ID PA_I77AA Reviewed; 716 AA. AC A4GBY4; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 02-OCT-2024, entry version 54. DE RecName: Full=Polymerase acidic protein {ECO:0000255|HAMAP-Rule:MF_04063}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04063}; DE AltName: Full=RNA-directed RNA polymerase subunit P2 {ECO:0000255|HAMAP-Rule:MF_04063}; GN Name=PA {ECO:0000255|HAMAP-Rule:MF_04063}; OS Influenza A virus (strain A/Brazil/11/1978 H1N1). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=393560; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y., RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.; RT "The NIAID influenza genome sequencing project."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RG The NIAID Influenza Genome Sequencing Consortium; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays an essential role in viral RNA transcription and CC replication by forming the heterotrimeric polymerase complex together CC with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using CC a unique mechanism called cap-snatching. It consists in the hijacking CC and cleavage of host capped pre-mRNAs. These short capped RNAs are then CC used as primers for viral mRNAs. The PB2 subunit is responsible for the CC binding of the 5' cap of cellular pre-mRNAs which are subsequently CC cleaved after 10-13 nucleotides by the PA subunit that carries the CC endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_04063}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_04063}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_04063}; CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1, CC PB2 and PA. Interacts (via C-terminus) with PB1 (via N-terminus). CC {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}. CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are CC transported in the host nucleus as a complex. CC {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Ribosomal frameshifting; Named isoforms=2; CC Name=PA; CC IsoId=A4GBY4-1; Sequence=Displayed; CC Name=PA-X; CC IsoId=P0CK67-1; Sequence=External; CC -!- PTM: Phosphorylated on serines and threonines by host kinases, CC including human casein kinase II. {ECO:0000250|UniProtKB:P03433, CC ECO:0000255|HAMAP-Rule:MF_04063}. CC -!- SIMILARITY: Belongs to the influenza viruses PA family. CC {ECO:0000255|HAMAP-Rule:MF_04063}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CY020298; ABO38072.1; -; Viral_cRNA. DR SMR; A4GBY4; -. DR MEROPS; S62.001; -. DR Proteomes; UP000008025; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR GO; GO:0039523; P:symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR Gene3D; 3.40.91.90; Influenza RNA-dependent RNA polymerase subunit PA, endonuclease domain; 1. DR HAMAP; MF_04063; INFV_PA; 1. DR InterPro; IPR037534; INFV_PA. DR InterPro; IPR001009; PA/PA-X. DR InterPro; IPR038372; PA/PA-X_sf. DR Pfam; PF00603; Flu_PA; 1. PE 3: Inferred from homology; KW Cap snatching; Endonuclease; KW Eukaryotic host gene expression shutoff by virus; KW Eukaryotic host transcription shutoff by virus; Host cytoplasm; KW Host gene expression shutoff by virus; Host nucleus; KW Host-virus interaction; Hydrolase; KW Inhibition of host RNA polymerase II by virus; Manganese; Metal-binding; KW Nuclease; Phosphoprotein; Ribosomal frameshifting. FT CHAIN 1..716 FT /note="Polymerase acidic protein" FT /id="PRO_0000373005" FT MOTIF 124..139 FT /note="Nuclear localization signal 1 (NLS1)" FT /evidence="ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP- FT Rule:MF_04063" FT MOTIF 184..247 FT /note="Nuclear localization signal 2 (NLS2)" FT /evidence="ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP- FT Rule:MF_04063" FT BINDING 41 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" FT BINDING 80 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" FT BINDING 108 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" FT BINDING 108 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" FT BINDING 119 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" FT BINDING 120 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063" SQ SEQUENCE 716 AA; 82761 MW; F7EC6B241DB645E7 CRC64; MEDFVRQCFN PMIVELAEKA MKEYGEDLKI ETNKFAAICT HLEVCFMYSD FHFINEQGES IIVELDDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGA EKPKFLPDLY DYKENRFIEI GVTRREVHIY YLEKANKIKS EKTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ EMASRGLWDS FRQSERGEET IEERFEITGT MRRLADQSLP PNFSCLENFR AYVDGFEPNG YIEGKLSQMS KEVNARIEPF LKTTPRPIRL PDGPPCSQRS KFLLMDALKL SIEDPSHEGE GIPLYDAIKC MRTFFGWKEP YVVKPHEKGI NPNYLLSWKQ VLAELQDIEN EGKIPRTKNM KKTSQLKWAL GENMAPEKVD FDDCKDISDL KQYDSDEPKL RSLSSWIQNE FNKACELTDS IWIELDEIGE DVAPIEHIAS MRRNYFTAEV SHCRATEYIM KGVYINTALL NASCAAMDDF QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY CVLEIGDMLL RSAIGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES SVKEKDMTKE FFENKSETWP IGESPKGVEE GSIGKVCRTL LAKSVFNSLY ASPQLEGFSA ESRKLLLVVQ ALRDNLEPGT FDLGGLYEAI EECLINDPWV LLNASWFNSF LTHALR //