PA_I96A0
ID PA_I96A0 Reviewed; 716 AA.
AC Q9Q0U9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN Name=PA {ECO:0000255|HAMAP-Rule:MF_04063};
OS Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=93838;
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=10484749; DOI=10.1006/viro.1999.9820;
RA Xu X., Subbarao K., Cox N.J., Guo Y.;
RT "Genetic characterization of the pathogenic influenza
RT A/Goose/Guangdong/1/96 (H5N1) virus: similarity of its hemagglutinin gene
RT to those of H5N1 viruses from the 1997 outbreaks in Hong Kong.";
RL Virology 261:15-19(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-256.
RX PubMed=19194458; DOI=10.1038/nature07720;
RA Yuan P., Bartlam M., Lou Z., Chen S., Zhou J., He X., Lv Z., Ge R., Li X.,
RA Deng T., Fodor E., Rao Z., Liu Y.;
RT "Crystal structure of an avian influenza polymerase PA(N) reveals an
RT endonuclease active site.";
RL Nature 458:909-913(2009).
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:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}.
CC -!- INTERACTION:
CC Q9Q0U9; Q9Q0V0: PB1; NbExp=3; IntAct=EBI-15715136, EBI-8290908;
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.
CC {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=PA;
CC IsoId=Q9Q0U9-1; Sequence=Displayed;
CC Name=PA-X;
CC IsoId=P0CK63-1; Sequence=External;
CC -!- PTM: Phosphorylated on serines and threonines by host kinases,
CC including human casein kinase II. {ECO:0000250|UniProtKB:P03433,
CC 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; AF144302; AAD51924.1; -; Genomic_RNA.
DR RefSeq; YP_308666.1; NC_007359.1. [Q9Q0U9-1]
DR PDB; 3EBJ; X-ray; 2.20 A; A/B/C/D=1-256.
DR PDB; 3HW3; X-ray; 1.90 A; A/B/C/D=1-256.
DR PDB; 3HW4; X-ray; 1.90 A; A/B/C/D=1-256.
DR PDB; 3HW5; X-ray; 1.81 A; A/B/C/D=1-256.
DR PDB; 3HW6; X-ray; 2.50 A; A/B/C/D=1-256.
DR PDBsum; 3EBJ; -.
DR PDBsum; 3HW3; -.
DR PDBsum; 3HW4; -.
DR PDBsum; 3HW5; -.
DR PDBsum; 3HW6; -.
DR SMR; Q9Q0U9; -.
DR DIP; DIP-59837N; -.
DR IntAct; Q9Q0U9; 1.
DR MEROPS; S62.001; -.
DR PRIDE; Q9Q0U9; -.
DR GeneID; 3654617; -.
DR KEGG; vg:3654617; -.
DR EvolutionaryTrace; Q9Q0U9; -.
DR Proteomes; UP000131152; Genome.
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:0039523; P:suppression by virus of host mRNA transcription via inhibition of 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 1: Evidence at protein level;
KW 3D-structure; 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; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..716
FT /note="Polymerase acidic protein"
FT /id="PRO_0000279246"
FT MOTIF 124..139
FT /note="Nuclear localization signal 1 (NLS1)"
FT /evidence="ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-
FT Rule:MF_04063"
FT MOTIF 184..247
FT /note="Nuclear localization signal 2 (NLS2)"
FT /evidence="ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-
FT Rule:MF_04063"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063"
FT HELIX 1..8
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:3HW5"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:3HW5"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:3HW5"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3HW5"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:3HW5"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:3HW5"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3HW5"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 165..184
FT /evidence="ECO:0007829|PDB:3HW5"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:3HW5"
SQ SEQUENCE 716 AA; 82673 MW; C89CE96EB4BB71CB CRC64;
MEDFVRQCFN PMIVELAEKA MKEYGEDPKI ETNKFAAICT HLEVCFMYSD FHFIDERGES
TIIESGDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGV EKPKFLPDLY DYKENRFIEI
GVTRREVHTY YLEKANKIKS EKTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ
EMASRGLWDS FRQSERGEET VEERFEITGT MCRLADQSLP PNFSSLEKFR AYVDGFEPNG
CIEGKLSQMS KEVNARIEPF LKTTPRPLRL PDGPPCSQRS KFLLMDALKL SIEDPSHEGE
GIPLYDAIKC MKTFFGWKEP NIVKPHEKGI NPNYLLAWKQ VLAELQDIEN EEKIPKTKNM
RKTSQLKWAL GENMAPEKVD FEDCKDVSDL RQYDSDEPKP RSLASWIQSE FNKACELTDS
SWIELDEIGE DVAPIEHIAS MRRNYFTAEV SHCRATEYIM KGVYINTALL NASCAAMDDF
QLIPMISKCR TKEGRRKTNL YGFLIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHRWEKY
CVLRIGDMLL RTEIGQVSRP MFLYVRTNGT SKIKMKWGME MRRCPFQSLQ QIESMIEAES
SVKEKDMTKE FFENKSETWP IGESPKGVEE GSIGKVCRTL LAKSVFNSLY ASPQLEGFSA
ESRKLLLIVQ ALRDNLEPGT FDLGGLYEAI EECLINDPWV LLNASWFNSF LTHALR
