ID B7UDH0_9INFA Unreviewed; 725 AA.
AC B7UDH0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:ACJ68807.1};
OS Influenza A virus (A/chicken/Henan/L3/2008(H9N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=543530 {ECO:0000313|EMBL:ACJ68807.1};
RN [1] {ECO:0000313|EMBL:ACJ68807.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/chicken/Henan/L3/2008 {ECO:0000313|EMBL:ACJ68807.1};
RX PubMed=20347894; DOI=10.1016/j.virusres.2010.03.010;
RA Huang Y., Hu B., Wen X., Cao S., Gavrilov B.K., Du Q., Khan M.I., Zhang X.;
RT "Diversified reassortant H9N2 avian influenza viruses in chicken flocks in
RT northern and eastern China.";
RL Virus Res. 151:26-32(2010).
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; FJ492969; ACJ68807.1; -; 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-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 254..451
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ68807.1"
SQ SEQUENCE 725 AA; 83115 MW; A58D3AF0CD45A65B CRC64;
GTGTGYTMDT VNRTHQYSEK GKWTTNTETK APQLNPIDGP LPDNNEPSGY AQTDCVLEAM
AFLEESHPGI FENSCLETIE VVQQTRVDKL TQGRQTYDWT LNRNQPAATA LANTIEVFRS
NGLTTNESGR LIDFLKDVMD SMDKEEMEVT THFQRKRRVR DNMTKKMITQ RTIGKKKQRL
NRRSYLIRAL TLNTMTKDAE RGKLKRRAIA TPGMQIRGFV YFVETLARSI CEKLEQSGLP
VGGNEKKAKL ANVVRKMMTN SQDTELSFTI TGDNTKWNEN QNPRVFLAMI TYITRNQPEW
FRNVLSIAPI MFSNKMARLG KGYMFESKIM RLRTQIPAEM LATIDLKYFN ESTRQKIEKI
RPLLIEGTAS LSPGMMMGMF NMLSTVLGVS ILNLGQKKYT KTTYWWDGLQ SSDDFALIVN
APNYEGIQAG VDRFYRTCKL VGINMSKKKS YINRTGTFEF TSFFYRYGFV ANFSMELPSF
GVSGVNESAD MSIGITVIKN NMINNDLGPA TAQMALQLFI KDYRYTYRCH RGDTQIQTRR
SFELKKLWEQ TRSKTGLLVS DGGPNLYNIR NLHIPEVCLK WELMDEDYRG RLCNPMNPFV
SHKEIESVNN AVVMPAHGPA KSMEYDAVAT THSWIPKRDR SILNTSQRGI LEDEQMYQKC
CNLFEKFFPS SSYRRPVGIS SMVEAMVSRA RIDARIDFES GRIKKEEFAE IMKICSTIEE
LRRQK
//
