ID Q9DRJ9_9INFA Unreviewed; 454 AA.
AC Q9DRJ9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00020035};
DE EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494};
DE Flags: Fragment;
GN Name=PB1 {ECO:0000313|EMBL:AAG48199.1};
OS Influenza A virus (A/Silky Chicken/Hong Kong/SF44/99(H9N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=138807 {ECO:0000313|EMBL:AAG48199.1};
RN [1] {ECO:0000313|EMBL:AAG48199.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/Silky Chicken/Hong Kong/SF44/99
RC {ECO:0000313|EMBL:AAG48199.1};
RX PubMed=11000205; DOI=10.1128/JVI.74.20.9372-9380.2000;
RA Guan Y., Shortridge K.F., Krauss S., Chin P.S., Dyrting K.C., Ellis T.M.,
RA Webster R.G., Peiris M.;
RT "H9N2 influenza viruses possessing H5N1-like internal genomes continue to
RT circulate in poultry in southeastern China.";
RL J. Virol. 74:9372-9380(2000).
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 -!- 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; AF222641; AAG48199.1; -; Genomic_RNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR001407; RNA_pol_PB1_influenza.
DR Pfam; PF00602; Flu_PB1; 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}; Membrane {ECO:0000256|SAM:Phobius};
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 Transferase {ECO:0000256|ARBA:ARBA00022484};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Viral transcription {ECO:0000256|ARBA:ARBA00023314}.
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..454
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG48199.1"
FT NON_TER 454
FT /evidence="ECO:0000313|EMBL:AAG48199.1"
SQ SEQUENCE 454 AA; 51739 MW; 64443C96170CD5AB CRC64;
QNAISTTFPY TGDPPYSHGT GTGYTMDTVN RTHQYSEKGK WTTNTETKAP QLNPIDGPLP
DNNEPSGYAQ TDCVLEAMAF LEESHPGIFE NSCLETIEVV QQTRVDKLTQ GRQTYDWTLN
RNQPAATALA NTIEVFRSNG LTTNESGRLI DFLKDVMDSM NKEEMEITTH FQRKRRVRDN
MTKKMVTQRT IGKKKQRLNR RSYLIRALTL NTMTKDAERG KLKRRAIATP GMQIRGFVYF
VETLARSICE KLEQSGLPVG GNEKKAKLAN VVRKMMTNSQ DTELSFTITG DNTKWNENQN
PRVFLAMITY ITRNQPEWFR NVLSIAPIMF SNKMARLGKG YMFESKSMKL RTQIPAEMLA
TIDLKYFNES TRQKIEKIRP LLIEGTASLS PGMMMGMFNM LSTVLGVSIL NLGQKRYTKT
TYWWDGLQSS DDFALIVNAP NHEGIQAGVD RFYR
//
