SUVR2_ARATH
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 03-AUG-2022, entry version 123.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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 encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT 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. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT 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 reference
RT 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., Hayashizaki Y.,
RA 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 WITH
RP SUVR1; CHR19; CHR27 AND CHR28, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 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., Chen S.,
RA Zhu J.K., He X.J.;
RT "SUVR2 is involved in transcriptional gene silencing by associating with
RT 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 RNA-
RT directed DNA methylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17666-17671(2014).
CC -!- FUNCTION: Probable inactive histone-lysine methyltransferase that acts
CC as regulator of transctiptional gene silencing independently of histone
CC H3K9 methylation. Contributes to transcriptional gene silencing at RNA-
CC directed DNA methylation (RdDM) target loci but also at RdDM-
CC independent target loci. Forms a complex with SUVR1 and associates with
CC the SNF2-related chromatin-remodeling proteins CHR19, CHR27, and CHR28,
CC thereby mediating nucleosome positioning and transcriptional silencing.
CC Does not possess histone-lysine methyltransferase activity in vitro,
CC and the conserved catalytic sites of SUVR2 are dispensable for its
CC function in transcriptional gene silencing.
CC {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}. Chromosome
CC {ECO:0000269|PubMed:25420628}. Note=Displays two nuclear localization
CC patterns, one forming condensed foci and the other showing diffused
CC 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 are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00913}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q9FNC7; -.
DR SMR; Q9FNC7; -.
DR BioGRID; 19672; 11.
DR STRING; 3702.AT5G43990.2; -.
DR PaxDb; Q9FNC7; -.
DR PRIDE; Q9FNC7; -.
DR ProteomicsDB; 226528; -. [Q9FNC7-1]
DR EnsemblPlants; AT5G43990.1; AT5G43990.1; AT5G43990. [Q9FNC7-1]
DR EnsemblPlants; AT5G43990.11; AT5G43990.11; 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; AT5G43990.1; AT5G43990.1; AT5G43990. [Q9FNC7-1]
DR Gramene; AT5G43990.11; AT5G43990.11; 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 InParanoid; Q9FNC7; -.
DR PhylomeDB; Q9FNC7; -.
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:gene silencing by RNA-directed DNA methylation; IDA:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR Gene3D; 1.10.8.850; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR025776; SUVR4/1/2.
DR InterPro; IPR043017; WIYLD_dom_sf.
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 SUPFAM; SSF82199; SSF82199; 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; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome;
KW RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..717
FT /note="Probable inactive histone-lysine N-methyltransferase
FT SUVR2"
FT /id="PRO_0000233366"
FT DOMAIN 458..547
FT /note="Pre-SET"
FT DOMAIN 550..679
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 690..706
FT /note="Post-SET"
FT REGION 61..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 561..563
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 635..636
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 638
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 678
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 701
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT MUTAGEN 32
FT /note="L->A: No effect on its function in transcriptional
FT gene silencing; when associated with A52, A636 and A638."
FT /evidence="ECO:0000269|PubMed:25420628"
FT MUTAGEN 52
FT /note="D->A: No effect on its function in transcriptional
FT gene silencing; when associated with A32, A636 and A638."
FT /evidence="ECO:0000269|PubMed:25420628"
FT MUTAGEN 636
FT /note="H->A: No effect on its function in transcriptional
FT gene silencing; when associated with A32, A52 and A638."
FT /evidence="ECO:0000269|PubMed:25420628"
FT MUTAGEN 638
FT /note="C->A: No effect on its function in transcriptional
FT gene silencing; when associated with A32, A52 and A636."
FT /evidence="ECO:0000269|PubMed:25420628"
FT CONFLICT 23
FT /note="R -> Q (in Ref. 1; AAK92218)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="L -> P (in Ref. 4; BAF02262)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="E -> D (in Ref. 1; AAK92218)"
FT /evidence="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
