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Q47282 (T1ME_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. 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:
Type I restriction enzyme EcoEI M protein

Short name=M.EcoEI
EC=2.1.1.72
Gene names
Name:hsdM
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoEI enzyme recognizes 5'-GAGN7ATGC-3'.

Catalytic activity

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

Subunit structure

The type I restriction/modification system is composed of three polypeptides R, M and S.

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Type I restriction enzyme EcoEI M protein
PRO_0000088021

Regions

Region163 – 1686S-adenosyl-L-methionine binding By similarity
Region193 – 1953S-adenosyl-L-methionine binding By similarity

Sites

Binding site2261S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47282 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A8643DEB39981FFB

FASTA49055,620
        10         20         30         40         50         60 
MSISSVIKSL QDIMRKDAGV DGDAQRLGQL SWLLFLKIFD TQEEELELEQ DDYQFPIPQR 

        70         80         90        100        110        120 
YLWRSWAANS EGITGDALLE FVNDDLFPTL KNLTAPIDKN PRGFVVKQAF SDAYNYMKNG 

       130        140        150        160        170        180 
TLLRQVINKL NEIDFSSSQE RHLFGDIYEQ ILRDLQSAGN AGEFYTPRAV TRFMVNRIDP 

       190        200        210        220        230        240 
KLGESIMDPA CGTGGFLACA FDHVKDNYVK TTEDHKTLQQ QIYGVEKKQL PHLLCTTNML 

       250        260        270        280        290        300 
LHGIEVPVQI RHDNTLNKPL SSWDEQVDVI VTNPPFGGTE EDGIEKNFPA EMQTRETADL 

       310        320        330        340        350        360 
FLQLIIEVLA DKGRAAVVLP DGTLFGEGVK TKIKKLLTEE CNLHTIVRLP NGVFNPYTGI 

       370        380        390        400        410        420 
KTNILFFTKG QPTKEVWFYE HPYPDGVKNY SKTKPMKFEE FQAEIDWWGN EADDFASREE 

       430        440        450        460        470        480 
NNQAWKVGID DIIARNFNLD IKNPYQGETI SHDPDELLAQ YQTQQAEIGE LRNQLRDILG 

       490 
AALAGNKGAN 

« Hide

References

[1]"Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes."
Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.
Mol. Microbiol. 9:133-143(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18759 Genomic DNA. Translation: AAD15049.1.
PIRI41293.

3D structure databases

ProteinModelPortalQ47282.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ47282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0286.

Family and domain databases

InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1ME_ECOLX
AccessionPrimary (citable) accession number: Q47282
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 66 of the entry and version 1 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