Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P00472 (MTE1_ECOLX)

Last modified September 22, 2009. Version 62. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 326325Modification methylase EcoRI
PRO_0000087959

Sequences

Sequence LengthMass (Da)Tools
P00472-1 [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: 6257703] [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: 6257701] [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: 6257702] [Abstract]
Cited for: CONFIRMATION OF AMINO AND CARBOXYL ENDS OF SEQUENCE BY AMINO ACID ANALYSIS.

Cross-references

Sequence databases

J01675 Genomic DNA. Translation: AAA26372.1.
PIRXYECP4. A92308.

3D structure databases

ModBaseSearch...

Protein family/group databases

REBASE3395. M.EcoRI.

Enzyme and pathway databases

BRENDA2.1.1.72. 246.

Family and domain databases

InterProIPR002052. DNA_methylase_N6_adenine_CS.
[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: September 22, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

SIMILARITY comments

Index of protein domains and families

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