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Protein

Type-2 restriction enzyme EcoRII

Gene

ecoRIIR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence CCWGG and cleaves before C-1.

Catalytic activityi

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei308Curated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BRENDAi3.1.21.4. 2026.

Protein family/group databases

REBASEi994. EcoRII.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme EcoRII (EC:3.1.21.4)
Short name:
R.EcoRII
Alternative name(s):
Endonuclease EcoRII
Type II restriction enzyme EcoRII
Gene namesi
Name:ecoRIIR
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi308Y → F: Abolishes cleavage activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000773041 – 404Type-2 restriction enzyme EcoRIIAdd BLAST404

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Beta strandi16 – 24Combined sources9
Helixi27 – 30Combined sources4
Beta strandi34 – 36Combined sources3
Helixi44 – 50Combined sources7
Helixi52 – 54Combined sources3
Beta strandi58 – 61Combined sources4
Beta strandi63 – 73Combined sources11
Beta strandi78 – 85Combined sources8
Helixi87 – 89Combined sources3
Beta strandi96 – 100Combined sources5
Helixi107 – 109Combined sources3
Helixi111 – 113Combined sources3
Beta strandi117 – 123Combined sources7
Beta strandi133 – 138Combined sources6
Helixi142 – 152Combined sources11
Beta strandi161 – 164Combined sources4
Helixi165 – 168Combined sources4
Beta strandi169 – 172Combined sources4
Helixi187 – 190Combined sources4
Helixi196 – 205Combined sources10
Helixi214 – 243Combined sources30
Helixi248 – 265Combined sources18
Beta strandi266 – 268Combined sources3
Helixi269 – 279Combined sources11
Beta strandi287 – 289Combined sources3
Beta strandi292 – 295Combined sources4
Beta strandi299 – 303Combined sources5
Helixi305 – 308Combined sources4
Beta strandi311 – 313Combined sources3
Helixi315 – 317Combined sources3
Beta strandi322 – 326Combined sources5
Helixi332 – 335Combined sources4
Beta strandi342 – 344Combined sources3
Beta strandi346 – 348Combined sources3
Helixi355 – 362Combined sources8
Turni363 – 365Combined sources3
Beta strandi366 – 369Combined sources4
Helixi372 – 375Combined sources4
Turni380 – 382Combined sources3
Helixi383 – 385Combined sources3
Helixi389 – 396Combined sources8
Turni400 – 402Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NA6X-ray2.10A/B3-404[»]
3HQGX-ray2.60A183-404[»]
ProteinModelPortaliP14633.
SMRiP14633.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14633.

Family & Domainsi

Family and domain databases

Gene3Di2.40.330.10. 1 hit.
InterProiIPR015300. DNA-bd_pseudobarrel.
IPR023372. Rest_endonuc_II_EcoRII_N.
IPR011335. Restrct_endonuc-II-like.
IPR015109. Restrct_endonuc_II_EcoRII_C.
[Graphical view]
PfamiPF09019. EcoRII-C. 1 hit.
PF09217. EcoRII-N. 1 hit.
[Graphical view]
SUPFAMiSSF101936. SSF101936. 1 hit.
SSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P14633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMSVFHNWL LEIACENYFV YIKRLSANDT GATGGHQVGL YIPSGIVEKL
60 70 80 90 100
FPSINHTREL NPSVFLTAHV SSHDCPDSEA RAIYYNSRHF GKTRNEKRIT
110 120 130 140 150
RWVEAAHFRI LKITGALTLL AFKLDEQGGD CKEVNIWVCA STDEEDVIET
160 170 180 190 200
AIGEVIPGAL ISGPAGQILG GLSLQQAPVN HKYILPEDWH LRFPSGSEII
210 220 230 240 250
QYAASHYVKN SLDPDEQLLD RRRVEYDIFL LVEELHVLDI IRKGFGSVDE
260 270 280 290 300
FIALANSVSN RRKSRAGKSL ELHLEHLFIE HGLRHFATQA ITEGNKKPDF
310 320 330 340 350
LFPSAGAYHD TEFPVENLRM LAVKTTCKDR WRQILNEADK IHQVHLFTLQ
360 370 380 390 400
EGVSLAQYRE MRESGVRLVV PSSLHKKYPE AVRAELMTLG AFIAELTGLY

ADIP
Length:404
Mass (Da):45,611
Last modified:August 1, 1990 - v2
Checksum:i91A047C7BA266495
GO

Sequence cautioni

The sequence CAA34158 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA39344 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103 – 113VEAAHFRILKI → GRGSPLQDPEN (PubMed:2597679).CuratedAdd BLAST11
Sequence conflicti103 – 113VEAAHFRILKI → GRGSPLQDPEN (PubMed:2612358).CuratedAdd BLAST11
Sequence conflicti250E → G (PubMed:2597679).Curated1
Sequence conflicti250E → G (PubMed:2612358).Curated1
Sequence conflicti255A → T (PubMed:2597679).Curated1
Sequence conflicti255A → T (PubMed:2612358).Curated1
Sequence conflicti274L → S (PubMed:2597679).Curated1
Sequence conflicti274L → S (PubMed:2612358).Curated1
Sequence conflicti290A → T (PubMed:2597679).Curated1
Sequence conflicti290A → T (PubMed:2612358).Curated1
Sequence conflicti311T → A (PubMed:2597679).Curated1
Sequence conflicti311T → A (PubMed:2612358).Curated1
Sequence conflicti357Q → E (PubMed:2597679).Curated1
Sequence conflicti357Q → E (PubMed:2612358).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26404 Genomic DNA. Translation: AAC15081.1.
X16025 Genomic DNA. Translation: CAA34158.1. Different initiation.
X55817 Genomic DNA. Translation: CAA39344.1. Different initiation.
PIRiA34919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26404 Genomic DNA. Translation: AAC15081.1.
X16025 Genomic DNA. Translation: CAA34158.1. Different initiation.
X55817 Genomic DNA. Translation: CAA39344.1. Different initiation.
PIRiA34919.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NA6X-ray2.10A/B3-404[»]
3HQGX-ray2.60A183-404[»]
ProteinModelPortaliP14633.
SMRiP14633.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi994. EcoRII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.21.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP14633.

Family and domain databases

Gene3Di2.40.330.10. 1 hit.
InterProiIPR015300. DNA-bd_pseudobarrel.
IPR023372. Rest_endonuc_II_EcoRII_N.
IPR011335. Restrct_endonuc-II-like.
IPR015109. Restrct_endonuc_II_EcoRII_C.
[Graphical view]
PfamiPF09019. EcoRII-C. 1 hit.
PF09217. EcoRII-N. 1 hit.
[Graphical view]
SUPFAMiSSF101936. SSF101936. 1 hit.
SSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiT2E2_ECOLX
AccessioniPrimary (citable) accession number: P14633
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.