ID   RPB9_ASFM2              Reviewed;         105 AA.
AC   P0CA23;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=DNA-directed RNA polymerase RPB9 homolog {ECO:0000250|UniProtKB:Q65157};
DE            Short=RPB9 homolog {ECO:0000305};
GN   OrderedLocusNames=Mal-073;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
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:P36954}.
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:Q65157}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:Q65157}.
CC   -!- SIMILARITY: Belongs to the Asfivirus DNA-directed RNA polymerase RPB9
CC       homolog family. {ECO:0000305}.
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DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000860; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Early protein; Host cytoplasm; Metal-binding;
KW   Transcription; Viral transcription; Zinc; Zinc-finger.
FT   CHAIN           1..105
FT                   /note="DNA-directed RNA polymerase RPB9 homolog"
FT                   /id="PRO_0000373487"
FT   ZN_FING         4..26
FT                   /note="C4-type; atypical"
FT                   /evidence="ECO:0000255"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P27999"
SQ   SEQUENCE   105 AA;  11787 MW;  187D6F39DE6FD9AF CRC64;
     MKICKACSSC MVRTYVDGNI IFRCSCGESV QGDSQNLLVS SKVYHTGEME DKYKIFIKNA
     PFDPTNCQIK KDCPNCHLDY LTQICIGSQK IIILVCRCGY TSNRG