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Reviewed, UniProtKB/Swiss-Prot P50196 (MTE8_ECOLX)

Last modified September 2, 2008. Version 40. 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 Eco47II
      Short name=M.Eco47II
    EC=2.1.1.37
Alternative name(s):
    Cytosine-specific methyltransferase Eco47II
Gene names
Name: eco47IIM
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GGNCC, causes specific methylation on C-? on both strands, and protects the DNA from cleavage by the Eco47II endonuclease.

Catalytic activity

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

Sequence similarities

Belongs to the C5-methyltransferase family.

Ontologies

Keywords

   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 417417Modification methylase Eco47II

Sites

Active site1531 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50196-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C399A49E00BDAFD3

FASTA41747,513
        10         20         30         40         50         60 
MLAWLLNMLK EEFSLSEVAD ILGVSKETLR RWDTAGKLVS QRNDENNYRF YKKEQLKNFE 

        70         80         90        100        110        120 
QAQFLFKSQW PDETKISNNV YTVLELFAGA GGMALGLEKA GLKSVLLNEI DSHACKTLRK 

       130        140        150        160        170        180 
NRPEWNVVEG DVSQVDFTPY RNTVDVLAGG FPCQAFSYAG KKLGFEDTRG TLFFEFARAA 

       190        200        210        220        230        240 
KEINPKVLLA ENVRGLLNHD AGRTLETIKN IITDLGYTLF EPRVLKAIFY KVPQKRERLI 

       250        260        270        280        290        300 
IVAVRNDLAD GIDYEWPSSY NKILTLKDAL KKGELYDSDV PESEGQKYPK RKAEILSMVP 

       310        320        330        340        350        360 
PGGYWRDLPE DIQKEYMLKS FYLGGGKTGM ARRLSWDEPS LTLTCAPAQK QTERCHPEET 

       370        380        390        400        410 
RPLTVREYAR IQTFPDEWVF EGPMSAKYKQ IGNAVPVNLS FAVGKSVVHL LDKINKR 

« Hide

References

[1]"Cloning and characterization of the unusual restriction-modification system comprising two restriction endonucleases and one methyltransferase."
Stankevicius K., Povilionis P., Lubys A., Menkevicius S., Janulaitis A.
Gene 157:49-53(1995) [PubMed: 7607524] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RFL47.

Cross-references

Sequence databases

X82105 Genomic DNA. Translation: CAA57629.1.

3D structure databases

HSSPHSSP built from PDB template 6MHT based on UniProtKB P05102.
ModBaseSearch...

Protein family/group databases

REBASE3372. M.Eco47II.

Family and domain databases

InterProIPR001525. C5_DNA_meth.
IPR000551. HTH_MerR.
[Graphical view]
PANTHERPTHR10629. C5_DNA_meth. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
PF00376. MerR. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
[Graphical view]
ProDomP50196.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameMTE8_ECOLX
AccessionPrimary (citable) accession number: P50196
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 2, 2008
This is version 40 of the entry and version 1 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