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Q94F87

- CMT2_ARATH

UniProt

Q94F87 - CMT2_ARATH

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Protein
DNA (cytosine-5)-methyltransferase CMT2
Gene
CMT2, At4g19020, F13C5.190
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

May be involved in the CpXpG methylation and in gene silencing By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei915 – 9151 By similarity

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
  2. DNA binding Source: UniProtKB-KW
  3. chromatin binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciARA:AT4G19020-MONOMER.

Protein family/group databases

REBASEi3168. M.AthCMT2.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase CMT2 (EC:2.1.1.37)
Alternative name(s):
Chromomethylase 2
Protein CHROMOMETHYLASE 2
Gene namesi
Name:CMT2
Ordered Locus Names:At4g19020
ORF Names:F13C5.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G19020.

Subcellular locationi

Nucleus By similarity

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 – 12951295DNA (cytosine-5)-methyltransferase CMT2
PRO_0000246692Add
BLAST

Proteomic databases

PaxDbiQ94F87.
PRIDEiQ94F87.

Expressioni

Gene expression databases

GenevestigatoriQ94F87.

Interactioni

Protein-protein interaction databases

BioGridi12933. 3 interactions.
DIPiDIP-60718N.

Structurei

3D structure databases

ProteinModelPortaliQ94F87.
SMRiQ94F87. Positions 523-1278.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini578 – 693116BAH
Add
BLAST
Domaini727 – 1268542SAM-dependent MTase C5-type
Add
BLAST
Domaini837 – 90266Chromo
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi822 – 8287Poly-Ser

Sequence similaritiesi

Contains 1 BAH domain.
Contains 1 chromo domain.

Phylogenomic databases

eggNOGiCOG0270.
InParanoidiQ94F87.
KOiK00558.
OMAiGCQLRRS.
PhylomeDBiQ94F87.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR001025. BAH_dom.
IPR001525. C5_MeTfrase.
IPR025821. C5_MeTfrase_pln.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR10629. PTHR10629. 1 hit.
PfamiPF01426. BAH. 1 hit.
PF00385. Chromo. 1 hit.
PF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 1 hit.
SM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 4 hits.
SSF54160. SSF54160. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q94F87-1 [UniParc]FASTAAdd to Basket

« Hide

MLSPAKCESE EAQAPLDLHS SSRSEPECLS LVLWCPNPEE AAPSSTRELI     50
KLPDNGEMSL RRSTTLNCNS PEENGGEGRV SQRKSSRGKS QPLLMLTNGC 100
QLRRSPRFRA LHANFDNVCS VPVTKGGVSQ RKFSRGKSQP LLTLTNGCQL 150
RRSPRFRAVD GNFDSVCSVP VTGKFGSRKR KSNSALDKKE SSDSEGLTFK 200
DIAVIAKSLE MEIISECQYK NNVAEGRSRL QDPAKRKVDS DTLLYSSINS 250
SKQSLGSNKR MRRSQRFMKG TENEGEENLG KSKGKGMSLA SCSFRRSTRL 300
SGTVETGNTE TLNRRKDCGP ALCGAEQVRG TERLVQISKK DHCCEAMKKC 350
EGDGLVSSKQ ELLVFPSGCI KKTVNGCRDR TLGKPRSSGL NTDDIHTSSL 400
KISKNDTSNG LTMTTALVEQ DAMESLLQGK TSACGAADKG KTREMHVNST 450
VIYLSDSDEP SSIEYLNGDN LTQVESGSAL SSGGNEGIVS LDLNNPTKST 500
KRKGKRVTRT AVQEQNKRSI CFFIGEPLSC EEAQERWRWR YELKERKSKS 550
RGQQSEDDED KIVANVECHY SQAKVDGHTF SLGDFAYIKG EEEETHVGQI 600
VEFFKTTDGE SYFRVQWFYR ATDTIMERQA TNHDKRRLFY STVMNDNPVD 650
CLISKVTVLQ VSPRVGLKPN SIKSDYYFDM EYCVEYSTFQ TLRNPKTSEN 700
KLECCADVVP TESTESILKK KSFSGELPVL DLYSGCGGMS TGLSLGAKIS 750
GVDVVTKWAV DQNTAACKSL KLNHPNTQVR NDAAGDFLQL LKEWDKLCKR 800
YVFNNDQRTD TLRSVNSTKE TSGSSSSSDD DSDSEEYEVE KLVDICFGDH 850
DKTGKNGLKF KVHWKGYRSD EDTWELAEEL SNCQDAIREF VTSGFKSKIL 900
PLPGRVGVIC GGPPCQGISG YNRHRNVDSP LNDERNQQII VFMDIVEYLK 950
PSYVLMENVV DILRMDKGSL GRYALSRLVN MRYQARLGIM TAGCYGLSQF 1000
RSRVFMWGAV PNKNLPPFPL PTHDVIVRYG LPLEFERNVV AYAEGQPRKL 1050
EKALVLKDAI SDLPHVSNDE DREKLPYESL PKTDFQRYIR STKRDLTGSA 1100
IDNCNKRTML LHDHRPFHIN EDDYARVCQI PKRKGANFRD LPGLIVRNNT 1150
VCRDPSMEPV ILPSGKPLVP GYVFTFQQGK SKRPFARLWW DETVPTVLTV 1200
PTCHSQALLH PEQDRVLTIR ESARLQGFPD YFQFCGTIKE RYCQIGNAVA 1250
VSVSRALGYS LGMAFRGLAR DEHLIKLPQN FSHSTYPQLQ ETIPH 1295
Length:1,295
Mass (Da):145,015
Last modified:February 8, 2011 - v3
Checksum:i33CE317C541825A6
GO

