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Protein
Submitted name:

Eco29kIR

Gene

eco29kIR

Organism
Escherichia coli
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

EndonucleaseImported, Hydrolase, Nuclease

Protein family/group databases

REBASEi2171. Eco29kI.

Names & Taxonomyi

Protein namesi
Submitted name:
Eco29kIRImported
Submitted name:
Restriction endonucleaseImported (EC:3.1.21.4Imported)
Gene namesi
Name:eco29kIRImported
Encoded oniPlasmid pECO29Imported
OrganismiEscherichia coliImported
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Interactioni

Protein-protein interaction databases

DIPiDIP-59011N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MX1X-ray2.30A2-214[»]
3MX4X-ray2.50A/B/C/D/E/F/G/H2-214[»]
3NICX-ray2.80A/B/C/D/E/F/G/H2-214[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

InterProiIPR018575. Restrct_endonuc_II_Eco29kI.
[Graphical view]
PfamiPF09517. RE_Eco29kI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46944-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHNKKFDRSE HVYRNDSFLE LIKDAVRFFS GTPVHSLPPP ERFQGAGVYA
60 70 80 90 100
LYYTGHYSLY DEYSRINRLA YNLPIYVGKA VPAGWRQSRI SDHETRAGSE
110 120 130 140 150
LSNRIREHGR NIAKTSNLDL CDFSCRFVIF EATGSDMIST VEAALIKIYK
160 170 180 190 200
PLWNTVVDGF GNHTPGAGRF AQAKSDWDVI HPGREWAEKC TGVHSEPYFI
210
EERIKQYFSK SNFT
Length:214
Mass (Da):24,567
Last modified:November 1, 1996 - v1
Checksum:i4899A02F9A9C3ECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76268 Genomic DNA. Translation: AAC37144.1.
AJ001708 Genomic DNA. Translation: CAA04943.1.
RefSeqiNP_052187.1. NC_001537.1.
WP_001529705.1. NC_001537.1.

Genome annotation databases

GeneIDi1238552.
KEGGipg:1238552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76268 Genomic DNA. Translation: AAC37144.1.
AJ001708 Genomic DNA. Translation: CAA04943.1.
RefSeqiNP_052187.1. NC_001537.1.
WP_001529705.1. NC_001537.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MX1X-ray2.30A2-214[»]
3MX4X-ray2.50A/B/C/D/E/F/G/H2-214[»]
3NICX-ray2.80A/B/C/D/E/F/G/H2-214[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59011N.

Protein family/group databases

REBASEi2171. Eco29kI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1238552.
KEGGipg:1238552.

Family and domain databases

InterProiIPR018575. Restrct_endonuc_II_Eco29kI.
[Graphical view]
PfamiPF09517. RE_Eco29kI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Eco29kI, a novel plasmid encoded restriction endonuclease from Escherichia coli."
    Pertzev A.V., Ruban N.M., Zakharova M.V., Beletzkaja I.V., Petrov S.I., Kravetz A.N., Solonin A.S.
    Nucleic Acids Res. 20:1991-1991(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 29kImported.
    Plasmid: pECO29
  2. Solonin A.S.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 29kImported.
    Plasmid: pECO29
  3. "Cloning and sequence analysis of the plasmid-borne genes encoding the Eco29kI restriction and modification enzymes."
    Zakharova M.V., Beletskaya I.V., Kravetz A.N., Pertzev A.V., Mayorov S.G., Shlyapnikov M.G., Solonin A.S.
    Gene 208:177-182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Folding, DNA recognition, and function of GIY-YIG endonucleases: crystal structures of R.Eco29kI."
    Mak A.N., Lambert A.R., Stoddard B.L.
    Structure 18:1321-1331(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-214.

Entry informationi

Entry nameiQ46944_ECOLX
AccessioniPrimary (citable) accession number: Q46944
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, PlasmidImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.