ID D9TZC7_9INFA Unreviewed; 757 AA.
AC D9TZC7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ADL39244.1};
OS Influenza A virus (A/Alaska/WRAIR1114P/2009(H1N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=871605 {ECO:0000313|EMBL:ADL39244.1};
RN [1] {ECO:0000313|EMBL:ADL39244.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Alaska/WRAIR1114P/2009 {ECO:0000313|EMBL:ADL39244.1};
RA Houng H.-S., Zhou Y., Lyons A., Kuschner R.A.;
RT "Full genome sequencing of Influenza by Roche 454 FLX.";
RL Submitted (AUG-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; CY069379; ADL39244.1; -; Viral_cRNA.
DR SMR; D9TZC7; -.
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-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..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"
SQ SEQUENCE 757 AA; 86320 MW; 646E7921E127C2F1 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS ERGRWTKNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCIET MEVVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLIANES GRLIDFLKDV MESMDRGEVE
VTTHFQRKRR VRDNVTKKMV TQRTIGKKKH KLDKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTEISF
TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNILSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLANIDLKY FNDSTKKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNYAGIQ AGVDRFYRTC KLLGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGVNES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFEIKKLW DQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NSAVIMPAHG PAKNMEYDAV
ATTHSWVPKR NRSILNTSQR GILEDEQMYQ RCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF AEIMKICSTI EDLRRQK
//