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RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48) (Polymerase basic protein 1) (PB1) (RNA-directed RNA polymerase subunit P1)

 RDRP_I34A1              Reviewed;         757 AA.
P03431; A4GXH1; Q20N30; Q8JUU7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
07-JUN-2017, entry version 105.
RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_04065};
EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04065};
AltName: Full=Polymerase basic protein 1 {ECO:0000255|HAMAP-Rule:MF_04065};
Short=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000255|HAMAP-Rule:MF_04065};
Name=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6281731; DOI=10.1093/nar/10.6.2135;
Winter G., Fields S.;
"Nucleotide sequence of human influenza A/PR/8/34 segment 2.";
Nucleic Acids Res. 10:2135-2143(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=8645093; DOI=10.1007/BF01718315;
Kobayashi M., Toyoda T., Ishihama A.;
"Influenza virus PB1 protein is the minimal and essential subunit of
RNA polymerase.";
Arch. Virol. 141:525-539(1996).
[6]
PHOSPHORYLATION BY HOST PRKCA.
STRAIN=A/WSN/33;
PubMed=19264651; DOI=10.1099/vir.0.009050-0;
Mahmoudian S., Auerochs S., Grone M., Marschall M.;
"Influenza A virus proteins PB1 and NS1 are subject to functionally
important phosphorylation by protein kinase C.";
J. Gen. Virol. 90:1392-1397(2009).
[7]
SUBCELLULAR LOCATION.
STRAIN=A/Victoria/3/75;
PubMed=19906916; DOI=10.1128/JVI.01533-09;
Huet S., Avilov S.V., Ferbitz L., Daigle N., Cusack S., Ellenberg J.;
"Nuclear import and assembly of influenza A virus RNA polymerase
studied in live cells by fluorescence cross-correlation
spectroscopy.";
J. Virol. 84:1254-1264(2010).
[8]
REVIEW ON FUNCTION.
PubMed=23600869; DOI=10.4149/av_2013_02_113;
Fodor E.;
"The RNA polymerase of influenza a virus: mechanisms of viral
transcription and replication.";
Acta Virol. 57:113-122(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-81, AND INTERACTION WITH
PA.
PubMed=18660801; DOI=10.1038/nature07225;
Obayashi E., Yoshida H., Kawai F., Shibayama N., Kawaguchi A.,
Nagata K., Tame J.R., Park S.Y.;
"The structural basis for an essential subunit interaction in
influenza virus RNA polymerase.";
Nature 454:1127-1131(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 678-757, AND INTERACTION
WITH PB2.
PubMed=19461581; DOI=10.1038/emboj.2009.138;
Sugiyama K., Obayashi E., Kawaguchi A., Suzuki Y., Tame J.R.,
Nagata K., Park S.Y.;
"Structural insight into the essential PB1-PB2 subunit contact of the
influenza virus RNA polymerase.";
EMBO J. 28:1803-1811(2009).
-!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
replication and transcription of virus RNA segments. The
transcription of viral mRNAs occurs by a unique mechanism called
cap-snatching. 5' methylated caps of cellular mRNAs are cleaved
after 10-13 nucleotides by PA. In turn, these short capped RNAs
are used as primers by PB1 for transcription of viral mRNAs.
During virus replication, PB1 initiates RNA synthesis and copy
vRNA into complementary RNA (cRNA) which in turn serves as a
template for the production of more vRNAs. {ECO:0000255|HAMAP-
Rule:MF_04065, ECO:0000269|PubMed:8645093,
ECO:0000305|PubMed:23600869}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_04065}.
-!- SUBUNIT: Influenza RNA polymerase is composed of three subunits:
PB1, PB2 and PA. Interacts (via N-terminus) with PA (via C-
terminus). Interacts (via C-terminus) with PB2 (via N-terminus);
this interaction is essential for transcription initiation.
{ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:18660801,
ECO:0000269|PubMed:19461581}.
-!- INTERACTION:
Q14318:FKBP8 (xeno); NbExp=5; IntAct=EBI-2547514, EBI-724839;
P03466:NP; NbExp=3; IntAct=EBI-2547514, EBI-2547640;
P03433:PA; NbExp=3; IntAct=EBI-2547514, EBI-2547616;
P03428:PB2; NbExp=3; IntAct=EBI-2547514, EBI-2547475;
Q99959:PKP2 (xeno); NbExp=8; IntAct=EBI-2547514, EBI-702235;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04065, ECO:0000269|PubMed:19906916}. Host cytoplasm
{ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19906916}.
