T2E2_ECOLX
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 25-MAY-2022, entry version 110.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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};
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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 PDBsum; 1NA6; -.
DR PDBsum; 3HQG; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 2.40.330.10; -; 1.
DR Gene3D; 3.40.91.80; -; 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; SSF101936; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
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 187..190
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
