Type-2 restriction enzyme EcoRV

Details

Name
Type-2 restriction enzyme EcoRV
Kind
protein
Synonyms
  • 3.1.21.4
  • Endonuclease EcoRV
  • R.EcoRV
  • Type II restriction enzyme EcoRV
Gene Name
ecoRVR
UniProtKB Entry
P04390Swiss-Prot
Organism
Escherichia coli
NCBI Taxonomy ID
562
Amino acid sequence
>lcl|BSEQ0017421|Type-2 restriction enzyme EcoRV
MSLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHG
YIVEEPKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKN
IVYPFDQYIAHWIIGYVYTRVATRKSSLKTYNINELNEIPKPYKGVKVFLQDKWVIAGDL
AGSGNTTNIGSIHAHYKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWI
YRGRK
Number of residues
245
Molecular Weight
28650.14
Theoretical pI
9.28
GO Classification
Functions
DNA binding / metal ion binding / Type II site-specific deoxyribonuclease activity
Processes
DNA restriction-modification system
General Function
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATATC-3' and cleaves after T-3.
Specific Function
DNA binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0017422|Type-2 restriction enzyme EcoRV (ecoRVR)
ATGAGTCTTCGTTCTGATTTAATTAATGCACTATATGATGAAAATCAAAAATATGATGTA
TGCGGAATAATATCTGCAGAAGGAAAAATATACCCATTGGGAAGTGACACAAAAGTTCTA
AGCACAATATTTGAGTTATTCTCAAGACCAATAATAAATAAAATAGCAGAAAAACATGGG
TATATTGTAGAAGAACCTAAACAACAAAATCATTATCCTGACTTTACTCTTTACAAACCA
AGCGAACCAAATAAAAAAATTGCAATAGATATAAAAACAACATATACAAACAAAGAAAAC
GAAAAAATCAAGTTCACTCTTGGTGGGTATACCAGCTTTATACGAAACAACACAAAAAAT
ATTGTTTATCCATTTGACCAATATATCGCCCATTGGATAATCGGATATGTATATACAAGA
GTTGCTACAAGAAAATCATCTTTAAAAACATATAATATAAATGAACTCAATGAAATCCCT
AAACCATACAAAGGCGTAAAGGTTTTCTTACAAGATAAATGGGTTATTGCTGGAGATTTG
GCAGGATCTGGAAACACAACAAATATAGGTAGCATTCATGCCCACTATAAAGACTTTGTA
GAAGGAAAAGGAATATTTGACTCAGAGGATGAGTTTTTAGACTATTGGAGAAATTATGAA
AGAACCAGTCAATTAAGAAATGACAAGTATAATAATATAAGCGAATACAGAAACTGGATA
TACCGAGGAAGAAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04390
UniProtKB Entry NameT2E5_ECOLX
GenBank Protein ID41325
GenBank Gene IDX00530
PDB ID(s)1AZ0, 1AZ3, 1AZ4, 1B94, 1B95, 1B96, 1B97, 1BGB, 1BSS, 1BSU, 1BUA, 1EO3, 1EO4, 1EON, 1EOO, 1EOP, 1RV5, 1RVA, 1RVB, 1RVC, 1RVE, 1STX, 1SUZ, 1SX5, 1SX8, 2B0D, 2B0E, 2GE5, 2RVE, 4ORJ, 4RVE
KEGG IDpg:14401263
NCBI Gene ID14401263
General References
  1. Bougueleret L, Schwarzstein M, Tsugita A, Zabeau M: Characterization of the genes coding for the Eco RV restriction and modification system of Escherichia coli. Nucleic Acids Res. 1984 Apr 25;12(8):3659-76. [Article]
  2. Thielking V, Selent U, Kohler E, Wolfes H, Pieper U, Geiger R, Urbanke C, Winkler FK, Pingoud A: Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis. Biochemistry. 1991 Jul 2;30(26):6416-22. [Article]
  3. Winkler FK, Banner DW, Oefner C, Tsernoglou D, Brown RS, Heathman SP, Bryan RK, Martin PD, Petratos K, Wilson KS: The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments. EMBO J. 1993 May;12(5):1781-95. [Article]
  4. Kostrewa D, Winkler FK: Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution. Biochemistry. 1995 Jan 17;34(2):683-96. [Article]
  5. Perona JJ, Martin AM: Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. J Mol Biol. 1997 Oct 17;273(1):207-25. [Article]
  6. Horton NC, Perona JJ: Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts. J Biol Chem. 1998 Aug 21;273(34):21721-9. [Article]
  7. Horton NC, Perona JJ: Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT). J Mol Biol. 1998 Apr 10;277(4):779-87. [Article]
  8. Thomas MP, Brady RL, Halford SE, Sessions RB, Baldwin GS: Structural analysis of a mutational hot-spot in the EcoRV restriction endonuclease: a catalytic role for a main chain carbonyl group. Nucleic Acids Res. 1999 Sep 1;27(17):3438-45. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
3'-THIO-THYMIDINE-5'-PHOSPHATEexperimentalunknowntargetDetails