SUVR1_ARATH
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 03-AUG-2022, entry version 124.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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 encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND INTERACTION WITH 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., 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).
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. {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 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=AAC16755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK77165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; 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 ProteomicsDB; 226527; -.
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 HOGENOM; CLU_011618_0_0_1; -.
DR InParanoid; Q946J2; -.
DR OMA; SDFHMPS; -.
DR OrthoDB; 260204at2759; -.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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; 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; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..734
FT /note="Probable inactive histone-lysine N-methyltransferase
FT SUVR1"
FT /id="PRO_0000233365"
FT DOMAIN 460..563
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 566..696
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 707..723
FT /note="Post-SET"
FT REGION 61..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 577..579
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 652..653
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 695
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 711
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 713
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT BINDING 718
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
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
