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BPPH6:RDRP

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Species (Taxon ID) Pseudomonas phage phi6 (Bacteriophage phi-6). (10879)
Gene Name(s) P2
Protein Name(s) RNA-directed RNA polymerase

Protein P2

External Links
UniProt P11124
EMBL M17461
PIR B29885
RefSeq NP_620346.1
PDB 1HHS
1HHT
1HI0
1HI1
1HI8
1UVI
1UVJ
1UVK
1UVL
1UVM
1UVN
1WAC
2JL9
2JLF
2JLG
4A8F
4A8K
4A8M
4A8O
4A8Q
4A8S
4A8W
4A8Y
4B02
PDBsum 1HHS
1HHT
1HI0
1HI1
1HI8
1UVI
1UVJ
1UVK
1UVL
1UVM
1UVN
1WAC
2JL9
2JLF
2JLG
4A8F
4A8K
4A8M
4A8O
4A8Q
4A8S
4A8W
4A8Y
4B02
ProteinModelPortal P11124
SMR P11124
GeneID 956436
EvolutionaryTrace P11124
Proteomes UP000002610
GO GO:0019012
GO:0046872
GO:0000166
GO:0003723
GO:0050265
GO:0003968
GO:0006351
GO:0001172
GO:0019079
InterPro IPR016406
IPR001205
IPR007096
Pfam PF00680
PIRSF PIRSF004131
PROSITE PS50522

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003968

RNA-directed RNA polymerase activity

PMID:18940872[1]

ECO:0000315

F

Figure 3B shows that the wild type protein synthesizes RNA from ssRNA template at a faster rate than a mutant RdRp.

complete
CACAO 5975

GO:0003968

RNA-directed RNA polymerase activity

PMID:17237359[2]

ECO:0000314

F

Figure 2A shows dsRNA generated by ϕ6 RdRP from ssRNA.

complete
CACAO 5976

GO:0003968

RNA-directed RNA polymerase activity

PMID:11602748[3]

ECO:0000314

F

Figure 3B shows purified phi6 RdRp reacts with ssRNA to make dsRNA.

complete
CACAO 5977

GO:0003968

RNA-directed RNA polymerase activity

PMID:10619851[4]

ECO:0000314

F

Figure 2 "Recombinant P2 catalyzes RNA-dependent RNA synthesis in vitro."

complete
CACAO 5980

GO:0003968

RNA-directed RNA polymerase activity

PMID:18614640[5]

ECO:0000315

F

Figure 1A lanes 1 and 2 show that purified wild type P2 catalyzes the polymerization of ssRNA into dsRNA, whereas a mutant P2 does not.

complete
CACAO 5981

GO:0050265

RNA uridylyltransferase activity

PMID:18614640[5]

ECO:0000314

F

Figure 2 shows that purified P2, when in the presence of ssRNA and excess UTP "the P2 polymerase typically added one or two extra nucleotides to a given acceptor ssRNA oligonucleotide"

complete
CACAO 5982

GO:0003968

RNA-directed RNA polymerase activity

PMID:11877396[6]

ECO:0000314

F

Figure 2B shows that wild type phi6 RdRp was able to utilize the ssRNA substrate and form dsRNA product.

complete
CACAO 5986

GO:0039696

RNA-templated viral transcription

PMID:11080173[7]

ECO:0000314

P

Figure 2b shows dsRNA formation proportional to P2 polymerase concentration(lanes 3-6). Also, no dsRNA was found when P2 polymerase was substituted with bovine serum albumin (lane 2).

complete
CACAO 12926

enables

GO:0050265

RNA uridylyltransferase activity

PMID:18614640[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

PMID:18940872[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

PMID:18614640[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

PMID:17237359[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

PMID:11602748[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

PMID:10619851[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000364

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000364

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000364

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000364

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000364

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

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

GO:0003968

P

Seeded From UniProt

complete

involved_in

GO:0001172

transcription, RNA-templated

GO_REF:0000108

ECO:0000366

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

GO:0003968

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001205

F

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001205
InterPro:IPR007096

F

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001205

P

Seeded From UniProt

complete

involved_in

GO:0019079

viral genome replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007096

P

Seeded From UniProt

complete

involved_in

GO:0039694

viral RNA genome replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016406

P

Seeded From UniProt

complete

enables

GO:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.48

F

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0548

F

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0946
UniProtKB-SubCell:SL-0274

C

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:0003968

RNA-directed 5'-3' RNA polymerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0696

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Poranen, MM et al. (2008) Structural explanation for the role of Mn2+ in the activity of phi6 RNA-dependent RNA polymerase. Nucleic Acids Res. 36 6633-44 PubMed GONUTS page
  2. 2.0 2.1 Aalto, AP et al. (2007) Large-scale production of dsRNA and siRNA pools for RNA interference utilizing bacteriophage phi6 RNA-dependent RNA polymerase. RNA 13 422-9 PubMed GONUTS page
  3. 3.0 3.1 Yang, H et al. (2001) Comparison of polymerase subunits from double-stranded RNA bacteriophages. J. Virol. 75 11088-95 PubMed GONUTS page
  4. 4.0 4.1 Makeyev, EV & Bamford, DH (2000) Replicase activity of purified recombinant protein P2 of double-stranded RNA bacteriophage phi6. EMBO J. 19 124-33 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 Poranen, MM et al. (2008) Nontemplated terminal nucleotidyltransferase activity of double-stranded RNA bacteriophage phi6 RNA-dependent RNA polymerase. J. Virol. 82 9254-64 PubMed GONUTS page
  6. Laurila, MR et al. (2002) Bacteriophage phi 6 RNA-dependent RNA polymerase: molecular details of initiating nucleic acid synthesis without primer. J. Biol. Chem. 277 17117-24 PubMed GONUTS page
  7. Makeyev, EV & Bamford, DH (2000) The polymerase subunit of a dsRNA virus plays a central role in the regulation of viral RNA metabolism. EMBO J. 19 6275-84 PubMed GONUTS page