ID C6Y5G8_9INFA Unreviewed; 751 AA.
AC C6Y5G8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ACT84290.1};
OS Influenza A virus (A/mallard/Minnesota/Sg-00448/2008(H6N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=657729 {ECO:0000313|EMBL:ACT84290.1};
RN [1] {ECO:0000313|EMBL:ACT84290.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/mallard/Minnesota/Sg-00448/2008
RC {ECO:0000313|EMBL:ACT84290.1};
RA Sreevatsan S., Ramakrishnan M.A., Wang P., Anderson T.L., Jindal N.,
RA Chander Y., Goyal S.M., Osterholm M.T.;
RT "unpublished.";
RL Submitted (JUL-2009) 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; CY042330; ACT84290.1; -; 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 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};
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 280..477
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 44..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACT84290.1"
SQ SEQUENCE 751 AA; 85822 MW; D3523F3B42994EE3 CRC64;
LLFLKVPVQN AISTTFPYTG DPPYSHGTGT GYTMDTVNRT HQYSEKGKWT TNTETGAPQL
NPIDGPLPED NEPSGYAQTD CVLEAMAFLE ESHPGIFENS CLETMEVVQQ TRVDKLTQGR
QTYDWTLNRN QPAATALANT IEVFRSNGLT ANESGRLIDF LKDVMESMDK EEMEITTHFQ
RKRRVRDNMT KKMVTQRTIG KKKQRLNKRS YLIRALTLNT MTKDAERGKL KRRAIATPGM
QIRGFVYFVE TLARSICEKL EQSGLPVGGN EKKAKLANVV RKMMTNSQDT ELSFTITGDN
TKWNENQNPR MFLAMITYIT RNQPEWFRNV LSIAPIMFSN KMARLGKGYM FESKSMKLRT
QIPAEMLASI DLKYFNESTR KKIERIRPLL IDGTASLSPG MMMGMFNMLS TVLGVSILNL
GQKRYTKTTY WWDGLQSSDD FALIVNAPNH EGIQAGVDRF YRACKLVGIN MSKKKSYINR
TGTFEFTSFF YRYGFVANFS MELPSFGVSG INESADMSIG VTVIKNNMIN NDLGPATAQM
ALQLFIKDYR YTYRCHRGDT QIQTRRSFEL KKLWEQTRSK AGLLVSDGGP NLYNIRNLHI
PEVCLKWELM DEDYQGRLCN PLNPFVSHKE IESVNNAVVM PAHGPAKSME YDAVATTHSW
IPKRNRSILN TSQRGILEDE QMYQKCCNLF EKFFPSSSYR RPVGISSMVE AMVSRARIDA
RIDFESGRIK KEEFAEIMKI CSTIEELRRR K
//
