RPB1_ASFK5
ID RPB1_ASFK5 Reviewed; 1450 AA.
AC P0C989;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=DNA-directed RNA polymerase RPB1 homolog {ECO:0000250|UniProtKB:P42486};
DE EC=2.7.7.6;
GN OrderedLocusNames=Ken-111;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
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 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 {ECO:0000250|UniProtKB:P42486}. Note=Found
CC in association with viral 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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C989; -.
DR Proteomes; UP000000861; 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_0000373088"
SQ SEQUENCE 1450 AA; 163832 MW; 456314BF07D01250 CRC64;
MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI
TCSHQRKQCM GHPGILQMHA PVLQPLFIAE IRRWLRVICL NCGAPIVDLK RYEHLIRPKR
LAEAASSQTE GKQCYVCKVI HPKIIKDSED YFTFWVDQQG KIDKLYPQII REIFSRVTYD
TVVKLGRSKN SHPEKLVLKA IQIPPISIRP GIRLGIGSGP QSFHDINNVI QYIVRKNLLI
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 DGKLVVSMLL 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 SQLLTDVRQV PVNVASIVKN ILLSSTSGVL PFDEKSILQK
YTMVKTFCKN LPYVFINNIQ ERLQTPIPVY LKRAASLMRI LIRIELATVK TLNITCEQMS
AILDLIRLQY TQSLINYGEA VGILAAQSVS EPLTQYMLDS HHRSVAGGTN KSGIVRPQEI
FSAKPVEAEQ SSEMLLRLKN PEVETNKTYA QEIANSIELI TFERLILQWH LLYETYSSTK
KNVMYPDFAS DVEWMTDFLE NHPLLQPPED IANWCIRLEL NKTTMILKSI SLESIVNSLR
AKHPNTYIMH SVENTASGIP IIIRIYLRES AFRRSTNTRM ATDEKIAVNL VDKLLNSTIR
GIPGIKNANV VKLMRHRVDA QGKLVRLDNI YAIKTNGTNI FGAMLDDNID PYTIVSSSIG
DTMELYGIEA ARQKIISEIR TVMGDKGPNH RHLLMYADLM TRTGQVTSLE KAGLNAREPS
NVLLRMALSS PVQVLTDAAI DSAVNPIYGI AAPTLMGSVP RIGTMYSDII MDEKYITENY
KSVDSMIDML
