GenomeNet

Database: UniProt
Entry: Q8W595
LinkDB: Q8W595
Original site: Q8W595 
ID   SUVR4_ARATH             Reviewed;         492 AA.
AC   Q8W595; Q3EBC4; Q9M848;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   13-FEB-2019, entry version 115.
DE   RecName: Full=Histone-lysine N-methyltransferase SUVR4;
DE            EC=2.1.1.43;
DE   AltName: Full=Protein SET DOMAIN GROUP 31;
DE   AltName: Full=Suppressor of variegation 3-9-related protein 4;
DE            Short=Su(var)3-9-related protein 4;
GN   Name=SUVR4; Synonyms=SDG31, SET31; OrderedLocusNames=At3g04380;
GN   ORFNames=T27C4.2;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
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   FUNCTION, INTERACTION WITH UBIQUITIN, AND CATALYTIC ACTIVITY.
RX   PubMed=21423664; DOI=10.1371/journal.pgen.1001325;
RA   Veiseth S.V., Rahman M.A., Yap K.L., Fischer A., Egge-Jacobsen W.,
RA   Reuter G., Zhou M.M., Aalen R.B., Thorstensen T.;
RT   "The SUVR4 histone lysine methyltransferase binds ubiquitin and
RT   converts H3K9me1 to H3K9me3 on transposon chromatin in Arabidopsis.";
RL   PLoS Genet. 7:E1001325-E1001325(2011).
RN   [5]
RP   STRUCTURE BY NMR OF 1-89, AND INTERACTION WITH UBIQUITIN.
RX   PubMed=24625295; DOI=10.1021/bi401436h;
RA   Rahman M.A., Kristiansen P.E., Veiseth S.V., Andersen J.T., Yap K.L.,
RA   Zhou M.M., Sandlie I., Thorstensen T., Aalen R.B.;
RT   "The Arabidopsis histone methyltransferase SUVR4 binds ubiquitin via a
RT   domain with a four-helix bundle structure.";
RL   Biochemistry 53:2091-2100(2014).
CC   -!- FUNCTION: Histone methyltransferase that converts monomethylated
CC       'Lys-9' of histone H3 (H3K9me1) to dimethylated 'Lys-9' (H3K9me2)
CC       in the absence of bound ubiquitin, and to trimethylated 'Lys-9'
CC       (H3K9me3) in the presence of bound ubiquitin. Acts in a locus-
CC       specific manner and contributes to the transcriptional silencing
CC       of pseudogenes and transposons. H3 'Lys-9' methylation represents
CC       a specific tag for epigenetic transcriptional repression.
CC       {ECO:0000269|PubMed:21423664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00913,
CC         ECO:0000269|PubMed:21423664};
CC   -!- SUBUNIT: Interacts with ubiquitin. {ECO:0000269|PubMed:21423664,
CC       ECO:0000269|PubMed:24625295}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Associates with euchromatic regions.
CC       {ECO:0000250}.
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=Q8W595-1; 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=AAF63769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF408062; AAL01113.2; -; mRNA.
DR   EMBL; AC022287; AAF63769.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74073.1; -; Genomic_DNA.
DR   RefSeq; NP_187088.2; NM_111309.3. [Q8W595-1]
DR   UniGene; At.27206; -.
DR   PDB; 2LXE; NMR; -; A=1-89.
DR   PDBsum; 2LXE; -.
DR   ProteinModelPortal; Q8W595; -.
DR   SMR; Q8W595; -.
DR   BioGrid; 4928; 6.
DR   IntAct; Q8W595; 3.
DR   STRING; 3702.AT3G04380.1; -.
DR   PaxDb; Q8W595; -.
DR   PRIDE; Q8W595; -.
DR   EnsemblPlants; AT3G04380.1; AT3G04380.1; AT3G04380. [Q8W595-1]
DR   GeneID; 819593; -.
DR   Gramene; AT3G04380.1; AT3G04380.1; AT3G04380. [Q8W595-1]
DR   KEGG; ath:AT3G04380; -.
DR   Araport; AT3G04380; -.
DR   TAIR; locus:2100885; AT3G04380.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000029715; -.
DR   InParanoid; Q8W595; -.
DR   OrthoDB; 260204at2759; -.
DR   PhylomeDB; Q8W595; -.
DR   Reactome; R-ATH-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q8W595; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8W595; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034968; P:histone lysine 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; PS50867; PRE_SET; 1.
DR   PROSITE; PS51580; SAM_MT43_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    492       Histone-lysine N-methyltransferase SUVR4.
FT                                /FTId=PRO_0000233368.
FT   DOMAIN      196    299       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      302    435       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      446    462       Post-SET.
FT   REGION      313    315       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   REGION      391    392       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       196    196       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       196    196       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       197    197       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       200    200       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       200    200       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       204    204       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       213    213       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       281    281       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       281    281       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       285    285       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       287    287       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       291    291       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       394    394       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       450    450       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       452    452       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       457    457       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   BINDING     434    434       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    302    302       C -> W (in Ref. 1; AAL01113).
FT                                {ECO:0000305}.
FT   CONFLICT    482    488       QGSKEVS -> ARFQRGV (in Ref. 1; AAL01113).
FT                                {ECO:0000305}.
FT   STRAND        7      9       {ECO:0000244|PDB:2LXE}.
FT   TURN         14     16       {ECO:0000244|PDB:2LXE}.
FT   HELIX        17     21       {ECO:0000244|PDB:2LXE}.
FT   HELIX        29     38       {ECO:0000244|PDB:2LXE}.
FT   HELIX        43     56       {ECO:0000244|PDB:2LXE}.
FT   HELIX        61     64       {ECO:0000244|PDB:2LXE}.
FT   TURN         65     68       {ECO:0000244|PDB:2LXE}.
FT   HELIX        70     80       {ECO:0000244|PDB:2LXE}.
SQ   SEQUENCE   492 AA;  55855 MW;  86DA23CF75DD158E CRC64;
     MISLSGLTSS VESDLDMQQA MLTNKDEKVL KALERTRQLD IPDEKTMPVL MKLLEEAGGN
     WSYIKLDNYT ALVDAIYSVE DENKQSEGSS NGNRGKNLKV IDSPATLKKT YETRSASSGS
     SIQVVQKQPQ LSNGDRKRKY KSRIADITKG SESVKIPLVD DVGSEAVPKF TYIPHNIVYQ
     SAYLHVSLAR ISDEDCCANC KGNCLSADFP CTCARETSGE YAYTKEGLLK EKFLDTCLKM
     KKEPDSFPKV YCKDCPLERD HDKGTYGKCD GHLIRKFIKE CWRKCGCDMQ CGNRVVQRGI
     RCQLQVYFTQ EGKGWGLRTL QDLPKGTFIC EYIGEILTNT ELYDRNVRSS SERHTYPVTL
     DADWGSEKDL KDEEALCLDA TICGNVARFI NHRCEDANMI DIPIEIETPD RHYYHIAFFT
     LRDVKAMDEL TWDYMIDFND KSHPVKAFRC CCGSESCRDR KIKGSQGKSI ERRKIVSAKK
     QQGSKEVSKK RK
//
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