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P00472 (MTE1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:
Modification methylase EcoRI

Short name=M.EcoRI
EC=2.1.1.72
Alternative name(s):
Adenine-specific methyltransferase EcoRI
Gene names
Name:ecoRIM
Encoded onPlasmid pMB1 Ref.1
Plasmid pMB4 Ref.2
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-3 on both strands, and protects the DNA from cleavage by the EcoRI endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Subunit structure

Monomer.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termPlasmid
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

site-specific DNA-methyltransferase (adenine-specific) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 326325Modification methylase EcoRI
PRO_0000087959

Sequences

Sequence LengthMass (Da)Tools
P00472 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5F6AFE1DD1CBB1A8

FASTA32638,044
        10         20         30         40         50         60 
MARNATNKLL HKAKKSKSDE FYTQYCDIEN ELQYYREHFS DKVVYCNCDD PRVSNFFKYF 

        70         80         90        100        110        120 
AVNFDNLGLK KLIASCYVEN KEGFSSSEAA KNGFYYEYHK ENGKKLVFDD ISVSSFCGDG 

       130        140        150        160        170        180 
DFRSSESIDL LKKSDIVVTN PPFSLFREYL DQLIKYDKKF LIIANVNSIT YKEVFNLIKE 

       190        200        210        220        230        240 
NKIWLGVHLG RGVSGFIVPE HYELYGTEAR IDSNGNRIIS PNNCLWLTNL DVFIRHKDLP 

       250        260        270        280        290        300 
LTRKYFGNES SYPKYDNYDA INVNKTKDIP LDYNGVMGVP ITFLHKFNPE QFELIKFRKG 

       310        320 
VDEKDLSING KCPYFRILIK NKRLQK 

« Hide

References

[1]"Sequence analysis of the DNA encoding the Eco RI endonuclease and methylase."
Greene P.J., Gupta M., Boyer H.W., Brown W.E., Rosenberg J.M.
J. Biol. Chem. 256:2143-2153(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequences of structural genes for Eco RI DNA restriction and modification enzymes."
Newman A.K., Rubin R.A., Kim S.-H., Modrich P.
J. Biol. Chem. 256:2131-2139(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C.
[3]"Partial NH2- and COOH-terminal sequence analyses of Eco RI DNA restriction and modification enzymes."
Rubin R.A., Modrich P., Vanaman T.C.
J. Biol. Chem. 256:2140-2142(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: CONFIRMATION OF AMINO AND CARBOXYL ENDS OF SEQUENCE BY AMINO ACID ANALYSIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01675 Genomic DNA. Translation: AAA26372.1.
PIRXYECP4. A92308.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3395. M.EcoRI.

Proteomic databases

PRIDEP00472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002052. DNA_methylase_N6_adenine_CS.
IPR025247. EcoRI_methylase.
[Graphical view]
PfamPF13651. EcoRI_methylase. 1 hit.
[Graphical view]
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTE1_ECOLX
AccessionPrimary (citable) accession number: P00472
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries