ID   RPB1_ASFB7              Reviewed;        1450 AA.
AC   P42486;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DNA-directed RNA polymerase RPB1 homolog {ECO:0000303|PubMed:23041356, ECO:0000303|PubMed:32725217};
DE            Short=RPB1 homolog {ECO:0000305};
DE            EC=2.7.7.6;
GN   OrderedLocusNames=Ba71V-99; ORFNames=NP1450L;
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 RPB2 (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:P24928}.
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: Virion {ECO:0000269|PubMed:30185597}. Note=Found
CC       in association with viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:8506138}.
CC   -!- DOMAIN: Lacks the typical C-terminal domain (CTD).
CC       {ECO:0000303|PubMed:32725217}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
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DR   EMBL; Z21489; CAA79697.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65328.1; -; Genomic_DNA.
DR   PIR; S78060; S78060.
DR   RefSeq; NP_042792.1; NC_001659.2.
DR   SMR; P42486; -.
DR   GeneID; 22220328; -.
DR   KEGG; vg:22220328; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:0039695; P:DNA-templated viral transcription; NAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   Gene3D; 3.30.1360.140; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   SMART; SM00663; RPOLA_N; 1.
PE   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Late protein; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase; Viral transcription;
KW   Virion.
FT   CHAIN           1..1450
FT                   /note="DNA-directed RNA polymerase RPB1 homolog"
FT                   /id="PRO_0000073916"
SQ   SEQUENCE   1450 AA;  163749 MW;  94D335C50B9A281B CRC64;
     MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI
     TCSHQRKQCM GHPGILQMHA PVLQPLFIAE IRRWLRVICL NCGAPIVDLK RYEHLIRPKR
     LIEAASSQTE GKQCYVCKAV HPKIVKDSED YFTFWVDQQG KIDKLYPQII REIFSRVTYD
     TVVKLGRSKN SHPEKLVLKA IQIPPISIRP GIRLGIGSGP QSFHDINNVI QYLVRKNLLI
     PKDLQIVRGQ KIPLNIDRNL QTIQQLYYNF LLDSVSTTAT QGGTGKRGIV MGARPAPSIM
     RRLPRKEGRI RKSLLGSQVW SISRSTICGN SDLHLDEVGY PISFARTLQV AETVQHYNIN
     RLMPYFLNGK RQYPGCSRVY KQITQSVHDI EGLKQDFRLE VGDILYRDVV TGDVAFFNRQ
     PSLERSSIGV HRIVVLENPK ISTFQMNVSA CAWYNADFDG DQMNLWVPWS VMSRVEAELL
     CSVRNWFIST KSSGPVNGQV QDSTVGSFLL TRTNTPMGKN VMNKLHAMGL FQTTQTDPPC
     FANYSPTDLL DGKSVVSMLL KQTPINYQRA PTWYSEVYAP YMHYNKQDIS TQIRNGELIE
     GVLDKKAVGA GSSGGIYHLI SRRYGPQQAL KMIFATQQLA LNYVRNAGFT VSTADMLLTP
     EAHQEVQEII NKLLLESEEI NNRLLHGDIM PPIGLTTHDF YEKLQLNALK FPDRILKPIM
     NSINPETNGL FQMVATGAKG SNPNMIHIMA GIGQIEINTQ RIQPQFSFGR TLVYYPRFAL
     EAQAYGFICN SYIAGLTSPE FIFGEMNGRF DLINKALSTS STGYANRKAI FGLQSCIVDY
     YRRVSIDTRL VQQLYGEDGL DARQLETVRF ETIMLSDQEL EDKFKYTGIQ SPLFEEEFSR
     LKKDRDKYRQ IFLNVENFNF SQLLTDVRQV PVNVASIVKN ILLSSTSGVL PFDEKSILQK
     YAMVKTFCKN LPYVFINNIQ ERLQTPIPVY LKRAAALMRM LIRIELATVK TLNITCEQMS
     AILDLIRLQY TQSLINYGEA VGILAAQSVS EPLTQYMLDS HHRSVAGGTN KSGIVRPQEI
     FSAKPVEAEQ SSEMLLRLKN PEVETNKTYA QEIANSIELI TFERLILQWH LLYETYSSTK
     KNVMYPDFAS DVEWMTDFLE NHPLLQPPED IANWCIRLEL NKTTMILKSI SLESIINSLR
     AKHPNTYIMH SVENTASGIP IIIRIYLRES AFRRSTNTRM ATDEKIAVNV VDKLLNSTIR
     GIPGIKNANV VKLMRHRVDA QGKLVRLDNI YAIKTNGTNI FGAMLDDNID PYTIVSSSIG
     DTMELYGIEA ARQKIISEIR TVMGDKGPNH RHLLMYADLM TRTGQVTSLE KAGLNAREPS
     NVLLRMALSS PVQVLTDAAV DSAVNPIYGI AAPTLMGSVP RIGTMYSDII MDEKYITENY
     KSVDSMIDML