ID B7NXJ0_9INFA Unreviewed; 754 AA.
AC B7NXJ0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:ACJ69076.1};
OS Influenza A virus (A/avian/New York/Sg-00377/2001(H5N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=578370 {ECO:0000313|EMBL:ACJ69076.1};
RN [1] {ECO:0000313|EMBL:ACJ69076.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/avian/New York/Sg-00377/2001 {ECO:0000313|EMBL:ACJ69076.1};
RA Sreevatsan S., Wang P., Ramakrishnan M.A., Anderson T.L., Goyal S.M.,
RA Osterholm M.T.;
RT "unpublished.";
RL Submitted (DEC-2008) 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; CY036383; ACJ69076.1; -; 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 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 283..480
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 47..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ69076.1"
SQ SEQUENCE 754 AA; 86145 MW; 6BC31E2F3B556E02 CRC64;
HPTLLFLKVP AQNAISTTFP YTGDPPYSHG TGTGYTMDTV NRTHQYSEKG KWTTNTETGA
PQLNPIDGPL PEDNEPSGYA QTDCVLEAMA FLEESHPGIF ENSCLETMEV VQQTRVDKLT
QGRQTYDWTL NRNQPAATAL ANTIEVFRSN GLTANESGRL IDFLKDVMES MDKREMEITT
HFQRKRRVRD NMTKKMVTQR TIGKKKQRLN KRSYLIRALT LNTMTKDAER GKLKRRAIAT
PGMQIRGFVY FVETLARSIC EKLEQSGLPV GGNEKKAKLA NVVRKMMTNS QDTEVSFTIT
GDNTKWNENQ NPRMFLAMIT YITRDQPEWF RNVLSIAPIM FSNKMARLGK GYMFESKSMK
LRTQIPAEML ANIDLKYFNE STRKKIEKIR PLLIDGTASL SPGMMMGMFN MLSTVLGVSI
LNLGQKRYTK TTYWWDGLQS SDDFALIVNA PNHEGIQAGV DRFYRTCKLV GINMSKKKSY
INRTGTFEFT SFFYRYGFVA NFSMELPSFG VSGINESADM SIGVTVIKNN MINNDLGPAT
AQMALQLFIK DYRYTYRCHR GDTQIQTRRS FELKKLWEQT RSKAGLLVSD GGPNLYNIRN
LHIPEVCLKW ELMDEDYQGR LCNPLNPFVS HKEIESVNNA VVMPAHGPAK SMEYDAVATT
HSWIPKRNRS ILNTSQRGIL EDEQMYQKCC NLFEKFFPSS SYRRPVGISS MVEAMVSRAR
IDARIDFESG RIKKEEFAEI MKICSTIEEL RRQK
//
