RP30_VACCC
ID RP30_VACCC Reviewed; 259 AA.
AC P21082;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DNA-directed RNA polymerase 30 kDa polypeptide;
DE EC=2.7.7.6;
GN Name=RPO30; ORFNames=E4L;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP REVIEW.
RX PubMed=12917449; DOI=10.1099/vir.0.18942-0;
RA Broyles S.S.;
RT "Vaccinia virus transcription.";
RL J. Gen. Virol. 84:2293-2303(2003).
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.
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, 35
CC kDa, 30 kDa, 22 kDa, 19 kDa, 18 kDa and 7 kDa totalling more than 500
CC kDa in mass. The same holoenzyme, with the addition of the
CC transcription-specificity factor RAP94, is used for early gene
CC expression.
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P21082-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P21082-2; Sequence=VSP_018892;
CC -!- SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 30
CC kDa subunit family. {ECO:0000305}.
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DR EMBL; M35027; AAA48041.1; -; Genomic_DNA.
DR PIR; H42508; H42508.
DR SMR; P21082; -.
DR Proteomes; UP000008269; 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 Alternative initiation; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Virion; Zinc; Zinc-finger.
FT CHAIN 1..259
FT /note="DNA-directed RNA polymerase 30 kDa polypeptide"
FT /id="PRO_0000121456"
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"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018892"
SQ SEQUENCE 259 AA; 29796 MW; C4878BB1C634FF16 CRC64;
MENVYISSYS SNEQTSMAVA ATDIRELLSQ YVDDANLEDL IEWAMEKSSK YYIKNIGNTK
SNIEETKFES KNNIGIEYSK DSRNKLSYRN KPSIATNLEY KTLCDMIKGT SGTEKEFLRY
LLFGIKCIKK GVEYNIDKIK DVSYNDYFNV LDEKYNTPCP NCKSRNTTPM MIQTRAADEP
PLVRHACRDC KQHFKPPKFR AFRNLNVTTQ SIHENKEITE ILPDNNPSPP ESPEPASPID
DGLIRATFDR NDEPPEDDE
