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Q94F88 (CMT3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA (cytosine-5)-methyltransferase CMT3

EC=2.1.1.37
Alternative name(s):
Chromomethylase 3
Protein CHROMOMETHYLASE 3
Gene names
Name:CMT3
Ordered Locus Names:At1g69770
ORF Names:T6C23.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length839 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the CpXpG methylation and in gene silencing. Methylates preferentially transposon-related sequences. Functionally redundant to DRM1/DRM2 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation. Ref.3 Ref.4 Ref.7 Ref.8

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Subunit structure

Homodimer. Interacts with HP1 and, through its chromodomain, with the N-terminal tail of histone H3 doubly methylated at 'Lys-9' and 'Lys-27'. Ref.5 Ref.6

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 BAH domain.

Contains 1 chromo domain.

Contains 1 SAM-dependent MTase C5-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 839839DNA (cytosine-5)-methyltransferase CMT3
PRO_0000246693

Regions

Domain108 – 227120BAH
Domain269 – 813545SAM-dependent MTase C5-type
Domain382 – 44766Chromo

Sites

Active site4601 By similarity

Experimental info

Mutagenesis2791G → E: Loss of activity. Ref.3
Mutagenesis3821F → A: Loss of binding to H3. Ref.5
Mutagenesis4561G → D: Loss of activity. Ref.3
Mutagenesis4651G → D: Loss of activity. Ref.3
Mutagenesis4701R → K in cmt3-10; partial loss of activity. Ref.4
Mutagenesis5411G → E in cmt3-6; loss of activity. Ref.4
Mutagenesis5421L → F: Loss of activity. Ref.3
Mutagenesis6831R → K: Loss of activity. Ref.3
Mutagenesis7241G → E in cmt3-4; loss of activity. Ref.4
Mutagenesis7331L → F: Loss of activity. Ref.3
Mutagenesis7481P → L: Loss of activity. Ref.3
Mutagenesis7631S → F in cmt3-8; partial loss of activity. Ref.4
Mutagenesis7691R → K in cmt3-3; loss of activity. Ref.4
Mutagenesis8071G → R: Loss of activity. Ref.3
Sequence conflict1381A → V in AAK71870. Ref.4
Sequence conflict1651K → N in AAK71870. Ref.4
Sequence conflict1661K → E in AAK69756. Ref.3
Sequence conflict266 – 2683HKK → QKE in AAK71870. Ref.4
Sequence conflict4331E → G in AAK71870. Ref.4
Sequence conflict821 – 8222LT → II in AAK71870. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q94F88 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: B1B4D5F7AE0A3AAC

FASTA83994,905
        10         20         30         40         50         60 
MAPKRKRPAT KDDTTKSIPK PKKRAPKRAK TVKEEPVTVV EEGEKHVARF LDEPIPESEA 

        70         80         90        100        110        120 
KSTWPDRYKP IEVQPPKASS RKKTKDDEKV EIIRARCHYR RAIVDERQIY ELNDDAYVQS 

       130        140        150        160        170        180 
GEGKDPFICK IIEMFEGANG KLYFTARWFY RPSDTVMKEF EILIKKKRVF FSEIQDTNEL 

       190        200        210        220        230        240 
GLLEKKLNIL MIPLNENTKE TIPATENCDF FCDMNYFLPY DTFEAIQQET MMAISESSTI 

       250        260        270        280        290        300 
SSDTDIREGA AAISEIGECS QETEGHKKAT LLDLYSGCGA MSTGLCMGAQ LSGLNLVTKW 

       310        320        330        340        350        360 
AVDMNAHACK SLQHNHPETN VRNMTAEDFL FLLKEWEKLC IHFSLRNSPN SEEYANLHGL 

       370        380        390        400        410        420 
NNVEDNEDVS EESENEDDGE VFTVDKIVGI SFGVPKKLLK RGLYLKVRWL NYDDSHDTWE 

       430        440        450        460        470        480 
PIEGLSNCRG KIEEFVKLGY KSGILPLPGG VDVVCGGPPC QGISGHNRFR NLLDPLEDQK 

       490        500        510        520        530        540 
NKQLLVYMNI VEYLKPKFVL MENVVDMLKM AKGYLARFAV GRLLQMNYQV RNGMMAAGAY 

       550        560        570        580        590        600 
GLAQFRLRFF LWGALPSEII PQFPLPTHDL VHRGNIVKEF QGNIVAYDEG HTVKLADKLL 

