ID   D9ZYE6_9INFA            Unreviewed;       757 AA.
AC   D9ZYE6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JUN-2015, entry version 25.
DE   RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|RuleBase:RU004330, ECO:0000256|SAAS:SAAS00075198};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU004330, ECO:0000256|SAAS:SAAS00075368};
GN   Name=PB1 {ECO:0000313|EMBL:ADG59448.1};
OS   Influenza A virus (A/chicken/Shandong/A-10/2006(H5N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=762394 {ECO:0000313|EMBL:ADG59448.1};
RN   [1] {ECO:0000313|EMBL:ADG59448.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Shandong/A-10/2006 {ECO:0000313|EMBL:ADG59448.1};
RX   PubMed=20538856; DOI=10.1128/JVI.00413-10;
RA   Li Y., Shi J., Zhong G., Deng G., Tian G., Ge J., Zeng X., Song J.,
RA   Zhao D., Liu L., Jiang Y., Guan Y., Bu Z., Chen H.;
RT   "Continued evolution of H5N1 influenza viruses in wild birds, domestic
RT   poultry, and humans in China from 2004 to 2009.";
RL   J. Virol. 84:8389-8397(2010).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC       replication and transcription of virus RNA segments. The
CC       transcription of viral mRNAs occurs by a unique mechanism called
CC       cap-snatching. 5' methylated caps of cellular mRNAs are cleaved
CC       after 10-13 nucleotides by PA. In turn, these short capped RNAs
CC       are used as primers by PB1 for transcription of viral mRNAs.
CC       During virus replication, PB1 initiates RNA synthesis and copy
CC       vRNA into complementary RNA (cRNA) which in turn serves as a
CC       template for the production of more vRNAs.
CC       {ECO:0000256|SAAS:SAAS00239651}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000256|RuleBase:RU004330,
CC       ECO:0000256|SAAS:SAAS00075363}.
CC   -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits:
CC       PB1, PB2 and PA. Interacts (via N-terminus) with PA (via C-
CC       terminus). Interacts (via C-terminus) with PB2 (via N-terminus);
CC       this interaction is essential for transcription initiation.
CC       {ECO:0000256|SAAS:SAAS00239426}.
CC   -!- SIMILARITY: Contains RdRp catalytic domain.
CC       {ECO:0000256|SAAS:SAAS00075384}.
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DR   EMBL; HM172376; ADG59448.1; -; Viral_cRNA.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
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   4: Predicted;
KW   Eukaryotic host gene expression shutoff by virus
KW   {ECO:0000256|SAAS:SAAS00239605};
KW   Eukaryotic host transcription shutoff by virus
KW   {ECO:0000256|SAAS:SAAS00239775};
KW   Host gene expression shutoff by virus {ECO:0000256|SAAS:SAAS00239728};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00239786};
KW   Inhibition of host RNA polymerase II by virus
KW   {ECO:0000256|SAAS:SAAS00239606};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00075381};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00075370};
KW   Phosphoprotein {ECO:0000256|SAAS:SAAS00239722};
KW   RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU004330,
KW   ECO:0000256|SAAS:SAAS00075383};
KW   Transferase {ECO:0000256|SAAS:SAAS00075364};
KW   Viral RNA replication {ECO:0000256|SAAS:SAAS00075204};
KW   Viral transcription {ECO:0000256|SAAS:SAAS00239449}.
SQ   SEQUENCE   757 AA;  86358 MW;  2402FB5EEC73EA47 CRC64;
     MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGALQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEIF RSNGLTVNES GRLIDFLKDV MESMDKEEME
     ITTHFQRKRR VRDNMTKKMV TRRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICDKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
     SMKLRTQIPA EMLANIDLKY FNELTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNASNHEGIQ AGVDRFYRTC KLVGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN
     IRNLHIPEAG LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARLDF ESGTIKTDEF AEIMTICSTI EELRRQK
//