RPB10_ASFB7
ID RPB10_ASFB7 Reviewed; 80 AA.
AC P42488;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA-directed RNA polymerase RPB10 homolog {ECO:0000303|PubMed:23041356, ECO:0000303|PubMed:32725217};
DE Short=RPB10 homolog {ECO:0000305};
GN OrderedLocusNames=Ba71V-95; ORFNames=CP80R;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP REVIEW.
RX PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA Rodriguez J.M., Salas M.L.;
RT "African swine fever virus transcription.";
RL Virus Res. 173:15-28(2013).
RN [3]
RP REVIEW.
RX PubMed=32725217; DOI=10.1042/bst20191108;
RA Cackett G., Sykora M., Werner F.;
RT "Transcriptome view of a killer: African swine fever virus.";
RL Biochem. Soc. Trans. 48:1569-1581(2020).
CC -!- FUNCTION: Component of the DNA-directed RNA polymerase (RNAP) that
CC catalyzes the transcription in the cytoplasm of viral DNA into RNA
CC using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250|UniProtKB:P22139}.
CC -!- SUBUNIT: Part of the viral DNA-directed RNA polymerase that consists of
CC 8 polII-like subunits (RPB1, RPB2, RPB3, RPB5, RPB6, RPB7, RPB9,
CC RPB10), a capping enzyme and a termination factor.
CC {ECO:0000303|PubMed:32725217}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the archaeal RpoN/eukaryotic RPB10 RNA
CC polymerase subunit family. {ECO:0000305}.
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DR EMBL; U18466; AAA65324.1; -; Genomic_DNA.
DR RefSeq; NP_042788.1; NC_001659.2.
DR GeneID; 22220324; -.
DR KEGG; vg:22220324; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR InterPro; IPR023580; RNA_pol_su_RPB10.
DR InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR InterPro; IPR000268; RPABC5/Rpb10.
DR Pfam; PF01194; RNA_pol_N; 1.
DR SUPFAM; SSF46924; SSF46924; 1.
DR PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Host cytoplasm; Metal-binding;
KW Reference proteome; Transcription; Viral transcription; Zinc.
FT CHAIN 1..80
FT /note="DNA-directed RNA polymerase RPB10 homolog"
FT /id="PRO_0000121343"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22139"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22139"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22139"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22139"
SQ SEQUENCE 80 AA; 9089 MW; 02B81894DD1AA834 CRC64;
MLIPVVCFTC GFPIGTYAAI FDKARTEYIK TKMDGTLPQN IPLDASLQIE LKDLITALGI
PMRVCCRTHL ITTLDYRKYY
