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Protein

DNA (cytosine-5)-methyltransferase DRM1

Gene

DRM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: TAIR
  2. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. C-5 methylation of cytosine Source: GOC
  2. defense response to fungus Source: TAIR
  3. DNA methylation Source: TAIR
  4. gene silencing Source: UniProtKB
  5. histone H3-K9 methylation Source: TAIR
  6. methylation-dependent chromatin silencing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

DNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciARA:AT5G15380-MONOMER.

Protein family/group databases

REBASEi15559. M.AthDRM1.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase DRM1 (EC:2.1.1.37)
Alternative name(s):
Protein DOMAINS REARRANGED METHYLASE 1
Gene namesi
Name:DRM1
Ordered Locus Names:At5g15380/At5g15370
ORF Names:F8M21.270/F8M21.260
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G15380.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 624624DNA (cytosine-5)-methyltransferase DRM1PRO_0000381941Add
BLAST

Proteomic databases

PaxDbiQ9LXE5.
PRIDEiQ9LXE5.

Expressioni

Gene expression databases

GenevestigatoriQ9LXE5.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G15380.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9LXE5.
SMRiQ9LXE5. Positions 272-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 14942UBA 1PROSITE-ProRule annotationAdd
BLAST
Domaini188 – 23144UBA 2PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 622332SAM-dependent MTase DRM-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. DRM-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase DRM-type domain.PROSITE-ProRule annotation
Contains 2 UBA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG70699.
HOGENOMiHOG000030355.
InParanoidiQ9LXE5.
OMAiMAREEDP.
PhylomeDBiQ9LXE5.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR030380. SAM_MeTfrase_DRM.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51680. SAM_MT_DRM. 1 hit.
PS50030. UBA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LXE5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVMSHIFLIS QIQEVEHGDS DDVNWNTDDD ELAIDNFQFS PSPVHISATS
60 70 80 90 100
PNSIQNRISD ETVASFVEMG FSTQMIARAI EETAGANMEP MMILETLFNY
110 120 130 140 150
SASTEASSSK SKVINHFIAM GFPEEHVIKA MQEHGDEDVG EITNALLTYA
160 170 180 190 200
EVDKLRESED MNININDDDD DNLYSLSSDD EEDELNNSSN EDRILQALIK
210 220 230 240 250
MGYLREDAAI AIERCGEDAS MEEVVDFICA AQMARQFDEI YAEPDKKELM
260 270 280 290 300
NNNKKRRTYT ETPRKPNTDQ LISLPKEMIG FGVPNHPGLM MHRPVPIPDI
310 320 330 340 350
ARGPPFFYYE NVAMTPKGVW AKISSHLYDI VPEFVDSKHF CAAARKRGYI
360 370 380 390 400
HNLPIQNRFQ IQPPQHNTIQ EAFPLTKRWW PSWDGRTKLN CLLTCIASSR
410 420 430 440 450
LTEKIREALE RYDGETPLDV QKWVMYECKK WNLVWVGKNK LAPLDADEME
460 470 480 490 500
KLLGFPRDHT RGGGISTTDR YKSLGNSFQV DTVAYHLSVL KPLFPNGINV
510 520 530 540 550
LSLFTGIGGG EVALHRLQIK MNVVVSVEIS DANRNILRSF WEQTNQKGIL
560 570 580 590 600
REFKDVQKLD DNTIERLMDE YGGFDLVIGG SPCNNLAGGN RHHRVGLGGE
610 620
HSSLFFDYCR ILEAVRRKAR HMRR
Length:624
Mass (Da):70,918
Last modified:September 1, 2009 - v2
Checksum:i9B3BBE10CAE68AB7
GO

Sequence cautioni

The sequence CAB89347.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At5g15370 and At5g15380.Curated
The sequence CAB89348.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At5g15370 and At5g15380.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL353993 Genomic DNA. Translation: CAB89347.1. Sequence problems.
AL353993 Genomic DNA. Translation: CAB89348.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92154.1.
AY530748 Genomic DNA. Translation: AAS45433.1.
PIRiT49972.
T49973.
RefSeqiNP_197042.2. NM_121542.2.
UniGeneiAt.50458.

Genome annotation databases

EnsemblPlantsiAT5G15380.1; AT5G15380.1; AT5G15380.
GeneIDi831390.
KEGGiath:AT5G15380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL353993 Genomic DNA. Translation: CAB89347.1. Sequence problems.
AL353993 Genomic DNA. Translation: CAB89348.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92154.1.
AY530748 Genomic DNA. Translation: AAS45433.1.
PIRiT49972.
T49973.
RefSeqiNP_197042.2. NM_121542.2.
UniGeneiAt.50458.

3D structure databases

ProteinModelPortaliQ9LXE5.
SMRiQ9LXE5. Positions 272-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G15380.1-P.

Protein family/group databases

REBASEi15559. M.AthDRM1.

Proteomic databases

PaxDbiQ9LXE5.
PRIDEiQ9LXE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G15380.1; AT5G15380.1; AT5G15380.
GeneIDi831390.
KEGGiath:AT5G15380.

Organism-specific databases

TAIRiAT5G15380.

Phylogenomic databases

eggNOGiNOG70699.
HOGENOMiHOG000030355.
InParanoidiQ9LXE5.
OMAiMAREEDP.
PhylomeDBiQ9LXE5.

Enzyme and pathway databases

BioCyciARA:AT5G15380-MONOMER.

Gene expression databases

GenevestigatoriQ9LXE5.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR030380. SAM_MeTfrase_DRM.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51680. SAM_MT_DRM. 1 hit.
PS50030. UBA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Efficient discovery of DNA polymorphisms in natural populations by Ecotilling."
    Comai L., Young K., Till B.J., Reynolds S.H., Greene E.A., Codomo C.A., Enns L.C., Johnson J.E., Burtner C., Odden A.R., Henikoff S.
    Plant J. 37:778-786(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 264-570.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
  6. "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.

Entry informationi

Entry nameiDRM1_ARATH
AccessioniPrimary (citable) accession number: Q9LXE5
Secondary accession number(s): Q6QPM0, Q9LXE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: January 7, 2015
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.