GenomeNet

Database: UniProt
Entry: Q8VZ17
LinkDB: Q8VZ17
Original site: Q8VZ17 
ID   SUVH6_ARATH             Reviewed;         790 AA.
AC   Q8VZ17; Q9C5P2; Q9ZQ40;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   13-FEB-2019, entry version 128.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 6;
DE            Short=H3-K9-HMTase 6;
DE   AltName: Full=Protein SET DOMAIN GROUP 23;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 6;
DE            Short=Su(var)3-9 homolog protein 6;
GN   Name=SUVH6; Synonyms=SDG23, SET23; OrderedLocusNames=At2g22740;
GN   ORFNames=T9I22.18;
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 [GENOMIC DNA], 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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
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;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=15014946; DOI=10.1007/s00412-004-0275-7;
RA   Jackson J.P., Johnson L., Jasencakova Z., Zhang X., PerezBurgos L.,
RA   Singh P.B., Cheng X., Schubert I., Jenuwein T., Jacobsen S.E.;
RT   "Dimethylation of histone H3 lysine 9 is a critical mark for DNA
RT   methylation and gene silencing in Arabidopsis thaliana.";
RL   Chromosoma 112:308-315(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16287862; DOI=10.1128/MCB.25.23.10507-10515.2005;
RA   Ebbs M.L., Bartee L., Bender J.;
RT   "H3 lysine 9 methylation is maintained on a transcribed inverted
RT   repeat by combined action of SUVH6 and SUVH4 methyltransferases.";
RL   Mol. Cell. Biol. 25:10507-10515(2005).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=16384625; DOI=10.1016/j.jplph.2005.10.015;
RA   Fischer A., Hofmann I., Naumann K., Reuter G.;
RT   "Heterochromatin proteins and the control of heterochromatic gene
RT   silencing in Arabidopsis.";
RL   J. Plant Physiol. 163:358-368(2006).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-9' of histone
CC       H3. H3 'Lys-9' methylation represents a specific tag for
CC       epigenetic transcriptional repression. Seems to act preferentially
CC       on dsMRNA. {ECO:0000269|PubMed:15014946,
CC       ECO:0000269|PubMed:16287862}.
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:PRU00908};
CC   -!- INTERACTION:
CC       C0SUW7:ARID6; NbExp=3; IntAct=EBI-15193239, EBI-15192335;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00358}. Chromosome, centromere {ECO:0000250}.
CC       Note=Associates with centromeric constitutive heterochromatin.
CC       {ECO:0000250}.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity.
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. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00908}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15582.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF344449; AAK28971.1; -; Genomic_DNA.
DR   EMBL; AC006340; AAD15582.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC07347.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07348.1; -; Genomic_DNA.
DR   EMBL; AY065374; AAL38815.1; -; mRNA.
DR   EMBL; BT002751; AAO22580.1; -; mRNA.
DR   PIR; C84616; C84616.
DR   RefSeq; NP_850030.1; NM_179699.3.
DR   RefSeq; NP_973514.1; NM_201785.1.
DR   UniGene; At.28511; -.
DR   PDB; 6A5K; X-ray; 1.90 A; A=264-790.
DR   PDB; 6A5M; X-ray; 2.30 A; A=264-790.
DR   PDB; 6A5N; X-ray; 2.40 A; A=264-790.
DR   PDBsum; 6A5K; -.
DR   PDBsum; 6A5M; -.
DR   PDBsum; 6A5N; -.
DR   ProteinModelPortal; Q8VZ17; -.
DR   SMR; Q8VZ17; -.
DR   BioGrid; 2157; 2.
DR   DIP; DIP-62061N; -.
DR   IntAct; Q8VZ17; 4.
DR   STRING; 3702.AT2G22740.1; -.
DR   PaxDb; Q8VZ17; -.
DR   EnsemblPlants; AT2G22740.1; AT2G22740.1; AT2G22740.
DR   EnsemblPlants; AT2G22740.2; AT2G22740.2; AT2G22740.
DR   GeneID; 816804; -.
DR   Gramene; AT2G22740.1; AT2G22740.1; AT2G22740.
DR   Gramene; AT2G22740.2; AT2G22740.2; AT2G22740.
DR   KEGG; ath:AT2G22740; -.
