Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RNA-directed RNA polymerase catalytic subunit

Gene

PB1

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.1 Publication1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase

Keywords - Biological processi

Eukaryotic 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, Viral transcription

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-168255. Influenza Life Cycle.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168275. Entry of Influenza Virion into Host Cell via Endocytosis.
R-HSA-168288. Fusion of the Influenza Virion to the Host Cell Endosome.
R-HSA-168298. Release.
R-HSA-168302. Budding.
R-HSA-168303. Packaging of Eight RNA Segments.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168330. Viral RNP Complexes in the Host Cell Nucleus.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-168336. Uncoating of the Influenza Virion.
R-HSA-192814. vRNA Synthesis.
R-HSA-192823. Viral mRNA Translation.
R-HSA-192869. cRNA Synthesis.
R-HSA-192905. vRNP Assembly.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PB1
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000009255 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000787631 – 757RNA-directed RNA polymerase catalytic subunitAdd BLAST757

Post-translational modificationi

Phosphorylated by host PRKCA.1 Publication

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus). Interacts (via C-terminus) with PB2 (via N-terminus); this interaction is essential for transcription initiation.2 Publications

Protein-protein interaction databases

DIPiDIP-56974N.
IntActiP03431. 38 interactors.

Structurei

Secondary structure

1757
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 10Combined sources6
Helixi687 – 699Combined sources13
Helixi714 – 731Combined sources18
Helixi737 – 755Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZNLX-ray2.30B1-81[»]
2ZTTX-ray2.10A/C679-757[»]
3A1GX-ray1.70A/C678-757[»]
ProteinModelPortaliP03431.
SMRiP03431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03431.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini286 – 483RdRp catalyticPROSITE-ProRule annotationAdd BLAST198

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni249 – 256Promoter-binding siteBy similarity8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi187 – 195Nuclear localization signalBy similarity9
Motifi203 – 216Nuclear localization signalBy similarityAdd BLAST14

Sequence similaritiesi

Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK19389.

Family and domain databases

InterProiIPR007099. RNA-dir_pol_NSvirus.
IPR001407. RNA_pol_PB1_influenza.
[Graphical view]
PfamiPF00602. Flu_PB1. 1 hit.
[Graphical view]
PIRSFiPIRSF000827. RdRPol_OMV. 1 hit.
PROSITEiPS50525. RDRP_SSRNA_NEG_SEG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS
60 70 80 90 100
EKGRWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP
110 120 130 140 150
GIFENSCIET MEVVQQTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEVF
160 170 180 190 200
RSNGLTANES GRLIDFLKDV MESMKKEEMG ITTHFQRKRR VRDNMTKKMI
210 220 230 240 250
TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG
260 270 280 290 300
FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
310 320 330 340 350
TITGDNTKWN ENQNPRMFLA MITYMTRNQP EWFRNVLSIA PIMFSNKMAR
360 370 380 390 400
LGKGYMFESK SMKLRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIEGT
410 420 430 440 450
ASLSPGMMMG MFNMLSTVLG VSILNLGQKR YTKTTYWWDG LQSSDDFALI
460 470 480 490 500
VNAPNHEGIQ AGVDRFYRTC KLLGINMSKK KSYINRTGTF EFTSFFYRYG
510 520 530 540 550
FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG PATAQMALQL
560 570 580 590 600
FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW EQTRSKAGLL VSDGGPNLYN
610 620 630 640 650
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESM NNAVMMPAHG
660 670 680 690 700
PAKNMEYDAV ATTHSWIPKR NRSILNTSQR GVLEDEQMYQ RCCNLFEKFF
710 720 730 740 750
PSSSYRRPVG ISSMVEAMVS RARIDARIDF ESGRIKKEEF TEIMKICSTI

EELRRQK
Length:757
Mass (Da):86,576
Last modified:October 2, 2007 - v2
Checksum:iFB23E4976E06C18F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53G → A in AAA43581 (PubMed:6281731).Curated1
Sequence conflicti175K → N in ABO21706 (Ref. 4) Curated1
Sequence conflicti175K → N in ABD77683 (PubMed:15163504).Curated1
Sequence conflicti205I → M in ABO21706 (Ref. 4) Curated1
Sequence conflicti205I → M in ABD77683 (PubMed:15163504).Curated1
Sequence conflicti208K → R in AAA43581 (PubMed:6281731).Curated1
Sequence conflicti300F → L in AAA43581 (PubMed:6281731).Curated1
Sequence conflicti394P → S in ABO21706 (Ref. 4) Curated1
Sequence conflicti394P → S in ABD77683 (PubMed:15163504).Curated1
Sequence conflicti473L → H in AAA43581 (PubMed:6281731).Curated1
Sequence conflicti517I → S in AAA43581 (PubMed:6281731).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02151 Genomic RNA. Translation: AAA43581.1.
AF389116 Genomic RNA. Translation: AAM75156.1.
CY009450 Genomic RNA. Translation: ABD77683.1.
EF467819 Genomic RNA. Translation: ABO21706.1.
PIRiA93418. P1IV34.
RefSeqiNP_040985.1. NC_002021.1.

Genome annotation databases

GeneIDi956534.
KEGGivg:956534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02151 Genomic RNA. Translation: AAA43581.1.
AF389116 Genomic RNA. Translation: AAM75156.1.
CY009450 Genomic RNA. Translation: ABD77683.1.
EF467819 Genomic RNA. Translation: ABO21706.1.
PIRiA93418. P1IV34.
RefSeqiNP_040985.1. NC_002021.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZNLX-ray2.30B1-81[»]
2ZTTX-ray2.10A/C679-757[»]
3A1GX-ray1.70A/C678-757[»]
ProteinModelPortaliP03431.
SMRiP03431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-56974N.
IntActiP03431. 38 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956534.
KEGGivg:956534.

Phylogenomic databases

KOiK19389.

Enzyme and pathway databases

ReactomeiR-HSA-168255. Influenza Life Cycle.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168275. Entry of Influenza Virion into Host Cell via Endocytosis.
R-HSA-168288. Fusion of the Influenza Virion to the Host Cell Endosome.
R-HSA-168298. Release.
R-HSA-168302. Budding.
R-HSA-168303. Packaging of Eight RNA Segments.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168330. Viral RNP Complexes in the Host Cell Nucleus.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-168336. Uncoating of the Influenza Virion.
R-HSA-192814. vRNA Synthesis.
R-HSA-192823. Viral mRNA Translation.
R-HSA-192869. cRNA Synthesis.
R-HSA-192905. vRNP Assembly.

Miscellaneous databases

EvolutionaryTraceiP03431.

Family and domain databases

InterProiIPR007099. RNA-dir_pol_NSvirus.
IPR001407. RNA_pol_PB1_influenza.
[Graphical view]
PfamiPF00602. Flu_PB1. 1 hit.
[Graphical view]
PIRSFiPIRSF000827. RdRPol_OMV. 1 hit.
PROSITEiPS50525. RDRP_SSRNA_NEG_SEG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRDRP_I34A1
AccessioniPrimary (citable) accession number: P03431
Secondary accession number(s): A4GXH1, Q20N30, Q8JUU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 2, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.