Q9M548 (DRM2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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
ORF Names:	T15N1.110, T15N1.120

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleoplasm. 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	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. The sequence CAB87630.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
Ligand	DNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-5 methylation of cytosine Inferred from electronic annotation. Source: GOC defense response to fungus Inferred from genetic interaction PubMed 22242006. Source: TAIR gene silencing Inferred from mutant phenotype Ref.6. Source: UniProtKB histone H3-K9 methylation Inferred from genetic interaction PubMed 17239600. Source: TAIR
Cellular_component	nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity Ref.1. Source: TAIR
Molecular_function	DNA (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 626	626	DNA (cytosine-5)-methyltransferase DRM2		PRO_0000381942
Regions
	Domain	109 – 150	42	UBA 1
	Domain	190 – 232	43	UBA 2

Sequences

	Sequence		Length	Mass (Da)
	Q9M548 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 10A38FC068636DB7	FASTA	626	70,431
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00542708.
PIR	T48635. T48636.
RefSeq	NP_196966.2. NM_121466.2.
UniGene	At.5084.
3D structure databases
ProteinModelPortal	Q9M548.
SMR	Q9M548. Positions 436-498, 502-622.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59279N.
STRING	3702.AT5G14620.1-P.
Protein family/group databases
REBASE	4601. M.AthDRM2.
Proteomic databases
PaxDb	Q9M548.
PRIDE	Q9M548.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G14620.1; AT5G14620.1; AT5G14620.
GeneID	831315.
KEGG	ath:AT5G14620.
Organism-specific databases
TAIR	At5g14620.
Phylogenomic databases
eggNOG	NOG70699.
HOGENOM	HOG000030355.
InParanoid	Q9M548.
OMA	RTKLNCI.
PhylomeDB	Q9M548.
ProtClustDB	CLSN2679951.
Gene expression databases
Genevestigator	Q9M548.
Family and domain databases
InterPro	IPR001525. C5_MeTfrase. IPR025822. C5_MeTrfase_DMR. IPR009060. UBA-like. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view]
Pfam	PF00145. DNA_methylase. 1 hit. [Graphical view]
SMART	SM00165. UBA. 3 hits. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit.
PROSITE	PS00094. C5_MTASE_1. False negative. PS00095. C5_MTASE_2. False negative. PS50030. UBA. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DRM2_ARATH

Accession

Primary (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:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program