ID   RP30_VAR67              Reviewed;         259 AA.
AC   P33796;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA-directed RNA polymerase 30 kDa polypeptide;
DE            EC=2.7.7.6;
GN   Name=RPO30; ORFNames=E4L;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
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 poxviridae DNA-directed RNA polymerase 30
CC       kDa subunit family. {ECO:0000305}.
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DR   EMBL; X69198; CAA48986.1; -; Genomic_DNA.
DR   PIR; G36841; G36841.
DR   RefSeq; NP_042089.1; NC_001611.1.
DR   SMR; P33796; -.
DR   GeneID; 1486410; -.
DR   KEGG; vg:1486410; -.
DR   Proteomes; UP000002060; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR009162; RNA_pol_30_chordopoxvir-type.
DR   InterPro; IPR024394; RNA_pol_30_chordopoxvir-type_N.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   Pfam; PF12410; rpo30_N; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF000745; VAC_RPO30; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..259
FT                   /note="DNA-directed RNA polymerase 30 kDa polypeptide"
FT                   /id="PRO_0000121458"
FT   ZN_FING         155..195
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   REGION          220..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ   SEQUENCE   259 AA;  29882 MW;  C8975613983764C0 CRC64;
     MENVYISSYS SNEQTSMAVA ATNIRELLSQ YVDDANLEDL IEWAMEKSSK YYIKNIGNTK
     SNIEETKFES KNNIGIEYSK DSRNKLSYRN KPFIATNLEY KTLCDMIKGT SGTEKEFLRY
     LLFGIKCIKK GVEYNIDKIK DVSYNDYFNV LNEKYNTPCP NCKSRNTTPM MIQTRAADEP
     PLVRHACRDC KQHFKPPKFR AFRNLNVTTQ SIHKNKEITE ILPDNNPSPP ESPEPASPID
     DGLIRVTFDR NDEPPEDDE