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Database: UniProt
Entry: Q9C5P0
LinkDB: Q9C5P0
Original site: Q9C5P0 
ID   SUVH8_ARATH             Reviewed;         755 AA.
AC   Q9C5P0; Q9TP24;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-FEB-2019, entry version 130.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH8;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase 8;
DE            Short=H3-K9-HMTase 8;
DE   AltName: Full=Protein SET DOMAIN GROUP 21;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 8;
DE            Short=Su(var)3-9 homolog protein 8;
GN   Name=SUVH8; Synonyms=SDG21, SET21; OrderedLocusNames=At2g24740;
GN   ORFNames=F27A10.5;
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   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}. 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: Cys residues in the pre-SET domain normally bind 3 zinc
CC       ions that are arranged in a triangular cluster, but here these Cys
CC       residues are only partially conserved, suggesting that the pre-Set
CC       domain may not bind a zinc cluster.
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=AAD26896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF344451; AAK28973.1; -; Genomic_DNA.
DR   EMBL; AC007266; AAD26896.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC07623.1; -; Genomic_DNA.
DR   PIR; C84640; C84640.
DR   RefSeq; NP_180049.2; NM_128034.2.
DR   UniGene; At.66241; -.
DR   ProteinModelPortal; Q9C5P0; -.
DR   SMR; Q9C5P0; -.
DR   STRING; 3702.AT2G24740.1; -.
DR   iPTMnet; Q9C5P0; -.
DR   PaxDb; Q9C5P0; -.
DR   EnsemblPlants; AT2G24740.1; AT2G24740.1; AT2G24740.
DR   GeneID; 817010; -.
DR   Gramene; AT2G24740.1; AT2G24740.1; AT2G24740.
DR   KEGG; ath:AT2G24740; -.
DR   Araport; AT2G24740; -.
DR   TAIR; locus:2047266; AT2G24740.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG3440; LUCA.
DR   HOGENOM; HOG000238382; -.
DR   InParanoid; Q9C5P0; -.
DR   KO; K11420; -.
DR   OMA; TASTNCM; -.
DR   OrthoDB; 197626at2759; -.
DR   PhylomeDB; Q9C5P0; -.
DR   PRO; PR:Q9C5P0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q9C5P0; AT.
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: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:0048366; P:leaf development; IMP:TAIR.
DR   GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
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; PS51575; SAM_MT43_SUVAR39_2; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
PE   3: Inferred from homology;
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    755       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific SUVH8.
FT                                /FTId=PRO_0000186079.
FT   DOMAIN      310    448       YDG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00358}.
FT   DOMAIN      528    578       Pre-SET.
FT   DOMAIN      581    723       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      739    755       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    174    186       A.T hook.
FT   REGION      591    593       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      679    680       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       682    682       Zinc. {ECO:0000250}.
FT   METAL       743    743       Zinc. {ECO:0000250}.
FT   METAL       745    745       Zinc. {ECO:0000250}.
FT   METAL       750    750       Zinc. {ECO:0000250}.
FT   BINDING     624    624       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     626    626       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     676    676       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   755 AA;  84528 MW;  4B5BF379B8BF0C27 CRC64;
     MVSTPPTLLM LFDDGDAGPS TGLVHREKSD AVNEEAHATS VPPHAPPQTL WLLDNFNIED
     SYDRDAGPST GPVHRERSDA VNEEAHATSI PPHAPPQTLW LLDNFNIEDS YDRDAGPSTS
     PIDREASHEV NEDAHATSAP PHVMVSPLQN RRPFDQFNNQ PYDASAGPST GPGKRGRGRP
     KGSKNGSRKP KKPKAYDNNS TDASAGPSSG LGKRRCGRPK GLKNRSRKPK KPKADDPNSK
     MVISCPDFDS RITEAERESG NQEIVDSILM RFDAVRRRLC QLNYRKDKIL TASTNCMNLG
     VRTNMTRRIG PIPGVQVGDI FYYWCEMCLV GLHRNTAGGI DSLLAKESGV DGPAATSVVT
     SGKYDNETED LETLIYSGHG GKPCDQVLQR GNRALEASVR RRNEVRVIRG ELYNNEKVYI
     YDGLYLVSDC WQVTGKSGFK EYRFKLLRKP GQPPGYAIWK LVENLRNHEL IDPRQGFILG
     DLSFGEEGLR VPLVNEVDEE DKTIPDDFDY IRSQCYSGMT NDVNVDSQSL VQSYIHQNCT
     CILKNCGQLP YHDNILVCRK PLIYECGGSC PTRMVETGLK LHLEVFKTSN CGWGLRSWDP
     IRAGTFICEF TGVSKTKEEV EEDDDYLFDT SRIYHSFRWN YEPELLCEDA CEQVSEDANL
     PTQVLISAKE KGNVGRFMNH NCWPNVFWQP IEYDDNNGHI YVRIGLFAMK HIPPMTELTY
     DYGISCVEKT GEDEVIYKGK KICLCGSVKC RGSFG
//
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