ID   RPB10_ASFWA             Reviewed;          80 AA.
AC   P0C981;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=DNA-directed RNA polymerase RPB10 homolog {ECO:0000250|UniProtKB:P42488};
DE            Short=RPB10 homolog {ECO:0000305};
GN   OrderedLocusNames=War-105;
OS   African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561444;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P42488}.
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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000858; 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   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; Transcription;
KW   Zinc.
FT   CHAIN           1..80
FT                   /note="DNA-directed RNA polymerase RPB10 homolog"
FT                   /id="PRO_0000373080"
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;  9031 MW;  BF0C8894DD1AABC7 CRC64;
     MLIPVVCFTC GFPIGTYAAI FDKARTEYIK TKMGGTLPQN IPLDASLQIE LKDLITALGI
     PMRVCCRTHL ITTLDYRKYY