Sequence cautioni

The sequence BX828439 differs from that shown. Reason: Erroneous termination at position 1226. Translated as Gln.
The sequence AAK69757.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAA16759.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB78904.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 552DN → ND in AAK69757. 1 Publication
Sequence conflicti110 – 1112AL → PV in AAK69757. 1 Publication
Sequence conflicti125 – 1251K → E in AAK69757. 1 Publication
Sequence conflicti132 – 1332KF → NS in AAK69757. 1 Publication
Sequence conflicti156 – 1561F → S in AAK69757. 1 Publication
Sequence conflicti229 – 2291R → K in AAK69757. 1 Publication
Sequence conflicti340 – 3401K → N in AAK69757. 1 Publication
Sequence conflicti501 – 5011K → N in AAK69757. 1 Publication
Sequence conflicti665 – 6651V → A in AAK69757. 1 Publication
Sequence conflicti705 – 7051C → W in AAK69757. 1 Publication
Sequence conflicti823 – 8231G → E in AAK69757. 1 Publication
Sequence conflicti850 – 8501H → P in AAK69757. 1 Publication
Sequence conflicti1132 – 11321K → N in AAK69757. 1 Publication
Sequence conflicti1144 – 11441L → I in AAK69757. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF383171 Genomic DNA. Translation: AAK69757.1. Sequence problems.
AL021711 Genomic DNA. Translation: CAA16759.1. Sequence problems.
AL161549 Genomic DNA. Translation: CAB78904.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84126.1.
BX828439 mRNA. No translation available.
PIRiT05039.
RefSeqiNP_193637.2. NM_118020.4.
UniGeneiAt.32846.

Genome annotation databases

EnsemblPlantsiAT4G19020.1; AT4G19020.1; AT4G19020.
GeneIDi827640.
KEGGiath:AT4G19020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF383171 Genomic DNA. Translation: AAK69757.1 . Sequence problems.
AL021711 Genomic DNA. Translation: CAA16759.1 . Sequence problems.
AL161549 Genomic DNA. Translation: CAB78904.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE84126.1 .
BX828439 mRNA. No translation available.
PIRi T05039.
RefSeqi NP_193637.2. NM_118020.4.
UniGenei At.32846.

3D structure databases

ProteinModelPortali Q94F87.
SMRi Q94F87. Positions 523-1278.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 12933. 3 interactions.
DIPi DIP-60718N.

Protein family/group databases

REBASEi 3168. M.AthCMT2.

Proteomic databases

PaxDbi Q94F87.
PRIDEi Q94F87.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G19020.1 ; AT4G19020.1 ; AT4G19020 .
GeneIDi 827640.
KEGGi ath:AT4G19020.

Organism-specific databases

TAIRi AT4G19020.

Phylogenomic databases

eggNOGi COG0270.
InParanoidi Q94F87.
KOi K00558.
OMAi GCQLRRS.
PhylomeDBi Q94F87.

Enzyme and pathway databases

BioCyci ARA:AT4G19020-MONOMER.

Gene expression databases

Genevestigatori Q94F87.

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR001025. BAH_dom.
IPR001525. C5_MeTfrase.
IPR025821. C5_MeTfrase_pln.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10629. PTHR10629. 1 hit.
Pfami PF01426. BAH. 1 hit.
PF00385. Chromo. 1 hit.
PF00145. DNA_methylase. 1 hit.
[Graphical view ]
PRINTSi PR00105. C5METTRFRASE.
SMARTi SM00439. BAH. 1 hit.
SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 4 hits.
SSF54160. SSF54160. 1 hit.
PROSITEi PS51038. BAH. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: cv. Wassilewskija.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
    Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
    Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1153-1295.
    Strain: cv. Columbia.

Entry informationi

Entry nameiCMT2_ARATH
AccessioniPrimary (citable) accession number: Q94F87
Secondary accession number(s): O49415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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