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Database: UniProt
Entry: Q9C5P4
LinkDB: Q9C5P4
Original site: Q9C5P4 
ID   SUVH3_ARATH             Reviewed;         669 AA.
AC   Q9C5P4; Q9SSL7;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   13-FEB-2019, entry version 138.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 3;
DE            Short=H3-K9-HMTase 3;
DE   AltName: Full=Protein SET DOMAIN GROUP 19;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 3;
DE            Short=Su(var)3-9 homolog protein 3;
GN   Name=SUVH3; Synonyms=SDG19, SET19; OrderedLocusNames=At1g73100;
GN   ORFNames=F3N23.30;
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=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;
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   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:
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 {ECO:0000255|PROSITE-
CC       ProRule:PRU00358, ECO:0000269|PubMed:11691919}. Chromosome,
CC       centromere {ECO:0000269|PubMed:11691919}. Note=Associates with
CC       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; AF344446; AAK28968.1; -; mRNA.
DR   EMBL; AC008017; AAD55657.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35414.1; -; Genomic_DNA.
DR   EMBL; AY099620; AAM20471.1; -; mRNA.
DR   EMBL; BT002137; AAN72148.1; -; mRNA.
DR   PIR; F96756; F96756.
DR   RefSeq; NP_565056.1; NM_105968.3.
DR   UniGene; At.11687; -.
DR   UniGene; At.43232; -.
DR   ProteinModelPortal; Q9C5P4; -.
DR   SMR; Q9C5P4; -.
DR   BioGrid; 28860; 8.
DR   IntAct; Q9C5P4; 6.
DR   STRING; 3702.AT1G73100.1; -.
DR   PaxDb; Q9C5P4; -.
DR   PRIDE; Q9C5P4; -.
DR   EnsemblPlants; AT1G73100.1; AT1G73100.1; AT1G73100.
DR   GeneID; 843641; -.
DR   Gramene; AT1G73100.1; AT1G73100.1; AT1G73100.
DR   KEGG; ath:AT1G73100; -.
DR   Araport; AT1G73100; -.
DR   TAIR; locus:2032592; AT1G73100.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG3440; LUCA.
DR   HOGENOM; HOG000238382; -.
DR   InParanoid; Q9C5P4; -.
DR   KO; K11420; -.
DR   OMA; YSISESW; -.
DR   OrthoDB; 274915at2759; -.
DR   PhylomeDB; Q9C5P4; -.
DR   PRO; PR:Q9C5P4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9C5P4; AT.
DR   GO; GO:0005694; C:chromosome; IDA:TAIR.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS: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   DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    669       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH3.
FT                                /FTId=PRO_0000186074.
FT   DOMAIN      208    355       YDG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00358}.
FT   DOMAIN      430    491       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      494    638       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      653    669       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    108    120       A.T hook.
FT   REGION      504    506       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      595    596       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       432    432       Zinc 1. {ECO:0000250}.
FT   METAL       432    432       Zinc 2. {ECO:0000250}.
FT   METAL       434    434       Zinc 1. {ECO:0000250}.
FT   METAL       438    438       Zinc 1. {ECO:0000250}.
FT   METAL       438    438       Zinc 3. {ECO:0000250}.
FT   METAL       445    445       Zinc 1. {ECO:0000250}.
FT   METAL       447    447       Zinc 2. {ECO:0000250}.
FT   METAL       473    473       Zinc 2. {ECO:0000250}.
FT   METAL       473    473       Zinc 3. {ECO:0000250}.
FT   METAL       477    477       Zinc 2. {ECO:0000250}.
FT   METAL       479    479       Zinc 3. {ECO:0000250}.
FT   METAL       483    483       Zinc 3. {ECO:0000250}.
FT   METAL       598    598       Zinc 4. {ECO:0000250}.
FT   METAL       657    657       Zinc 4. {ECO:0000250}.
FT   METAL       659    659       Zinc 4. {ECO:0000250}.
FT   METAL       664    664       Zinc 4. {ECO:0000250}.
FT   BINDING     540    540       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     542    542       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     592    592       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    416    416       S -> P (in Ref. 1; AAK28968).
FT                                {ECO:0000305}.
SQ   SEQUENCE   669 AA;  73439 MW;  8878E000747FD1AB CRC64;
     MQGVPGFNTV PNPNHYDKSI VLDIKPLRSL KPVFPNGNQG PPFVGCPPFG PSSSEYSSFF
     PFGAQQPTHD TPDLNQTQNT PIPSFVPPLR SYRTPTKTNG PSSSSGTKRG VGRPKGTTSV
     KKKEKKTVAN EPNLDVQVVK KFSSDFDSGI SAAEREDGNA YLVSSVLMRF DAVRRRLSQV
     EFTKSATSKA AGTLMSNGVR TNMKKRVGTV PGIEVGDIFF SRIEMCLVGL HMQTMAGIDY
     IISKAGSDEE SLATSIVSSG RYEGEAQDPE SLIYSGQGGN ADKNRQASDQ KLERGNLALE
     NSLRKGNGVR VVRGEEDAAS KTGKIYIYDG LYSISESWVE KGKSGCNTFK YKLVRQPGQP
     PAFGFWKSVQ KWKEGLTTRP GLILPDLTSG AESKPVSLVN DVDEDKGPAY FTYTSSLKYS
     ETFKLTQPVI GCSCSGSCSP GNHNCSCIRK NDGDLPYLNG VILVSRRPVI YECGPTCPCH
     ASCKNRVIQT GLKSRLEVFK TRNRGWGLRS WDSLRAGSFI CEYAGEVKDN GNLRGNQEED
     AYVFDTSRVF NSFKWNYEPE LVDEDPSTEV PEEFNLPSPL LISAKKFGNV ARFMNHSCSP
     NVFWQPVIRE GNGESVIHIA FFAMRHIPPM AELTYDYGIS PTSEARDESL LHGQRTCLCG
     SEQCRGSFG
//
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