ID F1AEB7_9INFA Unreviewed; 712 AA.
AC F1AEB7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00020035, ECO:0000256|RuleBase:RU004330};
DE EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494, ECO:0000256|RuleBase:RU004330};
DE Flags: Fragment;
GN Name=PB1 {ECO:0000313|EMBL:ADD64021.1};
OS Influenza A virus (A/duck/Taiwan/5906/2006(H4N6)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=706458 {ECO:0000313|EMBL:ADD64021.1};
RN [1] {ECO:0000313|EMBL:ADD64021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/duck/Taiwan/5906/2006 {ECO:0000313|EMBL:ADD64021.1};
RA Lin Y.-T., Chang N.-H., Cheng M.-C., Chiang Y.-C., Chi W.W.L.,
RA Tsai H.-H.L., Li A., Tsai H.-J.;
RT "Epidemiological and molecular analysis of H4N6 viruses isolated from wild
RT ducks and domestic ducks in Taiwan.";
RL Submitted (JAN-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 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|RuleBase:RU004330};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GU396955; ADD64021.1; -; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.720; -; 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 4: Predicted;
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023247};
KW Eukaryotic host transcription shutoff by virus
KW {ECO:0000256|ARBA:ARBA00022731};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Inhibition of host RNA polymerase II by virus
KW {ECO:0000256|ARBA:ARBA00023103};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000256|RuleBase:RU004330};
KW Transferase {ECO:0000256|ARBA:ARBA00022484, ECO:0000256|RuleBase:RU004330};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Viral transcription {ECO:0000256|ARBA:ARBA00023314}.
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 53..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 712
FT /evidence="ECO:0000313|EMBL:ADD64021.1"
SQ SEQUENCE 712 AA; 81070 MW; C1AAB12D63A59989 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGRWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLANIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKK YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
ATTHSWIPKR NRSILNTSQR GILEDGQMYQ KCCSLFEKFF PSSSYRRPVG IS
//