ID D9ZYG9_9INFA Unreviewed; 757 AA. AC D9ZYG9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 22-JUL-2015, entry version 26. 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:ADG59471.1}; OS Influenza A virus (A/chicken/Xinjiang/17/2005(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=762400 {ECO:0000313|EMBL:ADG59471.1}; RN [1] {ECO:0000313|EMBL:ADG59471.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/Xinjiang/17/2005 {ECO:0000313|EMBL:ADG59471.1}; 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:SAAS00276591}. 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:SAAS00276615}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HM172399; ADG59471.1; -; 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:SAAS00276578}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00276602}; KW Phosphoprotein {ECO:0000256|SAAS:SAAS00239722}; KW RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU004330, KW ECO:0000256|SAAS:SAAS00276589}; KW Transferase {ECO:0000256|SAAS:SAAS00276586}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00276580}; KW Viral transcription {ECO:0000256|SAAS:SAAS00239449}. SQ SEQUENCE 757 AA; 86371 MW; 8B0AAE352646CE79 CRC64; MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEIF RSNGLTANES GRLIDFLKDV MESMDKEEME ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKKSYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK SMKLRTQIPA EMLANIDLKY FNELTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK KSYINRTGTF EFTSFFYRYG FVANFSMELP SLGVSGINES ADMSIGVTVI KNNMINNDLG PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN IRNLHIPEAG LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK //