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BPT5:EXO5
Contents
| Species (Taxon ID) | Escherichia phage T5 (Enterobacteria phage T5). (10726) | |
| Gene Name(s) | D15 (synonyms: exo5 (ECO:0000312 with EMBL:AAX12058.1)) | |
| Protein Name(s) | T5 flap endonuclease
T5FEN 5'-3' exonuclease (ECO:0000305) Exodeoxyribonuclease (ECO:0000303 with PMID:2211703[1]) | |
| External Links | ||
| UniProt | P06229 | |
| EMBL | AY543070 AY587007 AY692264 | |
| PIR | A23610 | |
| RefSeq | YP_006958.1 | |
| PDB | 1EXN 1J5F 1UT5 1UT8 1XO1 | |
| PDBsum | 1EXN 1J5F 1UT5 1UT8 1XO1 | |
| ProteinModelPortal | P06229 | |
| SMR | P06229 | |
| GeneID | 2777611 | |
| KEGG | vg:2777611 | |
| KO | K18950 | |
| EvolutionaryTrace | P06229 | |
| Proteomes | UP000002107 UP000002141 UP000002503 | |
| GO | GO:0003677 GO:0004519 GO:0004527 GO:0046872 GO:0039693 | |
| Gene3D | 3.40.50.1010 | |
| InterPro | IPR020046 IPR020045 IPR002421 IPR008918 IPR029060 | |
| Pfam | PF01367 PF02739 | |
| SMART | SM00475 SM00279 | |
| SUPFAM | SSF47807 SSF88723 | |
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 |
ECO:0000314 |
F |
Figs. 7,9. D15 endonuclease activity was witnessed as it digested native T5 duplex DNA. The different bands produced in the gel electrophoresis proves that D15 (also referred to as flap endonuclease) has nuclease activity which cleaves the T5 genome. |
complete | |||||
| GO:0035312 |
5'-3' exodeoxyribonuclease activity |
ECO:0000315 |
F |
Figure 3 |
complete | |||||
| GO:0019086 |
late viral transcription |
ECO:0000315 |
P |
The D15 gene product is necessary for the proper turn-on of synthesis of late proteins. Figures 1 and 2 demonstrate that the T5 wild type produced late proteins whereas the amber mutants defective in D15 did not. D15 gene product is believed to be a 5'exonuclease. |
complete | |||||
| GO:0019034 |
viral replication complex |
ECO:0000315 |
C |
Fig. 11 shows the comparison of T5amD15 mutants and T5 wild type strains. This figure predicts that D15 plays a role in replication and transcription and may be an enzyme that modifies the T5 DNA. |
complete | |||||
|
enables |
GO:0008409 |
5'-3' exonuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0017108 |
5'-flap endonuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0090305 |
nucleic acid phosphodiester bond hydrolysis |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0008409 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0090305 |
nucleic acid phosphodiester bond hydrolysis |
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 |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004527 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0090305 |
nucleic acid phosphodiester bond hydrolysis |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002421 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0017108 |
5'-flap endonuclease activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0033567 |
DNA replication, Okazaki fragment processing |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003677 |
DNA binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004519 |
endonuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004518 |
nuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004527 |
exonuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0039693 |
viral DNA genome replication |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006260 |
DNA replication |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Sayers, JR & Eckstein, F (1990) Properties of overexpressed phage T5 D15 exonuclease. Similarities with Escherichia coli DNA polymerase I 5'-3' exonuclease. J. Biol. Chem. 265 18311-7 PubMed GONUTS page
- ↑ Moyer, RW & Rothe, CT (1977) Role of the T5 gene D15 nuclease in the generation of nicked bacteriophage T5 DNA. J. Virol. 24 177-93 PubMed GONUTS page
- ↑ 3.0 3.1 Garforth, SJ et al. (1999) Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavage. Proc. Natl. Acad. Sci. U.S.A. 96 38-43 PubMed GONUTS page
- ↑ Chinnadurai, G & McCorquodale, DJ (1973) Requirement of a phage-induced 5'-exonuclease for the expression of late genes of bacteriophage T5. Proc. Natl. Acad. Sci. U.S.A. 70 3502-5 PubMed GONUTS page
- ↑ Ficht, TA & Moyer, RW (1980) Isolation and characterization of a putative bacteriophage T5 transcription.replication enzyme complex from infected Escherichia coli. J. Biol. Chem. 255 7040-8 PubMed GONUTS page
- ↑ Feng, M et al. (2004) Roles of divalent metal ions in flap endonuclease-substrate interactions. Nat. Struct. Mol. Biol. 11 450-6 PubMed GONUTS page
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