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Q47163 (T1MP_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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 EcoprrI M protein

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

Protein attributes

Sequence length520 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 EcoprrI enzyme recognizes 5'-CCAN7ATGC-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 – 520520Type I restriction enzyme EcoprrI M protein
PRO_0000088024

Regions

Region198 – 2036S-adenosyl-L-methionine binding By similarity
Region230 – 2323S-adenosyl-L-methionine binding By similarity

Sites

Binding site2541S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47163 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 79401EC1720EB257

FASTA52058,015
        10         20         30         40         50         60 
MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS SYIEAGDDSI 

        70         80         90        100        110        120 
CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN TNDRLNADLN SIFVAIESSA 

       130        140        150        160        170        180 
YGYPSEADIK GLFADFDTTS NRLGNTVKDK NARLAAVLKG VEGLKLGDFN EHQIDLFGDA 

       190        200        210        220        230        240 
YEFLISNYAA NAGKSGGEFF TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ 

       250        260        270        280        290        300 
FDDHIIEEGF FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV 

       310        320        330        340        350        360 
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK GRAAIVCFPG 

       370        380        390        400        410        420 
IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN ILVLSKHKTD TKVQFIDASE 

       430        440        450        460        470        480 
LFKKETNNNI LTDAHIEQIM QVFASKEDVA HLAKSVAFET VVANDYNLSV SSYVEAKDTR 

       490        500        510        520 
EIIDIAELNA ELKTTVSKID QLRKDIDAIV AEIEGCEVQK 

« Hide

References

[1]"The Escherichia coli prr region encodes a functional type IC DNA restriction system closely integrated with an anticodon nuclease gene."
Tyndall C., Meister J., Bickle T.A.
J. Mol. Biol. 237:266-274(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CTR5X.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75452 Genomic DNA. Translation: CAA53205.1.

3D structure databases

ProteinModelPortalQ47163.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3552. M.EcoprrI.

Proteomic databases

PRIDEQ47163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR004546. Restrct_endonuc_typeI_HsdM.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
SUPFAMSSF53335. SSF53335. 2 hits.
TIGRFAMsTIGR00497. hsdM. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1MP_ECOLX
AccessionPrimary (citable) accession number: Q47163
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 68 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