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P14633

- T2E2_ECOLX

UniProt

P14633 - T2E2_ECOLX

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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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. Curated
The sequence CAA39344.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
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.
PIRi A34919.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 93 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