ID   D9ZYE6_9INFA            Unreviewed;       757 AA.
AC   D9ZYE6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   10-APR-2019, entry version 44.
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:ADG59448.1};
OS   Influenza A virus (A/chicken/Shandong/A-10/2006(H5N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Negarnaviricota; Polyploviricotina; Insthoviricetes; Articulavirales;
OC   Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=762394 {ECO:0000313|EMBL:ADG59448.1, ECO:0000313|Proteomes:UP000111231};
RN   [1] {ECO:0000313|EMBL:ADG59448.1, ECO:0000313|Proteomes:UP000111231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/chicken/Shandong/A-10/2006 {ECO:0000313|EMBL:ADG59448.1};
RX   PubMed=20538856; DOI=10.1128/JVI.00413-10;
RA   Li Y., Shi J., Zhong G., Deng G., Tian G., Ge J., Zeng X., Song J.,
RA   Zhao D., Liu L., Jiang Y., Guan Y., Bu Z., Chen H.;
RT   "Continued evolution of H5N1 influenza viruses in wild birds, domestic
RT   poultry, and humans in China from 2004 to 2009.";
RL   J. Virol. 84:8389-8397(2010).
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:SAAS01123477};
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}.
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DR   EMBL; HM172376; ADG59448.1; -; Viral_cRNA.
DR   Proteomes; UP000111231; 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:UP000111231};
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;  86358 MW;  2402FB5EEC73EA47 CRC64;
     MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGALQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEIVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEIF RSNGLTVNES GRLIDFLKDV MESMDKEEME
     ITTHFQRKRR VRDNMTKKMV TRRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICDKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
     SMKLRTQIPA EMLANIDLKY FNELTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNASNHEGIQ AGVDRFYRTC KLVGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN
     IRNLHIPEAG LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARLDF ESGTIKTDEF AEIMTICSTI EELRRQK
//