Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9M548 (DRM2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. 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 DRM2

EC=2.1.1.37
Alternative name(s):
Protein DOMAINS REARRANGED METHYLASE 2
Gene names
Name:DRM2
Ordered Locus Names:At5g14620/At5g14630
ORF Names:T15N1.110/T15N1.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in de novo DNA methylation. Controls asymmetric and CpNpG methylation. Required for FWA gene silencing but not for the maintenance of SUP gene silencing. Functionally redundant to CMT3 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation. Ref.5 Ref.6 Ref.7

Catalytic activity

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

Subunit structure

Interacts with RDM1. Ref.8

Subcellular location

Nucleusnucleoplasm. Note: Peri-nucleolar. Ref.8

Tissue specificity

Expressed in roots, inflorescences and at lower levels in leaves. Ref.1

Miscellaneous

DRM2 is expressed at much higher levels than DRM1, which is scarcely detected, suggesting that DRM2 is the predominant de novo methylase.

Sequence similarities

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

Contains 1 SAM-dependent MTase DRM-type domain.

Contains 2 UBA domains.

Sequence caution

The sequence CAB87629.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At5g14620 and At5g14630.

The sequence CAB87630.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At5g14620 and At5g14630.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626DNA (cytosine-5)-methyltransferase DRM2
PRO_0000381942

Regions

Domain109 – 15042UBA 1
Domain190 – 23243UBA 2
Domain295 – 626332SAM-dependent MTase DRM-type

Sequences

Sequence LengthMass (Da)Tools
Q9M548 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 10A38FC068636DB7

FASTA62670,431
        10         20         30         40         50         60 
MVIWNNDDDD FLEIDNFQSS PRSSPIHAMQ CRVENLAGVA VTTSSLSSPT ETTDLVQMGF 

        70         80         90        100        110        120 
SDEVFATLFD MGFPVEMISR AIKETGPNVE TSVIIDTISK YSSDCEAGSS KSKAIDHFLA 

       130        140        150        160        170        180 
MGFDEEKVVK AIQEHGEDNM EAIANALLSC PEAKKLPAAV EEEDGIDWSS SDDDTNYTDM 

       190        200        210        220        230        240 
LNSDDEKDPN SNENGSKIRS LVKMGFSELE ASLAVERCGE NVDIAELTDF LCAAQMAREF 

       250        260        270        280        290        300 
SEFYTEHEEQ KPRHNIKKRR FESKGEPRSS VDDEPIRLPN PMIGFGVPNE PGLITHRSLP 

       310        320        330        340        350        360 
ELARGPPFFY YENVALTPKG VWETISRHLF EIPPEFVDSK YFCVAARKRG YIHNLPINNR 

       370        380        390        400        410        420 
FQIQPPPKYT IHDAFPLSKR WWPEWDKRTK LNCILTCTGS AQLTNRIRVA LEPYNEEPEP 

       430        440        450        460        470        480 
PKHVQRYVID QCKKWNLVWV GKNKAAPLEP DEMESILGFP KNHTRGGGMS RTERFKSLGN 

       490        500        510        520        530        540 
SFQVDTVAYH LSVLKPIFPH GINVLSLFTG IGGGEVALHR LQIKMKLVVS VEISKVNRNI 

       550        560        570        580        590        600 
LKDFWEQTNQ TGELIEFSDI QHLTNDTIEG LMEKYGGFDL VIGGSPCNNL AGGNRVSRVG 

       610        620 
LEGDQSSLFF EYCRILEVVR ARMRGS 

« Hide

References

« Hide 'large scale' references
[1]"Conserved plant genes with similarity to mammalian de novo DNA methyltransferases."
Cao X., Springer N.M., Muszynski M.G., Phillips R.L., Kaeppler S., Jacobsen S.E.
Proc. Natl. Acad. Sci. U.S.A. 97:4979-4984(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Locus-specific control of asymmetric and CpNpG methylation by the DRM and CMT3 methyltransferase genes."
Cao X., Jacobsen S.E.
Proc. Natl. Acad. Sci. U.S.A. 99:16491-16498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Role of the arabidopsis DRM methyltransferases in de novo DNA methylation and gene silencing."
Cao X., Jacobsen S.E.
Curr. Biol. 12:1138-1144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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.
[8]"An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation."
Gao Z., Liu H.L., Daxinger L., Pontes O., He X., Qian W., Lin H., Xie M., Lorkovic Z.J., Zhang S., Miki D., Zhan X., Pontier D., Lagrange T., Jin H., Matzke A.J., Matzke M., Pikaard C.S., Zhu J.K.
Nature 465:106-109(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RDM1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF240695 mRNA. Translation: AAF66129.1.
AL163792 Genomic DNA. Translation: CAB87629.1. Sequence problems.
AL163792 Genomic DNA. Translation: CAB87630.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92056.1.
AK176138 mRNA. Translation: BAD43901.1.
AK220953 mRNA. Translation: BAD94486.1.
AK229197 mRNA. Translation: BAF01067.1.
PIRT48635.
T48636.
RefSeqNP_196966.2. NM_121466.2.
UniGeneAt.5084.

3D structure databases

ProteinModelPortalQ9M548.
SMRQ9M548. Positions 304-499, 502-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16592. 2 interactions.
DIPDIP-59279N.
IntActQ9M548. 1 interaction.
STRING3702.AT5G14620.1-P.

Protein family/group databases

REBASE4601. M.AthDRM2.

Proteomic databases

PaxDbQ9M548.
PRIDEQ9M548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G14620.1; AT5G14620.1; AT5G14620.
GeneID831315.
KEGGath:AT5G14620.

Organism-specific databases

TAIRAT5G14620.

Phylogenomic databases

eggNOGNOG70699.
HOGENOMHOG000030355.
InParanoidQ9M548.
OMADECRKWN.
PhylomeDBQ9M548.
ProtClustDBCLSN2679951.

Enzyme and pathway databases

BioCycARA:AT5G14620-MONOMER.

Gene expression databases

GenevestigatorQ9M548.

Family and domain databases

InterProIPR001525. C5_MeTfrase.
IPR025822. C5_MeTrfase_DMR.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 3 hits.
[Graphical view]
SUPFAMSSF46934. SSF46934. 3 hits.
PROSITEPS51680. SAM_MT_DRM. 1 hit.
PS50030. UBA. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRM2_ARATH
AccessionPrimary (citable) accession number: Q9M548
Secondary accession number(s): Q9LYJ7, Q9LYJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 91 of the entry and version 1 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