PA_I68A6
ID PA_I68A6 Reviewed; 716 AA.
AC P03434;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, 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/Northern Territory/60/1968 H3N2) (Influenza A
OS virus (strain NT60)) (Influenza A virus (strain A/NT/60/1968 H3N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384505;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7101732; DOI=10.1016/0042-6822(82)90049-6;
RA Bishop D.H.L., Jones K.L., Huddleston J.A., Brownlee G.G.;
RT "Influenza A virus evolution: complete sequences of influenza A/NT/60/68
RT RNA segment 3 and its predicted acidic P polypeptide compared with those of
RT influenza A/PR/8/34.";
RL Virology 120:481-489(1982).
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 -!- 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=P03434-1; Sequence=Displayed;
CC Name=PA-X;
CC IsoId=P0DJT7-1; 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; J02139; AAA43597.1; -; Genomic_RNA.
DR PIR; A04049; P2IV68.
DR PDB; 6QPG; X-ray; 3.34 A; A/D/G/J=1-716.
DR PDB; 6QX3; EM; 3.79 A; A=1-716.
DR PDB; 6QX8; EM; 4.07 A; A/E=1-716.
DR PDB; 6QXE; EM; 4.15 A; A/E=1-716.
DR PDB; 6RR7; EM; 3.01 A; A=1-716.
DR PDBsum; 6QPG; -.
DR PDBsum; 6QX3; -.
DR PDBsum; 6QX8; -.
DR PDBsum; 6QXE; -.
DR PDBsum; 6RR7; -.
DR SMR; P03434; -.
DR IntAct; P03434; 3.
DR MEROPS; S62.001; -.
DR ABCD; P03434; 1 sequenced antibody.
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; Ribosomal frameshifting.
FT CHAIN 1..716
FT /note="Polymerase acidic protein"
FT /id="PRO_0000078794"
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 2..8
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6QPG"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 165..185
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 331..349
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6QPG"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 434..451
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 454..475
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 481..491
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 496..506
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 517..526
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:6QPG"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 559..571
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 583..600
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 601..604
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 608..614
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 633..649
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 653..673
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 683..690
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 698..713
FT /evidence="ECO:0007829|PDB:6RR7"
SQ SEQUENCE 716 AA; 82996 MW; CF100DFFFC1F934F CRC64;
MEDFVRQCFN PMIVELAEKA MKEYGEDLKI ETNKFAAICT HLEVCFMYSD FHFINEQGES
IVVELDDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGA EKPKFLPDLY DYKENRFIEI
GVTRREVHIY YLEKANKIKS ENTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ
EMANRGLWDS FRQSERGEET IEERFEITGT MRRLADQSLP PNFSCLENFR AYVDGFEPNG
YIEGKLSQMS KEVNAKIEPF LKTTPRPIRL PDGPPCFQRS KFLLMDALKL SIEDPSHEGE
GIPLYDAIKC MRTFFGWKEP YIVKPHEKGI NPNYLLSWKQ VLAELQDIEN EEKIPRTKNM
KKTSQLKWAL GENMAPEKVD FDNCRDVSDL KQYDSDEPEL RSLSSWIQNE FNKACELTDS
TWIELDEIGE DVAPIEYIAS MRRNYFTAEV SHCRATEYIM KGVYINTALL NASCAAMDDF
QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY
CVLEIGDMLL RSAIGQMSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES
SVKEKDMTKE FFENKSETWP IGESPKGVED GSIGKVCRTL LAKSVFNSLY ASPQLEGFSA
ESRKLLLVVQ ALRDNLEPGT FDLEGLYEAI EECLINDPWV LLNASWFNSF LTHALR
