ID X2G6Y5_9INFA Unreviewed; 711 AA.
AC X2G6Y5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:AHN13757.1};
OS Influenza A virus (A/swine/Thailand/CU-S3631N/2012(H1N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=1470613 {ECO:0000313|EMBL:AHN13757.1};
RN [1] {ECO:0000313|EMBL:AHN13757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/swine/Thailand/CU-S3631N/2012 {ECO:0000313|EMBL:AHN13757.1};
RX PubMed=25504006; DOI=10.1007/s11262-014-1153-x;
RA Nonthabenjawan N., Chanvatik S., Chaiyawong S., Jairak W.,
RA Boonyapisusopha S., Tuanudom R., Thontiravong A., Bunpapong N., Amonsin A.;
RT "Genetic diversity of swine influenza viruses in Thai swine farms, 2011-
RT 2014.";
RL Virus Genes 50:221-230(2015).
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; KJ526040; AHN13757.1; -; 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 271..468
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 35..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHN13757.1"
FT NON_TER 711
FT /evidence="ECO:0000313|EMBL:AHN13757.1"
SQ SEQUENCE 711 AA; 81044 MW; BEB7C30FF9DA1533 CRC64;
NAISTTFPYT GDPPYSHGTG TGYTMDTVNR THQYSEKGKW TTNTETGAPQ LNPIDGPLPE
DNEPSGYAQT DCVLEAMAFL EESHPGIFEN SCLETMEVVQ QTRIDKLTQG RQTYDWTLNR
NQPAATALAN TIEVFRLNGL TANESGRLID FLKDVMESMN KEEMEITTHF QRKRRVRDNM
TKKMVTQRTI GKKKQRLNKR GYLIRALTLN TMTKDAERGK LKRRAIATPG MQIRGFVYFV
ETLARSICEK LEQSGLPVGG NEKKAKLANV VRKMMTNSQD TEISFTITGD NTKWNENQNP
RMFLAMITYI TRNQPEWFRN ILSMAPIMFS NKMARLGKGY MFESKRMKIR TQIPAEMLAS
IDLKYFNEST KKKIEKIRPL LIDGTASLSP GMMMGMFNML STVLGVSILN LGQKKYTKTI
YWWDGLQSSD DFALIVNAPN HEGIQAGVDR FYRTCKLVGI NMSKKKSYIN KTGTFEFTSF
FYRYGFVANF SMELPSFGVS GINESADMSI GVTVIKNNMI NNDLGPATAQ MALQLFIKDY
RYTYRCHRGD TQIQTRRSFE LKRLWDQTQS KVGLLVSDGG PNLYNIRNLH IPEVCLKWEL
MDDDYRGRLC NPLNPFVSHK EIDSVNNAVV MPAHGPAKSM EYDAVATTHS WIPKRNRSIL
NTSQRGILED EQMYQKCCNL FEKFFPSSSY RRPVGISSMV EAMVSRARID A
//
