ID C0LY68_9INFA Unreviewed; 716 AA. AC C0LY68; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 13-FEB-2019, entry version 39. DE RecName: Full=Polymerase acidic protein {ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280, ECO:0000256|SAAS:SAAS00956499}; DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04063}; DE AltName: Full=RNA-directed RNA polymerase subunit P2 {ECO:0000256|HAMAP-Rule:MF_04063}; GN Name=PA {ECO:0000256|HAMAP-Rule:MF_04063, GN 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; Alphainfluenzavirus. OX NCBI_TaxID=610169 {ECO:0000313|EMBL:ACN39478.1, ECO:0000313|Proteomes:UP000137183}; RN [1] {ECO:0000313|EMBL:ACN39478.1, ECO:0000313|Proteomes:UP000137183} 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|HAMAP-Rule:MF_04063, CC ECO:0000256|SAAS:SAAS00956500}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04063}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_04063}; 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:0000256|HAMAP-Rule:MF_04063, CC ECO:0000256|SAAS:SAAS00956438}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP- CC Rule:MF_04063}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04063, CC ECO:0000256|SAAS:SAAS00956481}. Note=PB1 and PA are transported in CC the host nucleus as a complex. {ECO:0000256|HAMAP-Rule:MF_04063}. CC -!- PTM: Phosphorylated on serines and threonines by host kinases, CC including human casein kinase II. {ECO:0000256|HAMAP- CC Rule:MF_04063}. CC -!- SIMILARITY: Belongs to the influenza viruses PA family. CC {ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280, CC ECO:0000256|SAAS:SAAS00956477}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|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; FJ784799; ACN39478.1; -; Viral_cRNA. DR Proteomes; UP000137183; 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:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR Gene3D; 3.40.91.90; -; 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 {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956454}; KW Complete proteome {ECO:0000313|Proteomes:UP000137183}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956462}; KW Eukaryotic host gene expression shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04063, ECO:0000256|SAAS:SAAS00956473}; KW Eukaryotic host transcription shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04063, ECO:0000256|SAAS:SAAS00956495}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956464}; KW Host gene expression shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04063, ECO:0000256|SAAS:SAAS00956469}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956475}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956496}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956466}; KW Inhibition of host RNA polymerase II by virus {ECO:0000256|HAMAP- KW Rule:MF_04063, ECO:0000256|SAAS:SAAS00956479}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956501}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956498}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04063, KW ECO:0000256|SAAS:SAAS00956446}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04063}; KW Ribosomal frameshifting {ECO:0000256|SAAS:SAAS00956468}. FT MOTIF 184 247 Nuclear localization signal 2 (NLS2). FT {ECO:0000256|HAMAP-Rule:MF_04063}. FT METAL 41 41 Manganese 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_04063}. FT METAL 80 80 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_04063}. FT METAL 108 108 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_04063}. FT METAL 108 108 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_04063}. FT METAL 119 119 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_04063}. FT METAL 120 120 Manganese 1; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04063}. 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 //