RNA-directed RNA polymerase catalytic subunit - Influenza A virus (strain A/Wilson-Smith/1933 H1N1)

Preferred order of sections

Names and origin

Protein names

Recommended 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

Organism

Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) [Complete proteome]

Taxonomic identifier

381518 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A ›

Virus host

Aves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the influenza viruses polymerase PB1 family. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	Host gene expression shutoff by virus Host transcription shutoff by virus Host-virus interaction Inhibition of host RNA polymerase II by virus Viral RNA replication
Ligand	Nucleotide-binding
Molecular function	Nucleotidyltransferase RNA-directed RNA polymerase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	suppression by virus of host RNA polymerase II activity Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 757

757

RNA-directed RNA polymerase catalytic subunit

PRO_0000078767

Regions

Domain

286 – 483

198

RdRp catalytic

Region

249 – 256

8

Promoter-binding site Probable

Motif

187 – 195

9

Nuclear localization signal Ref.2

Motif

203 – 216

14

Nuclear localization signal Ref.2

Experimental info

Mutagenesis

233

1

R → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

235

1

K → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

238

1

R → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

239

1

R → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

249

1

R → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

251

1

F → A: 20% loss of RNA synthesis in vitro. Ref.3

Mutagenesis

254

1

F → A: 50% loss of RNA synthesis in vitro. Ref.3

Mutagenesis

269

1

S → A: 70% loss of RNA synthesis in vitro. Ref.3

Mutagenesis

273

1

V → A: 80% loss of RNA synthesis in vitro. Ref.3

Mutagenesis

278

1

K → A: Complete loss of RNA synthesis in vitro. Ref.3

Mutagenesis

281

1

K → A: Complete loss of RNA synthesis in vitro. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P03430 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D5A0E8133CDE37F4
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FASTA

757

86,534

        10         20         30         40         50         60 
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS ERGRWTTNTE 

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

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

       190        200        210        220        230        240 
ITTHFQRKRR VRDNMTKKMV TQRTIGKRKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA 

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

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

       370        380        390        400        410        420 
SMKIRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG 

       430        440        450        460        470        480 
VSILNLGQKR HTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVNRFYRTC KLLGINMSKK 

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

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

       610        620        630        640        650        660 
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVNHKDIESV NNAVIMPAHG PAKNMEYDAV 

       670        680        690        700        710        720 
ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS 

       730        740        750 
RARIDARIDF ESGRIKKEEF TEIMKICSTI EELRRQK

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References

[1]	"Sequence analysis of the polymerase 1 gene and the secondary structure prediction of polymerase 1 protein of human influenza virus A/WSN/33." Sivasubramanian N., Nayak D.P. J. Virol. 44:321-329(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Function of two discrete regions is required for nuclear localization of polymerase basic protein 1 of A/WSN/33 influenza virus (H1 N1)." Nath S.T., Nayak D.P. Mol. Cell. Biol. 10:4139-4145(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEAR LOCALIZATION SIGNAL.
[3]	"A new promoter-binding site in the PB1 subunit of the influenza A virus polymerase." Jung T.E., Brownlee G.G. J. Gen. Virol. 87:679-688(2006) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-233; LYS-235; ARG-238; ARG-239; ARG-249; PHE-251; PHE-254; SER-269; VAL-273; LYS-278 AND LYS-281.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02178 Genomic RNA. Translation: AAA43582.1. Sequence problems.
PIR	P1IV33. A04046.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR007099. RNA-dir_pol_NSvirus. IPR001407. RNA_pol_PB1_influenza. [Graphical view]
Pfam	PF00602. Flu_PB1. 1 hit. [Graphical view]
PIRSF	PIRSF000827. RdRPol_OMV. 1 hit.
PROSITE	PS50525. RDRP_SSRNA_NEG_SEG. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RDRP_I33A0

Accession

Primary (citable) accession number: P03430

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents