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Database: UniProt
Entry: Q9FF80
LinkDB: Q9FF80
Original site: Q9FF80 
ID   SUVH1_ARATH             Reviewed;         670 AA.
AC   Q9FF80;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JAN-2019, entry version 126.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH1;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 1;
DE            Short=H3-K9-HMTase 1;
DE   AltName: Full=Protein SET DOMAIN GROUP 32;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 1;
DE            Short=Su(var)3-9 homolog protein 1;
GN   Name=SUVH1; Synonyms=SDG32, SET32; OrderedLocusNames=At5g04940;
GN   ORFNames=MUG13.20;
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], SUBCELLULAR LOCATION, NOMENCLATURE, AND
RP   TISSUE SPECIFICITY.
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned
RT   P1 clones.";
RL   DNA Res. 4:215-230(1997).
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, AND SUBCELLULAR LOCATION.
RX   PubMed=15775980; DOI=10.1038/sj.emboj.7600604;
RA   Naumann K., Fischer A., Hofmann I., Krauss V., Phalke S., Irmler K.,
RA   Hause G., Aurich A.-C., Dorn R., Jenuwein T., Reuter G.;
RT   "Pivotal role of AtSUVH2 in heterochromatic histone methylation and
RT   gene silencing in Arabidopsis.";
RL   EMBO J. 24:1418-1429(2005).
RN   [5]
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.
CC       {ECO:0000269|PubMed:15775980}.
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   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
CC       Note=Associates with centromeric constitutive heterochromatin.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves stems and flowers.
CC       {ECO:0000269|PubMed:11691919}.
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}.
DR   EMBL; AF344444; AAK28966.1; -; mRNA.
DR   EMBL; AB005245; BAB11516.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90806.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90807.1; -; Genomic_DNA.
DR   RefSeq; NP_196113.1; NM_120576.1.
DR   RefSeq; NP_850767.1; NM_180436.2.
DR   UniGene; At.8375; -.
DR   ProteinModelPortal; Q9FF80; -.
DR   SMR; Q9FF80; -.
DR   STRING; 3702.AT5G04940.1; -.
DR   PaxDb; Q9FF80; -.
DR   PRIDE; Q9FF80; -.
DR   EnsemblPlants; AT5G04940.1; AT5G04940.1; AT5G04940.
DR   EnsemblPlants; AT5G04940.2; AT5G04940.2; AT5G04940.
DR   GeneID; 830376; -.
DR   Gramene; AT5G04940.1; AT5G04940.1; AT5G04940.
DR   Gramene; AT5G04940.2; AT5G04940.2; AT5G04940.
DR   KEGG; ath:AT5G04940; -.
DR   Araport; AT5G04940; -.
DR   TAIR; locus:2175289; AT5G04940.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000238382; -.
DR   InParanoid; Q9FF80; -.
DR   KO; K11420; -.
DR   OMA; CNCASVC; -.
DR   OrthoDB; 274915at2759; -.
DR   PhylomeDB; Q9FF80; -.
DR   PRO; PR:Q9FF80; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FF80; baseline and differential.
DR   Genevisible; Q9FF80; AT.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; TAS: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; 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   2: Evidence at transcript level;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    670       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH1.
FT                                /FTId=PRO_0000186072.
FT   DOMAIN      211    357       YDG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00358}.
FT   DOMAIN      432    492       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      495    639       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      654    670       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      505    507       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      596    597       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       434    434       Zinc 1. {ECO:0000250}.
FT   METAL       434    434       Zinc 2. {ECO:0000250}.
FT   METAL       436    436       Zinc 1. {ECO:0000250}.
FT   METAL       440    440       Zinc 1. {ECO:0000250}.
FT   METAL       440    440       Zinc 3. {ECO:0000250}.
FT   METAL       447    447       Zinc 1. {ECO:0000250}.
FT   METAL       449    449       Zinc 2. {ECO:0000250}.
FT   METAL       475    475       Zinc 2. {ECO:0000250}.
FT   METAL       475    475       Zinc 3. {ECO:0000250}.
FT   METAL       479    479       Zinc 2. {ECO:0000250}.
FT   METAL       481    481       Zinc 3. {ECO:0000250}.
FT   METAL       484    484       Zinc 3. {ECO:0000250}.
FT   METAL       599    599       Zinc 4. {ECO:0000250}.
FT   METAL       658    658       Zinc 4. {ECO:0000250}.
FT   METAL       660    660       Zinc 4. {ECO:0000250}.
FT   METAL       665    665       Zinc 4. {ECO:0000250}.
FT   BINDING     541    541       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     543    543       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     593    593       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   670 AA;  74471 MW;  C92CE89FF5C630F1 CRC64;
     MERNGGHYTD KTRVLDIKPL RTLRPVFPSG NQAPPFVCAP PFGPFPPGFS SFYPFSSSQA
     NQHTPDLNQA QYPPQHQQPQ NPPPVYQQQP PQHASEPSLV TPLRSFRSPD VSNGNAELEG
     STVKRRIPKK RPISRPENMN FESGINVADR ENGNRELVLS VLMRFDALRR RFAQLEDAKE
     AVSGIIKRPD LKSGSTCMGR GVRTNTKKRP GIVPGVEIGD VFFFRFEMCL VGLHSPSMAG
     IDYLVVKGET EEEPIATSIV SSGYYDNDEG NPDVLIYTGQ GGNADKDKQS SDQKLERGNL
     ALEKSLRRDS AVRVIRGLKE ASHNAKIYIY DGLYEIKESW VEKGKSGHNT FKYKLVRAPG
     QPPAFASWTA IQKWKTGVPS RQGLILPDMT SGVESIPVSL VNEVDTDNGP AYFTYSTTVK
     YSESFKLMQP SFGCDCANLC KPGNLDCHCI RKNGGDFPYT GNGILVSRKP MIYECSPSCP
     CSTCKNKVTQ MGVKVRLEVF KTANRGWGLR SWDAIRAGSF ICIYVGEAKD KSKVQQTMAN
     DDYTFDTTNV YNPFKWNYEP GLADEDACEE MSEESEIPLP LIISAKNVGN VARFMNHSCS
     PNVFWQPVSY ENNSQLFVHV AFFAISHIPP MTELTYDYGV SRPSGTQNGN PLYGKRKCFC
     GSAYCRGSFG
//
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