GenomeNet

Database: UniProt
Entry: Q946J2
LinkDB: Q946J2
Original site: Q946J2 
ID   SUVR1_ARATH             Reviewed;         734 AA.
AC   Q946J2; O64498; Q9SAW1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   13-FEB-2019, entry version 111.
DE   RecName: Full=Probable inactive histone-lysine N-methyltransferase SUVR1;
DE   AltName: Full=Protein SET DOMAIN GROUP 13;
DE   AltName: Full=Suppressor of variegation 3-9-related protein 1;
DE            Short=Su(var)3-9-related protein 1;
GN   Name=SUVR1; Synonyms=SDG13, SET13; OrderedLocusNames=At1g04050;
GN   ORFNames=F20D22.16, F21M11.1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 85-734, AND NOMENCLATURE.
RC   STRAIN=cv. C24;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND INTERACTION WITH
RP   SUVR2.
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).
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.
CC       {ECO:0000250|UniProtKB:Q9FNC7}.
CC   -!- SUBUNIT: Interacts with SUVR2 and itself.
CC       {ECO:0000269|PubMed:25420628}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9FNC7}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9FNC7}.
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=AAC16755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAK77165.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AC002411; AAC16755.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC003027; AAD10665.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27650.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58278.1; -; Genomic_DNA.
DR   EMBL; AF394239; AAK77165.1; ALT_INIT; mRNA.
DR   PIR; G86171; G86171.
DR   PIR; T00966; T00966.
DR   RefSeq; NP_001320724.1; NM_001331459.1.
DR   RefSeq; NP_001320725.1; NM_001331458.1.
DR   RefSeq; NP_171901.3; NM_100286.4.
DR   UniGene; At.10585; -.
DR   ProteinModelPortal; Q946J2; -.
DR   SMR; Q946J2; -.
DR   BioGrid; 24555; 7.
DR   IntAct; Q946J2; 4.
DR   STRING; 3702.AT1G04050.1; -.
DR   iPTMnet; Q946J2; -.
DR   PaxDb; Q946J2; -.
DR   PRIDE; Q946J2; -.
DR   EnsemblPlants; AT1G04050.1; AT1G04050.1; AT1G04050.
DR   EnsemblPlants; AT1G04050.2; AT1G04050.2; AT1G04050.
DR   GeneID; 839320; -.
DR   Gramene; AT1G04050.1; AT1G04050.1; AT1G04050.
DR   Gramene; AT1G04050.2; AT1G04050.2; AT1G04050.
DR   KEGG; ath:AT1G04050; -.
DR   Araport; AT1G04050; -.
DR   TAIR; locus:2024229; AT1G04050.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000029715; -.
DR   InParanoid; Q946J2; -.
DR   OMA; ACDAMKL; -.
DR   OrthoDB; 260204at2759; -.
DR   Reactome; R-ATH-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q946J2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q946J2; baseline and differential.
DR   Genevisible; Q946J2; AT.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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   Chromatin regulator; Chromosome; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase;
KW   Zinc.
FT   CHAIN         1    734       Probable inactive histone-lysine N-
FT                                methyltransferase SUVR1.
FT                                /FTId=PRO_0000233365.
FT   DOMAIN      460    563       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      566    696       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      707    723       Post-SET.
FT   REGION      577    579       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   REGION      652    653       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H5I1}.
FT   COMPBIAS     65     80       Lys-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00012}.
FT   COMPBIAS    124    132       Ser-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00016}.
FT   METAL       460    460       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       464    464       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       464    464       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       468    468       Zinc 1. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       477    477       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       545    545       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       545    545       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       549    549       Zinc 2. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       551    551       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       555    555       Zinc 3. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       655    655       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       711    711       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       713    713       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   METAL       718    718       Zinc 4. {ECO:0000250|UniProtKB:Q9H5I1}.
FT   BINDING     695    695       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   734 AA;  82753 MW;  3AC7B653F5B4588A CRC64;
     MAPNLRIKKA CDAMKLLGIS ETKTRAFLRK LLKTYENNWD FIEEDAYKVL LDAIFDEADA
     QSTEKNKKEE EKKKKEEEKK SRSVATSRGR RKAPEPLVQD EEDDMDEDEF PLKRRLRSRR
     GRASSSSSSS SSYNNEDLKT QPEEEDEDDG VTELPPLKRY VRRNGERGLA MTVYNNASPS
     SSSRLSMEPE EVPPMVLLPA HPMETKVSEA SALVILNDEP NIDHKPVISD TGNCSAPMLE
     MGKSNIHVQE WDWETKDILN DTTAMDVSPS SAIGESSEHK VAAASVELAS STSGEAKICL
     SFAPATGETT NLHLPSMEDL RRAMEEKCLK SYKIVHPEFS VLGFMKDMCS CYIDLAKNST
     SQLLETETVC DMSKAGDESG AVGISMPLVV VPECEISGDG WKAISNMKDI TAGEENVEIP
     WVNEINEKVP SRFRYMPHSF VFQDAPVIFS LSSFSDEQSC STSCIEDCLA SEMSCNCAIG
     VDNGFAYTLD GLLKEEFLEA RISEARDQRK QVLRFCEECP LERAKKVEIL EPCKGHLKRG
     AIKECWFKCG CTKRCGNRVV QRGMHNKLQV FFTPNGKGWG LRTLEKLPKG AFICEYIGEI
     LTIPELYQRS FEDKPTLPVI LDAHWGSEER LEGDKALCLD GMFYGNISRF LNHRCLDANL
     IEIPVQVETP DQHYYHLAFF TTRDIEAMEE LAWDYGIDFN DNDSLMKPFD CLCGSRFCRN
     KKRSTKTMQI LNKA
//
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