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P14633 (T2E2_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 restriction enzyme EcoRII

Short name=R.EcoRII
EC=3.1.21.4
Alternative name(s):
Endonuclease EcoRII
Type II restriction enzyme EcoRII
Gene names
Name:ecoRIIR
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence caution

The sequence CAA34158.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA39344.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processRestriction system
   LigandMagnesium
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

Type II site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Type-2 restriction enzyme EcoRII
PRO_0000077304

Sites

Active site3081 Probable

Experimental info

Mutagenesis3081Y → F: Abolishes cleavage activity. Ref.4
Sequence conflict103 – 11311VEAAHFRILKI → GRGSPLQDPEN Ref.2
Sequence conflict103 – 11311VEAAHFRILKI → GRGSPLQDPEN Ref.3
Sequence conflict2501E → G Ref.2
Sequence conflict2501E → G Ref.3
Sequence conflict2551A → T Ref.2
Sequence conflict2551A → T Ref.3
Sequence conflict2741L → S Ref.2
Sequence conflict2741L → S Ref.3
Sequence conflict2901A → T Ref.2
Sequence conflict2901A → T Ref.3
Sequence conflict3111T → A Ref.2
Sequence conflict3111T → A Ref.3
Sequence conflict3571Q → E Ref.2
Sequence conflict3571Q → E Ref.3

Secondary structure

......................................................................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14633 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 91A047C7BA266495

FASTA40445,611
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-308.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26404 Genomic DNA. Translation: AAC15081.1.
X16025 Genomic DNA. Translation: CAA34158.1. Different initiation.
X55817 Genomic DNA. Translation: CAA39344.1. Different initiation.
PIRA34919.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NA6X-ray2.10A/B1-404[»]
3HQGX-ray2.60A183-404[»]
ProteinModelPortalP14633.
SMRP14633. Positions 4-402.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE994. EcoRII.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.330.10. 1 hit.
InterProIPR015300. DNA-bd_pseudobarrel.
IPR023372. Rest_endonuc_II_EcoRII_N.
IPR011335. Restrct_endonuc-II-like.
IPR015109. Restrct_endonuc_II_EcoRII_C.
[Graphical view]
PfamPF09019. EcoRII-C. 1 hit.
PF09217. EcoRII-N. 1 hit.
[Graphical view]
SUPFAMSSF101936. SSF101936. 1 hit.
SSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP14633.

Entry information

Entry nameT2E2_ECOLX
AccessionPrimary (citable) accession number: P14633
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references