ID M4H0R7_9INFA Unreviewed; 718 AA.
AC M4H0R7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:AFJ04357.1};
OS Influenza A virus (A/mallard/Jiangxi/38/2011(H9N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=1170410 {ECO:0000313|EMBL:AFJ04357.1};
RN [1] {ECO:0000313|EMBL:AFJ04357.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/mallard/Jiangxi/38/2011 {ECO:0000313|EMBL:AFJ04357.1};
RX PubMed=23830774; DOI=10.1016/j.vetmic.2013.05.013;
RA Zhu G., Wang R., Xuan F., Daszak P., Anthony S.J., Zhang S., Zhang L.,
RA He G.;
RT "Characterization of recombinant H9N2 influenza viruses isolated from wild
RT ducks in China.";
RL Vet. Microbiol. 166:327-336(2013).
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; JQ901620; AFJ04357.1; -; 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:AFJ04357.1"
FT NON_TER 718
FT /evidence="ECO:0000313|EMBL:AFJ04357.1"
SQ SEQUENCE 718 AA; 81669 MW; D118967E97C42866 CRC64;
NAISTTFPYT GDPPYSHGTG TGYTMDTVNR THQYSEKGKW TTNTETGAPQ LNPIDGPLPE
DNEPSGYAQT DCVLEAMAFL EESHPGLFEN SCIETMEVVQ QTRVDKLTQG RQTYDWTLNR
NQPAATALAN TIEVFRSNGL KANESGRLID FLKDVMESMD KEEVEITTHF QRKRRVRDNM
TKKMVTQRTI GKKKQKLTKK SYLIRALTLN TMTKDAERGK LKRRAIATPG MQIRGFVYFV
ETLARSICEK LEQSGLPVGG NEKKAKLANV VRKMMTNSQD TELSFTITGD NTKWNENQNP
RVFLAMITYI TRNQPEWFRN VLSVAPIMFS NKMARLGKGY MFESKSMKLR TQIPAEMLAT
IDLKYFNEST RKKIEKIRPL LIEGTASLSP GMMMGMFNML STVLGVSILN LGQKRHTKTT
YWWDGLQSSD DFALIVNAPN HEGIQAGVDR FYRTCKLVGI NMSKKKSYIN RTGTFEFTSF
FYRYGFVANF SMELPSFGVS GINESADMSI GVTVIKNNMI NNDLGPATAQ MALQLFIKDY
RYTYRCHRGD TQIQTRRSFE LKKLWEQTRS KAGLLVSDGG PNLYNIRNLH IPEVCLKWEL
MDEDYQGRLC NPLNPFVSHK EVDSVNNAVV MPAHGPAKSM EYDAVATTHS WIPKRNRSIL
NTSQRGILED EQMYQKCCTL FEKFFPSSSY RRPVGISSMM EAMVSRARID ARIDFESG
//
