ID A0A218KD47_9INFA Unreviewed; 757 AA. AC A0A218KD47; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 19-JAN-2022, entry version 21. 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:AKT07774.1}; OS Influenza A virus (A/goose/Guangxi/158/2013(H6N2)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1680663 {ECO:0000313|EMBL:AKT07774.1}; RN [1] {ECO:0000313|EMBL:AKT07774.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/goose/Guangxi/158/2013 {ECO:0000313|EMBL:AKT07774.1}; RA Li M., Xie Z.X., Xie L.J., Deng X.W., Xie Q.Z., Liu J.B., Fan Q., RA Pang Y.S., Luo S.S.; RT "Genetic Characterization of H6 Subtype Avian Influenza Virus."; RL Submitted (JUL-2015) 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 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 copies vRNA into complementary RNA (cRNA) which in CC turn serves as a template for the production of more vRNAs. CC {ECO:0000256|HAMAP-Rule:MF_04065}. 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|HAMAP-Rule:MF_04065, CC 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, ECO:0000256|HAMAP-Rule:MF_04065}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host CC nucleus {ECO:0000256|HAMAP-Rule:MF_04065}. Host cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_04065}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000256|HAMAP-Rule:MF_04065}. CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family. CC {ECO:0000256|HAMAP-Rule:MF_04065}. 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; KT267004; AKT07774.1; -; 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: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 mRNA transcription via inhibition of 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 Eukaryotic host gene expression shutoff by virus {ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|ARBA:ARBA00022731, ECO:0000256|HAMAP-Rule:MF_04065}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Host gene expression shutoff by virus {ECO:0000256|HAMAP-Rule:MF_04065}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04065}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|ARBA:ARBA00023103, ECO:0000256|HAMAP-Rule:MF_04065}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04065}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04065}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_04065}; KW RNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_04065, KW ECO:0000256|RuleBase:RU004330}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_04065}; KW Viral RNA replication {ECO:0000256|HAMAP-Rule:MF_04065}; KW Viral transcription {ECO:0000256|ARBA:ARBA00023314, ECO:0000256|HAMAP- KW Rule:MF_04065}. FT DOMAIN 286..483 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50525" FT REGION 50..82 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..256 FT /note="Promoter-binding site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065" FT MOTIF 187..195 FT /note="Nuclear localization signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065" FT MOTIF 203..216 FT /note="Nuclear localization signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04065" FT COMPBIAS 50..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 757 AA; 86386 MW; 334097406268785E CRC64; MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQRTRVD KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMNREEME ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNRRSYLIR ALTLNTMTKD AERGKLKRRA IATPGMQIRG FVYFVETLAK NICEKLEQSG LPVGGNEKKA KLANVVRKTM TNSQDTEPSF TITGDNTKWN ENQNPRIFLT MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK IMKLRTQISA EMLANIDLKY FNESTRKKIE KIRPLLIEGT ASLSPGMMMG MFNMLSTVLG VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFCRTC KLVGINMSKK KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG PATAQMALQL FIKDYRYTYR CHRGDTQIQT GRSFELKKLW EQTRSKAGLL VSDGGPNLYN IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK //