Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P14633

- T2E2_ECOLX

UniProt

P14633 - T2E2_ECOLX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Type-2 restriction enzyme EcoRII

Gene

ecoRIIR

Organism
Escherichia coli
Status
Reviewed - 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

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei308 – 3081Curated

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi308 – 3081Y → F: Abolishes cleavage activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Type-2 restriction enzyme EcoRIIPRO_0000077304Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511
Beta strandi16 – 249
Helixi27 – 304
Helixi44 – 507
Helixi52 – 543
Beta strandi58 – 614
Beta strandi63 – 7311
Beta strandi78 – 858
Helixi87 – 893
Beta strandi96 – 1005
Helixi107 – 1093
Helixi111 – 1133
Beta strandi117 – 1237
Beta strandi133 – 1386
Helixi142 – 15211
Beta strandi161 – 1644
Helixi165 – 1684
Beta strandi169 – 1724
Helixi187 – 1904
Helixi196 – 20510
Helixi214 – 24330
Helixi248 – 26518
Beta strandi266 – 2683
Helixi269 – 27911
Beta strandi287 – 2893
Beta strandi292 – 2954
Beta strandi299 – 3035
Helixi305 – 3084
Helixi315 – 3173
Beta strandi322 – 3265
Helixi332 – 3354
Beta strandi346 – 3483
Helixi355 – 3628
Turni363 – 3653
Beta strandi366 – 3694
Helixi372 – 3754
Turni380 – 3823
Helixi383 – 3853
Helixi389 – 3968
Turni400 – 4023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NA6X-ray2.10A/B3-404[»]
3HQGX-ray2.60A183-404[»]
ProteinModelPortaliP14633.
SMRiP14633. Positions 4-402.
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 CAA34158.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA39344.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 11311VEAAHFRILKI → GRGSPLQDPEN(PubMed:2597679)CuratedAdd
BLAST
Sequence conflicti103 – 11311VEAAHFRILKI → GRGSPLQDPEN(PubMed:2612358)CuratedAdd
BLAST
Sequence conflicti250 – 2501E → G(PubMed:2597679)Curated
Sequence conflicti250 – 2501E → G(PubMed:2612358)Curated
Sequence conflicti255 – 2551A → T(PubMed:2597679)Curated
Sequence conflicti255 – 2551A → T(PubMed:2612358)Curated
Sequence conflicti274 – 2741L → S(PubMed:2597679)Curated
Sequence conflicti274 – 2741L → S(PubMed:2612358)Curated
Sequence conflicti290 – 2901A → T(PubMed:2597679)Curated
Sequence conflicti290 – 2901A → T(PubMed:2612358)Curated
Sequence conflicti311 – 3111T → A(PubMed:2597679)Curated
Sequence conflicti311 – 3111T → A(PubMed:2612358)Curated
Sequence conflicti357 – 3571Q → E(PubMed:2597679)Curated
Sequence conflicti357 – 3571Q → E(PubMed:2612358)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M26404 Genomic DNA. Translation: AAC15081.1 .
X16025 Genomic DNA. Translation: CAA34158.1 . Different initiation.
X55817 Genomic DNA. Translation: CAA39344.1 . Different initiation.
PIRi A34919.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NA6 X-ray 2.10 A/B 3-404 [» ]
3HQG X-ray 2.60 A 183-404 [» ]
ProteinModelPortali P14633.
SMRi P14633. Positions 4-402.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 994. EcoRII.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14633.

Family and domain databases

Gene3Di 2.40.330.10. 1 hit.
InterProi IPR015300. DNA-bd_pseudobarrel.
IPR023372. Rest_endonuc_II_EcoRII_N.
IPR011335. Restrct_endonuc-II-like.
IPR015109. Restrct_endonuc_II_EcoRII_C.
[Graphical view ]
Pfami PF09019. EcoRII-C. 1 hit.
PF09217. EcoRII-N. 1 hit.
[Graphical view ]
SUPFAMi SSF101936. SSF101936. 1 hit.
SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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: October 1, 2014
This is version 92 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

External Data

Dasty 3