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BPT7:ENDO

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Species (Taxon ID) Enterobacteria phage T7 (Bacteriophage T7). (10760)
Gene Name(s) No Information Provided.
Protein Name(s) Endonuclease I

Gene product 3 Gp3 Junction-resolving enzyme gp3

External Links
UniProt P00641
EMBL V01127
V01146
PIR B94615
RefSeq NP_041972.1
PDB 1FZR
1M0D
1M0I
2PFJ
3CAE
PDBsum 1FZR
1M0D
1M0I
2PFJ
3CAE
ProteinModelPortal P00641
SMR P00641
DIP DIP-41668N
IntAct P00641
MINT MINT-1513471
GeneID 1261079
KEGG vg:1261079
EvolutionaryTrace P00641
Proteomes UP000000840
GO GO:0008833
GO:0003677
GO:0015074
GO:0039657
Gene3D 3.40.91.30
InterPro IPR008029
IPR011335
IPR011578
Pfam PF05367
SUPFAM SSF52980

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:1990238

double-stranded DNA endodeoxyribonuclease activity

PMID:5263754[1]

ECO:0000315

F

Figure 1 shows significant degradation of both double and single stranded DNA upon infection with T7. The researchers, therefore, mutated a number of genes, and found out that only the mutants in genes 1 or 3 did not induce an increased endonuclease activity. It is, furthermore, stated that the product of gene 1 (RNA polymerase factor) is needed for the transcription of most of the T7 genome. Mutants in gene 3 were still synthesizing all essential T7 proteins, only lacking the increased endonuclease activity.

complete
CACAO 11613

GO:1990238

double-stranded DNA endodeoxyribonuclease activity

PMID:5541763[2]

ECO:0000315

F

Figure 1 shows endonuclease activity after T7 infection of E. coli B. The endonuclease activity was not seen after infection with a mutant in gene 3 (Table 1).

complete
CACAO 11615

GO:1990238

double-stranded DNA endodeoxyribonuclease activity

PMID:5541763[2]

ECO:0000314

F

The enzyme was purified and tested against various sources DNA. Breaks in the DNA strands were found (3-4 breaks per single strand before double strand breakage (see Figure 3).

complete
CACAO 11617

GO:0008821

crossover junction endodeoxyribonuclease activity

PMID:9236119[3]

ECO:0000314

F

After binding to the DNA junction as a dimer, the two subunits of the T7 endonuclease 1 catalyze cleavages independently but rather simultaneously before either is released from the junction (within the lifetime of the protein-junction complex) (Figure 6 and text around it, and Discussion). Similar characteristics have been found in T4 endonuclease VII.

complete
CACAO 11618

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004519

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011578

F

Seeded From UniProt

complete

enables

GO:0004536

deoxyribonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011578

F

Seeded From UniProt

complete

enables

GO:0008833

deoxyribonuclease IV (phage-T4-induced) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008029

F

Seeded From UniProt

complete

involved_in

GO:0015074

DNA integration

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008029

P

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008029

P

Seeded From UniProt

complete

enables

GO:0008833

deoxyribonuclease IV (phage-T4-induced) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.21.2

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

involved_in

GO:0039657

suppression by virus of host gene expression

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1190

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

involved_in

GO:0099015

degradation of host chromosome by virus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1247

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Center, MS et al. (1970) The structural gene for a T7 endonuclease essential for phage DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 65 242-8 PubMed GONUTS page
  2. 2.0 2.1 Sadowski, PD (1971) Bacteriophage T7 endonuclease. I. Properties of the enzyme purified from T7 phage-infected Escherichia coli B. J. Biol. Chem. 246 209-16 PubMed GONUTS page
  3. Parkinson, MJ & Lilley, DM (1997) The junction-resolving enzyme T7 endonuclease I: quaternary structure and interaction with DNA. J. Mol. Biol. 270 169-78 PubMed GONUTS page