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RP132_VARV
ID   RP132_VARV              Reviewed;        1164 AA.
AC   P0DST4; P33811; Q76PX7; Q90027; Q90031;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=DNA-directed RNA polymerase 133 kDa polypeptide;
DE            EC=2.7.7.6;
GN   Name=RPO132; ORFNames=A24R, A25R;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RA   Shchelkunov S.N., Totmenin A.V., Sosnovtsev S.V., Safronov P.F.,
RA   Resenchuk S.M., Blinov V.M., Sandakhchiev L.S.;
RT   "XhoI-D DNA fragment of Variola minor virus strain Garcia-1966.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RX   PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA   Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA   Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT   "Alastrim smallpox variola minor virus genome DNA sequences.";
RL   Virology 266:361-386(2000).
CC   -!- FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the
CC       transcription of viral DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Responsible for the transcription of
CC       early, intermediate and late genes. DNA-dependent RNA polymerase
CC       associates with the early transcription factor (ETF) thereby allowing
CC       the early genes transcription. Late transcription, and probably also
CC       intermediate transcription, require newly synthesized RNA polymerase
CC       (By similarity). {ECO:0000250}.
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=2.7.7.6;
CC   -!- SUBUNIT: The DNA-dependent RNA polymerase used for intermediate and
CC       late genes expression consists of eight subunits (147) kDa, (133) kDa,
CC       (35) kDa, (30) kDa, (22) kDa, (19) kDa, (18) kDa and (7) kDa totalling
CC       more than 500 kDa in mass. The same holoenzyme, with the addition of
CC       the transcription-specificity factor RAP94, is used for early gene
CC       expression (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC       other proteins required to synthesize early mRNAs are packaged within
CC       the virion core along with the DNA genome. This is necessary because
CC       viral early mRNAs are synthesized within minutes after virus entry into
CC       the cell and are extruded through pores in the core particle (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; L22579; AAA60876.1; -; Genomic_DNA.
DR   EMBL; X76268; CAA53897.1; -; Genomic_DNA.
DR   EMBL; Y16780; CAB54728.1; -; Genomic_DNA.
DR   PIR; F72166; F72166.
DR   PIR; T28566; T28566.
DR   SMR; P0DST4; -.
DR   Proteomes; UP000111493; Genome.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR024390; RNA_pol_132_poxvirus.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   Pfam; PF12415; rpo132; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Transcription; Transferase; Virion.
FT   CHAIN           1..1164
FT                   /note="DNA-directed RNA polymerase 133 kDa polypeptide"
FT                   /id="PRO_0000448122"
FT   VARIANT         48
FT                   /note="E -> G (in strain: Garcia-1966)"
FT   VARIANT         296
FT                   /note="V -> I (in strain: Garcia-1966)"
FT   VARIANT         976
FT                   /note="L -> S (in strain: Garcia-1966)"
SQ   SEQUENCE   1164 AA;  133402 MW;  D28A83F6EDB8101B CRC64;
     MKKNTDSEMD QRLGYKFLVP DPKAGVFYRP LHFQYVSYSN FILHRLHEIL TVKRPLLSFK
     NNTERIMIEI SNVKVTPPDY SPIIASIKGK SYDALATFTV NIFKEVMAKE GISITKISSY
     EGKDSHLIKI PLLIGYGNKN PLDTAKYLVP NVIGGVFINK QSVEKVGINL VEKITTWPKF
     RVVKPNSFTF SFSSVSPPNI LPTRYRHYKI SLDISQLEAS NISSTKTFIT VNIVLLSQYL
     SRVSLGFIRR SLSYDMPPEV VYLVNAIIDS AKRLTESITD FNIDTYINDL VEAEHVKQKS
     QLTINEFKYE MLHNFLPHMN YTPDQLKGFY MISLLRKFLY CIYYTSRYPD RDSMVCHRIL
     TYGKYFETLA HDELENYIGN IRNDIMNNHK NRGTYAVNIH VLTTPGLNHA FSSLLSGKFK
     KSDGSYRTHP HYSWMQNISI PRSVGFYPDQ VKISKMFSVR KYHPSQYLYF CSSDVPERGP
     QVGLVSQLSV LSSITNILTS EYLDLEKKIC EYIRSYYKDD ISYFETGFPI TIENALVASL
     NPNMICDFVT DFRRRKRMGF FGNLEVGITL VRDHMNEIRI NIGAGRLVRP FLVVDNGELM
     MDVCPELESR LDDMTFSDIQ KEFPHVIEMV DIEQFTFSNV CESVQKFRMM SKDERKQYDL
     CDFPAEFRDG YVASSLVGIN HNSGPRAILG CAQAKQAISC LSSDIRNKID NGIHLMYPER
     PIVISKALET SKIAANCFGQ HVTIALMSYK GINQEDGIII KKQFIQRGGL DIVTAKKHQV
     EIPLENFNNK ERDRSNAYSK LESNGLVRLN AFLESGDAMA RNISSRTLED DFARDNQISF
     DVSEKYTDMY KSRVERVQVE LTDKVKVRVL TMKERRPILG DKFTTRTSQK GTVAYIADET
     ELPYDENGIT PDVIINSTSI FSRKTISMLI EVILTAAYSA KPYNNKGENR PVCFPSSNET
     SIDTYMQFAK QCYEHLNPKL TEKELSDKIF CEKILYDPET DKPYASKVFF GPIYYLRLRH
     LTQDKATVRC RGKKTKLIRQ ANEGRKRGGG IKFGEMERDC LIAHGAANTI TEVLKDSEED
     YQDVYICENC GDIAAQIKSI NTCLRCSKLN LSPLLTKIDT THVSKVFLTQ MNARGVKVKL
     DFERRPPSFY KPLDKVDLKP SFLK
 
 
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