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Protein

Excisionase

Gene

xis

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Part of the excision complex necessary for the excision of prophage from the host genome by site-specific recombination at the att site.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA recombination, Viral genome excision

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Excisionase
Gene namesi
Name:xis
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000001711 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7272ExcisionasePRO_0000077714Add
BLAST

Interactioni

Subunit structurei

Interacts (via C-terminus) with the integrase (via N-terminus) (PubMed:12832614). Part of the excision complex made of the integrase tetramer, IHF, Fis and Xis (PubMed:25114241).2 Publications

Protein-protein interaction databases

DIPiDIP-60872N.
IntActiP03699. 2 interactions.

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi5 – 106Combined sources
Beta strandi12 – 143Combined sources
Helixi18 – 269Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 445Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LX8NMR-A1-55[»]
1RH6X-ray1.70A/B1-55[»]
2IEFX-ray2.60A/B/C1-55[»]
2OG0X-ray1.90A/B1-52[»]
ProteinModelPortaliP03699.
SMRiP03699. Positions 1-72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03699.

Family & Domainsi

Family and domain databases

Gene3Di1.10.1660.20. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR012884. Excisionase-like.
[Graphical view]
PfamiPF07825. Exc. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.

Sequencei

Sequence statusi: Complete.

P03699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLTLQEWNA RQRRPRSLET VRRWVRECRI FPPPVKDGRE YLFHESAVKV
60 70
DLNRPVTGGL LKRIRNGKKA KS
Length:72
Mass (Da):8,605
Last modified:July 21, 1986 - v1
Checksum:i0E6A4843502200AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96563.1.
PIRiC94164. RSBPXL.
RefSeqiNP_040610.1. NC_001416.1.

Genome annotation databases

GeneIDi2703504.
KEGGivg:2703504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96563.1.
PIRiC94164. RSBPXL.
RefSeqiNP_040610.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LX8NMR-A1-55[»]
1RH6X-ray1.70A/B1-55[»]
2IEFX-ray2.60A/B/C1-55[»]
2OG0X-ray1.90A/B1-52[»]
ProteinModelPortaliP03699.
SMRiP03699. Positions 1-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60872N.
IntActiP03699. 2 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703504.
KEGGivg:2703504.

Miscellaneous databases

EvolutionaryTraceiP03699.

Family and domain databases

Gene3Di1.10.1660.20. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR012884. Excisionase-like.
[Graphical view]
PfamiPF07825. Exc. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "DNA sequence of the int-xis-Pi region of the bacteriophage lambda; overlap of the int and xis genes."
    Davies R.W.
    Nucleic Acids Res. 8:1765-1782(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Site-specific recombination functions of bacteriophage lambda: DNA sequence of regulatory regions and overlapping structural genes for Int and Xis."
    Hoess R.H., Foeller C., Bidwell K., Landy A.
    Proc. Natl. Acad. Sci. U.S.A. 77:2482-2486(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation."
    Warren D., Sam M.D., Manley K., Sarkar D., Lee S.Y., Abbani M., Wojciak J.M., Clubb R.T., Landy A.
    Proc. Natl. Acad. Sci. U.S.A. 100:8176-8181(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE INTEGRASE.
  5. "Nucleoprotein architectures regulating the directionality of viral integration and excision."
    Seah N.E., Warren D., Tong W., Laxmikanthan G., Van Duyne G.D., Landy A.
    Proc. Natl. Acad. Sci. U.S.A. 111:12372-12377(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE EXCISION COMPLEX.
  6. "Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein."
    Sam M.D., Papagiannis C.V., Connolly K.M., Corselli L., Iwahara J., Lee J., Phillips M., Wojciak J.M., Johnson R.C., Clubb R.T.
    J. Mol. Biol. 324:791-805(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-55.
  7. "Crystal structure of the excisionase-DNA complex from bacteriophage lambda."
    Sam M.D., Cascio D., Johnson R.C., Clubb R.T.
    J. Mol. Biol. 338:229-240(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-55.
  8. "Fis targets assembly of the Xis nucleoprotein filament to promote excisive recombination by phage lambda."
    Papagiannis C.V., Sam M.D., Abbani M.A., Yoo D., Cascio D., Clubb R.T., Johnson R.C.
    J. Mol. Biol. 367:328-343(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-52.
  9. "Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly."
    Abbani M.A., Papagiannis C.V., Sam M.D., Cascio D., Johnson R.C., Clubb R.T.
    Proc. Natl. Acad. Sci. U.S.A. 104:2109-2114(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-55.

Entry informationi

Entry nameiVXIS_LAMBD
AccessioniPrimary (citable) accession number: P03699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.