UniProtKB - P03433 (PA_I34A1)
Polymerase acidic protein
PA
Functioni
Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.
UniRule annotation3 PublicationsCofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 41 | Manganese 1; via tele nitrogenUniRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 80 | Manganese 2UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 108 | Manganese 1UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 108 | Manganese 2UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 119 | Manganese 1UniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 120 | Manganese 1; via carbonyl oxygenUniRule annotationCombined sources2 Publications | 1 |
GO - Molecular functioni
- endonuclease activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- RNA binding Source: UniProtKB-UniRule
GO - Biological processi
- cap snatching Source: UniProtKB-UniRule
- suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity Source: UniProtKB-UniRule
- transcription, DNA-templated Source: UniProtKB-UniRule
- viral RNA genome replication Source: InterPro
Keywordsi
Enzyme and pathway databases
BRENDAi | 2.7.7.48, 7479 |
Reactomei | R-HSA-168255, Influenza Infection 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 |
Protein family/group databases
MEROPSi | S62.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Polymerase acidic proteinUniRule annotation (EC:3.1.-.-UniRule annotation)Alternative name(s): RNA-directed RNA polymerase subunit P2UniRule annotation |
Gene namesi | Name:PAUniRule annotation |
Organismi | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
Taxonomic identifieri | 211044 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Polyploviricotina › Insthoviricetes › Articulavirales › Orthomyxoviridae › Alphainfluenzavirus › |
Virus hosti | Aves [TaxID: 8782] Homo sapiens (Human) [TaxID: 9606] Sus scrofa (Pig) [TaxID: 9823] |
Proteomesi |
|
Subcellular locationi
- Host cytoplasm UniRule annotation
- Host nucleus UniRule annotation Note: PB1 and PA are transported in the host nucleus as a complex.UniRule annotation3 Publications
Keywords - Cellular componenti
Host cytoplasm, Host nucleusPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL1169598 |
DrugBanki | DB13997, Baloxavir marboxil |
DrugCentrali | P03433 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000078796 | 1 – 716 | Polymerase acidic proteinAdd BLAST | 716 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinInteractioni
Subunit structurei
Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.
Interacts (via C-terminus) with PB1 (via N-terminus).
UniRule annotation1 PublicationBinary interactionsi
P03433
With | #Exp. | IntAct |
---|---|---|
M [P03485] | 2 | EBI-2547616,EBI-2547543 |
NP [P03466] | 3 | EBI-2547616,EBI-2547640 |
PB1 [P03431] | 6 | EBI-2547616,EBI-2547514 |
Protein-protein interaction databases
DIPi | DIP-43996N |
IntActi | P03433, 57 interactors |
MINTi | P03433 |
Chemistry databases
BindingDBi | P03433 |
Structurei
Secondary structure
3D structure databases
SMRi | P03433 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03433 |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 124 – 139 | Nuclear localization signal 1 (NLS1)UniRule annotation1 PublicationAdd BLAST | 16 | |
Motifi | 184 – 247 | Nuclear localization signal 2 (NLS2)UniRule annotation1 PublicationAdd BLAST | 64 |
Sequence similaritiesi
Family and domain databases
Gene3Di | 3.40.91.90, 1 hit |
HAMAPi | MF_04063, INFV_PA, 1 hit |
InterProi | View protein in InterPro IPR037534, INFV_PA IPR001009, PA/PA-X IPR038372, PA/PA-X_sf |
Pfami | View protein in Pfam PF00603, Flu_PA, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MEDFVRQCFN PMIVELAEKT MKEYGEDLKI ETNKFAAICT HLEVCFMYSD
