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Polymerase acidic protein (EC 3.1.-.-) (RNA-directed RNA polymerase subunit P2)

 C6ZEV6_9INFA            Unreviewed;       716 AA.
C6ZEV6;
22-SEP-2009, integrated into UniProtKB/TrEMBL.
22-SEP-2009, sequence version 1.
05-DEC-2018, entry version 35.
RecName: Full=Polymerase acidic protein {ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280, ECO:0000256|SAAS:SAAS00956499};
EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04063};
AltName: Full=RNA-directed RNA polymerase subunit P2 {ECO:0000256|HAMAP-Rule:MF_04063};
Name=PA {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|RuleBase:RU361280, ECO:0000313|EMBL:ACE81827.1};
Influenza A virus (A/donkey/Xinjiang/5/2007(H3N8)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=690878 {ECO:0000313|EMBL:ACE81827.1, ECO:0000313|Proteomes:UP000132750};
[1] {ECO:0000313|EMBL:ACE81827.1, ECO:0000313|Proteomes:UP000132750}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/donkey/Xinjiang/5/2007 {ECO:0000313|EMBL:ACE81827.1};
Li X.F., Dai L.L., Guo W., Xiang W.H., Zhou J.H.;
"Equine influenza virus in Hetian of Xinjiang Uyghur Autonomous
Region, China, 2007.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays an essential role in viral RNA transcription and
replication by forming the heterotrimeric polymerase complex
together with PB1 and PB2 subunits. The complex transcribes viral
mRNAs by using a unique mechanism called cap-snatching. It
consists in the hijacking and cleavage of host capped pre-mRNAs.
These short capped RNAs are then used as primers for viral mRNAs.
The PB2 subunit is responsible for the binding of the 5' cap of
cellular pre-mRNAs which are subsequently cleaved after 10-13
nucleotides by the PA subunit that carries the endonuclease
activity. {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956500}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_04063};
Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_04063};
-!- SUBUNIT: Influenza RNA polymerase is composed of three subunits:
PB1, PB2 and PA. Interacts (via C-terminus) with PB1 (via N-
terminus). {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956438}.
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04063}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956481}. Note=PB1 and PA are transported in
the host nucleus as a complex. {ECO:0000256|HAMAP-Rule:MF_04063}.
-!- PTM: Phosphorylated on serines and threonines by host kinases,
including human casein kinase II. {ECO:0000256|HAMAP-
Rule:MF_04063}.
-!- SIMILARITY: Belongs to the influenza viruses PA family.
{ECO:0000256|HAMAP-Rule:MF_04063, ECO:0000256|RuleBase:RU361280,
ECO:0000256|SAAS:SAAS00956477}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04063}.
-----------------------------------------------------------------------
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EMBL; EU794574; ACE81827.1; -; Viral_cRNA.
Proteomes; UP000132750; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule.
GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-UniRule.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
Gene3D; 3.40.91.90; -; 1.
HAMAP; MF_04063; INFV_PA; 1.
InterPro; IPR037534; INFV_PA.
InterPro; IPR001009; PA/PA-X.
InterPro; IPR038372; PA/PA-X_sf.
Pfam; PF00603; Flu_PA; 1.
3: Inferred from homology;
Cap snatching {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956454};
Complete proteome {ECO:0000313|Proteomes:UP000132750};
Endonuclease {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956462};
Eukaryotic host gene expression shutoff by virus {ECO:0000256|HAMAP-
Rule:MF_04063, ECO:0000256|SAAS:SAAS00956479};
Eukaryotic host transcription shutoff by virus {ECO:0000256|HAMAP-
Rule:MF_04063, ECO:0000256|SAAS:SAAS00956479};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956464};
Host gene expression shutoff by virus {ECO:0000256|HAMAP-
Rule:MF_04063, ECO:0000256|SAAS:SAAS00956479};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956475};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956479};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956462};
Inhibition of host RNA polymerase II by virus {ECO:0000256|HAMAP-
Rule:MF_04063, ECO:0000256|SAAS:SAAS00956479};
Manganese {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956501};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956498};
Nuclease {ECO:0000256|HAMAP-Rule:MF_04063,
ECO:0000256|SAAS:SAAS00956462};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04063};
Ribosomal frameshifting {ECO:0000256|SAAS:SAAS00956468}.
MOTIF 184 247 Nuclear localization signal 2 (NLS2).
{ECO:0000256|HAMAP-Rule:MF_04063}.
METAL 41 41 Manganese 1; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_04063}.
METAL 80 80 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_04063}.
METAL 108 108 Manganese 1. {ECO:0000256|HAMAP-
Rule:MF_04063}.
METAL 108 108 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_04063}.
METAL 119 119 Manganese 1. {ECO:0000256|HAMAP-
Rule:MF_04063}.
METAL 120 120 Manganese 1; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_04063}.
SEQUENCE 716 AA; 82847 MW; 0FC2F48B6A9D4ABF CRC64;
MEDFVRQCFN PMIVELAEKA MKEYGEDPKI ETNKFAAICT HLEVCFMYSD FHFINELGES
VVIDSGDPNA LLKHRFEIIE GRDRTIAWTV VNSICNTTRA EKPKFLPDLY DYKKNRFVEI
GVTRREVHIY YLEKANKIKS EKTHIHIFSF TGEEMATRAD YTLDEESRAR IKTRLFTIRQ
EMASRGLWDS FRQSERGEET IEERFEITGT MRKLANYSLP PNFSSLENFR VYVDGFKPNG
CIESKLSQMS KEVNARIEPF SKTTPRPLKM PGGPPCHQRS KFLLMDALKL SIEDPSHEGE
GIPLYDAIKC MKTFFGWKEP NIVKPHEKGI NPNYLQTWKQ VLEEIQDLEK EERIPKTKNM
KKTSQLKWAL GENMAPEKVD FEDCKDISDL KQYDSDEPET RSLASWIQSE FNKACELTDS
SWIELDEIGE DVAPIEYIAS MRRNYFTAEI SHCRATEYIM KGVYINTALL NASCATMDEF
QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RFEPHKWEKY
CVLEIGDMLL RTAVGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES
SVKEKDMTKE FFENKSETWP IGESPRGVEE GSIGKVCRTL LAKSVFNSLY ASPQLEGFSA
ESRKLLLIVQ ALRDNLEPGT FDIGGLYESI EECLINDPWV LLNASWFNSF LTHALK


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