ID A0A514CA69_9INFA Unreviewed; 757 AA. AC A0A514CA69; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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:QDH76436.1}; OS Influenza A virus. OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; OC Alphainfluenzavirus. OX NCBI_TaxID=11320 {ECO:0000313|EMBL:QDH76436.1}; RN [1] {ECO:0000313|EMBL:QDH76436.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/goose/Guangdong/A-Goose-Guangdong-GS119- 2015 RC {ECO:0000313|EMBL:QDH76436.1}; RA Jiao P.; RT "Different Pathogenicity and Transmissibility of Goose-Origin H5N6 RT Avian Influenza Viruses in Chickens."; RL Submitted (JUL-2019) 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: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04065, ECO:0000256|RuleBase:RU004330, CC ECO:0000256|SAAS:SAAS01176592}; 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; MN128673; QDH76436.1; -; Viral_cRNA. 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 {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:SAAS01176568}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS01176569}; 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:SAAS01176590}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS01176594}; KW Viral RNA replication {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|SAAS:SAAS01176589}; KW Viral transcription {ECO:0000256|HAMAP-Rule:MF_04065}. FT DOMAIN 286 483 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50525}. FT REGION 53 78 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. 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; 86387 MW; 33A5987AB9EFDD9E CRC64; MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGEWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESVDKEVME ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK SMKLRTQIPA EMLANIDLKY FNESTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG VSILNLGQKR YTKTTYWWDG LQSSDDFALI INAPNHEGIQ AGVDRFYRTC KLVGINMSKK KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHREIESV NNAIVMPAHG PAKGIEYDAV ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCSLFEKFF PSSSYRRPVG ISSMVEAMVS RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK //