RDRP_I33A0
ID RDRP_I33A0 Reviewed; 757 AA.
AC P03430;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_04065};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=Polymerase basic protein 1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE Short=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000255|HAMAP-Rule:MF_04065};
GN Name=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
OS Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus
OS (strain A/WS/1933 H1N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=381518;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7143569; DOI=10.1128/jvi.44.1.321-329.1982;
RA Sivasubramanian N., Nayak D.P.;
RT "Sequence analysis of the polymerase 1 gene and the secondary structure
RT prediction of polymerase 1 protein of human influenza virus A/WSN/33.";
RL J. Virol. 44:321-329(1982).
RN [2]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=2196448; DOI=10.1128/mcb.10.8.4139-4145.1990;
RA Nath S.T., Nayak D.P.;
RT "Function of two discrete regions is required for nuclear localization of
RT polymerase basic protein 1 of A/WSN/33 influenza virus (H1 N1).";
RL Mol. Cell. Biol. 10:4139-4145(1990).
RN [3]
RP MUTAGENESIS OF ARG-233; LYS-235; ARG-238; ARG-239; ARG-249; PHE-251;
RP PHE-254; SER-269; VAL-273; LYS-278 AND LYS-281.
RX PubMed=16476991; DOI=10.1099/vir.0.81453-0;
RA Jung T.E., Brownlee G.G.;
RT "A new promoter-binding site in the PB1 subunit of the influenza A virus
RT polymerase.";
RL J. Gen. Virol. 87:679-688(2006).
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:0000255|HAMAP-Rule:MF_04065}.
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:0000255|HAMAP-Rule:MF_04065};
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:0000255|HAMAP-
CC Rule:MF_04065}.
CC -!- INTERACTION:
CC P03430; P03427: PB2; NbExp=3; IntAct=EBI-8434155, EBI-8430745;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}.
CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04065}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02178; AAA43582.1; ALT_SEQ; Genomic_RNA.
DR PIR; A04046; P1IV33.
DR SMR; P03430; -.
DR IntAct; P03430; 23.
DR MINT; P03430; -.
DR Proteomes; UP000000834; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
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:0019083; P:viral transcription; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
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; Inhibition of host RNA polymerase II by virus;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Viral transcription.
FT CHAIN 1..757
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000078767"
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
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:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 187..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065,
FT ECO:0000269|PubMed:2196448"
FT MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065,
FT ECO:0000269|PubMed:2196448"
FT MUTAGEN 233
FT /note="R->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 235
FT /note="K->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 238
FT /note="R->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 239
FT /note="R->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 249
FT /note="R->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 251
FT /note="F->A: 20% loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 254
FT /note="F->A: 50% loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 269
FT /note="S->A: 70% loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 273
FT /note="V->A: 80% loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 278
FT /note="K->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
FT MUTAGEN 281
FT /note="K->A: Complete loss of RNA synthesis in vitro."
FT /evidence="ECO:0000269|PubMed:16476991"
SQ SEQUENCE 757 AA; 86534 MW; D5A0E8133CDE37F4 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS ERGRWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFETSCLET MEVVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMNKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKRKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTEISF
TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKIRTQIPA EMLASIDLKY FNDSTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR HTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVNRFYRTC KLLGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW EQTHSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVNHKDIESV NNAVIMPAHG PAKNMEYDAV
ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF TEIMKICSTI EELRRQK
