ID B5SN21_9INFA Unreviewed; 757 AA. AC B5SN21; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 29-SEP-2021, entry version 62. 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:ACH85528.1}; OS Influenza A virus (A/turkey/England/N28/1973(H5N2)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. 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 China, RT 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 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 -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1, CC PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus). CC Interacts (via C-terminus) with PB2 (via N-terminus); this interaction CC is essential for transcription initiation. CC {ECO:0000256|ARBA:ARBA00011318}. 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}. 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' 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:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW. 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:ARBA00023103}; 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:ARBA00023103}; 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 Nucleotidyltransferase {ECO:0000256|RuleBase:RU004330}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU004330}; KW Transferase {ECO:0000256|RuleBase:RU004330}; KW Viral transcription {ECO:0000256|ARBA:ARBA00023314}. FT DOMAIN 286..483 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50525" FT REGION 50..81 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: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 //