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P03431 (RDRP_I34A1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-directed RNA polymerase catalytic subunit

EC=2.7.7.48
Alternative name(s):
Polymerase basic protein 1
Short name=PB1
RNA-directed RNA polymerase subunit P1
Gene names
Name:PB1
OrganismInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1) [Reference proteome]
Taxonomic identifier211044 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-dependent RNA polymerase which is responsible for replication and transcription of virus segments. Binds the promoter sequence of the encapsidated viral RNA. Displays an endonuclease activity involved in cap-stealing. Cleaves cellular pre-mRNA to generate primers for viral transcription.

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Subunit structure

Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.

Subcellular location

Host nucleus Potential.

Sequence similarities

Belongs to the influenza viruses polymerase PB1 family.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processEukaryotic host gene expression shutoff by virus
Eukaryotic host transcription shutoff by virus
Host gene expression shutoff by virus
Host-virus interaction
Inhibition of host RNA polymerase II by virus
Viral RNA replication
   Cellular componentHost nucleus
   LigandNucleotide-binding
   Molecular functionNucleotidyltransferase
RNA-directed RNA polymerase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host plasma membrane

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

receptor-mediated endocytosis of virus by host cell

Traceable author statement. Source: Reactome

suppression by virus of host RNA polymerase II activity

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

uncoating of virus

Traceable author statement. Source: Reactome

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral entry into host cell

Traceable author statement. Source: Reactome

viral genome maturation

Traceable author statement. Source: Reactome

viral genome packaging

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 757757RNA-directed RNA polymerase catalytic subunit
PRO_0000078763

Regions

Domain286 – 483198RdRp catalytic
Region249 – 2568Promoter-binding site By similarity
Motif187 – 1959Nuclear localization signal By similarity
Motif203 – 21614Nuclear localization signal By similarity

Experimental info

Sequence conflict531G → A in AAA43581. Ref.1
Sequence conflict1751K → N in ABO21706. Ref.4
Sequence conflict1751K → N in ABD77683. Ref.3
Sequence conflict2051I → M in ABO21706. Ref.4
Sequence conflict2051I → M in ABD77683. Ref.3
Sequence conflict2081K → R in AAA43581. Ref.1
Sequence conflict3001F → L in AAA43581. Ref.1
Sequence conflict3941P → S in ABO21706. Ref.4
Sequence conflict3941P → S in ABD77683. Ref.3
Sequence conflict4731L → H in AAA43581. Ref.1
Sequence conflict5171I → S in AAA43581. Ref.1

Secondary structure

......... 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03431 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: FB23E4976E06C18F

FASTA75786,576
        10         20         30         40         50         60 
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGRWTTNTE 

        70         80         90        100        110        120 
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCIET MEVVQQTRVD 

       130        140        150        160        170        180 
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMKKEEMG 

       190        200        210        220        230        240 
ITTHFQRKRR VRDNMTKKMI TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA 

       250        260        270        280        290        300 
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF 

       310        320        330        340        350        360 
TITGDNTKWN ENQNPRMFLA MITYMTRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK 

       370        380        390        400        410        420 
SMKLRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIEGT ASLSPGMMMG MFNMLSTVLG 

       430        440        450        460        470        480 
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLLGINMSKK 

       490        500        510        520        530        540 
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG 

       550        560        570        580        590        600 
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW EQTRSKAGLL VSDGGPNLYN 

       610        620        630        640        650        660 
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESM NNAVMMPAHG PAKNMEYDAV 

       670        680        690        700        710        720 
ATTHSWIPKR NRSILNTSQR GVLEDEQMYQ RCCNLFEKFF PSSSYRRPVG ISSMVEAMVS 

       730        740        750 
RARIDARIDF ESGRIKKEEF TEIMKICSTI EELRRQK 

« Hide

References

[1]"Nucleotide sequence of human influenza A/PR/8/34 segment 2."
Winter G., Fields S.
Nucleic Acids Res. 10:2135-2143(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Plasmid-only rescue of influenza A virus vaccine candidates."
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L., Garcia-Sastre A., Palese P.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
[4]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02151 Genomic RNA. Translation: AAA43581.1.
AF389116 Genomic RNA. Translation: AAM75156.1.
CY009450 Genomic RNA. Translation: ABD77683.1.
EF467819 Genomic RNA. Translation: ABO21706.1.
PIRP1IV34. A93418.
RefSeqNP_040985.1. NC_002021.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNLX-ray2.30B1-81[»]
2ZTTX-ray2.10A/C679-757[»]
3A1GX-ray1.70A/C678-757[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-56974N.
IntActP03431. 32 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956534.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

InterProIPR007099. RNA-dir_pol_NSvirus.
IPR001407. RNA_pol_PB1_influenza.
[Graphical view]
PfamPF00602. Flu_PB1. 1 hit.
[Graphical view]
PIRSFPIRSF000827. RdRPol_OMV. 1 hit.
PROSITEPS50525. RDRP_SSRNA_NEG_SEG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03431.

Entry information

Entry nameRDRP_I34A1
AccessionPrimary (citable) accession number: P03431
Secondary accession number(s): A4GXH1, Q20N30, Q8JUU7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 2, 2007
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references