ID C7RWI0_9INFA Unreviewed; 757 AA.
AC C7RWI0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|HAMAP-Rule:MF_04065};
DE EC=2.7.7.48 {ECO:0000256|HAMAP-Rule:MF_04065};
DE AltName: Full=Polymerase basic protein 1 {ECO:0000256|HAMAP-Rule:MF_04065};
DE Short=PB1 {ECO:0000256|HAMAP-Rule:MF_04065};
DE AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000256|HAMAP-Rule:MF_04065};
GN Name=PB1 {ECO:0000256|HAMAP-Rule:MF_04065,
GN ECO:0000313|EMBL:ACU79912.1};
OS Influenza A virus (A/Hong Kong/1-6-MA21-1/1968(H3N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=506386 {ECO:0000313|EMBL:ACU79912.1, ECO:0000313|Proteomes:UP000120831};
RN [1] {ECO:0000313|EMBL:ACU79912.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Hong Kong/1-6-MA21-1/1968 {ECO:0000313|EMBL:ACU79912.1};
RA Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J.,
RA Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M.,
RA Sitz J., Katzel D., Brown E.G., Keleta L., Bao Y., Sanders R., Dernovoy D.,
RA Kiryutin B., Lipman D.J., Tatusova T.;
RT "The NIAID Influenza Genome Sequencing Project.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACU79912.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Hong Kong/1-6-MA21-1/1968 {ECO:0000313|EMBL:ACU79912.1};
RG The NIAID Influenza Genome Sequencing Consortium;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADM13421.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Hong Kong/1-6-MA21-1/1968 {ECO:0000313|EMBL:ADM13421.1};
RX PubMed=20702632; DOI=10.1128/JVI.01187-10;
RA Ping J., Dankar S.K., Forbes N.E., Keleta L., Zhou Y., Tyler S.,
RA Brown E.G.;
RT "PB2 and hemagglutinin mutations are major determinants of host range and
RT virulence in mouse-adapted influenza A virus.";
RL J. Virol. 84:10606-10618(2010).
RN [4] {ECO:0000313|EMBL:ADM13421.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Hong Kong/1-6-MA21-1/1968 {ECO:0000313|EMBL:ADM13421.1};
RA Ping J., Keleta L., Forbes N.E., Tyler S., Brown E.G.;
RT "Genomic and Structural Map of Adaptive Evolution of Human Influenza A
RT Virus to Increased Virulence in a Novel Mammalian Host.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ACU79912.1, ECO:0000313|Proteomes:UP000120831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A/Hong Kong/1-6-MA21-1/1968 {ECO:0000313|EMBL:ACU79912.1};
RX PubMed=21738783; DOI=10.1371/journal.pone.0021740;
RA Ping J., Keleta L., Forbes N.E., Dankar S., Stecho W., Tyler S., Zhou Y.,
RA Babiuk L., Weingartl H., Halpin R.A., Boyne A., Bera J., Hostetler J.,
RA Fedorova N.B., Proudfoot K., Katzel D.A., Stockwell T.B., Ghedin E.,
RA Spiro D.J., Brown E.G.;
RT "Genomic and protein structural maps of adaptive evolution of human
RT influenza a virus to increased virulence in the mouse.";
RL PLoS ONE 6:E21740-E21740(2011).
CC -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC replication and transcription of virus RNA segments. The transcription
CC of viral mRNAs occurs by a unique mechanism called cap-snatching. 5'
CC methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides
CC by PA. In turn, these short capped RNAs are used as primers by PB1 for
CC transcription of viral mRNAs. During virus replication, PB1 initiates
CC RNA synthesis and copies vRNA into complementary RNA (cRNA) which in
CC turn serves as a template for the production of more vRNAs.
CC {ECO:0000256|HAMAP-Rule:MF_04065}.
CC -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC replication and transcription of virus RNA segments. The transcription
CC of viral mRNAs occurs by a unique mechanism called cap-snatching. 5'
CC methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides
CC by PA. In turn, these short capped RNAs are used as primers by PB1 for
CC transcription of viral mRNAs. During virus replication, PB1 initiates
CC RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn
CC serves as a template for the production of more vRNAs.
CC {ECO:0000256|ARBA:ARBA00002148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000256|HAMAP-Rule:MF_04065,
CC ECO:0000256|RuleBase:RU004330};
CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1,
CC PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus).
CC Interacts (via C-terminus) with PB2 (via N-terminus); this interaction
CC is essential for transcription initiation. {ECO:0000256|HAMAP-
CC Rule:MF_04065}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC nucleus {ECO:0000256|HAMAP-Rule:MF_04065}. Host cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_04065}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000256|HAMAP-Rule:MF_04065}.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000256|HAMAP-Rule:MF_04065}.
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DR EMBL; CY044291; ACU79912.1; -; Viral_cRNA.
DR EMBL; HM641147; ADM13421.1; -; Viral_cRNA.
DR SMR; C7RWI0; -.
DR Proteomes; UP000120831; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; 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:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.720; -; 1.
DR HAMAP; MF_04065; INFV_RDRP; 1.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR001407; RNA_pol_PB1_influenza.
DR Pfam; PF00602; Flu_PB1; 1.
DR PIRSF; PIRSF000827; RdRPol_OMV; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 3: Inferred from homology;
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023247, ECO:0000256|HAMAP-Rule:MF_04065};
KW Eukaryotic host transcription shutoff by virus
KW {ECO:0000256|ARBA:ARBA00022731, ECO:0000256|HAMAP-Rule:MF_04065};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995,
KW ECO:0000256|HAMAP-Rule:MF_04065};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Inhibition of host RNA polymerase II by virus
KW {ECO:0000256|ARBA:ARBA00023103, ECO:0000256|HAMAP-Rule:MF_04065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000256|HAMAP-Rule:MF_04065};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04065};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, ECO:0000256|HAMAP-
KW Rule:MF_04065};
KW Viral transcription {ECO:0000256|ARBA:ARBA00023314, ECO:0000256|HAMAP-
KW Rule:MF_04065}.
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 50..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..256
FT /note="Promoter-binding site"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT MOTIF 187..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 86413 MW; 178E54ED5B3D6F94 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
RLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELEKLW EQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK
//
