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Reviewed, UniProtKB/Swiss-Prot O82486 (MTA70_ARATH)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N6-adenosine-methyltransferase MT-A70-like
    EC=2.1.1.62
Alternative name(s):
    Protein EMBRYO DEFECTIVE 1706
Gene names
Name: EMB1706
Ordered Locus Names: At4g10760
ORF Names: T12H20.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probable N6-methyltransferase that methylates adenosine residues of some mRNAs. N6-methyladenosine (m6A), which is present at internal sites of some mRNAs, may play a role in the efficiency of mRNA splicing, transport or translation By similarity.

Catalytic activity

S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am.

Subcellular location

Nucleus Ref.3.

Sequence similarities

Belongs to the MT-A70-like family.

Sequence caution

The sequence AAC35526.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AK227385 differs from that shown. Reason: Frameshift at position 206.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FIP37Q9ZSZ83EBI-1797380,EBI-1641243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 685685N6-adenosine-methyltransferase MT-A70-like
PRO_0000207632

Regions

Compositional bias259 – 29032Met-rich

Amino acid modifications

Modified residue6641Phosphoserine Ref.3 Ref.4

Sequences

Sequence LengthMass (Da)Tools
O82486-1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 1DBB54FBE7C5034D

FASTA68576,645
        10         20         30         40         50         60 
METESDDATI TVVKDMRVRL ENRIRTQHDA HLDLLSSLQS IVPDIVPSLD LSLKLISSFT 

        70         80         90        100        110        120 
NRPFVATPPL PEPKVEKKHH PIVKLGTQLQ QLHGHDSKSM LVDSNQRDAE ADGSSGSPMA 

       130        140        150        160        170        180 
LVRAMVAECL LQRVPFSPTD SSTVLRKLEN DQNARPAEKA ALRDLGGECG PILAVETALK 

       190        200        210        220        230        240 
SMAEENGSVE LEEFEVSGKP RIMVLAIDRT RLLKELPESF QGNNESNRVV ETPNSIENAT 

       250        260        270        280        290        300 
VSGGGFGVSG SGNFPRPEMW GGDPNMGFRP MMNAPRGMQM MGMHHPMGIM GRPPPFPLPL 

       310        320        330        340        350        360 
PLPVPSNQKL RSEEEDLKDV EALLSKKSFK EKQQSRTGEE LLDLIHRPTA KEAATAAKFK 

       370        380        390        400        410        420 
SKGGSQVKYY CRYLTKEDCR LQSGSHIACN KRHFRRLIAS HTDVSLGDCS FLDTCRHMKT 

       430        440        450        460        470        480 
CKYVHYELDM ADAMMAGPDK ALKPLRADYC SEAELGEAQW INCDIRSFRM DILGTFGVVM 

       490        500        510        520        530        540 
ADPPWDIHME LPYGTMADDE MRTLNVPSLQ TDGLIFLWVT GRAMELGREC LELWGYKRVE 

       550        560        570        580        590        600 
EIIWVKTNQL QRIIRTGRTG HWLNHSKEHC LVGIKGNPEV NRNIDTDVIV AEVRETSRKP 

       610        620        630        640        650        660 
DEMYAMLERI MPRARKLELF ARMHNAHAGW LSLGNQLNGV RLINEGLRAR FKASYPEIDV 

       670        680 
QPPSPPRASA METDNEPMAI DSITA 

« Hide

References

[1]"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. expand/collapse author list , 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: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[4]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, MASS SPECTROMETRY.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF080119 Genomic DNA. Translation: AAC35526.1. Sequence problems.
AL161518 Genomic DNA. Translation: CAB81177.1.
AK227385 mRNA. No translation available.
IPIIPI00534419.
PIRE85112.
T01901.
RefSeqNP_192814.1.
UniGeneAt.20163
At.63691

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO82486. 1 interaction.
STRINGO82486.

Proteomic databases

PRIDEO82486.

Genome annotation databases

GeneID826670.
GenomeReviewsGene locus AT4G10760 in contig CT486007_GR.
KEGGath:AT4G10760.
NMPDRfig|3702.1.peg.18737.

Organism-specific databases

GeneFarm4529. 449.
TAIRAt4g10760.

Phylogenomic databases

eggNOGKOG2098.
HOGENOMHBG318286.
InParanoidO82486.
OMAMADDEMR.
PhylomeDBO82486.

Enzyme and pathway databases

BRENDA2.1.1.62. 302.

Gene expression databases

GenevestigatorO82486.
GermOnlineAT4G10760. Arabidopsis thaliana.

Family and domain databases

InterProIPR007757. MT-A70.
[Graphical view]
PfamPF05063. MT-A70. 1 hit.
[Graphical view]
PROSITEPS51143. MT_A70. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTA70_ARATH
AccessionPrimary (citable) accession number: O82486
Secondary accession number(s): Q9M0N2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: August 16, 2005
Last modified: February 9, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents