RPB1_ASFP4
ID RPB1_ASFP4 Reviewed; 1450 AA.
AC P0C987;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=Pret-111;
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 [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 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}.
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DR EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C987; -.
DR Proteomes; UP000000859; 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_0000373086"
SQ SEQUENCE 1450 AA; 163880 MW; EEA0A96497974246 CRC64;
MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI
TCSHQRKQCM GHPGILQMHA PVLQPLFIAE IRRWLRVICL NCGAPIVDLK RYEHLIRPKR
LIEAASSQTE GKQCYVCKTV HPKIIKDSED 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 RQTPINYQRA 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 SQLLTDVRQV PVNVASIVKN ILLSSATGVL PFDEKTILQK
YTMVKTFCKN LPYVFINNIQ ERLQTPIPVY LKRAASLMRM 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
