RDRP_INBP9
ID RDRP_INBP9 Reviewed; 752 AA.
AC O36430;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 23-FEB-2022, entry version 68.
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/Panama/45/1990).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=408929;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9281500; DOI=10.1006/viro.1997.8682;
RA Jambrina E., Barcena J., Uez O., Portela A.;
RT "The three subunits of the polymerase and the nucleoprotein of influenza B
RT virus are the minimum set of viral proteins required for expression of a
RT model RNA template.";
RL Virology 235:209-217(1997).
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; AF005736; AAB72043.1; -; mRNA.
DR PDB; 6QWL; EM; 4.10 A; K=1-752.
DR PDBsum; 6QWL; -.
DR SMR; O36430; -.
DR IntAct; O36430; 1.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000078775"
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"
SQ SEQUENCE 752 AA; 84269 MW; 10DF3475B891168D CRC64;
MNINPYFLFI DVPIQAAIST TFPYTGVPPY SHGTGTGHTI DTVIRTHEYS NKGKQYVSDV
TGCTMVDPTN 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 PDLFSIPLER YNEETRAKLK KLKPFFNEEG TASLSPGMMM GMFNMLSTVL
GVAALGIKNI GNKEYLWDGL QSSDDFALFV NAKDEETCME GINDFYRTCK LLGINMSKKK
SYCNETGMFE FTSMFYRDGF VSNFAMEIPS FGVAGVNESA DMAIGMTIIK NNMINNGMGP
ATAQTAIQLF IADYRYTYKC HRGDSKVEGK RMKIIKELWE NTKGRDGLLV ADGGPNIYNL
RNLHIPEIVL KYNLMDPEYK GRLLHPQNPF VGHLSIEGIK EADITPAHGP VKKMDYDAVS
GTHSWRTKRN RSILNTDQRN MILEEQCYAK CCNLFEACFN SASYRKPVGQ HSMLEAMAHR
LRMDARLDYE SGRMSKDDFE KAMAHLGEIG YI