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Database: UniProt
Entry: D2SHW2_9INFA
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Original site: D2SHW2_9INFA 
ID   D2SHW2_9INFA            Unreviewed;       703 AA.
AC   D2SHW2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:ADB25468.1};
OS   Influenza A virus (A/goose/Nigeria/08VIR4337-544/2007(H5N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=684468 {ECO:0000313|EMBL:ADB25468.1};
RN   [1] {ECO:0000313|EMBL:ADB25468.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/goose/Nigeria/08VIR4337-544/2007
RC   {ECO:0000313|EMBL:ADB25468.1};
RX   PubMed=20071565; DOI=10.1128/JVI.02385-09;
RA   Fusaro A., Nelson M.I., Joannis T., Bertolotti L., Monne I., Salviato A.,
RA   Olaleye O., Shittu I., Sulaiman L., Lombin L.H., Capua I., Holmes E.C.,
RA   Cattoli G.;
RT   "Evolutionary dynamics of multiple sublineages of H5N1 influenza viruses in
RT   Nigeria from 2006 to 2008.";
RL   J. Virol. 84:3239-3247(2010).
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; CY048073; ADB25468.1; -; 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   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          269..466
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50525"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADB25468.1"
FT   NON_TER         703
FT                   /evidence="ECO:0000313|EMBL:ADB25468.1"
SQ   SEQUENCE   703 AA;  80175 MW;  49C8A081A33BDB9C CRC64;
     ISTTFPYTGD PPYSHGTGTG YTMDTVNRTH QYSEKGKWTT NTETGAPQLN PIDGPLPEDN
     EPSGYAQTDC VLEAMAFLEE SHPGIFENSC LETMEIVQQT RVDKLTQGRQ TYDWTLNRNQ
     PAATALANTI EIFRSNGLTA NESGRLIDFL KDVMESMDKE EMEITTHFQR KRRVRDNMTK
     KMVTQRTIGK KKQRLNKKSY LIRALTLNTM TKDAERGKLK RRAIATPGMQ IRGFVYFVET
     LARSICEKLE QSGLPVGGNE KKAKLANVVR KMMTNSQDTE LSFTITGDNT KWNENQNPRM
     FLAMITYITR NQPEWFRNVL SIAPIMFSNK MARLGRGYMF ESKSMKLRTQ IPAEMLANID
     LKYFNELTKK KIEKIRPLLI DGTASLSPGM MMGMFNMLST VLGVSILNLG QKRYTKTTYW
     WDGLQSSDDF ALIVNAPNHE GIQAGVDRFY RTCKLVGINM SKKKSYINRT GTFEFTSFFY
     RYGFVANFSM ELPSFGVSGI NESADMSIGI TVIKNNMINN DLGPATAQMA LQLFIKDYRY
     TYRCHRGDTQ IQTRRSFELK KLWEQTRSKA GLLVSDGGPN LYNIRNLHIP EVCLKWELMD
     EDYQGRLCNP LNPFVSHKEI ESVNNAVVMP AHGPAKAMEY DAVATTHSWI PKRNRSILNT
     SQRGILEDEQ MYQKCCNLFE KFFPSSSYRR PVGISSMVEA MVS
//
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