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BPT5:HEL10
Contents
Species (Taxon ID) | Escherichia phage T5 (Enterobacteria phage T5). (10726) | |
Gene Name(s) | D10 | |
Protein Name(s) | Probable helicase D10 (ECO:0000312 with EMBL:AAX12052.1)
Protein D10 | |
External Links | ||
UniProt | P11107 | |
EMBL | AY543070 AY692264 AY587007 | |
PIR | S01931 | |
RefSeq | YP_006952.1 | |
ProteinModelPortal | P11107 | |
GeneID | 2777605 | |
KEGG | vg:2777605 | |
Proteomes | UP000002107 UP000002141 UP000002503 | |
GO | GO:0005524 GO:0003677 GO:0004386 | |
Gene3D | 3.40.50.300 | |
InterPro | IPR006935 IPR014001 IPR001650 IPR027417 | |
Pfam | PF00271 PF04851 | |
SMART | SM00487 SM00490 | |
SUPFAM | SSF52540 | |
PROSITE | PS51192 PS51194 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004386 |
helicase activity |
ECO:0000247 |
|
F |
Shown in Figure 1, alignment of the T5 gene that codes for helicase with conserved segments of the helicase superfamily showed a sufficient alignment score and definitive evidence that this T5 protein is a helicase |
complete | ||||
GO:0008094 |
DNA-dependent ATPase activity |
ECO:0000315 |
F |
Figure 1b shows the mass of the eluted molecules to be consistent with those in DNA-dependent ATPase activity. Figure 1c shows enzymatic activity was only stimulated in the presence of duplex DNA. Figure 1d shows after cloning of D10 protein, D10-R389N (motif VI) was expressed and purified. When compared to wild type, a point mutation of the motif stopped all DNA-dependent ATPase activity. |
complete | |||||
GO:1990163 |
ATP-dependent four-way junction helicase activity |
ECO:0000314 |
F |
The authors use a ATPase assay to determine if the helicase D10 can unwind complex branched DNA substrates. Figure 2b shows the ATP dependent unwinding of cruciform (four-way junction) DNA molecules by the T5 helicase gene D10. |
complete | |||||
GO:0032508 |
DNA duplex unwinding |
ECO:0000314 |
P |
Figure 3 shows how d10 protein functions to unwind DNA. It uses partially homologous Holliday junction substrates and results in two products, including fork DNA and recombined duplex DNA. These gels prove that d10 can act as a DNA helicase. |
complete | |||||
enables |
GO:0003677 |
DNA binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004386 |
helicase activity |
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:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Blinov, VM et al. (1989) Two early genes of bacteriophage T5 encode proteins containing an NTP-binding sequence motif and probably involved in DNA replication, recombination and repair. FEBS Lett. 252 47-52 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Wong, IN et al. (2016) Bacteriophage T5 gene D10 encodes a branch-migration protein. Sci Rep 6 39414 PubMed GONUTS page