ID A0A2D0XSV2_9INFA Unreviewed; 716 AA. AC A0A2D0XSV2; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 28-FEB-2018, entry version 2. DE RecName: Full=Polymerase acidic protein {ECO:0000256|RuleBase:RU361280, ECO:0000256|SAAS:SAAS00956499}; GN Name=PA {ECO:0000256|RuleBase:RU361280, ECO:0000313|EMBL:ASM80799.1}; OS Influenza A virus (A/environment/Beijing/1/2016(H9N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. 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., RA Zhang D., 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 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 -!- SUBCELLULAR LOCATION: Host nucleus CC {ECO:0000256|SAAS:SAAS00956481}. 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|RuleBase:RU361280, 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; MF440702; ASM80799.1; -; Viral_cRNA. DR HAMAP; MF_04063; INFV_PA; 1. DR InterPro; IPR037534; INFV_PA. DR InterPro; IPR001009; PA/PA-X. 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 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|HAMAP-Rule:MF_04063, KW 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; 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 //