DR   Araport; AT2G22740; -.
DR   TAIR; locus:2065988; AT2G22740.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG3440; LUCA.
DR   HOGENOM; HOG000154454; -.
DR   InParanoid; Q8VZ17; -.
DR   KO; K11420; -.
DR   OMA; DHDNISM; -.
DR   OrthoDB; 75825at2759; -.
DR   PhylomeDB; Q8VZ17; -.
DR   PRO; PR:Q8VZ17; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q8VZ17; AT.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008327; F:methyl-CpG binding; IDA:TAIR.
DR   GO; GO:0010428; F:methyl-CpNpG binding; IDA:TAIR.
DR   GO; GO:0010429; F:methyl-CpNpN binding; IDA:TAIR.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016571; P:histone methylation; IDA:TAIR.
DR   Gene3D; 2.30.280.10; -; 1.
DR   InterPro; IPR025794; Hist-Lys_N-MeTrfase_plant.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00466; SRA; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Centromere; Chromatin regulator; Chromosome;
KW   Complete proteome; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    790       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH6.
FT                                /FTId=PRO_0000186077.
FT   DOMAIN      330    482       YDG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00358}.
FT   DOMAIN      551    613       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      616    760       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      774    790       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      626    628       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      717    718       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       553    553       Zinc 1. {ECO:0000250}.
FT   METAL       553    553       Zinc 2. {ECO:0000250}.
FT   METAL       554    554       Zinc 1. {ECO:0000250}.
FT   METAL       554    554       Zinc 2. {ECO:0000250}.
FT   METAL       555    555       Zinc 1. {ECO:0000250}.
FT   METAL       559    559       Zinc 1. {ECO:0000250}.
FT   METAL       559    559       Zinc 3. {ECO:0000250}.
FT   METAL       567    567       Zinc 1. {ECO:0000250}.
FT   METAL       569    569       Zinc 2. {ECO:0000250}.
FT   METAL       595    595       Zinc 2. {ECO:0000250}.
FT   METAL       595    595       Zinc 3. {ECO:0000250}.
FT   METAL       599    599       Zinc 2. {ECO:0000250}.
FT   METAL       601    601       Zinc 3. {ECO:0000250}.
FT   METAL       605    605       Zinc 3. {ECO:0000250}.
FT   METAL       720    720       Zinc 4. {ECO:0000250}.
FT   METAL       778    778       Zinc 4. {ECO:0000250}.
FT   METAL       780    780       Zinc 4. {ECO:0000250}.
FT   METAL       785    785       Zinc 4. {ECO:0000250}.
FT   BINDING     662    662       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     664    664       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     714    714       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    386    386       N -> D (in Ref. 4; AAL38815).
FT                                {ECO:0000305}.
FT   HELIX       268    292       {ECO:0000244|PDB:6A5K}.
FT   HELIX       296    298       {ECO:0000244|PDB:6A5M}.
FT   TURN        301    304       {ECO:0000244|PDB:6A5K}.
FT   HELIX       307    317       {ECO:0000244|PDB:6A5K}.
FT   STRAND      340    343       {ECO:0000244|PDB:6A5K}.
FT   HELIX       344    349       {ECO:0000244|PDB:6A5K}.
FT   STRAND      359    365       {ECO:0000244|PDB:6A5K}.
FT   STRAND      368    376       {ECO:0000244|PDB:6A5K}.
FT   STRAND      378    380       {ECO:0000244|PDB:6A5N}.
FT   HELIX       384    386       {ECO:0000244|PDB:6A5M}.
FT   STRAND      389    393       {ECO:0000244|PDB:6A5K}.
FT   HELIX       419    430       {ECO:0000244|PDB:6A5K}.
FT   STRAND      434    439       {ECO:0000244|PDB:6A5K}.
FT   STRAND      453    468       {ECO:0000244|PDB:6A5K}.
FT   STRAND      474    482       {ECO:0000244|PDB:6A5K}.
FT   HELIX       490    497       {ECO:0000244|PDB:6A5K}.
FT   STRAND      505    508       {ECO:0000244|PDB:6A5K}.
FT   TURN        510    513       {ECO:0000244|PDB:6A5K}.
FT   STRAND      514    517       {ECO:0000244|PDB:6A5K}.
