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Database: UniProt
Entry: Q9C5P1
LinkDB: Q9C5P1
Original site: Q9C5P1 
ID   SUVH7_ARATH             Reviewed;         693 AA.
AC   Q9C5P1; Q9LMU9;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   19-MAR-2014, entry version 98.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH7;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 7;
DE            Short=H3-K9-HMTase 7;
DE   AltName: Full=Protein SET DOMAIN GROUP 17;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 7;
DE            Short=Su(var)3-9 homolog protein 7;
GN   Name=SUVH7; Synonyms=SDG17, SET17; OrderedLocusNames=At1g17770;
GN   ORFNames=F2H15.1;
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 [MRNA], 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=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   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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. Methylates 'Lys-9' of histone
CC       H3. H3 'Lys-9' methylation represents a specific tag for
CC       epigenetic transcriptional repression.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome,
CC       centromere (By similarity). Note=Associates with centromeric
CC       constitutive heterochromatin (By similarity).
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   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily.
CC   -!- SIMILARITY: Contains 1 A.T hook DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 pre-SET domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SIMILARITY: Contains 1 YDG domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF97258.1; Type=Erroneous gene model prediction;
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DR   EMBL; AF344450; AAK28972.1; -; mRNA.
DR   EMBL; AC034106; AAF97258.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29634.1; -; Genomic_DNA.
DR   PIR; G86312; G86312.
DR   RefSeq; NP_564036.1; NM_101640.1.
DR   UniGene; At.15818; -.
DR   ProteinModelPortal; Q9C5P1; -.
DR   SMR; Q9C5P1; 223-691.
DR   BioGrid; 23594; 1.
DR   PaxDb; Q9C5P1; -.
DR   PRIDE; Q9C5P1; -.
DR   EnsemblPlants; AT1G17770.1; AT1G17770.1; AT1G17770.
DR   GeneID; 838355; -.
DR   KEGG; ath:AT1G17770; -.
DR   TAIR; AT1G17770; -.
DR   eggNOG; COG3440; -.
DR   HOGENOM; HOG000238382; -.
DR   InParanoid; Q9C5P1; -.
DR   KO; K11420; -.
DR   OMA; QVSEFIN; -.
DR   PhylomeDB; Q9C5P1; -.
DR   ProtClustDB; CLSN2687844; -.
DR   BioCyc; ARA:AT1G17770-MONOMER; -.
DR   Genevestigator; Q9C5P1; -.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0018022; P:peptidyl-lysine methylation; IEA:GOC.
DR   Gene3D; 2.30.280.10; -; 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
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_domain.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR003105; SRA_YDG.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00384; AT_hook; 1.
DR   SMART; SM00508; PostSET; 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   DNA-binding; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    693       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH7.
FT                                /FTId=PRO_0000186078.
FT   DOMAIN      227    373       YDG.
FT   DOMAIN      454    516       Pre-SET.
FT   DOMAIN      519    660       SET.
FT   DOMAIN      677    693       Post-SET.
FT   DNA_BIND    129    141       A.T hook.
SQ   SEQUENCE   693 AA;  77632 MW;  E03E22BC2863E2D7 CRC64;
     MDKSIPIKAI PVACVRPDLV DDVTKNTSTI PTMVSPVLTN MPSATSPLLM VPPLRTIWPS
     NKEWYDGDAG PSSTGPIKRE ASDNTNDTAH NTFAPPPEMV IPLITIRPSD DSSNYSCDAG
     AGPSTGPVKR GRGRPKGSKN STPTEPKKPK VYDPNSLKVT SRGNFDSEIT EAETETGNQE
     IVDSVMMRFD AVRRRLCQIN HPEDILTTAS GNCTKMGVKT NTRRRIGAVP GIHVGDIFYY
     WGEMCLVGLH KSNYGGIDFF TAAESAVEGH AAMCVVTAGQ YDGETEGLDT LIYSGQGGTD
     VYGNARDQEM KGGNLALEAS VSKGNDVRVV RGVIHPHENN QKIYIYDGMY LVSKFWTVTG
     KSGFKEFRFK LVRKPNQPPA YAIWKTVENL RNHDLIDSRQ GFILEDLSFG AELLRVPLVN
     EVDEDDKTIP EDFDYIPSQC HSGMMTHEFH FDRQSLGCQN CRHQPCMHQN CTCVQRNGDL
     LPYHNNILVC RKPLIYECGG SCPCPDHCPT RLVQTGLKLH LEVFKTRNCG WGLRSWDPIR
     AGTFICEFAG LRKTKEEVEE DDDYLFDTSK IYQRFRWNYE PELLLEDSWE QVSEFINLPT
     QVLISAKEKG NVGRFMNHSC SPNVFWQPIE YENRGDVYLL IGLFAMKHIP PMTELTYDYG
     VSCVERSEED EVLLYKGKKT CLCGSVKCRG SFT
//
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