ID B5SN21_9INFA Unreviewed; 757 AA. AC B5SN21; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 30-NOV-2016, entry version 43. DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|RuleBase:RU004330, ECO:0000256|SAAS:SAAS00509014}; DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU004330, ECO:0000256|SAAS:SAAS00518168}; DE Flags: Fragment; GN Name=PB1 {ECO:0000313|EMBL:ACH85528.1}; OS Influenza A virus (A/turkey/England/N28/1973(H5N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=511839 {ECO:0000313|EMBL:ACH85528.1}; RN [1] {ECO:0000313|EMBL:ACH85528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/turkey/England/N28/1973 {ECO:0000313|EMBL:ACH85528.1}; RX PubMed=18774155; DOI=10.1016/j.virol.2008.07.038; RA Duan L., Bahl J., Smith G.J., Wang J., Vijaykrishna D., Zhang L.J., RA Zhang J.X., Li K.S., Fan X.H., Cheung C.L., Huang K., Poon L.L., RA Shortridge K.F., Webster R.G., Peiris J.S., Chen H., Guan Y.; RT "The development and genetic diversity of H5N1 influenza virus in RT China, 1996-2006."; RL Virology 380:243-254(2008). 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:SAAS00509027}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|RuleBase:RU004330, CC ECO:0000256|SAAS:SAAS00605060}. 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:SAAS00508961}. CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 CC family. {ECO:0000256|SAAS:SAAS00565435}. 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; CY030991; ACH85528.1; -; 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 3: Inferred from homology; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|SAAS:SAAS00509101}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|SAAS:SAAS00509023}; KW Host gene expression shutoff by virus {ECO:0000256|SAAS:SAAS00509081}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00509044}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|SAAS:SAAS00508975}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00605058}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00605055}; KW RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU004330, KW ECO:0000256|SAAS:SAAS00605053}; KW Transferase {ECO:0000256|SAAS:SAAS00605061}; KW Viral RNA replication {ECO:0000256|SAAS:SAAS00605045}; KW Viral transcription {ECO:0000256|SAAS:SAAS00509109}. FT DOMAIN 286 483 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50525}. FT NON_TER 757 757 {ECO:0000313|EMBL:ACH85528.1}. SQ SEQUENCE 757 AA; 86508 MW; BF6D02909363CF5F CRC64; MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPR GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK SMKLRTQIPA EMLANIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYKRPVG ISSMVEAMVS RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK //