ID A0A2D0XSV2_9INFA Unreviewed; 716 AA. AC A0A2D0XSV2; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 02-OCT-2024, entry version 20. DE RecName: Full=Polymerase acidic protein {ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280}; 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:ASM80799.1}; OS Influenza A virus (A/environment/Beijing/1/2016(H9N2)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=2018099 {ECO:0000313|EMBL:ASM80799.1}; RN [1] {ECO:0000313|EMBL:ASM80799.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/environment/Beijing/1/2016 {ECO:0000313|EMBL:ASM80799.1}; RX PubMed=29104171; RA Pan Y., Cui S., Sun Y., Zhang X., Ma C., Shi W., Peng X., Lu G., Zhang D., RA Liu Y., Wu S., Yang P., Wang Q.; RT "Human Infection with H9N2 Avian Influenza in Northern China."; RL Clin. Microbiol. Infect. 0:0-0(2017). 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:0000256|HAMAP-Rule:MF_04063}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-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: PB1, CC PB2 and PA. Interacts (via C-terminus) with PB1 (via N-terminus). CC {ECO:0000256|ARBA:ARBA00011723, ECO:0000256|HAMAP-Rule:MF_04063}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04063}. CC Host nucleus {ECO:0000256|HAMAP-Rule:MF_04063}. Note=PB1 and PA are CC transported in the host nucleus as a complex. {ECO:0000256|HAMAP- CC Rule:MF_04063}. CC -!- PTM: Phosphorylated on serines and threonines by host kinases, CC including human casein kinase II. {ECO:0000256|HAMAP-Rule:MF_04063}. CC -!- SIMILARITY: Belongs to the influenza viruses PA family. CC {ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280}. CC -!- SIMILARITY: Belongs to the influenza viruses PA-X family. CC {ECO:0000256|ARBA:ARBA00008953}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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; MF440702; ASM80799.1; -; Viral_cRNA. 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 {ECO:0000256|ARBA:ARBA00022715, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|ARBA:ARBA00023247, ECO:0000256|HAMAP-Rule:MF_04063}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|ARBA:ARBA00022731, ECO:0000256|HAMAP-Rule:MF_04063}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995, KW ECO:0000256|HAMAP-Rule:MF_04063}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04063}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|ARBA:ARBA00023103, ECO:0000256|HAMAP-Rule:MF_04063}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_04063}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_04063}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_04063}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_04063}; Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758}. FT MOTIF 184..247 FT /note="Nuclear localization signal 2 (NLS2)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 41 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 80 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 108 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 108 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 119 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" FT BINDING 120 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04063" SQ SEQUENCE 716 AA; 82759 MW; 1F948BA9F632994C CRC64; MEDFVRQCFN PMIVELAEKA MKEYGEDPKI ETNKFASICT HLEVCFMYSD FHFIDERGES TIIEPGDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGV EKPKFLPDLY DYKENRFIEI GVTRREVHIY YLEKANKIKS EKTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ EMASRGLWDS FRQSERGEET IEERFEITGT MRRLADQSLP PNFSSLENFR AYVDGFEPNG CIEGKLSQMS KEVNARIEPF LRTTPRPLIL PNGPPCSQRS KFLLMDALKL SIEDPSHEGE GIPLYDAIKC MKTFFGWKEP NIIKPHEKGI NPNYLLTWKQ VLAELQDIEN EEKIPRTKNM KKTSQLKWAL GENMAPEKVD FEDCRDVNDL KQYDSDEPEP RSLACWIQNE FNKACELTDS SWVELDEIGE DVAPIEHIAS MRRNYFTAEV SHCRATEYIM KGVYINTALL NASCAAMDDF QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY CVLEIGDMLL RTAVGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES SVKEKDLTKE FFENKSETWP IGESPKGVEE GSIGKVCRTL LAKSVFNSLY ASPQLEGFSA ESRKLLLIVQ ALRDNLEPGT FDLEGLYEAI EECLINDPWV LLNASWFNSF LTHALR //