ID X2DR70_9INFA Unreviewed; 757 AA. AC X2DR70; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 28-MAR-2018, entry version 23. DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|HAMAP-Rule:MF_04065}; DE EC=2.7.7.48 {ECO:0000256|HAMAP-Rule:MF_04065}; DE AltName: Full=Polymerase basic protein 1 {ECO:0000256|HAMAP-Rule:MF_04065}; DE Short=PB1 {ECO:0000256|HAMAP-Rule:MF_04065}; DE AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000256|HAMAP-Rule:MF_04065}; GN Name=PB1 {ECO:0000256|HAMAP-Rule:MF_04065, GN ECO:0000313|EMBL:AHL81439.1}; OS Influenza A virus (A/Tennessee/F1080/2010(H1N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=1452594 {ECO:0000313|EMBL:AHL81439.1, ECO:0000313|Proteomes:UP000115638}; RN [1] {ECO:0000313|EMBL:AHL81439.1, ECO:0000313|Proteomes:UP000115638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Tennessee/F1080/2010 {ECO:0000313|EMBL:AHL81439.1}; RA Wentworth D.E., Halpin R.A., Lin X., Bera J., Ransier A., Fedorova N., RA Tsitrin T., McLellan M., Stockwell T., Amedeo P., Appalla L., RA Bishop B., Edworthy P., Gupta N., Hoover J., Katzel D., Li K., RA Schobel S., Shrivastava S., Thovarai V., Wang S., Oshansky C.M., RA Wong S.S., Webby R., Bao Y., Sanders R., Zhdanov S., Kiryutin B., RA Lipman D.J., Tatusova T., Thomas P.G.; RT "The NIAID Influenza Genome Sequencing Project."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AHL81439.1, ECO:0000313|Proteomes:UP000115638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Tennessee/F1080/2010 {ECO:0000313|EMBL:AHL81439.1}; RG The NIAID Influenza Genome Sequencing Consortium; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. 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 copies CC vRNA into complementary RNA (cRNA) which in turn serves as a CC template for the production of more vRNAs. {ECO:0000256|HAMAP- CC Rule:MF_04065}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|HAMAP-Rule:MF_04065, CC ECO:0000256|RuleBase:RU004330, 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|HAMAP-Rule:MF_04065}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04065}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04065}. CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000256|HAMAP- CC Rule:MF_04065}. CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 CC family. {ECO:0000256|HAMAP-Rule:MF_04065, CC ECO:0000256|SAAS:SAAS00997533}. 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; CY167786; AHL81439.1; -; Viral_cRNA. DR Proteomes; UP000115638; Genome. 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:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR GO; GO:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule. 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 Complete proteome {ECO:0000313|Proteomes:UP000115638}; KW Eukaryotic host gene expression shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Eukaryotic host transcription shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04065}; Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04065}; KW Host gene expression shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04065}; Host nucleus {ECO:0000256|HAMAP-Rule:MF_04065}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04065}; KW Inhibition of host RNA polymerase II by virus {ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS00605058}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS00605055}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04065}; KW RNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|RuleBase:RU004330, ECO:0000256|SAAS:SAAS00605053}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS00605061}; KW Viral RNA replication {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS00605045}; KW Viral transcription {ECO:0000256|HAMAP-Rule:MF_04065}. FT DOMAIN 286 483 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50525}. FT REGION 249 256 Promoter-binding site. FT {ECO:0000256|HAMAP-Rule:MF_04065}. FT MOTIF 187 195 Nuclear localization signal. FT {ECO:0000256|HAMAP-Rule:MF_04065}. FT MOTIF 203 216 Nuclear localization signal. FT {ECO:0000256|HAMAP-Rule:MF_04065}. SQ SEQUENCE 757 AA; 86323 MW; E99C4D5A768A9223 CRC64; MDVNPTLLFL KIPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMNKEEIE ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRGYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTEISF TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNILSMA PIMFSNKMAR LGKGYMFESK RMKIRTQIPA EMLASIDLKY FNESTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG VSILNLGQKK YTKTIYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK KSYINKTGTF EFTSFFYRYG FVANFSMELP SFGVSGVNES ADMSIGVTVI KNNMINNDLG PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW DQTQSKVGLL VSDGGPNLYN IRNLHIPEVC LKWELMDDDY RGRLCNPLNP FVSHKEIDSV NNAVVMPAHG PAKSMEYDAV ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS RARIDARVDF ESGRIGKEEF SEIMKICSTI EELRRQK //