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 15-MAR-2017, entry version 32. DE RecName: Full=Polymerase acidic protein; DE AltName: Full=RNA-directed RNA polymerase subunit P2; GN Name=PA; OS Influenza A virus (strain A/Brazil/11/1978 H1N1). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. 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 CC together with PB1 and PB2 subunits. The complex transcribes viral CC mRNAs by using a unique mechanism called cap-snatching. It CC consists in the hijacking and cleavage of host capped pre-mRNAs. CC These short capped RNAs are then used as primers for viral mRNAs. CC The PB2 subunit is responsible for the binding of the 5' cap of CC cellular pre-mRNAs which are subsequently cleaved after 10-13 CC nucleotides by the PA subunit that carries the endonuclease CC activity. In addition of its function in viral transcription, PA CC also plays an essential role in viral RNA synthesis and promotes CC the formation of the trimeric polymerase complex. CC {ECO:0000250|UniProtKB:P03433}. CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: CC PB1, PB2 and PA. Interacts (via C-terminus) with PB1 (via N- CC terminus). {ECO:0000250|UniProtKB:P03433}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. Note=PB1 and CC PA are transported in the host nucleus as a complex. CC {ECO:0000250|UniProtKB:P03433}. 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 -!- SIMILARITY: Belongs to the influenza viruses PA family. CC {ECO:0000305}. 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 OrthoDB; VOG0900002P; -. DR PRO; PR:A4GBY4; -. 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:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro. DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW. DR GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR001009; RNA-dir_pol_influenzavirus. DR Pfam; PF00603; Flu_PA; 1. PE 3: Inferred from homology; KW Cap snatching; Complete proteome; 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; Inhibition of host RNA polymerase II by virus; KW Phosphoprotein; Ribosomal frameshifting. FT CHAIN 1 716 Polymerase acidic protein. FT /FTId=PRO_0000373005. FT MOTIF 124 139 Nuclear localization signal 1 (NLS1). FT {ECO:0000250|UniProtKB:P03433}. FT MOTIF 184 247 Nuclear localization signal 2 (NLS2). FT {ECO:0000250|UniProtKB:P03433}. 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 //