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RDRP_I96A0
ID   RDRP_I96A0              Reviewed;         757 AA.
AC   Q9Q0V0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   23-FEB-2022, entry version 93.
DE   RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_04065};
DE            EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04065};
DE   AltName: Full=Polymerase basic protein 1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE            Short=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE   AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000255|HAMAP-Rule:MF_04065};
GN   Name=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
OS   Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=93838;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH   NCBI_TaxID=9694; Panthera tigris (Tiger).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10484749; DOI=10.1006/viro.1999.9820;
RA   Xu X., Subbarao K., Cox N.J., Guo Y.;
RT   "Genetic characterization of the pathogenic influenza
RT   A/Goose/Guangdong/1/96 (H5N1) virus: similarity of its hemagglutinin gene
RT   to those of H5N1 viruses from the 1997 outbreaks in Hong Kong.";
RL   Virology 261:15-19(1999).
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:0000255|HAMAP-Rule:MF_04065}.
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:0000255|HAMAP-Rule:MF_04065};
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:0000255|HAMAP-
CC       Rule:MF_04065}.
CC   -!- INTERACTION:
CC       Q9Q0V0; Q9Q0U9: PA; NbExp=3; IntAct=EBI-8290908, EBI-15715136;
CC       Q9Q0V0; Q9Q0V0: PB1; NbExp=6; IntAct=EBI-8290908, EBI-8290908;
CC       Q9Q0V0; Q9Q0V1: PB2; NbExp=2; IntAct=EBI-8290908, EBI-8290926;
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}.
CC       Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}.
CC   -!- PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065}.
CC   -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04065}.
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DR   EMBL; AF144301; AAD51923.1; -; Genomic_RNA.
DR   RefSeq; YP_308665.1; NC_007358.1.
DR   PDB; 3J9B; EM; 4.30 A; B/I=1-24.
DR   PDBsum; 3J9B; -.
DR   SMR; Q9Q0V0; -.
DR   DIP; DIP-59838N; -.
DR   IntAct; Q9Q0V0; 2.
DR   MINT; Q9Q0V0; -.
DR   GeneID; 3654616; -.
DR   KEGG; vg:3654616; -.
DR   Proteomes; UP000131152; Genome.
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:0042802; F:identical protein binding; IPI:IntAct.
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-directed 5'-3' RNA polymerase activity; 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:0006351; P:transcription, DNA-templated; 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   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   1: Evidence at protein level;
KW   3D-structure; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host nucleus;
KW   Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Reference proteome; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication; Viral transcription.
FT   CHAIN           1..757
FT                   /note="RNA-directed RNA polymerase catalytic subunit"
FT                   /id="PRO_0000279596"
FT   DOMAIN          286..483
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   REGION          50..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..256
FT                   /note="Promoter-binding site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   MOTIF           187..195
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   MOTIF           203..216
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  86177 MW;  D3F07429E0421159 CRC64;
     MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
     KLTQGRQTYD WTLKRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKGEME
     IITHFQRKRR 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 VNAPNHEGIE AGVDRFYRTC KLVGINMTKK
     KSYINRTGTC EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMMDNDLG
     PATAQMALQL FIKDYRYPYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNPYN
     IRNLHIPEAG LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF AEIMKICSTI EELGRQK
 
 
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