ID T2E2_ECOLX Reviewed; 404 AA. AC P14633; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 2. DT 02-SEP-2026, entry version 116. DE RecName: Full=Type II restriction enzyme EcoRII {ECO:0000303|PubMed:12654995}; DE Short=R.EcoRII; DE EC=3.1.21.4 {ECO:0000269|PubMed:2104830}; DE AltName: Full=Endonuclease EcoRII; DE AltName: Full=Type-2 restriction enzyme EcoRII; GN Name=ecoRIIR; OS Escherichia coli. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2104830; DOI=10.1016/s0021-9258(19)40116-6; RA Bhagwat A.S., Johnson B., Weule K., Roberts R.J.; RT "Primary sequence of the EcoRII endonuclease and properties of its fusions RT with beta-galactosidase."; RL J. Biol. Chem. 265:767-773(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=R245; RX PubMed=2597679; DOI=10.1016/0167-4781(89)90117-6; RA Kossykh V.G., Repyk A.V., Kaliman A.V., Bur'Yanov Y.I.; RT "Nucleotide sequence of the EcoRII restriction endonuclease gene."; RL Biochim. Biophys. Acta 1009:290-292(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=R245; RX PubMed=2612358; RA Kossykh V.G., Repyk A.V., Kaliman A.V., Bur'Yanov Y.I., Baev A.A.; RT "Primary structure of the gene of restriction endonuclease EcoRII."; RL Dokl. Akad. Nauk SSSR 308:1497-1499(1989). RN [4] RP MUTAGENESIS OF TYR-308. RX PubMed=8392701; DOI=10.1093/nar/21.11.2599; RA Topal M.D., Conrad M.; RT "Changing endonuclease EcoRII Tyr308 to Phe abolishes cleavage but not RT recognition: possible homology with the Int-family of recombinases."; RL Nucleic Acids Res. 21:2599-2603(1993). RN [5] RP NOMENCLATURE, AND SUBTYPES. 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: An E and P subtype restriction enzyme that recognizes the CC double-stranded sequence 5'-CCWGG-3' and cleaves before C-1. CC {ECO:0000269|PubMed:2104830, 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:2104830}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homodimer. CC -!- SEQUENCE CAUTION: CC Sequence=CAA34158.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA39344.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; M26404; AAC15081.1; -; Genomic_DNA. DR EMBL; X16025; CAA34158.1; ALT_INIT; Genomic_DNA. DR EMBL; X55817; CAA39344.1; ALT_INIT; Genomic_DNA. DR PIR; A34919; A34919. DR PDB; 1NA6; X-ray; 2.10 A; A/B=3-404. DR PDB; 3HQG; X-ray; 2.60 A; A=183-404. DR AlphaFoldDB; P14633; -. DR SMR; P14633; -. DR REBASE; 203802; Keu1446ORF816P. DR REBASE; 233042; RspNXC24ORF2358P. DR REBASE; 994; EcoRII. DR BRENDA; 3.1.21.4; 2026. DR EvolutionaryTrace; P14633; -. DR PRO; PR:P14633; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; EXP:UniProtKB. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR CDD; cd22322; EcoRII-like; 1. DR CDD; cd10016; EcoRII_N; 1. DR Gene3D; 3.40.91.80; -; 1. DR Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1. DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf. DR InterPro; IPR038365; EcoRII_C_sf. DR InterPro; IPR023372; Rest_endonuc_II_EcoRII_N. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR015109; Restrct_endonuc_II_EcoRII_C. DR Pfam; PF09019; EcoRII-C; 1. DR Pfam; PF09217; EcoRII-N; 1. DR SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. DR PDBsum; 1NA6; -. DR PDBsum; 3HQG; -. PE 1: Evidence at protein level; KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Nuclease; KW Restriction system. FT CHAIN 1..404 FT /note="Type II restriction enzyme EcoRII" FT /id="PRO_0000077304" FT ACT_SITE 308 FT /evidence="ECO:0000305" FT MUTAGEN 308 FT /note="Y->F: Abolishes cleavage activity." FT /evidence="ECO:0000269|PubMed:8392701" FT CONFLICT 103..113 FT /note="VEAAHFRILKI -> GRGSPLQDPEN (in Ref. 2; CAA34158 and FT 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="E -> G (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="A -> T (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="L -> S (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 290 FT /note="A -> T (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="T -> A (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT CONFLICT 357 FT /note="Q -> E (in Ref. 2; CAA34158 and 3; CAA39344)" FT /evidence="ECO:0000305" FT HELIX 5..15 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 16..24 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 44..50 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 63..73 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 133..138 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 142..152 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 196..205 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 214..243 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 248..265 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 269..279 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:3HQG" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:3HQG" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:3HQG" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 332..335 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 355..362 FT /evidence="ECO:0007829|PDB:1NA6" FT TURN 363..365 FT /evidence="ECO:0007829|PDB:1NA6" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:3HQG" FT HELIX 372..375 FT /evidence="ECO:0007829|PDB:1NA6" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:1NA6" FT HELIX 389..396 FT /evidence="ECO:0007829|PDB:1NA6" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:3HQG" SQ SEQUENCE 404 AA; 45611 MW; 91A047C7BA266495 CRC64; MLMSVFHNWL LEIACENYFV YIKRLSANDT GATGGHQVGL YIPSGIVEKL FPSINHTREL NPSVFLTAHV SSHDCPDSEA RAIYYNSRHF GKTRNEKRIT RWVEAAHFRI LKITGALTLL AFKLDEQGGD CKEVNIWVCA STDEEDVIET AIGEVIPGAL ISGPAGQILG GLSLQQAPVN HKYILPEDWH LRFPSGSEII QYAASHYVKN SLDPDEQLLD RRRVEYDIFL LVEELHVLDI IRKGFGSVDE FIALANSVSN RRKSRAGKSL ELHLEHLFIE HGLRHFATQA ITEGNKKPDF LFPSAGAYHD TEFPVENLRM LAVKTTCKDR WRQILNEADK IHQVHLFTLQ EGVSLAQYRE MRESGVRLVV PSSLHKKYPE AVRAELMTLG AFIAELTGLY ADIP //