ID D1LNI1_9INFA Unreviewed; 746 AA.
AC D1LNI1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:ACZ45850.1};
OS Influenza A virus (A/blackhead gull/Astrakhan/1421/1979(H13N6)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=680696 {ECO:0000313|EMBL:ACZ45850.1};
RN [1] {ECO:0000313|EMBL:ACZ45850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A/blackhead gull/Astrakhan/1421/1979
RC {ECO:0000313|EMBL:ACZ45850.1};
RA Kim L.M., Scott M.A., Suarez D.L., Spackman E., Swayne D.E., Afonso C.L.;
RT "USDA Agriculture Research Service Avian Influenza Virus Sequencing
RT Project.";
RL Submitted (OCT-2009) 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; GU052238; ACZ45850.1; -; 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 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 275..472
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50525"
FT REGION 39..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ45850.1"
SQ SEQUENCE 746 AA; 85106 MW; A57D888B1F2B6E78 CRC64;
VPAQNAISTT FPYTGDPPYS HGTGTGYTMD TVNRTHQYSE KGKWTTNTET GAPQLNPIDG
PLPEDNEPSG YAQTDCVLEA MAFLEESHPG IFENSCLETM EVVQQTRVDK LTQGRQTYDW
TLNRNQPAAT ALANTIEVFR SNGLTANESG RLIDFLKDVM ESMDKEELEI TTHFQRKRRV
RDNMTKKMVT QRTIGKKKQR LNKKNYLIRA LTLNTMTKDA ERGKLKRRAI ATPGMQIRGF
VYFVETLARS ICEKLEQSGL PVGGNEKKAK LANVVRKMMT NSQDTELSFT ITGDNTKWNE
NQNPRMFLAM ITYITRNQPE WFRNVLSIAP IMFSNKMARL GKGYMFESKS MKLRTQIPAE
MLASIDLKYF NESTRKKIEK IRPLLIDGTA SLSPGMMMGM FNMLSTVLGV SILNLGQKRY
TKTTYWWDGL QSSDDFALIV NAPNHEGIQA GVDRFYRTCK LVGINMSKKK SYINRTGTFE
FTSFFYRYGF VANFSMELPS FGVSGINESA DMSIGVTVIK NNMINNDLGP ATAQMALQLF
IKDYRYTYRC HRGDTQIQTR RSFELKKLWD QTRSKAGLLV SDGGPNLYNI RNLHIPEVCL
KWELMDEDYQ GRLCNPLNPF VSHKEIESVN NAVVMPAHGP AKSMEYDAVA TTHSWVPKRN
RSILNTSQRG ILEDEQMYQK CCNLFEKFFP SSSYRRPVGI SSMVEAMVSR ARIDARIDFE
SGRIKKEEFA EIMKICSTIE ELRRQK
//
