GenomeNet

Database: UniProt
Entry: Q9FNC7
LinkDB: Q9FNC7
Original site: Q9FNC7 
ID   SUVR2_ARATH             Reviewed;         717 AA.
AC   Q9FNC7; Q0WKU5; Q941L4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   10-APR-2019, entry version 110.
DE   RecName: Full=Probable inactive histone-lysine N-methyltransferase SUVR2;
DE   AltName: Full=Protein SET DOMAIN GROUP 18;
DE   AltName: Full=Suppressor of variegation 3-9-related protein 2;
DE            Short=Su(var)3-9-related protein 2;
GN   Name=SUVR2; Synonyms=SDG18, SET18; OrderedLocusNames=At5g43990;
GN   ORFNames=MRH10.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II.
RT   Sequence features of the regions of 1,044,062 bp covered by thirteen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, INTERACTION
RP   WITH SUVR1; CHR19; CHR27 AND CHR28, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF LEU-32; ASP-52; HIS-636 AND CYS-638.
RX   PubMed=25420628; DOI=10.1038/cr.2014.156;
RA   Han Y.F., Dou K., Ma Z.Y., Zhang S.W., Huang H.W., Li L., Cai T.,
RA   Chen S., Zhu J.K., He X.J.;
RT   "SUVR2 is involved in transcriptional gene silencing by associating
RT   with SNF2-related chromatin-remodeling proteins in Arabidopsis.";
RL   Cell Res. 24:1445-1465(2014).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CHR27.
RX   PubMed=25425661; DOI=10.1073/pnas.1420515111;
RA   Groth M., Stroud H., Feng S., Greenberg M.V., Vashisht A.A.,
RA   Wohlschlegel J.A., Jacobsen S.E., Ausin I.;
RT   "SNF2 chromatin remodeler-family proteins FRG1 and -2 are required for
RT   RNA-directed DNA methylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:17666-17671(2014).
CC   -!- FUNCTION: Probable inactive histone-lysine methyltransferase that
CC       acts as regulator of transctiptional gene silencing independently
CC       of histone H3K9 methylation. Contributes to transcriptional gene
CC       silencing at RNA-directed DNA methylation (RdDM) target loci but
CC       also at RdDM-independent target loci. Forms a complex with SUVR1
CC       and associates with the SNF2-related chromatin-remodeling proteins
CC       CHR19, CHR27, and CHR28, thereby mediating nucleosome positioning
CC       and transcriptional silencing. Does not possess histone-lysine
CC       methyltransferase activity in vitro, and the conserved catalytic
CC       sites of SUVR2 are dispensable for its function in transcriptional
CC       gene silencing. {ECO:0000269|PubMed:25420628}.
CC   -!- SUBUNIT: Interacts with SUVR1, CHR19, CHR28 and itself
CC       (PubMed:25420628). Interacts with CHR27 (PubMed:25420628,
CC       PubMed:25425661). {ECO:0000269|PubMed:25420628,
CC       ECO:0000269|PubMed:25425661}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25420628}.
CC       Chromosome {ECO:0000269|PubMed:25420628}. Note=Displays two
CC       nuclear localization patterns, one forming condensed foci and the
CC       other showing diffused signals. {ECO:0000269|PubMed:25420628}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FNC7-1; Sequence=Displayed;
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. {ECO:0000255|PROSITE-ProRule:PRU00913}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY045576; AAK92218.1; -; mRNA.
DR   EMBL; AB006703; BAB09059.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95042.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95043.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95044.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70135.1; -; Genomic_DNA.
DR   EMBL; AK230468; BAF02262.1; -; mRNA.
DR   RefSeq; NP_001078702.1; NM_001085233.2. [Q9FNC7-1]
DR   RefSeq; NP_001078703.1; NM_001085234.2. [Q9FNC7-1]
DR   RefSeq; NP_001331767.1; NM_001344514.1. [Q9FNC7-1]
DR   RefSeq; NP_568631.1; NM_123766.3. [Q9FNC7-1]
DR   UniGene; At.26569; -.
DR   ProteinModelPortal; Q9FNC7; -.
DR   SMR; Q9FNC7; -.
DR   BioGrid; 19672; 11.
DR   STRING; 3702.AT5G43990.2; -.
DR   PaxDb; Q9FNC7; -.
DR   EnsemblPlants; AT5G43990.11; AT5G43990.11; AT5G43990. [Q9FNC7-1]
DR   EnsemblPlants; AT5G43990.1; AT5G43990.1; AT5G43990. [Q9FNC7-1]
DR   EnsemblPlants; AT5G43990.3; AT5G43990.3; AT5G43990. [Q9FNC7-1]
DR   EnsemblPlants; AT5G43990.4; AT5G43990.4; AT5G43990. [Q9FNC7-1]
DR   GeneID; 834422; -.
