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Database: UniProt
Entry: F0TZB5_9INFA
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ID   F0TZB5_9INFA            Unreviewed;       755 AA.
AC   F0TZB5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:ADY71315.1};
OS   Influenza A virus (A/swine/Hong Kong/1111/2004(H1N2)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=991680 {ECO:0000313|EMBL:ADY71315.1};
RN   [1] {ECO:0000313|EMBL:ADY71315.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/swine/Hong Kong/1111/2004 {ECO:0000313|EMBL:ADY71315.1};
RX   PubMed=21614079; DOI=10.1038/nature10004;
RA   Vijaykrishna D., Smith G.J., Pybus O.G., Zhu H., Bhatt S., Poon L.L.,
RA   Riley S., Bahl J., Ma S.K., Cheung C.L., Perera R.A., Chen H.,
RA   Shortridge K.F., Webby R.J., Webster R.G., Guan Y., Peiris J.S.;
RT   "Long-term evolution and transmission dynamics of swine influenza A
RT   virus.";
RL   Nature 473:519-522(2011).
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; CY085660; ADY71315.1; -; 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..76
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         755
FT                   /evidence="ECO:0000313|EMBL:ADY71315.1"
SQ   SEQUENCE   755 AA;  86279 MW;  D9A67B4B8EFCDCA9 CRC64;
     MDVNPTLLFL KIPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEIE
     ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRGYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNILSMA PIMFSNKMAR LGKGYMFESK
     RMKLRTQIPA EMLANIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKK YTRTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKR
     KSYINKTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW DQTQSKAGLL VSDGGPNLYN
     IRNLHIPEVC LKWELMDEDY RGRLCNPLNP FVSHKEIDSV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTNQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF SEIMKICSTI EELRR
//
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