Reviewed, UniProtKB/Swiss-Prot P14633 (T2E2_ECOLX)

Names and origin

Protein names

Recommended name:
    Type-2 restriction enzyme EcoRII
      Short name=R.EcoRII
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme EcoRII
    Endonuclease EcoRII

Gene names

Name:

ecoRIIR

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequence CCWGG and cleaves before C-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Magnesium.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 404

404

Type-2 restriction enzyme EcoRII

PRO_0000077304

Sites

Active site

308

1

Probable

Experimental info

Mutagenesis

308

1

Y → F: Abolishes cleavage activity. Ref.4

Sequence conflict

103 – 113

11

VEAAHFRILKI → GRGSPLQDPEN Ref.2

Sequence conflict

103 – 113

11

VEAAHFRILKI → GRGSPLQDPEN Ref.3

Sequence conflict

250

1

E → G Ref.2

Sequence conflict

250

1

E → G Ref.3

Sequence conflict

255

1

A → T Ref.2

Sequence conflict

255

1

A → T Ref.3

Sequence conflict

274

1

L → S Ref.2

Sequence conflict

274

1

L → S Ref.3

Sequence conflict

290

1

A → T Ref.2

Sequence conflict

290

1

A → T Ref.3

Sequence conflict

311

1

T → A Ref.2

Sequence conflict

311

1

T → A Ref.3

Sequence conflict

357

1

Q → E Ref.2

Sequence conflict

357

1

Q → E Ref.3

Secondary structure

1

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404

Helix Strand Turn

Details...

Helix

5 – 15

11

Beta strand

16 – 24

9

Turn

27 – 29

3

Helix

47 – 50

4

Helix

52 – 54

3

Beta strand

58 – 61

4

Beta strand

63 – 73

11

Beta strand

78 – 85

8

Helix

87 – 89

3

Beta strand

96 – 100

5

Helix

107 – 109

3

Helix

111 – 113

3

Beta strand

117 – 123

7

Beta strand

133 – 138

6

Helix

142 – 151

10

Helix

187 – 190

4

Helix

198 – 205

8

Helix

215 – 242

28

Helix

248 – 265

18

Helix

269 – 279

11

Beta strand

322 – 326

5

Helix

332 – 335

4

Beta strand

346 – 348

3

Helix

355 – 362

8

Helix

372 – 375

4

Turn

380 – 382

3

Helix

383 – 385

3

Helix

392 – 396

5

Sequences

	Sequence		Length	Mass (Da)
	P14633-1 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: 91A047C7BA266495	FASTA	404	45,611
	10 20 30 40 50 60 MLMSVFHNWL LEIACENYFV YIKRLSANDT GATGGHQVGL YIPSGIVEKL FPSINHTREL 70 80 90 100 110 120 NPSVFLTAHV SSHDCPDSEA RAIYYNSRHF GKTRNEKRIT RWVEAAHFRI LKITGALTLL 130 140 150 160 170 180 AFKLDEQGGD CKEVNIWVCA STDEEDVIET AIGEVIPGAL ISGPAGQILG GLSLQQAPVN 190 200 210 220 230 240 HKYILPEDWH LRFPSGSEII QYAASHYVKN SLDPDEQLLD RRRVEYDIFL LVEELHVLDI 250 260 270 280 290 300 IRKGFGSVDE FIALANSVSN RRKSRAGKSL ELHLEHLFIE HGLRHFATQA ITEGNKKPDF 310 320 330 340 350 360 LFPSAGAYHD TEFPVENLRM LAVKTTCKDR WRQILNEADK IHQVHLFTLQ EGVSLAQYRE 370 380 390 400 MRESGVRLVV PSSLHKKYPE AVRAELMTLG AFIAELTGLY ADIP

References

[1]	"Primary sequence of the EcoRII endonuclease and properties of its fusions with beta-galactosidase." Bhagwat A.S., Johnson B., Weule K., Roberts R.J. J. Biol. Chem. 265:767-773(1990) [PubMed: 2104830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the EcoRII restriction endonuclease gene." Kossykh V.G., Repyk A.V., Kaliman A.V., Bur'Yanov Y.I. Biochim. Biophys. Acta 1009:290-292(1989) [PubMed: 2597679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R245.
[3]	"Primary structure of the gene of restriction endonuclease EcoRII." Kossykh V.G., Repyk A.V., Kaliman A.V., Bur'Yanov Y.I., Baev A.A. Dokl. Akad. Nauk SSSR 308:1497-1499(1989) [PubMed: 2612358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R245.
[4]	"Changing endonuclease EcoRII Tyr308 to Phe abolishes cleavage but not recognition: possible homology with the Int-family of recombinases." Topal M.D., Conrad M. Nucleic Acids Res. 21:2599-2603(1993) [PubMed: 8392701] [Abstract] Cited for: MUTAGENESIS OF TYR-308.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M26404 Genomic DNA. Translation: AAC15081.1.
X16025 Genomic DNA. Translation: CAA34158.1. Different initiation.
X55817 Genomic DNA. Translation: CAA39344.1. Different initiation.

PIR

A34919.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NA6	X-ray	2.10	A/B	1-404	[»]
3HQG	X-ray	2.60	A	183-404	[»]

ModBase

Search...

Protein family/group databases

REBASE

994. EcoRII.

Enzyme and pathway databases

BRENDA

3.1.21.4. 246.

Family and domain databases

InterPro

IPR015109. Restrict_endonuc_II_EcoRII_C.
IPR015300. Restrict_endonuc_II_EcoRII_N.
[Graphical view]

Pfam

PF09019. EcoRII-C. 1 hit.
PF09217. EcoRII-N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

T2E2_ECOLX

Accession

Primary (citable) accession number: P14633

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 3, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)