DR   Gramene; AT5G43990.11; AT5G43990.11; AT5G43990. [Q9FNC7-1]
DR   Gramene; AT5G43990.1; AT5G43990.1; AT5G43990. [Q9FNC7-1]
DR   Gramene; AT5G43990.3; AT5G43990.3; AT5G43990. [Q9FNC7-1]
DR   Gramene; AT5G43990.4; AT5G43990.4; AT5G43990. [Q9FNC7-1]
DR   KEGG; ath:AT5G43990; -.
DR   Araport; AT5G43990; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000029715; -.
DR   InParanoid; Q9FNC7; -.
DR   OrthoDB; 260204at2759; -.
DR   PhylomeDB; Q9FNC7; -.
DR   Reactome; R-ATH-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q9FNC7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNC7; baseline and differential.
DR   Genevisible; Q9FNC7; AT.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0080188; P:RNA-directed DNA methylation; IDA:UniProtKB.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR025776; SUVR4/1/2.
DR   InterPro; IPR018848; WIYLD_domain.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF10440; WIYLD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51580; SAM_MT43_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; RNA-mediated gene silencing;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    717       Probable inactive histone-lysine N-
FT                                methyltransferase SUVR2.
FT                                /FTId=PRO_0000233366.
FT   DOMAIN      458    547       Pre-SET.
FT   DOMAIN      550    679       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      690    706       Post-SET.
FT   REGION      561    563       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   REGION      635    636       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   COMPBIAS    445    462       Cys-rich.
FT   METAL       445    445       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       445    445       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       446    446       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       449    449       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       449    449       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       453    453       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       462    462       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       529    529       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       529    529       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       533    533       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       535    535       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       539    539       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       638    638       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       694    694       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       696    696       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       701    701       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   BINDING     678    678       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MUTAGEN      32     32       L->A: No effect on its function in
FT                                transcriptional gene silencing; when
FT                                associated with A52, A636 and A638.
FT                                {ECO:0000269|PubMed:25420628}.
FT   MUTAGEN      52     52       D->A: No effect on its function in
FT                                transcriptional gene silencing; when
FT                                associated with A32, A636 and A638.
FT                                {ECO:0000269|PubMed:25420628}.
FT   MUTAGEN     636    636       H->A: No effect on its function in
FT                                transcriptional gene silencing; when
FT                                associated with A32, A52 and A638.
FT                                {ECO:0000269|PubMed:25420628}.
FT   MUTAGEN     638    638       C->A: No effect on its function in
FT                                transcriptional gene silencing; when
FT                                associated with A32, A52 and A636.
FT                                {ECO:0000269|PubMed:25420628}.
FT   CONFLICT     23     23       R -> Q (in Ref. 1; AAK92218).
FT                                {ECO:0000305}.
FT   CONFLICT     32     32       L -> P (in Ref. 4; BAF02262).
FT                                {ECO:0000305}.
FT   CONFLICT     36     36       E -> D (in Ref. 1; AAK92218).
FT                                {ECO:0000305}.
SQ   SEQUENCE   717 AA;  79363 MW;  20B82033F384EC54 CRC64;
     MAPNLHIKKA FMAMRAMGIE DARVKPVLKN LLALYEKNWE LIAEDNYRVL ADAIFDSHED
     QAIQESEEKK ADEVKEDEGC AAEVDRGKKK LHESIEDDED VMAESDRPLK RLRRRGEGGS
     ALASPSLGSP TLEGPSINDE ENAPILLPYH PVPIENDHDA GELILTKVEP ITNMPLSSIP
     DSVDRGDSSM LEIDKSNGHV EEKAGETVST ADGTTNDISP TTVARFSDHK LAATIEEPPA
     LELASSASGE VKINLSFAPA TGGSNPHLPS MEELRRAMEE KCLRSYKILD PNFSVLGFMN
     DICSCYLDLA TNGRDSANQL PKNLPFVTTN IDALKKSAAR MAYTSQASND VVEICSNEHM
     RDAENGAVGD SMALVVVPEC QLSADEWRLI SSVGDISLGK ETVEIPWVNE VNDKVPPVFH
     YIAQSLVYQD AAVKFSLGNI RDDQCCSSCC GDCLAPSMAC RCATAFNGFA YTVDGLLQED
     FLEQCISEAR DPRKQMLLYC KECPLEKAKK EVILEPCKGH LKRKAIKECW SKCGCMKNCG
     NRVVQQGIHN KLQVFFTPNG RGWGLRTLEK LPKGAFVCEL AGEILTIPEL FQRISDRPTS
     PVILDAYWGS EDISGDDKAL SLEGTHYGNI SRFINHRCLD ANLIEIPVHA ETTDSHYYHL
     AFFTTREIDA MEELTWDYGV PFNQDVFPTS PFHCQCGSDF CRVRKQISKG KNVKKRA
//
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