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Database: UniProt
Entry: D8KVY1_9INFA
LinkDB: D8KVY1_9INFA
Original site: D8KVY1_9INFA 
ID   D8KVY1_9INFA            Unreviewed;       757 AA.
AC   D8KVY1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
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:ADK33979.1};
OS   Influenza A virus (A/Bonn/INS284/2009(H1N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=856420 {ECO:0000313|EMBL:ADK33979.1, ECO:0000313|Proteomes:UP000101919};
RN   [1] {ECO:0000313|EMBL:ADK33979.1, ECO:0000313|Proteomes:UP000101919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Bonn/INS284/2009 {ECO:0000313|EMBL:ADK33979.1};
RA   Spiro D., Halpin R., Bera J., Ghedin E., Hostetler J., Fedorova N.,
RA   Hine E., Overton L., Kim M., Szczypinski B., Stockwell T., Sitz J.,
RA   Katzel D., Li K., Axelrod N., Safford T., Amedeo P., Schobel S.,
RA   Shrivastava S., Wang S., Resnick A., Thovarai V., Lynfield R., Losso M.,
RA   Davey R., Dwyer D., Neaton J., Lane C., Lin X., Wentworth D.E., Bao Y.,
RA   Sanders R., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADK33979.1, ECO:0000313|Proteomes:UP000101919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Bonn/INS284/2009 {ECO:0000313|EMBL:ADK33979.1};
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (JUL-2010) 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. {ECO:0000256|HAMAP-
CC       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}.
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DR   EMBL; CY067181; ADK33979.1; -; Viral_cRNA.
DR   SMR; D8KVY1; -.
DR   Proteomes; UP000101919; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; 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-dependent RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:DNA-templated transcription; 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:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.720; -; 1.
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:ARBA00023247, ECO:0000256|HAMAP-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|ARBA:ARBA00022995,
KW   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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW   ECO:0000256|HAMAP-Rule:MF_04065};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_04065};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, ECO:0000256|HAMAP-
KW   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..76
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;  86394 MW;  E99C4D5A76832463 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 ESGRIKKEEF SEIMKICSTI EELRRQK
//
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