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P14633

- T2E2_ECOLX

UniProt

P14633 - T2E2_ECOLX

Protein

Type-2 restriction enzyme EcoRII

Gene

ecoRIIR

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    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

    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

    MLMSVFHNWL LEIACENYFV YIKRLSANDT GATGGHQVGL YIPSGIVEKL    50
    FPSINHTREL NPSVFLTAHV SSHDCPDSEA RAIYYNSRHF GKTRNEKRIT 100
    RWVEAAHFRI LKITGALTLL AFKLDEQGGD CKEVNIWVCA STDEEDVIET 150
    AIGEVIPGAL ISGPAGQILG GLSLQQAPVN HKYILPEDWH LRFPSGSEII 200
    QYAASHYVKN SLDPDEQLLD RRRVEYDIFL LVEELHVLDI IRKGFGSVDE 250
    FIALANSVSN RRKSRAGKSL ELHLEHLFIE HGLRHFATQA ITEGNKKPDF 300
    LFPSAGAYHD TEFPVENLRM LAVKTTCKDR WRQILNEADK IHQVHLFTLQ 350
    EGVSLAQYRE MRESGVRLVV PSSLHKKYPE AVRAELMTLG AFIAELTGLY 400
    ADIP 404
    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