ing 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|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}.
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DR EMBL; KJ130195; AHI97755.1; -; Viral_cRNA.
DR Proteomes; UP000139950; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule.
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:UP000139950};
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 SEQUEN
