RDRP_INBAD
ID RDRP_INBAD Reviewed; 752 AA.
AC P13872; Q84079;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 75.
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 B virus (strain B/Ann Arbor/1/1966 [wild-type]).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=11523;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3354202; DOI=10.1016/0042-6822(88)90284-x;
RA Deborde D.C., Donabedian A.M., Herlocher M.L., Naeve C.W., Maassab H.F.;
RT "Sequence comparison of wild-type and cold-adapted B/Ann Arbor/1/66
RT influenza virus genes.";
RL Virology 163:429-443(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3660943; DOI=10.1016/0168-1702(87)90038-4;
RA Deborde D.C., Herlocher M.L., Maassab H.F.;
RT "Nucleotide sequences of the PA and PB1 genes of B/Ann Arbor/1/66 virus:
RT comparison with genes of B/Lee/40 and type A influenza viruses.";
RL Virus Res. 8:33-41(1987).
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 -!- 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}.
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DR EMBL; M20170; AAA43770.1; -; Genomic_RNA.
DR EMBL; M20479; AAA43768.1; -; Genomic_RNA.
DR PIR; D28604; P1IVBW.
DR SMR; P13872; -.
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-directed 5'-3' RNA polymerase activity; 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: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 3: Inferred from homology;
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 RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW Viral transcription.
FT CHAIN 1..752
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000078773"
FT DOMAIN 286..482
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
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 MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT CONFLICT 239
FT /note="R -> E (in Ref. 2; AAA43768)"
SQ SEQUENCE 752 AA; 84322 MW; 18240F96457A7C00 CRC64;
MNINPYFLFI DVPIQAAIST TFPYTGVPPY SHGTGTGYTI DTVIRTHEYS NKGKQYISDV
TGCAMVDPTN GPLPEDNEPS AYAQLDCVLE ALDRMDEEHP GLFQAASQNA MEALMVTTVD
KLTQGRQTFD WTVCRNQPAA TALNTTITSF RLNDLNGADK GGLVPFCQDI IDSLDKPEMT
FFSVKNIKKK LPAKNRKGFL IKRIPMKVKD RITRVEYIKR ALSLNTMTKD AERGKLKRRA
IATAGIQIRG FVLVVENLAK NICENLEQSG LPVGGNEKKA KLSNAVAKML SNCPPGGISM
TVTGDNTKWN ECLNPRIFLA MTERITRDSP IWFRDFCSIA PVLFSNKIAR LGKGFMITSK
TKRLKAQIPC PDLFNIPLER YNEETRAKLK KLKPFFNEEG TASLSPGMMM GMFNMLSTVL
GVAALGIKNI GNREYLWDGL QSSDDFALFV NAKDEETCME GINDFYRTCK LLGINMSKKK
SYCNETGMFE FTSMFYRDGF VSNFAMELPS FGVAGVNESA DMAIGMTIIK NNMINNGMGP
ATAQTAIQLF IADYRYTYKC HRGDSKVEGK RMKIIKELWE NTKGRDGLLV ADGGPNIYNL
RNLHIPEIVL KYNLMDPEYK GRLLHPQNPF VGHLSIEGIK EADITPAHGP IKKMDYDAVS
GTHSWRTKRN RSILNTDQRN MILEEQCYAK CCNLFEACFN SASYRKPVGQ HSMLEAMAHR
LRMDARLDYE SGRMSKDDFE KAMAHLGEIG HI
