T2R1_CERSP
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 25-MAY-2022, entry version 96.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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}.
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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 Gene3D; 3.40.580.10; -; 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; SSF52980; 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
