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CAEEL:RFS1

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Species (Taxon ID) Caenorhabditis elegans. (6239)
Gene Name(s) rfs-1
Protein Name(s) RAD51-like protein 1
External Links
UniProt P34348
EMBL FO080290
PIR S44775
RefSeq NP_001293630.1
ProteinModelPortal P34348
SMR P34348
IntAct P34348
MINT P34348
STRING 6239.C30A5.2
PaxDb P34348
EnsemblMetazoa C30A5.2
GeneID 24104262
KEGG cel:CELE_C30A5.2
CTD 24104262
WormBase C30A5.2
eggNOG ENOG410K7J5
ENOG4110MBP
HOGENOM HOG000020888
InParanoid P34348
OMA IVCKRVE
OrthoDB EOG091G0QIY
PhylomeDB P34348
PRO PR:P34348
Proteomes UP000001940
Bgee WBGene00004342
GO GO:0033061
GO:0033063
GO:0005657
GO:0005524
GO:0051117
GO:0008094
GO:0003690
GO:0000400
GO:0000150
GO:0003697
GO:0000707
GO:0006312
GO:0000712
GO:0010212
GO:0042148
InterPro IPR013632
IPR027417
IPR020588
Pfam PF08423
SUPFAM SSF52540
PROSITE PS50162

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0000730

DNA recombinase assembly

PMID:27867009[1]

ECO:0000316

UniProtKB:Q21621


P

Figure 1 depicts the cessation of the dissociation of RAD-51 from ssDNA due to the presence of protein RFS-1/RIP-1. Figure 1, Part H [(i), (ii)] shows the known mechanism of RAD-51 by demonstrating that it’s presence prohibits the binding of ScRPA-eGFP-ssDNA. The incapability of RAD-51 to be expressed due to the lack of ATP is found in Figure 1, Part H (ii). Figure 1 ultimately illustrates that in the precence of the protein RFS-1/RIP-1 and ATP; RAD-51 along with the protein RFS-1/RIP-1 is present but the ScRPA-eGFP-ssDNA are not [(Figure 1, Part H (iii)]. The same events occur when the protein RFS-1/RIP-1 is present but not ATP [(Figure 1, Part H (iv)].

complete
CACAO 13210

GO:0000730

DNA recombinase assembly

PMID:26186187[2]

ECO:0000316

UniProtKB:Q21621


P

Figure 2 provides the biochemical properties of the RFS-1/RIP-1 complex. The western blot in part A of this figure confirms the precence of the two proteins (RFS-1/RIP-1) after co-purifying the recombinant proteins from budding yeast cells. The Electrophoretic mobility shift assays (EMSA) shown in part B of the figure reveals that the RFS-1/RIP-1 complex binds in a nucleotide independent manner weakly to ssDNA but not dsDNA. Bands are observed only for ssDNA. The RFS-1/RIP-1 complex can also stimulate D loop formations with RAD51 (C) and the fact that ATP is required to do so (D).

complete
CACAO 13251

part_of

GO:0033061

DNA recombinase mediator complex

PMID:26186187[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051117

ATPase binding

PMID:20122407[3]

ECO:0000353

physical interaction evidence used in manual assertion

WB:WBGene00004297

F

Seeded From UniProt

complete

involved_in

GO:0000712

resolution of meiotic recombination intermediates

PMID:20122407[3]

ECO:0000316

genetic interaction evidence used in manual assertion

WB:WBGene00021905

P

Seeded From UniProt

complete

involved_in

GO:0000712

resolution of meiotic recombination intermediates

PMID:20122407[3]

ECO:0000316

genetic interaction evidence used in manual assertion

WB:WBGene00009124

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:IPR020588

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:IPR020588

F

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020588

P

Seeded From UniProt

complete

enables

GO:0008094

DNA-dependent ATPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020588

F

Seeded From UniProt

complete

involved_in

GO:0006310

DNA recombination

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0233

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0051321

meiotic cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0469

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0234

P

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0227

P

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

Notes

References

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

  1. Taylor, MRG et al. (2016) A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling. Mol. Cell 64 926-939 PubMed GONUTS page
  2. 2.0 2.1 Taylor, MRG et al. (2015) Rad51 Paralogs Remodel Pre-synaptic Rad51 Filaments to Stimulate Homologous Recombination. Cell 162 271-286 PubMed GONUTS page
  3. 3.0 3.1 3.2 Ward, JD et al. (2010) Overlapping mechanisms promote postsynaptic RAD-51 filament disassembly during meiotic double-strand break repair. Mol. Cell 37 259-72 PubMed GONUTS page