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P50187

- T2N1_NOCAE

UniProt

P50187 - T2N1_NOCAE

Protein

Type-2 restriction enzyme NaeI

Gene

naeIR

Organism
Lechevalieria aerocolonigenes (Nocardia aerocolonigenes) (Saccharothrix aerocolonigenes)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (16 Apr 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Recognizes the double-stranded unmethylated sequence GCCGGC and cleaves after C-3.

    Catalytic activityi

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

    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

    Protein family/group databases

    REBASEi1294. NaeI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type-2 restriction enzyme NaeI (EC:3.1.21.4)
    Short name:
    R.NaeI
    Alternative name(s):
    Endonuclease NaeI
    Type II restriction enzyme NaeI
    Gene namesi
    Name:naeIR
    OrganismiLechevalieria aerocolonigenes (Nocardia aerocolonigenes) (Saccharothrix aerocolonigenes)
    Taxonomic identifieri68170 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeLechevalieria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431L → K: Change of function; becomes a topoisomerase that recognizes single-stranded mismatched DNA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Type-2 restriction enzyme NaeIPRO_0000077343Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2513
    Beta strandi26 – 294
    Helixi30 – 4415
    Helixi46 – 494
    Helixi54 – 563
    Helixi59 – 635
    Helixi65 – 7713
    Beta strandi83 – 897
    Beta strandi92 – 10110
    Helixi109 – 1113
    Beta strandi114 – 1229
    Turni123 – 1264
    Beta strandi127 – 1348
    Helixi137 – 1393
    Helixi153 – 1564
    Beta strandi160 – 1634
    Helixi173 – 1753
    Helixi179 – 1868
    Beta strandi191 – 1944
    Helixi196 – 20712
    Beta strandi210 – 2134
    Helixi215 – 2228
    Helixi228 – 2303
    Beta strandi232 – 24110
    Helixi242 – 2443
    Beta strandi246 – 2494
    Helixi255 – 2617
    Beta strandi262 – 2643
    Beta strandi272 – 2798
    Beta strandi288 – 29811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EV7X-ray2.38A/B1-317[»]
    1IAWX-ray2.40A/B1-317[»]
    ProteinModelPortaliP50187.
    SMRiP50187. Positions 10-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50187.

    Family & Domainsi

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.600.10. 1 hit.
    InterProiIPR011337. DNA_rep_MutH/RE_typeII.
    IPR011335. Restrct_endonuc-II-like.
    IPR015210. Restrct_endonuc_NaeI.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF09126. NaeI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52980. SSF52980. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P50187-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTELPLQFAE PDDDLERVRA TLYSLDPDGD RTAGVLRDTL DQLYDGQRTG    50
    RWNFDQLHKT EKTHMGTLVE INLHREFQFG DGFETDYEIA GVQVDCKFSM 100
    SQGAWMLPPE SIGHICLVIW ASDQQCAWTA GLVKVIPQFL GTANRDLKRR 150
    LTPEGRAQVV KLWPDHGKLQ ENLLLHIPGD VRDQIFSAKS SRGNQHGQAR 200
    VNELFRRVHG RLIGRAVIAT VAQQDDFMKR VRGSGGARSI LRPEGIIILG 250
    HQDNDPKVAN DLGLPVPRKG QVVAARVVPA DEGDQRQTAE IQGRRWAVAV 300
    PGDPIVEAPV VPRKSAE 317
    Length:317
    Mass (Da):35,335
    Last modified:October 1, 1996 - v1
    Checksum:i2D646D6814935B97
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09581 Genomic DNA. Translation: AAC43324.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09581 Genomic DNA. Translation: AAC43324.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EV7 X-ray 2.38 A/B 1-317 [» ]
    1IAW X-ray 2.40 A/B 1-317 [» ]
    ProteinModelPortali P50187.
    SMRi P50187. Positions 10-313.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 1294. NaeI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P50187.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.40.600.10. 1 hit.
    InterProi IPR011337. DNA_rep_MutH/RE_typeII.
    IPR011335. Restrct_endonuc-II-like.
    IPR015210. Restrct_endonuc_NaeI.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF09126. NaeI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52980. SSF52980. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the NaeI restriction endonuclease-encoding gene and sequence analysis of the NaeI restriction-modification system."
      Taron C.H., van Cott E.M., Wilson G.G., Moran L.S., Slatko B.E., Hornstra L.J., Benner J.S., Kucera R.B., Guthrie E.P.
      Gene 155:19-25(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 23870 / BCRC 13661 / DSM 40034 / JCM 4614 / NBRC 13195 / NCIMB 12944 / NRRL B-3298.
    2. "DNA topoisomerase and recombinase activities in Nae I restriction endonuclease."
      Jo K., Topal M.D.
      Science 267:1817-1820(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF MUTANT LYS-43.
    3. "Effects on NaeI-DNA recognition of the leucine to lysine substitution that transforms restriction endonuclease NaeI to a topoisomerase: a model for restriction endonuclease evolution."
      Jo K., Topal M.D.
      Nucleic Acids Res. 24:4171-4175(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF MUTANT LYS-43.
    4. "Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase."
      Huai Q., Colandene J.D., Chen Y., Luo F., Zhao Y., Topal M.D., Ke H.
      EMBO J. 19:3110-3118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).

    Entry informationi

    Entry nameiT2N1_NOCAE
    AccessioniPrimary (citable) accession number: P50187
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: April 16, 2014
    This is version 72 of the entry and version 1 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