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BPT5:HEL10

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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

PMID:2547651[1]

ECO:0000247

PMID:2547651[1]


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
CACAO 11947

GO:0008094

DNA-dependent ATPase activity

PMID:28009009[2]

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
CACAO 12443

GO:1990163

ATP-dependent four-way junction helicase activity

PMID:28009009[2]

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
CACAO 12594

GO:0032508

DNA duplex unwinding

PMID:28009009[2]

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
CACAO 12644

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006935

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006935

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006935

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0347

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: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:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

Notes

References

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

  1. 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. 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