ID   RPB1_ASFM2              Reviewed;        1450 AA.
AC   Q65215;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=DNA-directed RNA polymerase RPB1 homolog {ECO:0000250|UniProtKB:P42486};
DE            Short=RPB1 homolog {ECO:0000305};
DE            EC=2.7.7.6;
GN   OrderedLocusNames=Mal-107; ORFNames=g2L;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-332.
RX   PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA   Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA   Hammond J.M., Smith G.L.;
RT   "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT   a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL   J. Gen. Virol. 75:1655-1684(1994).
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:0000250|UniProtKB:P42486}.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Found in association with viral
CC       nucleoid. {ECO:0000250|UniProtKB:P42486}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- DOMAIN: Lacks the typical C-terminal domain (CTD).
CC       {ECO:0000250|UniProtKB:P42486}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA50804.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X71982; CAA50804.1; ALT_FRAME; Genomic_DNA.
DR   SMR; Q65215; -.
DR   Proteomes; UP000000860; 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase; Viral transcription; Virion.
FT   CHAIN           1..1450
FT                   /note="DNA-directed RNA polymerase RPB1 homolog"
FT                   /id="PRO_5000146089"
FT   CONFLICT        294
FT                   /note="Missing (in Ref. 2; CAA50804)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1450 AA;  163812 MW;  930544E892505596 CRC64;
     MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI
     TCSHQRKQCM GHPGILQMHA PVLQPLFIAE IRRWLRVICL NCGAPIVDLK RYEHLIRPKR
     LVEAASGQTE GKQCYVCKVI HPKIIKDSED YFTFWVDQQG KIDKLYPQII REIFSRVTYD
     TVVKLGRSKN SHPEKLVLKA IQIPPISIRP GIRLGIGSGP QSFHDINNVI QYLVRKNLLI
     PKDLQIVRGQ KIPLNVDRNL 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 NELLLESEEI NNRLLHGDIM PPIGLTTHDF YEKLQLNALK FPDRILKPIM
     NSINPETNGL FQMVATGAKG SNPNMIHIMA GIGQIEINTQ RIQPQFSFGR TLVYYPRFAL
     EAQAYGFICN SYIAGLTSPE FIFGEMNGRF DLINKALSTS STGYANRKAI FGLQSCIVDY
     YRRVSIDTRL VQQLYGEDGL DARQLETVRF ETIMLSDQEL EDKFKYTGIQ SPLFEEEFSR
     LKKDRDKYRQ IFLNIENFNF SQLLTDIRQV PVNVASIVKN ILLSSTSGVL PFDEKSILQK
     YTMVKTFCKN LPYVFINNIQ ERLQTPIPVY LKRAASLMRM LIRIELATVK TLNITCEQMS
     AILDLIRLQY TQSLINYGEA VGILAAQSVS EPLTQYMLDS HHRSVAGGTN KSGIVRPQEI
     FSAKPVEAEQ SSEMLLRLKN PEVETNKTYA QEIANSIELI TFERLILQWH LLYETYSSTK
     KNVMYPDFAS DVEWMTDFLE NHPLLQPPED IANWCIRLEL NKTTMILKSI SLESIINSLR
     AKHPNSYIMH SVENTASGIP IIIRIYLRES AFRRSTNTRM ATDEKIAVNM VDKLLNSTIR
     GIPGIKNANV VKLMRHRVDA QGKLARLDNI YAIKTNGTNI FGAMLDDNID PYTIVSSSIG
     DTMELYGIEA ARQKIISEIR TVMGDKGPNH RHLLMYADLM TRTGQVTSLE KAGLNAREPS
     NVLLRMALSS PVQVLTDAAV DSAVNPIYGI AAPTLMGSVP RIGTMYSDII MDEKYITENY
     KSVDSMIDML