RPO5_FOWPN
ID RPO5_FOWPN Reviewed; 182 AA.
AC Q9J5C0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, 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=FPV100;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
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 (By similarity).
CC {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: This enzyme consists of at least eight subunits.
CC -!- SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 30
CC kDa subunit family. {ECO:0000305}.
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DR EMBL; AF198100; AAF44444.1; -; Genomic_DNA.
DR RefSeq; NP_039063.1; NC_002188.1.
DR SMR; Q9J5C0; -.
DR GeneID; 1486648; -.
DR KEGG; vg:1486648; -.
DR Proteomes; UP000008597; 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; Zinc; Zinc-finger.
FT CHAIN 1..182
FT /note="DNA-directed RNA polymerase 30 kDa polypeptide"
FT /id="PRO_0000121459"
FT ZN_FING 135..175
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 182 AA; 21373 MW; 1D33E3B9D0DCCBEB CRC64;
MDMMKIIKKY INSEEEAQKL LKWAIDNANI YYLRNIVNTK VNIEETKFKT VHNIGIEYSK
DNKYKLSYRN KPSIATNEKY KELCNLIRST NGIEKETLRY LLFGIKCVHA KVEYDIEKVP
DYDYSNYFDV LKEKSTIRCV ACKSNNTIPM ILQTRSSDEE PTVRVVCKDC GKNFAPPRLK
FN