Q47163 (T1MP_ECOLX) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 66. History...
Names and origin
|Sequence length||520 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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'.
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
The type I restriction/modification system is composed of three polypeptides R, M and S.
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.
Belongs to the N(4)/N(6)-methyltransferase family.
|Biological process||Restriction system|
|Gene Ontology (GO)|
|Biological_process||DNA restriction-modification system|
Inferred from electronic annotation. Source: UniProtKB-KW
Inferred from electronic annotation. Source: InterProN-methyltransferase activity
Inferred from electronic annotation. Source: InterProsite-specific DNA-methyltransferase (adenine-specific) activity
Inferred from electronic annotation. Source: EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 520||520||Type I restriction enzyme EcoprrI M protein||PRO_0000088024|
|Region||198 – 203||6||S-adenosyl-L-methionine binding By similarity|
|Region||230 – 232||3||S-adenosyl-L-methionine binding By similarity|
|Binding site||254||1||S-adenosyl-L-methionine By similarity|
|X75452 Genomic DNA. Translation: CAA53205.1.|
3D structure databases
Protein family/group databases
|REBASE||3552. M.EcoprrI. |
Protocols and materials databases
Family and domain databases
|InterPro||IPR022749. D12N6_MeTrfase_N. |
|Pfam||PF12161. HsdM_N. 1 hit. |
PF02384. N6_Mtase. 1 hit.
|PRINTS||PR00507. N12N6MTFRASE. |
|TIGRFAMs||TIGR00497. hsdM. 1 hit. |
|PROSITE||PS00092. N6_MTASE. 1 hit. |
|Accession||Primary (citable) accession number: Q47163|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|