene; AT2G33290.1; AT2G33290.1; AT2G33290.
Gramene; AT2G33290.2; AT2G33290.2; AT2G33290.
Gramene; AT2G33290.3; AT2G33290.3; AT2G33290.
Gramene; AT2G33290.4; AT2G33290.4; AT2G33290.
KEGG; ath:AT2G33290; -.
Araport; AT2G33290; -.
TAIR; locus:2051083; AT2G33290.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG2940; LUCA.
eggNOG; COG3440; LUCA.
HOGENOM; HOG000238382; -.
InParanoid; O22781; -.
KO; K11420; -.
OMA; RIVEYWF; -.
OrthoDB; EOG093603OW; -.
PhylomeDB; O22781; -.
Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
PRO; PR:O22781; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; O22781; AT.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005720; C:nuclear heterochromatin; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042054; F:histone methyltransferase activity; ISS:TAIR.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016571; P:histone methylation; IDA:TAIR.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
GO; GO:0080188; P:RNA-directed DNA methylation; IMP:UniProtKB.
Gene3D; 2.30.280.10; -; 1.
InterPro; IPR025794; Hist-Lys_N-MeTrfase_plant.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR001214; SET_dom.
InterPro; IPR036987; SRA-YDG_sf.
InterPro; IPR003105; SRA_YDG.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF02182; SAD_SRA; 1.
Pfam; PF00856; SET; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SMART; SM00466; SRA; 1.
SUPFAM; SSF88697; SSF88697; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS51015; YDG; 1.
1: Evidence at protein level;
Centromere; Chromatin regulator; Chromosome; Complete proteome;
DNA-binding; Metal-binding; Nucleus; Reference proteome; Zinc.
CHAIN 1 651 Histone-lysine N-methyltransferase family
member SUVH2.
/FTId=PRO_0000186073.
DOMAIN 202 358 YDG. {ECO:0000255|PROSITE-
ProRule:PRU00358}.
DOMAIN 434 492 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 495 638 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
METAL 436 436 Zinc 1. {ECO:0000250}.
METAL 436 436 Zinc 2. {ECO:0000250}.
METAL 438 438 Zinc 1. {ECO:0000250}.
METAL 442 442 Zinc 1. {ECO:0000250}.
METAL 442 442 Zinc 3. {ECO:0000250}.
METAL 446 446 Zinc 1. {ECO:0000250}.
METAL 448 448 Zinc 2. {ECO:0000250}.
METAL 474 474 Zinc 2. {ECO:0000250}.
METAL 474 474 Zinc 3. {ECO:0000250}.
METAL 478 478 Zinc 2. {ECO:0000250}.
METAL 480 480 Zinc 3. {ECO:0000250}.
METAL 484 484 Zinc 3. {ECO:0000250}.
MUTAGEN 143 143 E->D: In 5-1; ectopic nuclear
localization.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 351 351 R->K: In 5-2; loss of 5-methylcytosine,
H3K9 dimethylation and H4K20
monomethylation.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 385 385 V->A: In 5-3; loss of 5-methylcytosine,
H3K9 dimethylation and H4K20
monomethylation.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 411 411 R->I: In 5-4; loss of H3K9 and H4K20
methylation.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 584 584 V->G: In 5-5; loss of H3K9 and H4K20
methylation.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 620 620 M->T: In 5-6; loss of H3K9 and H4K20
methylation; when associated with T-630.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 630 630 L->V: In 5-6; loss of H3K9 and H4K20
methylation; when associated with V-620.
{ECO:0000269|PubMed:15775980}.
MUTAGEN 645 645 G->S: In 5-7; loss of H3K9 and H4K20
methylation.
{ECO:0000269|PubMed:15775980}.
SEQUENCE 651 AA; 72848 MW; 412AD76C8869ACF9 CRC64;
MSTLLPFPDL NLMPDSQSST AGTTAGDTVV TGKLEVKSEP IEEWQTPPSS TSDQSANTDL
IAEFIRISEL FRSAFKPLQV KGLDGVSVYG LDSGAIVAVP EKENRELIEP PPGFKDNRVS
TVVVSPKFER PRELARIAIL GHEQRKELRQ VMKRTRMTYE SLRIHLMAES MKNHVLGQGR
RRRSDMAAAY IMRDRGLWLN YDKHIVGPVT GVEVGDIFFY RMELCVLGLH GQTQAGIDCL
TAERSATGEP IATSIVVSGG YEDDEDTGDV LVYTGHGGQD HQHKQCDNQR LVGGNLGMER
SMHYGIEVRV IRGIKYENSI SSKVYVYDGL YKIVDWWFAV GKSGFGVFKF RLVRIEGQPM
MGSAVMRFAQ TLRNKPSMVR PTGYVSFDLS NKKENVPVFL YNDVDGDQEP RHYEYIAKAV
FPPGIFGQGG ISRTGCECKL SCTDDCLCAR KNGGEFAYDD NGHLLKGKHV VFECGEFCTC
GPSCKSRVTQ KGLRNRLEVF RSKETGWGVR TLDLIEAGAF ICEYAGVVVT RLQAEILSMN
GDVMVYPGRF TDQWRNWGDL SQVYPDFVRP NYPSLPPLDF SMDVSRMRNV ACYISHSKEP
NVMVQFVLHD HNHLMFPRVM LFALENISPL AELSLDYGLA DEVNGKLAIC N


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