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P03012 (TNR1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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:
Transposon gamma-delta resolvase
Alternative name(s):
Transposon Tn1000 resolvase
Gene names
Name:tnpR
Ordered Locus Names:ECOK12F009
Encoded onPlasmid F Ref.4
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition.

Sequence similarities

Belongs to the site-specific recombinase resolvase family.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
   LigandDNA-binding
   Technical term3D-structure
Plasmid
Transposable element
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

recombinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183Transposon gamma-delta resolvase
PRO_0000196367

Regions

DNA binding161 – 18020H-T-H motif Potential

Sites

Active site101O-(5'-phospho-DNA)-serine intermediate Ref.5

Secondary structure

................................ 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03012 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B2EBA6037F926FAB

FASTA18320,362
        10         20         30         40         50         60 
MRLFGYARVS TSQQSLDIQV RALKDAGVKA NRIFTDKASG SSSDRKGLDL LRMKVEEGDV 

        70         80         90        100        110        120 
ILVKKLDRLG RDTADMIQLI KEFDAQGVSI RFIDDGISTD GEMGKMVVTI LSAVAQAERQ 

       130        140        150        160        170        180 
RILERTNEGR QEAMAKGVVF GRKRKIDRDA VLNMWQQGLG ASHISKTMNI ARSTVYKVIN 


ESN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of gamma delta resolvase gene and demonstration that its gene product acts as a repressor of transcription."
Reed R.R., Shibuya G.I., Steitz J.A.
Nature 300:381-383(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of the region that determines the specificity of binding of the transposases encoded by Tn3 and gamma delta to the terminal inverted repeat sequences."
Maekawa T., Ohtsubo E.
Jpn. J. Genet. 69:269-285(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence of a transposon identified as Tn1000 (gamma delta)."
Broom J.E., Hill D.F., Hughes G., Jones W.A., McNaughton J.C., Stockwell P.A., Petersen G.B.
DNA Seq. 5:185-189(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete nucleotide sequence of the F plasmid: its implications for organization and diversification of plasmid genomes."
Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / CR63.
[5]"Resolvase-mediated recombination intermediates contain a serine residue covalently linked to DNA."
Reed R.R., Moser C.D.
Cold Spring Harb. Symp. Quant. Biol. 49:245-249(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE SER-10.
[6]"Mutants of the gamma delta resolvase: a genetic analysis of the recombination function."
Newman B.J., Grindley N.D.F.
Cell 38:463-469(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta resolvase at 2.7-A resolution."
Sanderson M.R., Freemont P.S., Rice P.A., Goldman A., Hatfull G.F., Grindley N.D.F., Steitz T.A.
Cell 63:1323-1329(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-140.
[8]"Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site."
Yang W., Steitz T.A.
Cell 82:193-207(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]"Determination of the structure of the DNA binding domain of gamma delta resolvase in solution."
Liu T., Derose E.F., Mullen G.P.
Protein Sci. 3:1286-1295(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 141-183.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01844 Genomic DNA. No translation available.
X60200 Genomic DNA. Translation: CAA42759.1.
D16449 Genomic DNA. Translation: BAA03915.1.
AP001918 Genomic DNA. Translation: BAA97879.1.
PIRRPECTG. A03542.
RefSeqNP_061388.1. NC_002483.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GDRX-ray3.50A1-140[»]
1GDTX-ray3.00A/B1-183[»]
1GHTNMR-A1-105[»]
1HX7NMR-A1-105[»]
1RESNMR-A141-183[»]
1RETNMR-A141-183[»]
1ZR2X-ray3.90A/B3-183[»]
1ZR4X-ray3.40A/B/D/E3-183[»]
2GM4X-ray3.50A/B3-183[»]
2GM5X-ray2.10A/B/C/D3-134[»]
2RSLX-ray2.30A/B/C1-140[»]
ProteinModelPortalP03012.
SMRP03012. Positions 1-183.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP03012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1263577.

Phylogenomic databases

HOGENOMHOG000275578.
OMAERPQLMA.
PhylomeDBP03012.
ProtClustDBCLSK861849.

Gene expression databases

GenevestigatorP03012.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.40.50.1390. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR006118. Recombinase_CS.
IPR006119. Resolv_N.
IPR006120. Resolvase_HTH_dom.
[Graphical view]
PfamPF02796. HTH_7. 1 hit.
PF00239. Resolvase. 1 hit.
[Graphical view]
SMARTSM00857. Resolvase. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF53041. SSF53041. 1 hit.
PROSITEPS00397. RECOMBINASES_1. 1 hit.
PS00398. RECOMBINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03012.
PROP03012.

Entry information

Entry nameTNR1_ECOLI
AccessionPrimary (citable) accession number: P03012
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references