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Database: UniProt
Entry: Q3EC60
LinkDB: Q3EC60
Original site: Q3EC60 
ID   SUVHA_ARATH             Reviewed;         312 AA.
AC   Q3EC60; V9H0G5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   13-FEB-2019, entry version 97.
DE   RecName: Full=Putative inactive histone-lysine N-methyltransferase family member SUVH10;
DE   AltName: Full=Histone H3-K9 methyltransferase 10;
DE            Short=H3-K9-HMTase 10;
DE   AltName: Full=Protein SET DOMAIN GROUP 11;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 10;
DE            Short=Su(var)3-9 homolog protein 10;
GN   Name=SUVH10; Synonyms=SDG11, SET11; OrderedLocusNames=At2g05900;
GN   ORFNames=T6P5.10;
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=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   [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   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   [4]
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 family member that may lack
CC       methyltransferase activity. May methylate 'Lys-9' of histone H3.
CC       H3 'Lys-9' methylation represents a specific tag for epigenetic
CC       transcriptional repression (Potential). {ECO:0000305}.
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 both SET and pre-SET domains are present, the
CC       absence of the post-SET domain may alter the methyltransferase
CC       activity.
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:PRU00190}.
CC   -!- CAUTION: The S-adenosyl-L-methionine binding sites are not
CC       conserved, suggesting that this protein lacks methyltransferase
CC       activity. Likewise, the zinc-binding Cys residues in the pre-SET
CC       domain are only partially conserved. {ECO:0000305}.
DR   EMBL; AC005970; AAC95167.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05982.1; -; Genomic_DNA.
DR   PIR; G84472; G84472.
DR   RefSeq; NP_178647.1; NM_126603.1.
DR   UniGene; At.41135; -.
DR   ProteinModelPortal; Q3EC60; -.
DR   BioGrid; 541; 3.
DR   IntAct; Q3EC60; 3.
DR   STRING; 3702.AT2G05900.1; -.
DR   PaxDb; Q3EC60; -.
DR   PRIDE; Q3EC60; -.
DR   EnsemblPlants; AT2G05900.1; AT2G05900.1; AT2G05900.
DR   GeneID; 815142; -.
DR   Gramene; AT2G05900.1; AT2G05900.1; AT2G05900.
DR   KEGG; ath:AT2G05900; -.
DR   Araport; AT2G05900; -.
DR   TAIR; locus:2064676; AT2G05900.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000154456; -.
DR   InParanoid; Q3EC60; -.
DR   OMA; DMEFIGV; -.
DR   OrthoDB; 1183452at2759; -.
DR   PhylomeDB; Q3EC60; -.
DR   PRO; PR:Q3EC60; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q3EC60; AT.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.280.10; -; 1.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00466; SRA; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
PE   3: Inferred from homology;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN         1    312       Putative inactive histone-lysine N-
FT                                methyltransferase family member SUVH10.
FT                                /FTId=PRO_0000233364.
FT   DOMAIN        1    132       YDG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00358}.
FT   DOMAIN      126    290       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      163    219       Pre-SET.
FT   DOMAIN      296    312       Post-SET.
FT   METAL       250    250       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       300    300       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       302    302       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       307    307       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
SQ   SEQUENCE   312 AA;  35023 MW;  9349BB5A6D07CCB6 CRC64;
     MGLVGLHSGT IDMEFIGVED HGDEEGKQIA VSVISSGKNA DKTEDPDSLI FTGFGGTDMY
     HGQPCNQKLE RLNIPLEAAF RKKSIVRVVR CMKDEKRTNG NIYIYDGTYM ITNRWEEEGQ
     NGFIVFKFKL VREPDQKPAF GIWKSIQNWR NGLSIRPGLI LEDLSNGAEN LKVCLVNEVD
     KENGPALFRY VTSLIHEVIN NIPSMVDRCA CGRRSCGSKH VFREKLSVSS SLVISAKKSG
     NVARFMNHSC SPNVFWQSIA REQNGLWCLY IGFFAMKHIP PLTELRYDYG KSRGGGKKMC
     LCRTKKCCGS FG
//
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