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P50187 (T2N1_NOCAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 restriction enzyme NaeI

Short name=R.NaeI
EC=3.1.21.4
Alternative name(s):
Endonuclease NaeI
Type II restriction enzyme NaeI
Gene names
Name:naeIR
OrganismLechevalieria aerocolonigenes (Nocardia aerocolonigenes) (Saccharothrix aerocolonigenes)
Taxonomic identifier68170 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeLechevalieria

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer.

Ontologies

Keywords
   Biological processRestriction system
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

Type II site-specific deoxyribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Type-2 restriction enzyme NaeI
PRO_0000077343

Experimental info

Mutagenesis431L → K: Change of function; becomes a topoisomerase that recognizes single-stranded mismatched DNA.

Secondary structure

....................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50187 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2D646D6814935B97

FASTA31735,335
        10         20         30         40         50         60 
MTELPLQFAE PDDDLERVRA TLYSLDPDGD RTAGVLRDTL DQLYDGQRTG RWNFDQLHKT 

        70         80         90        100        110        120 
EKTHMGTLVE INLHREFQFG DGFETDYEIA GVQVDCKFSM SQGAWMLPPE SIGHICLVIW 

       130        140        150        160        170        180 
ASDQQCAWTA GLVKVIPQFL GTANRDLKRR LTPEGRAQVV KLWPDHGKLQ ENLLLHIPGD 

       190        200        210        220        230        240 
VRDQIFSAKS SRGNQHGQAR VNELFRRVHG RLIGRAVIAT VAQQDDFMKR VRGSGGARSI 

       250        260        270        280        290        300 
LRPEGIIILG HQDNDPKVAN DLGLPVPRKG QVVAARVVPA DEGDQRQTAE IQGRRWAVAV 

       310 
PGDPIVEAPV VPRKSAE 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09581 Genomic DNA. Translation: AAC43324.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EV7X-ray2.38A/B1-317[»]
1IAWX-ray2.40A/B1-317[»]
ProteinModelPortalP50187.
SMRP50187. Positions 10-313.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE1294. NaeI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.40.600.10. 1 hit.
InterProIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015210. Restrct_endonuc_NaeI.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF09126. NaeI. 1 hit.
[Graphical view]
SUPFAMSSF52980. SSF52980. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP50187.

Entry information

Entry nameT2N1_NOCAE
AccessionPrimary (citable) accession number: P50187
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references