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Database: UniProt
Entry: Q1AQR6_9INFA
LinkDB: Q1AQR6_9INFA
Original site: Q1AQR6_9INFA 
ID   Q1AQR6_9INFA            Unreviewed;       757 AA.
AC   Q1AQR6;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 75.
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:ABF82871.1};
OS   Influenza A virus (A/Waikato/10/2001(H1N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=383136 {ECO:0000313|EMBL:ABF82871.1, ECO:0000313|Proteomes:UP000159459};
RN   [1] {ECO:0000313|EMBL:ABF82871.1, ECO:0000313|Proteomes:UP000159459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Waikato/10/2001 {ECO:0000313|EMBL:ABF82871.1};
RA   Ghedin E., Spiro D., Sengamalay N., Zaborsky J., Feldblyum T., Subbu V.,
RA   Sparenborg J., Groveman L., Halpin R., Shumway M., Sitz J., Katzel D.,
RA   Koo H., Salzberg S.L., Jennings L., Smit M., Wells V., Bao Y., Bolotov P.,
RA   Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABF82871.1, ECO:0000313|Proteomes:UP000159459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Waikato/10/2001 {ECO:0000313|EMBL:ABF82871.1};
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000159459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bedford T., Riley S., Barr I.G., Broor S., Chadha M., Cox N.J.,
RA   Daniels R.S., Gunasekaran C.P., Hurt A.C., Kelso A., Klimov A., Lewis N.S.,
RA   Li X., McCauley J.W., Odagiri T., Potdar V., Rambaut A., Shu Y.,
RA   Skepner E., Smith D.J., Suchard M.A., Tashiro M., Wang D., Xu X., Lemey P.,
RA   Russell C.A.;
RT   "Global circulation patterns of seasonal influenza viruses vary with rates
RT   of antigenic drift.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; CY011190; ABF82871.1; -; Genomic_RNA.
DR   Proteomes; UP000159459; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; 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          53..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"
SQ   SEQUENCE   757 AA;  86442 MW;  0C2A6182080EDD9F CRC64;
     MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS ERGRWTKNTE
     TGAPQLNPID GPLPKDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCIET MEVVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLIANES GRLIDFLKDV MESMDRDEVE
     ITTHFQRKRR VRDNVTKKMV TQRTIGKKKH KLDKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTEISF
     TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNILSIA PIMFSNKMAR LGKGYMFESK
     SMKLRTQIPA EMLANIDLKY FNDSTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNASNYAGIQ AGVDRFYRTC KLLGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGVNES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW DQTRSKAGLL VSDGGPNLYN
     IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVMMPAHG PAKNMEYDAV
     ATTHSWVPKR NRSILNTSQR GILEDEQMYQ RCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF AEIMKTCSTI EDLRRQK
//
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