Q47281 · T1RE_ECOLX
- ProteinType I restriction enzyme EcoEI endonuclease subunit
- GenehsdR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids813 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
The restriction (R) subunit of a type I restriction enzyme that recognizes 5'-GAGN7ATGC-3' and cleaves a random distance away. Subunit R is required for both nuclease and ATPase activities, but not for modification. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
Miscellaneous
Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and magnesium as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.
Catalytic activity
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | type I site-specific deoxyribonuclease activity | |
Biological Process | DNA restriction-modification system |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameType I restriction enzyme EcoEI endonuclease subunit
- EC number
- Short namesEcoEI ; R protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ47281
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000077258 | 1-813 | Type I restriction enzyme EcoEI endonuclease subunit | |||
Sequence: MAGVNKTHLTETDIITKFILPAVKDAGWDVMSQIRQEVKLRDGKIVVRGKLASRIKVKSADIVLYHKPNLPLAVIEAKANKHAISKGMQQGLDYASLLDVPFVFASNGDGFIFHDKTNPQQLESEIALSDFPTPEQLWQKYCAWKGFTQEQLPVISQDYFDDGSGKAPRYYQMQAINRTVDAVSAGKNRILLVMATGTGKTYTAFQIIWRLWKAKNKKRILFLADRNILVDQTKRNDFQPFGNAMTKVTGRTIDPAYEVHLALYQAITGPEEHQKAYKQVAPDFFDLIVIDECHRGSASEDSAWREILEYFGSATQVGLTATPKETEDVSNIDYFGEPVYTYSLKEGIEDGFLAPYKVVRVDIDVDVQGWRPVKGQLDKYGEEIEDRIYNLKDFDRTLVIDERTMLVAQTITDYLKRTNPMDKTIVFCNDIDHADRMRHALVVLNPEQVLKNEKYVMKITGDDDIGKAQLDNFINPKKAYPVIATTSELMTTGVDAQTCKLVVLDQNIQSMTKFKQIIGRGTRINEKHGKLWFTILDFKKATELFADPRFDGLPEKVLVVKPGDISDKDSDFNEQLDAENNADGGDNDASEAREDVADYQVNRDKQAGNGEFHDDDENKVRKFYVNGVDVKVLAKRVQYYDSDGKLVTESFQDYTRKTMLKDSEYASLDSFVRKWQDAPRKQVIIEELEQLGILWDVLAEEVGKDLDPFDLLCHVVYGQPPLTRQERVANVRKRNYFTKYAEPAQQVLNTLLDKYADEGVQEIEDVQVLKLKPFDTLGRPIEIIKTRFGDKKAYEQAVNELENEIYQLPPRSA |
Interaction
Subunit
The type I restriction/modification system is composed of three polypeptides R, M and S; the restriction enzyme has stoichiometry R2M2S1 while the methyltransferase is M2S1.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 181-341 | Helicase ATP-binding | ||||
Sequence: DAVSAGKNRILLVMATGTGKTYTAFQIIWRLWKAKNKKRILFLADRNILVDQTKRNDFQPFGNAMTKVTGRTIDPAYEVHLALYQAITGPEEHQKAYKQVAPDFFDLIVIDECHRGSASEDSAWREILEYFGSATQVGLTATPKETEDVSNIDYFGEPVYT | ||||||
Domain | 410-561 | Helicase C-terminal | ||||
Sequence: TITDYLKRTNPMDKTIVFCNDIDHADRMRHALVVLNPEQVLKNEKYVMKITGDDDIGKAQLDNFINPKKAYPVIATTSELMTTGVDAQTCKLVVLDQNIQSMTKFKQIIGRGTRINEKHGKLWFTILDFKKATELFADPRFDGLPEKVLVVK | ||||||
Region | 568-591 | Disordered | ||||
Sequence: KDSDFNEQLDAENNADGGDNDASE |
Sequence similarities
Belongs to the HsdR family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length813
- Mass (Da)92,627
- Last updated1996-11-01 v1
- ChecksumA1EB1794123F0ADD