RDRP_INCAA
ID RDRP_INCAA Reviewed; 754 AA.
AC Q6I7C3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 59.
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 C virus (strain C/Ann Arbor/1/1950).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX NCBI_TaxID=11553;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15218173; DOI=10.1099/vir.0.79937-0;
RA Muraki Y., Washioka H., Sugawara K., Matsuzaki Y., Takashita E., Hongo S.;
RT "Identification of an amino acid residue on influenza C virus M1 protein
RT responsible for formation of the cord-like structures of the virus.";
RL J. Gen. Virol. 85:1885-1893(2004).
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; AB126192; BAD24938.1; -; Genomic_RNA.
DR RefSeq; YP_089653.1; NC_006308.1.
DR SMR; Q6I7C3; -.
DR GeneID; 3077364; -.
DR KEGG; vg:3077364; -.
DR Proteomes; UP000008286; Genome.
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 Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Viral transcription.
FT CHAIN 1..754
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000269452"
FT DOMAIN 288..484
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT REGION 251..258
FT /note="Promoter-binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 189..197
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 205..218
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
SQ SEQUENCE 754 AA; 86071 MW; 231868DA7F7032A0 CRC64;
MEINPYLMFL NNDVTSLIST TYPYTGPPPM SHGSSTKYTL ETIKRTYDYS RTSVEKTSKV
FNIPRRKFCN CLEDKDELVK PTGNVDISSL LGLAEMMEKR MGEGFFKHCV MEAETEILKM
HFSRLTEGRQ TYDWTSERNM PAATALQLTV DAIKETEGPF KGTTMLEYCN KMIEMLDWKE
VKFRKVKTMV RREKDKRSGK EIKTKVPVMG IDSIKHDEFL IRALTINTMA KDGERGKLQR
RAIATPGMIV RPFSKIVETV AQKICEKLKE SGLPVGGNEK KAKLKTTVTS LNARMNSDQF
AVNITGDNSK WNECQQPEAY LALLAYITKD SSDLMKDLCS VAPVLFCNKF VKLGQGIRLS
NKRKTKEVII KAEKMGKYKN LMREEYKNLF EPLEKYIQKD VCFLPGGMLM GMFNMLSTVL
GVSTLCYMDE ELKAKGCFWT GLQSSDDFVL FAVASNWSNI HWTIRRFNAV CKLIGINMSL
EKSYGSLPEL FEFTSMFFDG EFVSNLAMEL PAFTTAGVNE GVDFTAAMSI IKTNMINNSL
SPSTALMALR ICLQEFRATY RVHPWDSRVK GGRMKIINEF IKTIENKDGL LIADGGKLMN
NISTLHIPEE VLKFEKMDEQ YRNRVFNPKN PFTNFDKTID IFRAHGPIRV EENEAVVSTH
SFRTRANRTL LNTDMRAMMA EEKRYQMVCD MFKSVFESAD INPPIGAMSI GEAIEEKLLE
RAKMKRDIGA IEDSEYEEIK DIIRDAKKAR IESR
