ID C0LY68_9INFA Unreviewed; 716 AA. AC C0LY68; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=Polymerase acidic protein {ECO:0000256|RuleBase:RU361280, ECO:0000256|SAAS:SAAS00405176}; GN Name=PA {ECO:0000256|RuleBase:RU361280, ECO:0000313|EMBL:ACN39478.1}; OS Influenza A virus (A/chicken/Hunan/1793/2007(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=610169 {ECO:0000313|EMBL:ACN39478.1, ECO:0000313|Proteomes:UP000137183}; RN [1] {ECO:0000313|EMBL:ACN39478.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/chicken/Hunan/1793/2007 {ECO:0000313|EMBL:ACN39478.1}; RX PubMed=19720095; DOI=10.1016/j.virusres.2009.08.010; RA Chen J., Fang F., Yang Z., Liu X., Zhang H., Zhang Z., Zhang X., RA Chen Z.; RT "Characterization of highly pathogenic H5N1 avian influenza viruses RT isolated from poultry markets in central China."; RL Virus Res. 146:19-28(2009). 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. {ECO:0000256|SAAS:SAAS00836215}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00836355}; CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: CC PB1, PB2 and PA. {ECO:0000256|RuleBase:RU361280}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm CC {ECO:0000256|SAAS:SAAS00836308}. CC -!- SUBCELLULAR LOCATION: Host nucleus CC {ECO:0000256|SAAS:SAAS00836205}. CC -!- SIMILARITY: Belongs to the influenza viruses PA family. CC {ECO:0000256|RuleBase:RU361280, ECO:0000256|SAAS:SAAS00589177}. 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; FJ784799; ACN39478.1; -; Viral_cRNA. DR Proteomes; UP000137183; Genome. 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: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 {ECO:0000256|SAAS:SAAS00836340}; KW Complete proteome {ECO:0000313|Proteomes:UP000137183}; KW Endonuclease {ECO:0000256|SAAS:SAAS00836319}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|SAAS:SAAS00836303}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|SAAS:SAAS00836335}; KW Host cytoplasm {ECO:0000256|SAAS:SAAS00836347}; KW Host gene expression shutoff by virus {ECO:0000256|SAAS:SAAS00836242}; KW Host nucleus {ECO:0000256|SAAS:SAAS00836298}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00836258}; KW Hydrolase {ECO:0000256|SAAS:SAAS00836216}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|SAAS:SAAS00836208}; KW Manganese {ECO:0000256|SAAS:SAAS00836185}; KW Metal-binding {ECO:0000256|SAAS:SAAS00836270}; KW Nuclease {ECO:0000256|SAAS:SAAS00836231}; KW Ribosomal frameshifting {ECO:0000256|SAAS:SAAS00836323}. SQ SEQUENCE 716 AA; 82385 MW; 81D023E9086E7728 CRC64; MEDFVRQCFN PMIVELAEKA MKEYGEDPKI ETNKFAAICT HLEVCFMYSD FHFIDERSES IIVESGDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGV EKPKFLPDLY DYKENRFIEI GVTRREVHTY YLEKANKIKS EKTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ EMASRGLWDS FRQSERGEET IEEKFEITGT MRRLADQSLP PNFSSLENFR AYVDGFEPNG CIEGKLSQMS KEVNAKIEPF LKTTPRPLRL PDGPPCSQRS KFLLMDALKL SIEDPSHEGE GIPLYDAIKC MKTFFGWKEP NIVKPHEKGI NPNYLLAWKQ VMAELQDIEN EEKISKTKNM KKTSQLKWAL GENMAPEKVD FEDCKDISDL RQYGSDEPES RSLASWIQSE FNKACELTDS SWIELDEIGE DVAPIEHIAS MRRNYFTAEV SHCRATEYIM KGVYINTALL NASCAAMDDF QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY CVLEIGDMLL RTAVGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES SVKEKDMTKE FFENKSETWP IGESPKGVEE GSIGKVCRTL LAKSVFNSLY ASSQLEGFSA ESRKLLLIAQ ALRDDLEPGT FDLGGLYEAI EECLINDPWV LLNASWFNSF LAHALK //