PA_I03A0
ID PA_I03A0 Reviewed; 712 AA.
AC Q6J844;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Polymerase acidic protein {ECO:0000255|HAMAP-Rule:MF_04063};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04063};
DE AltName: Full=RNA-directed RNA polymerase subunit P2 {ECO:0000255|HAMAP-Rule:MF_04063};
DE Flags: Fragment;
GN Name=PA {ECO:0000255|HAMAP-Rule:MF_04063};
OS Influenza A virus (strain A/Hong Kong/212/2003 H5N1 genotype Z+).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=279794;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH NCBI_TaxID=9694; Panthera tigris (Tiger).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15148370; DOI=10.1073/pnas.0402443101;
RA Guan Y., Poon L.L.M., Cheung C.Y., Ellis T.M., Lim W., Lipatov A.S.,
RA Chan K.H., Sturm-Ramirez K.M., Cheung C.L., Leung Y.H.C., Yuen K.Y.,
RA Webster R.G., Peiris J.S.M.;
RT "H5N1 influenza: a protean pandemic threat.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8156-8161(2004).
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:0000255|HAMAP-Rule:MF_04063}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04063};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_04063}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are
CC transported in the host nucleus as a complex. {ECO:0000255|HAMAP-
CC Rule:MF_04063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=PA;
CC IsoId=Q6J844-1; Sequence=Displayed;
CC Name=PA-X;
CC IsoId=Q6J844-2; Sequence=Not described;
CC -!- PTM: Phosphorylated on serines and threonines by host kinases,
CC including human casein kinase II. {ECO:0000255|HAMAP-Rule:MF_04063}.
CC -!- SIMILARITY: Belongs to the influenza viruses PA family.
CC {ECO:0000255|HAMAP-Rule:MF_04063}.
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DR EMBL; AY576404; AAT39053.1; -; Genomic_DNA.
DR SMR; Q6J844; -.
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:InterPro.
DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
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; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host RNA polymerase II by virus; Manganese; Metal-binding;
KW Nuclease; Phosphoprotein; Ribosomal frameshifting.
FT CHAIN <1..712
FT /note="Polymerase acidic protein"
FT /id="PRO_0000311140"
FT MOTIF 120..135
FT /note="Nuclear localization signal 1 (NLS1)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT MOTIF 180..243
FT /note="Nuclear localization signal 2 (NLS2)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT NON_TER 1
SQ SEQUENCE 712 AA; 81966 MW; 07D64AEA561CA4BE CRC64;
VRQCFNPMIV ELAEKAMKEY GEDPKIETNK FAAICTHLEV CFMYSDFHFI DERSESIIVE
SGDPNALLKH RFEIIEGRDR TMAWTVVNSI CNTTGVEKPK FLPDLYDYKE NRFIEIGVTR
REVHTYYLEK ANKIKSEKTH IHIFSFTGEE MATKADYTLD EESRARIKTR LFTIRQEMAS
RGLWDSFRQS ERGEETIEEK FEITGTMRRL ADQSLPPNFS SLENFRTYVD GFEPNGCIEG
KLSQMSKEVN ARIEPFLKTT PRPLRLPDGP PCSQRSKFLL MDALKLSIED PSHEGEGIPL
YDAIKCMKTF FGWKEPNIVK PHEKGINPNY LLAWKQVLAE LQDIENEEKI PKTKNMKKTS
QLKWALGENM APEKVDFEDC KDVSDLRQYD SDEPESRSLA SWIQSEFNKA CELTDSSWIE
LDEIGEDVAP IEHIASMRRN YFTAEVSHCR ATEYIMKGVY INTALLNASC AAMDDFQLIP
MISKCRTKEG RRKTNLYGFI IKGRSHLRND TDVVNFVSME FSLTDPRLEP HKWEKYCVLE
IGDMLLRTAV GQVSRPMFLY VRTNGTSKIK MKWGMEMRRC LLQSLQQIES MIEAESSVKE
KDMTKEFFEN KSETWPIGES PKGVEEGSIG KVCRTLLAKS VFNSLYASPQ LEGFSAESRK
LLLIAQALRD NLEPGTFDLG GLYEAIEECL INDPWVLLNA SWFNSFLAHA LK
