ID   RPB2_ASFP4              Reviewed;        1242 AA.
AC   P0C8K4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=DNA-directed RNA polymerase RPB2 homolog {ECO:0000250|UniProtKB:P42487};
DE            Short=RPB2 homolog {ECO:0000305};
DE            EC=2.7.7.6;
GN   OrderedLocusNames=Pret-065;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
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: Catalytic component of the DNA-directed RNA polymerase (RNAP)
CC       that catalyzes the transcription in the cytoplasm of viral DNA into RNA
CC       using the four ribonucleoside triphosphates as substrates (By
CC       similarity). Forms the polymerase active center together with RPB1 (By
CC       similarity). Part of the core element with the central large cleft, the
CC       clamp element that moves to open and close the cleft and the jaws that
CC       are thought to grab the incoming DNA template (By similarity).
CC       {ECO:0000250|UniProtKB:P30876}.
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: 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:P42487}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Virion
CC       {ECO:0000250|UniProtKB:P42487}. Note=Found in association with viral
CC       nucleoid. {ECO:0000250|UniProtKB:P42487}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC       polymerase transcribing complex probably involves a two-step mechanism.
CC       The initial binding seems to occur at the entry (E) site and involves a
CC       magnesium ion coordinated by three conserved aspartate residues of the
CC       two largest RNA Pol subunits. {ECO:0000250|UniProtKB:P30876}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C8K4; -.
DR   Proteomes; UP000000859; 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:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Host cytoplasm; Late protein; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Viral transcription;
KW   Virion; Zinc; Zinc-finger.
FT   CHAIN           1..1242
FT                   /note="DNA-directed RNA polymerase RPB2 homolog"
FT                   /id="PRO_0000355627"
FT   ZN_FING         1180..1201
FT                   /note="C4-type"
SQ   SEQUENCE   1242 AA;  139864 MW;  10E23F427C1CA48E CRC64;
     MEPLRPQITY GPIETVDNEE LTEADMLSFI SAAVNSTGLI GYNIKSFDDL MDNGIPQIVK
     QMFNVDITYK DQRDHTEIDK LRESVQIQFN FTDVNIERPQ HRNYSQGNKI NLLPNKARLC
     GLSYSGPVNL AAEVILTAHY SNGRQEVKRA SIPPFQVSTF PIMRGSNRCH THHLSKTAKK
     EIGEDPNEPG GYFIARGGEW VVDLLENIRF NTLHIHYHTM QQGNNEIIRG EFISQPGGAF
     ENSSQIIIRY MTTGAITIEI NSTKFSKLRI PWYLIFRMFG MTGDDSIIEQ VVFDLESNSL
     VNTFMIEILE KSIHVLDPIF QPVQHELNRE KIIQFLSEKV SKFVSNPSAY KSDENAVQYL
     NERQLTILDK ILLPHMGQTA DTRVRKLRFL GLLIHKILLV IMNVFPPTDR DSYRTKRVHG
     SGVSLAKAFK AIFNTSVIAP IINGFKELLK QTAFEELTQR NIIEAFSAAL SKNTASDLNR
     SMEQSIISGN KTIMVRQRPI VNRVSTQSLE RKNLLNTISA LRTVNTHNTT NASKQTERAD
     MMRRVHASYP GYICVAQSAD TGEKVGMSKQ LAITANVCTA GEVLSLKQRL LSDPAIQQLA
     DVSNKDIVRK GLARVFINGE WIGCCTNAFE LAQRYRMLRR EGKIVHPHTT IYWDSMVDEV
     EFWLDVGRLT RPLLIVDNNI EKYNQACYKA AEARKKGDKD WEKHKIPFVQ NTRFTSQMAK
     DILAGTLTLE DLVAQGICEF ITPEEAENCL VAFSIIELRK HKHDVTRRFT HVDVPQAILG
     LAALVSPYAN CTQPARVTYE TNQGRQTGGW YCFSWPYRVD MNRFFQFYNE MPLVKTIAHN
     YVIPNGLNTI VAYMIYGGYN QEDSVIVSQS FIDRGGFAGT FYREEKVELE SDIESFGKPD
     PLITKNLKPG ANYEKLVDGF VPVGTVVKKG DIIIGKVAKI RGEKDELNKY IDRSVMYGFD
     EPAVVDAVMR PHGPNDEIFG LMRLRYERNL NIGDKMSSRS GNKGIAALAL PTSDMPFTED
     GLQPDLIVNP HSHPSRMTNG QMIETTVGLA NALQGVVTDG TAFLPINVQL LSERLAQEGL
     RFNGCQKMFN GQTGEYFDAA IFIGPTYHQR LQKFVLDDRY AVASYGPTDA LTGQPLDGKR
     SHGGLRLGEM EHWVLTAQGA MQTIIEKSHD DSDGCISYVC RNCGEPAIYN ASHPIYKCMN
     CDVQADIGMV DSRRSSIVFQ HEMRAANVNI TSVLSPRVFQ PA