ID   RPO5_VACCA              Reviewed;         259 AA.
AC   O57187;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase 30 kDa polypeptide;
DE            EC=2.7.7.6;
GN   Name=RPO30; OrderedLocusNames=MVA051L, ACAM3000_MVA_051;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Rpo30 may have a role in RNA chain elongation.
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: This enzyme consists of at least eight subunits.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O57187-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O57187-2; Sequence=VSP_018891;
CC   -!- SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 30
CC       kDa subunit family. {ECO:0000305}.
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DR   EMBL; U94848; AAB96429.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10449.1; -; Genomic_DNA.
DR   PIR; T30797; T30797.
DR   PDB; 6RIE; EM; 3.10 A; S=1-259.
DR   PDBsum; 6RIE; -.
DR   SMR; O57187; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; DNA-directed RNA polymerase;
KW   Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..259
FT                   /note="DNA-directed RNA polymerase 30 kDa polypeptide"
FT                   /id="PRO_0000121455"
FT   ZN_FING         155..195
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   REGION          214..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_018891"
FT   HELIX           37..50
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   TURN            105..109
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   HELIX           114..130
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6RIE"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:6RIE"
SQ   SEQUENCE   259 AA;  29812 MW;  C4878BB1C6222516 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
     DGLIRSTFDR NDEPPEDDE