位置:首页 > 蛋白库 > RDRP_I77A4
RDRP_I77A4
ID   RDRP_I77A4              Reviewed;         757 AA.
AC   Q9EA41; Q288Y8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 72.
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/Swine/Colorado/1/1977 H3N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=385645;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9721; Cetacea (whales).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9709; Phocidae (true seals).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10930664; DOI=10.1016/s0168-1702(00)00154-4;
RA   Karasin A.I., Schutten M.M., Cooper L.A., Smith C.B., Subbarao K.,
RA   Anderson G.A., Carman S., Olsen C.W.;
RT   "Genetic characterization of H3N2 influenza viruses isolated from pigs in
RT   North America, 1977-1999: evidence for wholly human and reassortant virus
RT   genotypes.";
RL   Virus Res. 68:71-85(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA   Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA   Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA   Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (MAR-2006) 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: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   -!- 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}.
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; AF251390; AAG01744.1; -; Genomic_RNA.
DR   EMBL; CY009306; ABD61559.1; -; Genomic_RNA.
DR   SMR; Q9EA41; -.
DR   Proteomes; UP000009193; 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: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   3: Inferred from homology;
KW   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   RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW   Viral transcription.
FT   CHAIN           1..757
FT                   /note="RNA-directed RNA polymerase catalytic subunit"
FT                   /id="PRO_0000279619"
FT   DOMAIN          286..483
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   REGION          50..81
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"
FT   CONFLICT        12
FT                   /note="E -> V (in Ref. 2; ABD61559)"
FT   CONFLICT        85
FT                   /note="Q -> T (in Ref. 2; ABD61559)"
FT   CONFLICT        121
FT                   /note="R -> K (in Ref. 2; ABD61559)"
FT   CONFLICT        127
FT                   /note="K -> Q (in Ref. 2; ABD61559)"
FT   CONFLICT        565
FT                   /note="H -> D (in Ref. 2; ABD61559)"
FT   CONFLICT        590
FT                   /note="F -> L (in Ref. 2; ABD61559)"
SQ   SEQUENCE   757 AA;  86596 MW;  E96D9EE022AAD4DB CRC64;
     MDVNPTLLFL KEPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGAPQLNPID GPLPEDNEPS GYAQQDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
     RLTQGRKTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEME
     ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNILSIA PIMFSNKMAR LGKGYMFESK
     RMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKK YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGHTQIQT RRSFELKKLW EQTRSKAGLF VSDGGPNLYN
     IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF SEIMKICSTI EELRRQK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024