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P50187

- T2N1_NOCAE

UniProt

P50187 - T2N1_NOCAE

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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

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
Complete GO annotation...

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 NaeI
PRO_0000077343Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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.

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

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