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Database: UniProt
Entry: B2Z8E9_9INFA
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ID   B2Z8E9_9INFA            Unreviewed;       742 AA.
AC   B2Z8E9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 61.
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:ACD12288.1};
OS   Influenza A virus (A/duck/Thailand/CU-329/07(H5N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=519101 {ECO:0000313|EMBL:ACD12288.1};
RN   [1] {ECO:0000313|EMBL:ACD12288.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/duck/Thailand/CU-329/07 {ECO:0000313|EMBL:ACD12288.1};
RX   PubMed=18976558; DOI=10.3201/eid1411.080683;
RA   Amonsin A., Choatrakol C., Lapkuntod J., Tantilertcharoen R.,
RA   Thanawongnuwech R., Suradhat S., Suwannakan K., Theamboonlers A.,
RA   Poovorawan Y.;
RT   "Influenza virus (H5N1) in live bird markets and food markets, Thailand.";
RL   Emerg. Infect. Dis. 14:1739-1742(2008).
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; EU616849; ACD12288.1; -; 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          49..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD12288.1"
FT   NON_TER         742
FT                   /evidence="ECO:0000313|EMBL:ACD12288.1"
SQ   SEQUENCE   742 AA;  84611 MW;  7BD59DD28C8E25AA CRC64;
     NPTLLFLKVP VQNAISTTFP YTGDPPYSHG TGTGYTMDTV NRTHQYSEKG KWTTNTETGA
     PQLNPIDGPL PEDNEPSGYA QTDCVLEAMA FLEESHPGIF ENSCLETMEI VQQTRVDKLT
     QGRQTYDWTL NRNQPAATAL ANTIEIFRSN GLTANESGRL IDFLKDVMES MDKEEMEMTT
     HFQRKRRVRD NMTKKMVTQR TIGKKKQKLN KKSYLIRALT LNTMTKDAER GKLKRRAIAT
     PGMQIRGFVY FVETLARSIC EKLEQSGLPV GGNEKKAKLA NVVRKMMTSS QDTELSFTIT
     GDNTKWNENQ NPRMFLAMIT YITRNQPEWF RNVLSIAPIM FSNKMARLGK GYMFESKSMK
     LRTQIPAEML ANIDLKYFNE ITKKKIEKIR 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 SYRRPVGLSS MVEAMVSRAR
     IDARIDFESG KIKKEEFAEI MK
//
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