ID   RP132_CAMPM             Reviewed;        1164 AA.
AC   Q8V2N1;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA-directed RNA polymerase 132 kDa polypeptide;
DE            EC=2.7.7.6;
GN   Name=RPO132; OrderedLocusNames=CMLV142;
OS   Camelpox virus (strain M-96).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=203173;
OH   NCBI_TaxID=9836; Camelus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12033760; DOI=10.1006/viro.2001.1343;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Sandybaev N.T., Kerembekova U.Z.,
RA   Zaitsev V.L., Kutish G.F., Rock D.L.;
RT   "The genome of camelpox virus.";
RL   Virology 295:1-9(2002).
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), itself composed
CC       of D6 and A7, thereby allowing the early genes transcription. Late
CC       transcription, and probably also intermediate transcription, require
CC       newly synthesized RNA polymerase (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:0000250}. 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; AF438165; AAL73849.1; -; Genomic_DNA.
DR   RefSeq; NP_570532.1; NC_003391.1.
DR   SMR; Q8V2N1; -.
DR   GeneID; 932669; -.
DR   KEGG; vg:932669; -.
DR   Proteomes; UP000152221; 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 132 kDa polypeptide"
FT                   /id="PRO_0000048063"
SQ   SEQUENCE   1164 AA;  133479 MW;  0E47088EC0FA64C8 CRC64;
     MKKNTDSEMD QRLGYKFLVP DPKAGVFYRP LHFQYVSYSN FILHRLHEIL TVKRPLLSFK
     NNTERIMIEI SNVKVTPPDY SPIIASIKGK SYDALATFTV NIFKEVMTKE GISITKISSY
     EGKDSHLIKI PLLIGYGNKN PLDTAKYLVP NVIGGVFINK QSVEKVGINL VEKITTWPKF
     RVVKPNSFTF SFSSVSPPNV LPTRYRHYKI SLDISQLEAS NISSTKTFIT VNIVLLSQYL
     SRVSLEFIRR SLSYDMPPEV VYLVNAIIDS AKRLTESITD FNIDTYINDL VEAEHIKQKS
     QLTINEFKYE MLYNFLPHMN YTPDQLKGFY MISLLRKFLY CIYHTSRYPD 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 EVILTAAYSV KPYNNKGENR PVCFPSSNET
     SIDTYMQFAK QCYEHSNPKL SEEELSDKIF CEKILYDPET DKPYGSKVFF GPIYYLRLRH
     LTQDKATVRC RGKKTKLIRQ ANEGRKRGGG IKFGEMERDC LIAHGAANTI TEVLKDSEED
     YQDVYICENC GDIAAQIKSI NTCLRCSKLN LSPLLTKIDT THVSKVFLTQ MNARGVKVKL
     DFERRPPSFY KPLDKVDLKP SFLK