FT   STRAND      520    522       {ECO:0000244|PDB:6A5K}.
FT   STRAND      524    527       {ECO:0000244|PDB:6A5K}.
FT   HELIX       543    545       {ECO:0000244|PDB:6A5K}.
FT   STRAND      561    563       {ECO:0000244|PDB:6A5M}.
FT   HELIX       568    572       {ECO:0000244|PDB:6A5K}.
FT   STRAND      585    587       {ECO:0000244|PDB:6A5K}.
FT   STRAND      590    593       {ECO:0000244|PDB:6A5K}.
FT   HELIX       610    612       {ECO:0000244|PDB:6A5K}.
FT   STRAND      618    622       {ECO:0000244|PDB:6A5K}.
FT   STRAND      624    626       {ECO:0000244|PDB:6A5K}.
FT   STRAND      628    634       {ECO:0000244|PDB:6A5K}.
FT   STRAND      641    644       {ECO:0000244|PDB:6A5K}.
FT   STRAND      647    651       {ECO:0000244|PDB:6A5K}.
FT   HELIX       652    657       {ECO:0000244|PDB:6A5K}.
FT   STRAND      658    660       {ECO:0000244|PDB:6A5K}.
FT   HELIX       662    664       {ECO:0000244|PDB:6A5K}.
FT   STRAND      665    669       {ECO:0000244|PDB:6A5K}.
FT   HELIX       675    683       {ECO:0000244|PDB:6A5K}.
FT   STRAND      699    705       {ECO:0000244|PDB:6A5K}.
FT   STRAND      707    710       {ECO:0000244|PDB:6A5K}.
FT   HELIX       712    715       {ECO:0000244|PDB:6A5K}.
FT   STRAND      723    732       {ECO:0000244|PDB:6A5K}.
FT   STRAND      740    747       {ECO:0000244|PDB:6A5K}.
FT   STRAND      754    757       {ECO:0000244|PDB:6A5K}.
FT   STRAND      763    767       {ECO:0000244|PDB:6A5N}.
FT   STRAND      769    773       {ECO:0000244|PDB:6A5M}.
FT   STRAND      787    790       {ECO:0000244|PDB:6A5K}.
SQ   SEQUENCE   790 AA;  87477 MW;  AEA7AC629AD23E6B CRC64;
     MEMGVMENLM VHTEISKVKS QSNGEVEKRG VSVLENGGVC KLDRMSGLKF KRRKVFAVRD
     FPPGCGSRAM EVKIACENGN VVEDVKVVES LVKEEESLGQ RDASENVSDI RMAEPVEVQP
     LRICLPGGDV VRDLSVTAGD ECSNSEQIVA GSGVSSSSGT ENIVRDIVVY ADESSLGMDN
     LDQTQPLEIE MSDVAVAKPR LVAGRKKAKK GIACHSSLKV VSREFGEGSR KKKSKKNLYW
     RDRESLDSPE QLRILGVGTS SGSSSGDSSR NKVKETLRLF HGVCRKILQE DEAKPEDQRR
     KGKGLRIDFE ASTILKRNGK FLNSGVHILG EVPGVEVGDE FQYRMELNIL GIHKPSQAGI
     DYMKYGKAKV ATSIVASGGY DDHLDNSDVL TYTGQGGNVM QVKKKGEELK EPEDQKLITG
     NLALATSIEK QTPVRVIRGK HKSTHDKSKG GNYVYDGLYL VEKYWQQVGS HGMNVFKFQL
     RRIPGQPELS WVEVKKSKSK YREGLCKLDI SEGKEQSPIS AVNEIDDEKP PLFTYTVKLI
     YPDWCRPVPP KSCCCTTRCT EAEARVCACV EKNGGEIPYN FDGAIVGAKP TIYECGPLCK
     CPSSCYLRVT QHGIKLPLEI FKTKSRGWGV RCLKSIPIGS FICEYVGELL EDSEAERRIG
     NDEYLFDIGN RYDNSLAQGM SELMLGTQAG RSMAEGDESS GFTIDAASKG NVGRFINHSC
     SPNLYAQNVL YDHEDSRIPH VMFFAQDNIP PLQELCYDYN YALDQVRDSK GNIKQKPCFC
     GAAVCRRRLY
//
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