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Database: UniProt
Entry: G7WS77_9INFA
LinkDB: G7WS77_9INFA
Original site: G7WS77_9INFA 
ID   G7WS77_9INFA            Unreviewed;       757 AA.
AC   G7WS77;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00020035, ECO:0000256|RuleBase:RU004330};
DE            EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494, ECO:0000256|RuleBase:RU004330};
DE   Flags: Fragment;
GN   Name=PB1 {ECO:0000313|EMBL:AER24145.1};
OS   Influenza A virus (A/Hong Kong/HKU104/2005(H3N2)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=1101409 {ECO:0000313|EMBL:AER24145.1};
RN   [1] {ECO:0000313|EMBL:AER24145.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Hong Kong/HKU104/2005 {ECO:0000313|EMBL:AER24145.1};
RA   Bahl J., Nelson M.I., Kwok C.H., Rubing C., Vijakrishna D., Halpin R.,
RA   Stockwell T., Lin X., Wentworth D.E., Ghedin E., Guan Y., Peirisa M.J.,
RA   Riley S., Rambaut A., Holmes E.C., Smith G.J.;
RT   "Temporally structured meta-population dynamics and persistence of human
RT   influenza A H3N2 virus.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002148}.
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:0000256|RuleBase:RU004330};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus
CC       {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CY100162; AER24145.1; -; Viral_cRNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.720; -; 1.
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   {ECO:0000256|ARBA:ARBA00023247};
KW   Eukaryotic host transcription shutoff by virus
KW   {ECO:0000256|ARBA:ARBA00022731};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Inhibition of host RNA polymerase II by virus
KW   {ECO:0000256|ARBA:ARBA00023103};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW   ECO:0000256|RuleBase:RU004330};
KW   Transferase {ECO:0000256|ARBA:ARBA00022484, ECO:0000256|RuleBase:RU004330};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Viral transcription {ECO:0000256|ARBA:ARBA00023314}.
FT   DOMAIN          286..483
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50525"
FT   REGION          50..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         757
FT                   /evidence="ECO:0000313|EMBL:AER24145.1"
SQ   SEQUENCE   757 AA;  86364 MW;  B29748776AF0083F CRC64;
     MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEAVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV VESMDKEEME
     ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRGYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNILSIA PIMFSNKMAR LGKGYMFESK
     RMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKK YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
     KSYINKTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW DQTQSRAGLL VSDGGPNLYN
     IRNLHIPEVC LKWELMDENY RGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPIG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF SEIMKICSTI EELRRQK
//
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