-!- PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-
Rule:MF_04065, ECO:0000269|PubMed:19264651}.
-!- SIMILARITY: Belongs to the influenza viruses polymerase PB1
family. {ECO:0000255|HAMAP-Rule:MF_04065}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J02151; AAA43581.1; -; Genomic_RNA.
EMBL; AF389116; AAM75156.1; -; Genomic_RNA.
EMBL; CY009450; ABD77683.1; -; Genomic_RNA.
EMBL; EF467819; ABO21706.1; -; Genomic_RNA.
PIR; A93418; P1IV34.
RefSeq; NP_040985.1; NC_002021.1.
PDB; 2ZNL; X-ray; 2.30 A; B=1-81.
PDB; 2ZTT; X-ray; 2.10 A; A/C=679-757.
PDB; 3A1G; X-ray; 1.70 A; A/C=678-757.
PDBsum; 2ZNL; -.
PDBsum; 2ZTT; -.
PDBsum; 3A1G; -.
ProteinModelPortal; P03431; -.
SMR; P03431; -.
DIP; DIP-56974N; -.
IntAct; P03431; 141.
GeneID; 956534; -.
KEGG; vg:956534; -.
KO; K19389; -.
OrthoDB; VOG09000028; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-192814; vRNA Synthesis.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-192869; cRNA Synthesis.
Reactome; R-HSA-192905; vRNP Assembly.
EvolutionaryTrace; P03431; -.
PRO; PR:P03431; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000109386; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; TAS:Reactome.
GO; GO:0019070; P:viral genome maturation; TAS:Reactome.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0019076; P:viral release from host cell; TAS:Reactome.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
HAMAP; MF_04065; INFV_RDRP; 1.
InterPro; IPR007099; RNA-dir_pol_NSvirus.
InterPro; IPR001407; RNA_pol_PB1_influenza.
Pfam; PF00602; Flu_PB1; 1.
PIRSF; PIRSF000827; RdRPol_OMV; 1.
PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
1: Evidence at protein level;
3D-structure; Complete proteome;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host nucleus;
Host-virus interaction; Inhibition of host RNA polymerase II by virus;
Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Reference proteome; RNA-directed RNA polymerase; Transferase;
Viral RNA replication; Viral transcription.
CHAIN 1 757 RNA-directed RNA polymerase catalytic
subunit.
/FTId=PRO_0000078763.
DOMAIN 286 483 RdRp catalytic. {ECO:0000255|HAMAP-
Rule:MF_04065}.
REGION 249 256 Promoter-binding site.
{ECO:0000255|HAMAP-Rule:MF_04065}.
MOTIF 187 195 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04065}.
MOTIF 203 216 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04065}.
CONFLICT 53 53 G -> A (in Ref. 1; AAA43581).
{ECO:0000305}.
CONFLICT 175 175 K -> N (in Ref. 4; ABO21706 and 3;
ABD77683). {ECO:0000305}.
CONFLICT 205 205 I -> M (in Ref. 4; ABO21706 and 3;
ABD77683). {ECO:0000305}.
CONFLICT 208 208 K -> R (in Ref. 1; AAA43581).
{ECO:0000305}.
CONFLICT 300 300 F -> L (in Ref. 1; AAA43581).
{ECO:0000305}.
CONFLICT 394 394 P -> S (in Ref. 4; ABO21706 and 3;
ABD77683). {ECO:0000305}.
CONFLICT 473 473 L -> H (in Ref. 1; AAA43581).
{ECO:0000305}.
CONFLICT 517 517 I -> S (in Ref. 1; AAA43581).
{ECO:0000305}.
HELIX 5 10 {ECO:0000244|PDB:2ZNL}.
HELIX 687 699 {ECO:0000244|PDB:3A1G}.
HELIX 714 731 {ECO:0000244|PDB:3A1G}.
HELIX 737 755 {ECO:0000244|PDB:3A1G}.
SEQUENCE 757 AA; 86576 MW; FB23E4976E06C18F CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGRWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCIET MEVVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMKKEEMG
ITTHFQRKRR VRDNMTKKMI TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYMTRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIEGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLLGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW EQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESM NNAVMMPAHG PAKNMEYDAV
ATTHSWIPKR NRSILNTSQR GVLEDEQMYQ RCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF TEIMKICSTI EELRRQK


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