60 70 80 90 100
FHFINEQGES IIVELGDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGA
110 120 130 140 150
EKPKFLPDLY DYKENRFIEI GVTRREVHIY YLEKANKIKS EKTHIHIFSF
160 170 180 190 200
TGEEMATKAD YTLDEESRAR IKTRLFTIRQ EMASRGLWDS FRQSERGEET
210 220 230 240 250
IEERFEITGT MRKLADQSLP PNFSSLENFR AYVDGFEPNG YIEGKLSQMS
260 270 280 290 300
KEVNARIEPF LKTTPRPLRL PNGPPCSQRS KFLLMDALKL SIEDPSHEGE
310 320 330 340 350
GIPLYDAIKC MRTFFGWKEP NVVKPHEKGI NPNYLLSWKQ VLAELQDIEN
360 370 380 390 400
EEKIPKTKNM KKTSQLKWAL GENMAPEKVD FDDCKDVGDL KQYDSDEPEL
410 420 430 440 450
RSLASWIQNE FNKACELTDS SWIELDEIGE DVAPIEHIAS MRRNYFTSEV
460 470 480 490 500
SHCRATEYIM KGVYINTALL NASCAAMDDF QLIPMISKCR TKEGRRKTNL
510 520 530 540 550
YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY CVLEIGDMLI
560 570 580 590 600
RSAIGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES
610 620 630 640 650
SVKEKDMTKE FFENKSETWP IGESPKGVEE SSIGKVCRTL LAKSVFNSLY
660 670 680 690 700
ASPQLEGFSA ESRKLLLIVQ ALRDNLEPGT FDLGGLYEAI EECLINDPWV
710
LLNASWFNSF LTHALS
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 550 | I → L in CAA24295 (PubMed:7060132). | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01106 Genomic RNA Translation: CAA24295.1 AF389117 Genomic RNA Translation: AAM75157.1 EF467820 Genomic RNA Translation: ABO21708.1 CY009449 Genomic RNA Translation: ABD77682.1 |
RefSeqi | NP_040986.1, NC_002022.1 |
Genome annotation databases
GeneIDi | 956535 |
KEGGi | vg:956535 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01106 Genomic RNA Translation: CAA24295.1 AF389117 Genomic RNA Translation: AAM75157.1 EF467820 Genomic RNA Translation: ABO21708.1 CY009449 Genomic RNA Translation: ABD77682.1 |
RefSeqi | NP_040986.1, NC_002022.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ZNL | X-ray | 2.30 | A | 239-716 | [»] | |
4YYL | X-ray | 1.91 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
4ZHZ | X-ray | 2.50 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
4ZI0 | X-ray | 1.80 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
4ZQQ | X-ray | 1.80 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
5FDD | X-ray | 2.51 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
5FDG | X-ray | 2.10 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
5I13 | X-ray | 2.15 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
5JHT | X-ray | 1.75 | A | 1-50 | [»] | |
A | 73-197 | [»] | ||||
5JHV | X-ray | 2.75 | A/B | 1-50 | [»] | |
A/B | 73-197 | [»] | ||||
SMRi | P03433 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-43996N |
IntActi | P03433, 57 interactors |
MINTi | P03433 |
Chemistry databases
BindingDBi | P03433 |
ChEMBLi | CHEMBL1169598 |
DrugBanki | DB13997, Baloxavir marboxil |
DrugCentrali | P03433 |
Protein family/group databases
MEROPSi | S62.001 |
Genome annotation databases
GeneIDi | 956535 |
KEGGi | vg:956535 |
Enzyme and pathway databases
BRENDAi | 2.7.7.48, 7479 |
Reactomei | R-HSA-168255, Influenza Infection 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
EvolutionaryTracei | P03433 |
Family and domain databases
Gene3Di | 3.40.91.90, 1 hit |
HAMAPi | MF_04063, INFV_PA, 1 hit |
InterProi | View protein in InterPro IPR037534, INFV_PA IPR001009, PA/PA-X IPR038372, PA/PA-X_sf |
Pfami | View protein in Pfam PF00603, Flu_PA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PA_I34A1 | |
Accessioni | P03433Primary (citable) accession number: P03433 Secondary accession number(s): A4GXH3, Q20N31, Q8JUU6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | October 2, 2007 | |
Last modified: | February 23, 2022 | |
This is version 131 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families