       610        620        630        640        650        660 
LKDVISDLPA VANSEKRDEI TYDKDPTTPF QKFIRLRKDE ASGSQSKSKS KKHVLYDHHP 

       670        680        690        700        710        720 
LNLNINDYER VCQVPKRKGA NFRDFPGVIV GPGNVVKLEE GKERVKLESG KTLVPDYALT 

       730        740        750        760        770        780 
YVDGKSCKPF GRLWWDEIVP TVVTRAEPHN QVIIHPEQNR VLSIRENARL QGFPDDYKLF 

       790        800        810        820        830 
GPPKQKYIQV GNAVAVPVAK ALGYALGTAF QGLAVGKDPL LTLPEGFAFM KPTLPSELA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Arabidopsis cmt3 chromomethylase mutations block non-CG methylation and silencing of an endogenous gene."
Bartee L., Malagnac F., Bender J.
Genes Dev. 15:1753-1758(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-279; GLY-456; GLY-465; LEU-542; ARG-683; LEU-733; PRO-748 AND GLY-807, FUNCTION.
Strain: cv. Wassilewskija.
[4]"Requirement of CHROMOMETHYLASE3 for maintenance of CpXpG methylation."
Lindroth A.M., Cao X., Jackson J.P., Zilberman D., McCallum C.M., Henikoff S., Jacobsen S.E.
Science 292:2077-2080(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ARG-470; GLY-541; GLY-724; SER-763 AND ARG-769, FUNCTION.
Strain: cv. Landsberg erecta.
[5]"Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3."
Lindroth A.M., Shultis D., Jasencakova Z., Fuchs J., Johnson L., Schubert D., Patnaik D., Pradhan S., Goodrich J., Schubert I., Jenuwein T., Khorasanizadeh S., Jacobsen S.E.
EMBO J. 23:4286-4296(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH H3, MUTAGENESIS OF PHE-382.
[6]"Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase."
Jackson J.P., Lindroth A.M., Cao X., Jacobsen S.E.
Nature 416:556-560(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HP1.
[7]"Genome-wide profiling of DNA methylation reveals transposon targets of CHROMOMETHYLASE3."
Tompa R., McCallum C.M., Delrow J., Henikoff J.G., van Steensel B., Henikoff S.
Curr. Biol. 12:65-68(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Role of the DRM and CMT3 methyltransferases in RNA-directed DNA methylation."
Cao X., Aufsatz W., Zilberman D., Mette M.F., Huang M.S., Matzke M., Jacobsen S.E.
Curr. Biol. 13:2212-2217(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC013289 Genomic DNA. Translation: AAG52543.1.
CP002684 Genomic DNA. Translation: AEE34973.1.
AF383170 Genomic DNA. Translation: AAK69756.1.
AF364174 Genomic DNA. Translation: AAK71870.1.
PIRG96719.
RefSeqNP_177135.1. NM_105645.3.
UniGeneAt.35376.

3D structure databases

ProteinModelPortalQ94F88.
SMRQ94F88. Positions 46-827.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28534. 1 interaction.
DIPDIP-60719N.

Protein family/group databases

REBASE4853. M.AthCMT3.

Proteomic databases

PaxDbQ94F88.
PRIDEQ94F88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G69770.1; AT1G69770.1; AT1G69770.
GeneID843313.
KEGGath:AT1G69770.

Organism-specific databases

TAIRAT1G69770.

Phylogenomic databases

eggNOGCOG0270.
HOGENOMHOG000082844.
InParanoidQ94F88.
KOK00558.
OMAHRPLELN.
PhylomeDBQ94F88.

Enzyme and pathway databases

BioCycARA:AT1G69770-MONOMER.

Gene expression databases

ArrayExpressQ94F88.
GenevestigatorQ94F88.

Family and domain databases

Gene3D3.40.50.150. 2 hits.
InterProIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025821. C5_MeTfrase_pln.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF01426. BAH. 1 hit.
PF00385. Chromo. 1 hit.
PF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
SMARTSM00439. BAH. 1 hit.
SM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 4 hits.
SSF54160. SSF54160. 1 hit.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS51038. BAH. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCMT3_ARATH
AccessionPrimary (citable) accession number: Q94F88
Secondary accession number(s): Q94FN4, Q9C9L8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names