ID T2R1_CERSP Reviewed; 277 AA. AC P21763; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 03-MAY-2023, entry version 99. DE RecName: Full=Type II restriction enzyme RsrI {ECO:0000303|PubMed:12654995}; DE Short=R.RsrI; DE EC=3.1.21.4 {ECO:0000269|PubMed:2843805}; DE AltName: Full=Endonuclease RsrI; DE AltName: Full=Type-2 restriction enzyme RsrI; GN Name=rsrIR; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-35. RX PubMed=2695392; DOI=10.1016/0378-1119(89)90458-7; RA Stephenson F.H., Ballard B.T., Boyer H.W., Rosenberg J.M., Greene P.J.; RT "Comparison of the nucleotide and amino acid sequences of the RsrI and RT EcoRI restriction endonucleases."; RL Gene 85:1-13(1989). RN [2] RP PRELIMINARY PROTEIN SEQUENCE OF 2-41, FUNCTION, CATALYTIC ACTIVITY, AND RP SUBUNIT. RX PubMed=2843805; DOI=10.1093/nar/16.16.7901; RA Aiken C., Gumport R.I.; RT "Restriction endonuclease RsrI from Rhodobacter sphaeroides, an RT isoschizomer of EcoRI: purification and properties."; RL Nucleic Acids Res. 16:7901-7916(1988). RN [3] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-GAATTC-3' and cleaves after G-1. CC {ECO:0000269|PubMed:2843805, ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; CC Evidence={ECO:0000269|PubMed:2843805}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2843805}. CC -!- SIMILARITY: Belongs to the EcoRI type II restriction endonuclease CC family. {ECO:0000303|PubMed:2843805}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14697; CAA32827.1; -; Genomic_DNA. DR PIR; JW0016; JW0016. DR PIR; S03688; S03688. DR AlphaFoldDB; P21763; -. DR SMR; P21763; -. DR REBASE; 1572; RsrI. DR PRO; PR:P21763; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR CDD; cd00943; EcoRI-like; 1. DR Gene3D; 3.40.580.10; Eco RI Endonuclease, subunit A; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR004221; Restrct_endonuc_II_EcoRI. DR InterPro; IPR011336; Restrct_endonuc_II_EcoRI/MunI. DR InterPro; IPR018131; Restrct_endonuc_II_EcoRI_Pbac. DR Pfam; PF02963; EcoRI; 1. DR PIRSF; PIRSF001002; Restrict_endonuc_II_EcoRI; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease; KW Restriction system. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2695392" FT CHAIN 2..277 FT /note="Type II restriction enzyme RsrI" FT /id="PRO_0000077357" SQ SEQUENCE 277 AA; 30630 MW; 672E812D258E70B2 CRC64; MAGEVEFKGK GQALRLGIQQ ELGGGPLSIF GAAAQKHDLS IREVTAGVLT KLAEDFPNLE FQLRTSLTKK AINEKLRSFD PRLGQALFVE SASIRPDGGI TEVKDRHGNW RVILVGESKH QGNDVEKILA GVLQGKAKDQ DFMAAGNAIE RMHKNVLELR NYMLDEKHFP YVVFLQGSNF ATESFEVTRP DGRVVKIVHD SGMLNRIDRV TASSLSREIN QNYCENIVVR AGSFDHMFQI ASLYCKAAPW TAGEMAEAML AVAKTSLRII ADDLDQN //