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Protein

Integrase

Gene

int

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome.1 Publication1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei342 – 3421O-(3'-phospho-DNA)-tyrosine intermediateCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

DNA integration, DNA recombination, Viral genome excision, Viral genome integration, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Gene namesi
Name:int
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000001711 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471E → A: Complete loss of interaction with the integrase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356IntegrasePRO_0000197527Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-41000N.
IntActiP03700. 9 interactions.
MINTiMINT-120644.

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi16 – 183Combined sources
Beta strandi24 – 274Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 396Combined sources
Helixi41 – 5717Combined sources
Helixi76 – 9015Combined sources
Helixi94 – 11017Combined sources
Helixi116 – 1183Combined sources
Helixi121 – 13313Combined sources
Helixi137 – 15620Combined sources
Turni164 – 1674Combined sources
Helixi182 – 19110Combined sources
Helixi192 – 1943Combined sources
Helixi198 – 20912Combined sources
Helixi213 – 2186Combined sources
Helixi221 – 2233Combined sources
Beta strandi228 – 2325Combined sources
Turni234 – 2363Combined sources
Beta strandi239 – 2435Combined sources
Turni249 – 2524Combined sources
Helixi255 – 26511Combined sources
Beta strandi269 – 2724Combined sources
Helixi282 – 29615Combined sources
Beta strandi301 – 3033Combined sources
Helixi309 – 32113Combined sources
Helixi324 – 3318Combined sources
Beta strandi334 – 3363Combined sources
Helixi339 – 3424Combined sources
Beta strandi349 – 3524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AE9X-ray1.90A/B177-355[»]
1KJKNMR-A1-64[»]
1M97model-A76-171[»]
1P7DX-ray2.95A/B74-356[»]
1Z19X-ray2.80A/B74-356[»]
1Z1BX-ray3.80A/B1-356[»]
1Z1GX-ray4.40A/B/C/D1-356[»]
2OXOX-ray2.00A75-176[»]
2WCCNMR-31-64[»]
ProteinModelPortaliP03700.
SMRiP03700. Positions 7-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03700.

Family & Domainsi

Sequence similaritiesi

Belongs to the 'phage' integrase family.Curated

Family and domain databases

Gene3Di1.10.150.130. 1 hit.
1.10.443.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR011010. DNA_brk_join_enz.
IPR013762. Integrase-like_cat.
IPR002104. Integrase_catalytic.
IPR015094. Integrase_lambda-typ_DNA-bd_N.
IPR023109. Integrase_recombinase_N.
IPR004107. Integrase_SAM-like_N.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF02899. Phage_int_SAM_1. 1 hit.
PF09003. Phage_integ_N. 1 hit.
PF00589. Phage_integrase. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
SSF56349. SSF56349. 1 hit.

Sequencei

Sequence statusi: Complete.

P03700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRRSHERR DLPPNLYIRN NGYYCYRDPR TGKEFGLGRD RRIAITEAIQ
60 70 80 90 100
ANIELFSGHK HKPLTARINS DNSVTLHSWL DRYEKILASR GIKQKTLINY
110 120 130 140 150
MSKIKAIRRG LPDAPLEDIT TKEIAAMLNG YIDEGKAASA KLIRSTLSDA
160 170 180 190 200
FREAIAEGHI TTNHVAATRA AKSEVRRSRL TADEYLKIYQ AAESSPCWLR
210 220 230 240 250
LAMELAVVTG QRVGDLCEMK WSDIVDGYLY VEQSKTGVKI AIPTALHIDA
260 270 280 290 300
LGISMKETLD KCKEILGGET IIASTRREPL SSGTVSRYFM RARKASGLSF
310 320 330 340 350
EGDPPTFHEL RSLSARLYEK QISDKFAQHL LGHKSDTMAS QYRDDRGREW

DKIEIK
Length:356
Mass (Da):40,304
Last modified:July 21, 1986 - v1
Checksum:i708D52B96E89209C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181D → V (PubMed:6253947).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96562.1.
PIRiA04322. RSBPIL.
RefSeqiNP_040609.1. NC_001416.1.

Genome annotation databases

GeneIDi2703464.
KEGGivg:2703470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96562.1.
PIRiA04322. RSBPIL.
RefSeqiNP_040609.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AE9X-ray1.90A/B177-355[»]
1KJKNMR-A1-64[»]
1M97model-A76-171[»]
1P7DX-ray2.95A/B74-356[»]
1Z19X-ray2.80A/B74-356[»]
1Z1BX-ray3.80A/B1-356[»]
1Z1GX-ray4.40A/B/C/D1-356[»]
2OXOX-ray2.00A75-176[»]
2WCCNMR-31-64[»]
ProteinModelPortaliP03700.
SMRiP03700. Positions 7-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41000N.
IntActiP03700. 9 interactions.
MINTiMINT-120644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703464.
KEGGivg:2703470.

Miscellaneous databases

EvolutionaryTraceiP03700.

Family and domain databases

Gene3Di1.10.150.130. 1 hit.
1.10.443.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR011010. DNA_brk_join_enz.
IPR013762. Integrase-like_cat.
IPR002104. Integrase_catalytic.
IPR015094. Integrase_lambda-typ_DNA-bd_N.
IPR023109. Integrase_recombinase_N.
IPR004107. Integrase_SAM-like_N.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF02899. Phage_int_SAM_1. 1 hit.
PF09003. Phage_integ_N. 1 hit.
PF00589. Phage_integrase. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
SSF56349. SSF56349. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
  3. "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].
  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 EXCISIONASE, MUTAGENESIS OF GLU-47.
  5. "Lambda integrase: armed for recombination."
    Van Duyne G.D.
    Curr. Biol. 15:R658-R660(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  6. "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: IDENTIFICATION IN THE EXCISION COMPLEX, SUBUNIT.
  7. "Flexibility in DNA recombination: structure of the lambda integrase catalytic core."
    Kwon H.J., Tirumalai R., Landy A., Ellenberger T.
    Science 276:126-131(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 177-356.
  8. "Arm-site binding by lambda-integrase: solution structure and functional characterization of its amino-terminal domain."
    Wojciak J.M., Sarkar D., Landy A., Clubb R.T.
    Proc. Natl. Acad. Sci. U.S.A. 99:3434-3439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-64.
  9. "A conformational switch controls the DNA cleavage activity of lambda integrase."
    Aihara H., Kwon H.J., Nunes-Duby S.E., Landy A., Ellenberger T.
    Mol. Cell 12:187-198(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 74-356 IN COMPLEX WITH PHOSPHOTYROSINE.
  10. "A structural basis for allosteric control of DNA recombination by lambda integrase."
    Biswas T., Aihara H., Radman-Livaja M., Filman D., Landy A., Ellenberger T.
    Nature 435:1059-1066(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 74-356 IN COMPLEX WITH PHOSPHOTYROSINE, ACTIVE SITE.
  11. "Crystallization and structure determination of the core-binding domain of bacteriophage lambda integrase."
    Kamadurai H.B., Jain R., Foster M.P.
    Acta Crystallogr. F 64:470-473(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 75-176.
  12. "NMR structure of the amino-terminal domain of the lambda integrase protein in complex with DNA: immobilization of a flexible tail facilitates beta-sheet recognition of the major groove."
    Fadeev E.A., Sam M.D., Clubb R.T.
    J. Mol. Biol. 388:682-690(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-64.

Entry informationi

Entry nameiVINT_LAMBD
AccessioniPrimary (citable) accession number: P03700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 117 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
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.