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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
 
 
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