ID B6JRB2_9INFA Unreviewed; 753 AA.
AC B6JRB2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, 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:ACI89529.1};
OS Influenza A virus (A/mallard/Minnesota/Sg-00176/2007(H4N6)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=569256 {ECO:0000313|EMBL:ACI89529.1};
RN [1] {ECO:0000313|EMBL:ACI89529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/mallard/Minnesota/Sg-00176/2007
RC {ECO:0000313|EMBL:ACI89529.1};
RA Sreevatsan S., Ramakrishnan M.A., Wang P., Goyal S.M., Osterholm M.T.;
RT "unpublished.";
RL Submitted (OCT-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; CY035301; ACI89529.1; -; 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 282..479
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 47..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACI89529.1"
SQ SEQUENCE 753 AA; 85948 MW; 32F49D8938E1D996 CRC64;
PTLLFLKVPA QNAISTTFPY TGDPPYSHGT GTGYTMDTVN RTHQCSEKGK WTTNSETGAP
QLNPIDGPLP EDNEPSGYAQ TDCVLEAMAF LEESHPGIFE NSCLETMEVV QQTRVDKLTQ
GRQTYDWTLN RNQPAATALA NTIEVFRSNG LTANESGRLI DFLKDVMESM DKEEMEITTH
FQRKRRVRDN MTKKMVTQRT IGKKKQRLNK RSYLIRALTL NTMTKDAERG KLKRRAIATP
GMQIRGFVYF VETLARSICE KLEQSGLPVG GNEKKAKLAN VVRKMMTNSQ DTELSFTITG
DNTKWNENQN PRMFLAMITY ITRNQPEWFR NVLSIAPIMF SNKMARLGKG YMFESKSMKL
RTQIPAEMLA SIDLKYFNES TRKKIERMRP LLIDGTASLS PGMMMGMFNM LSTVLGVSIL
NLGQKRYTKT TYWWDGLQSS DDFALIVNAP NHEGIQAGVD RFYRTCKLVG INMSKKKSYI
NRTGTFEFTS FFYRYGFVAN FSMELPSFGV SGINESADMS IGVTVIKNNM INNDLGPATA
QMALQLFIKD YRYTYRCHRG DTQIQTRRSF ELRKLWEQTH SKAGLLVSDG GPNLYNIRNL
HIPEVCLKWE LMDEDYQGRL CNPLNPFVSH KEIESVNNAV VMPAHGPAKS MEYDAVATTH
SWIPKRNRSI LNTSQRGILE DEQMYQKCCN LFEKFFPSSS YRRPVGISSM VEAMVSRARI
DARIDFESGR IKKEEFAEIM KICSTIEELR RQK
//