ID   RPB2_ASFB7              Reviewed;        1242 AA.
AC   P42487;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=DNA-directed RNA polymerase RPB2 homolog {ECO:0000303|PubMed:23041356, ECO:0000303|PubMed:32725217};
DE            Short=RPB2 homolog {ECO:0000305};
DE            EC=2.7.7.6;
GN   OrderedLocusNames=Ba71V-053; ORFNames=EP1242L;
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 [GENOMIC DNA], AND INDUCTION.
RX   PubMed=8506138; DOI=10.1093/nar/21.10.2423;
RA   Yanez R.J., Boursnell M.E., Nogal M.L., Yuste L., Vinuela E.;
RT   "African swine fever virus encodes two genes which share significant
RT   homology with the two largest subunits of DNA-dependent RNA polymerases.";
RL   Nucleic Acids Res. 21:2423-2427(1993).
RN   [2]
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   [3]
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [5]
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: 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:0000303|PubMed:32725217}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Virion
CC       {ECO:0000269|PubMed:30185597}. Note=Found in association with viral
CC       nucleoid. {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:8506138}.
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}.
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DR   EMBL; Z21490; CAA79698.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65283.1; -; Genomic_DNA.
DR   PIR; S78061; S78061.
DR   RefSeq; NP_042747.1; NC_001659.2.
DR   SMR; P42487; -.
DR   GeneID; 22220435; -.
DR   KEGG; vg:22220435; -.
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: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:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Host cytoplasm; Late protein; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Viral transcription; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..1242
FT                   /note="DNA-directed RNA polymerase RPB2 homolog"
FT                   /id="PRO_0000048056"
FT   ZN_FING         1180..1201
FT                   /note="C4-type"
SQ   SEQUENCE   1242 AA;  139894 MW;  F77FFE780DF11EE8 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 VVFDLESNSP
     VNTFMIEILE KSIHVLDPIF QPVQHEPNRE 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 LAQRYRMFRR EGKIVHPHTT IYWDSMVDEV
     EFWLDVGRLT RPLLIVDNNI EKYNQACYKA AEARKKGDKD WEKHKIPFIQ 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 DSDGCISYIC RNCGEPAIYN ASHPIYKCMN
     CDVQADIGMV DSRRSSIVFQ HEMRAANVNI TSVLSPRVFQ PA