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Protein

Polymerase acidic protein

Gene

PA

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

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 Publications

Cofactori

Mn2+UniRule annotation2 PublicationsNote: Binds 2 manganese ions per subunit.UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Manganese 1; via tele nitrogenUniRule annotationCombined sources2 Publications1
Metal bindingi80Manganese 2UniRule annotationCombined sources1 Publication1
Metal bindingi108Manganese 1UniRule annotationCombined sources1 Publication1
Metal bindingi108Manganese 2UniRule annotationCombined sources1 Publication1
Metal bindingi119Manganese 1UniRule annotationCombined sources1 Publication1
Metal bindingi120Manganese 1; via carbonyl oxygenUniRule annotationCombined sources2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processCap snatching, 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
LigandManganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.7.48 7479
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:
Polymerase acidic proteinUniRule annotation (EC:3.1.-.-UniRule annotation)
Alternative name(s):
RNA-directed RNA polymerase subunit P2UniRule annotation
Gene namesi
Name:PAUniRule annotation
OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Taxonomic identifieri211044 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000116373 Componenti: Genome
  • UP000170967 Componenti: Genome
  • UP000009255 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1169598

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000787961 – 716Polymerase acidic proteinAdd BLAST716

Post-translational modificationi

Phosphorylated on serines and threonines by host kinases, including human casein kinase II.UniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Interactioni

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 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

DIPiDIP-43996N
IntActiP03433, 57 interactors
MINTiP03433

Chemistry databases

BindingDBiP03433

Structurei

Secondary structure

1716
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 8Combined sources8
Helixi11 – 23Combined sources13
Turni28 – 30Combined sources3
Helixi32 – 50Combined sources19
Turni73 – 75Combined sources3
Beta strandi76 – 78Combined sources3
Helixi84 – 98Combined sources15
Beta strandi108 – 111Combined sources4
Turni112 – 115Combined sources4
Beta strandi116 – 125Combined sources10
Helixi127 – 138Combined sources12
Beta strandi141 – 149Combined sources9
Beta strandi154 – 156Combined sources3
Helixi157 – 159Combined sources3
Helixi165 – 184Combined sources20
Helixi188 – 194Combined sources7
Beta strandi273 – 275Combined sources3
Beta strandi290 – 294Combined sources5
Turni298 – 301Combined sources4
Helixi303 – 311Combined sources9
Beta strandi317 – 324Combined sources8
Beta strandi327 – 329Combined sources3
Helixi331 – 345Combined sources15
Helixi364 – 369Combined sources6
Helixi406 – 414Combined sources9
Beta strandi419 – 421Combined sources3
Helixi437 – 450Combined sources14
Beta strandi451 – 453Combined sources3
Helixi454 – 474Combined sources21
Beta strandi477 – 479Combined sources3
Beta strandi481 – 490Combined sources10
Beta strandi496 – 506Combined sources11
Beta strandi517 – 526Combined sources10
Helixi530 – 532Combined sources3
Turni534 – 539Combined sources6
Beta strandi541 – 548Combined sources8
Beta strandi559 – 571Combined sources13
Helixi572 – 579Combined sources8
Helixi580 – 582Combined sources3
Helixi583 – 602Combined sources20
Helixi608 – 613Combined sources6
Beta strandi619 – 624Combined sources6
Beta strandi627 – 631Combined sources5
Helixi633 – 649Combined sources17
Helixi653 – 674Combined sources22
Helixi686 – 691Combined sources6
Helixi698 – 714Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZNLX-ray2.30A239-716[»]
4YYLX-ray1.91A1-50[»]
A73-197[»]
4ZHZX-ray2.50A1-50[»]
A73-197[»]
4ZI0X-ray1.80A1-50[»]
A73-197[»]
4ZQQX-ray1.80A1-50[»]
A73-197[»]
5FDDX-ray2.51A1-50[»]
A73-197[»]
5FDGX-ray2.10A1-50[»]
A73-197[»]
5I13X-ray2.15A1-50[»]
A73-197[»]
5JHTX-ray1.75A1-50[»]
A73-197[»]
5JHVX-ray2.75A/B1-50[»]
A/B73-197[»]
ProteinModelPortaliP03433
SMRiP03433
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03433

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi124 – 139Nuclear localization signal 1 (NLS1)UniRule annotation1 PublicationAdd BLAST16
Motifi184 – 247Nuclear localization signal 2 (NLS2)UniRule annotation1 PublicationAdd BLAST64

Sequence similaritiesi

Belongs to the influenza viruses PA family.UniRule annotation

Phylogenomic databases

KOiK19390
OrthoDBiVOG0900002P

Family and domain databases

Gene3Di3.40.91.90, 1 hit
HAMAPiMF_04063 INFV_PA, 1 hit
InterProiView protein in InterPro
IPR037534 INFV_PA
IPR001009 PA/PA-X
IPR038372 PA/PA-X_sf
PfamiView protein in Pfam
PF00603 Flu_PA, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Isoform PA (identifier: P03433-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:716
Mass (Da):82,588
Last modified:October 2, 2007 - v2
Checksum:i8829F53525814394
GO
Isoform PA-X (identifier: P0CK64-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0CK64.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:252
Mass (Da):29,423
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti550I → 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
RefSeqiNP_040986.1, NC_002022.1

Genome annotation databases

GeneIDi956535
KEGGivg:956535

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPA_I34A1
AccessioniPrimary (citable) accession number: P03433
Secondary accession number(s): A4GXH3, Q20N31, Q8JUU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 2, 2007
Last modified: April 25, 2018
This is version 115 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health