GenomeNet

Database: UniProt
Entry: R4P7A2_9INFA
LinkDB: R4P7A2_9INFA
Original site: R4P7A2_9INFA 
ID   R4P7A2_9INFA            Unreviewed;       757 AA.
AC   R4P7A2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000256|HAMAP-Rule:MF_04065};
DE            EC=2.7.7.48 {ECO:0000256|HAMAP-Rule:MF_04065};
DE   AltName: Full=Polymerase basic protein 1 {ECO:0000256|HAMAP-Rule:MF_04065};
DE            Short=PB1 {ECO:0000256|HAMAP-Rule:MF_04065};
DE   AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000256|HAMAP-Rule:MF_04065};
GN   Name=PB1 {ECO:0000256|HAMAP-Rule:MF_04065,
GN   ECO:0000313|EMBL:AGL52458.1};
OS   Influenza A virus (A/northern shoveler/Interior
OS   Alaska/9BM12350R0/2009(H8N4)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=1323030 {ECO:0000313|EMBL:AGL52458.1};
RN   [1] {ECO:0000313|EMBL:AGL52458.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/northern shoveler/Interior Alaska/9BM12350R0/2009
RC   {ECO:0000313|EMBL:AGL52458.1};
RA   Wentworth D.E., Dugan V., Halpin R., Lin X., Bera J., Ghedin E.,
RA   Fedorova N., Overton L., Tsitrin T., Stockwell T., Amedeo P., Bishop B.,
RA   Chen H., Edworthy P., Gupta N., Katzel D., Li K., Schobel S.,
RA   Shrivastava S., Thovarai V., Wang S., Runstadler J., Lindberg M.,
RA   Huettmann F., Petrula M., Meixell B., Gingrich J.P., Gildehaus L.A.,
RA   Vick L., Kokx K., Dillon D., Aldehoff F., Felker E.P., Marcotte R.W.,
RA   Schmidt J.C., Moore J.R., Gerdes K.E., Bao Y., Sanders R., Dernovoy D.,
RA   Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGL52458.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/northern shoveler/Interior Alaska/9BM12350R0/2009
RC   {ECO:0000313|EMBL:AGL52458.1};
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (MAY-2013) 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 copies vRNA into complementary RNA (cRNA) which in
CC       turn serves as a template for the production of more vRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_04065}.
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|HAMAP-Rule:MF_04065,
CC         ECO:0000256|RuleBase:RU004330};
CC   -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1,
CC       PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus).
CC       Interacts (via C-terminus) with PB2 (via N-terminus); this interaction
CC       is essential for transcription initiation. {ECO:0000256|HAMAP-
CC       Rule:MF_04065}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       nucleus {ECO:0000256|HAMAP-Rule:MF_04065}. Host cytoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_04065}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- PTM: Phosphorylated by host PRKCA. {ECO:0000256|HAMAP-Rule:MF_04065}.
CC   -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_04065}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CY141381; AGL52458.1; -; 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-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-Rule:MF_04065};
KW   Eukaryotic host transcription shutoff by virus
KW   {ECO:0000256|ARBA:ARBA00022731, ECO:0000256|HAMAP-Rule:MF_04065};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995,
KW   ECO:0000256|HAMAP-Rule:MF_04065};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Inhibition of host RNA polymerase II by virus
KW   {ECO:0000256|ARBA:ARBA00023103, ECO:0000256|HAMAP-Rule:MF_04065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW   ECO:0000256|HAMAP-Rule:MF_04065};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_04065};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, ECO:0000256|HAMAP-
KW   Rule:MF_04065};
KW   Viral transcription {ECO:0000256|ARBA:ARBA00023314, ECO:0000256|HAMAP-
KW   Rule:MF_04065}.
FT   DOMAIN          286..483
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50525"
FT   REGION          51..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..256
FT                   /note="Promoter-binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT   MOTIF           187..195
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT   MOTIF           203..216
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04065"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  86369 MW;  56E285A226E5D443 CRC64;
     MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNSE
     TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
     KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
     ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
     SMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGIDRFYRTC KLVGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN
     IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCSLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEVF AEIMKICSTI EELRRQK
//
DBGET integrated database retrieval system