ID   RP132_SHEVK             Reviewed;         919 AA.
AC   P16716;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA-directed RNA polymerase 132 kDa polypeptide;
DE            EC=2.7.7.6;
DE   AltName: Full=HM1 protein;
DE   Flags: Fragment;
GN   Name=RPO132;
OS   Sheeppox virus (strain KS-1) (SPPV) (Capripoxvirus (strain KS-1)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Capripoxvirus.
OX   NCBI_TaxID=10269;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2795717; DOI=10.1128/jvi.63.11.4703-4708.1989;
RA   Gershon P.D., Ansell D.M., Black D.N.;
RT   "A comparison of the genome organization of capripoxvirus with that of the
RT   orthopoxviruses.";
RL   J. Virol. 63:4703-4708(1989).
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}.
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; M30039; AAC32897.1; -; Genomic_DNA.
DR   PIR; A33325; RNVZCA.
DR   SMR; P16716; -.
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; 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; 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..919
FT                   /note="DNA-directed RNA polymerase 132 kDa polypeptide"
FT                   /id="PRO_0000048065"
FT   NON_TER         1
SQ   SEQUENCE   919 AA;  105702 MW;  5395E8E1008AB6D6 CRC64;
     SFIKHSLSYD MPSEISYLVN TIIESTKELI KTINDFDIDT YINDLIISEY NKQKSQLILE
     EFKHEMINNF LPHMNDTPNQ LKGFYIMSLL RKFIYCIYYT SRYPDRDSMV CHRVLTYGKY
     FEILAHDELE NYIGNIRTDI INNHKNRGTY SVNIHVLTTP GFNHAFSGLL SGKFKKTDGS
     YRTHSHYSWM QNISIPRSVG YYPDQVKISK MFSVRKYHPS QYAYFCPSDV PERGPQVGLV
     SQLSVLTSIT NICTNEYLEL EKKICNYIRS YNHNDISYFE TGYYITLENS LIACLNPNLV
     DDFVIDFRRK KRMNYFGNLE IGITLVNDHM NEIRINIGGG RLIRPFLVID NGNLIMDEIF
     SELEFKIDDM TFSDIQKEFP HVIEIVDIEQ FTFSNVCESV QKFRALPKSE KCKYHLCDFP
     AEFKDGYVAS SLVGINHNSG PRAILGCAQR KQAISCLSSD IRNKIDNGIH LIYPERPIVI
     SKALETSKIA VNCFGQHVTI ALMSYKGINQ EDGIIIKKQF VERGGLDIIT AKKHQVEIPL
     ENFNNKERVK STAYSKLESN GLVRLNAFLE SGDAIARNIS SRTLEDDFVQ DNQISFDISD
     RYTDMYQSRV ERVQVDLTDK VKVRVLTMKE RRPVLGDKFT SRTSQKGTVA YIADETELPY
     DENGIKPDVI INSTSIFSRK TVSMLIEVIL TSAYEVSPYN NDGQNRPICF PSSNETSIDT
     YLDFAKRCHR DRYPSLSDDD INDKMFCDTI LYDPETDKPY SSKIFMGPIY YLRLRHLTQD
     KATVRCRGKK TKLIRQANEG RRRGGGIKFG EMERDCLIAH GAANTITEVL KDSEEDYQDV
     YVCENCGDIT AQIQGNKVCI RCSKQNLSTI LTKVDTTHVA KVFITQMNAR GVKVKLEFEK
     RNPLFYKPLD VVDLSPNFL