RP132_FOWPN
ID RP132_FOWPN Reviewed; 1161 AA.
AC Q9J544;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA-directed RNA polymerase 132 kDa polypeptide;
DE EC=2.7.7.6;
GN Name=RPO132; OrderedLocusNames=FPV189;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
CC -!- FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the
CC transcription of viral DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. Responsible for the transcription of
CC early, intermediate and late genes. DNA-dependent RNA polymerase
CC associates with the early transcription factor (ETF), itself composed
CC of D6 and A7, thereby allowing the early genes transcription. Late
CC transcription, and probably also intermediate transcription, require
CC newly synthesized RNA polymerase (By similarity). {ECO:0000250}.
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: The DNA-dependent RNA polymerase used for intermediate and
CC late genes expression consists of eight subunits (147) kDa, (133) kDa,
CC (35) kDa, (30) kDa, (22) kDa, (19) kDa, (18) kDa and (7) kDa totalling
CC more than 500 kDa in mass. The same holoenzyme, with the addition of
CC the transcription-specificity factor RAP94, is used for early gene
CC expression (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=All the enzymes and
CC other proteins required to synthesize early mRNAs are packaged within
CC the virion core along with the DNA genome. This is necessary because
CC viral early mRNAs are synthesized within minutes after virus entry into
CC the cell and are extruded through pores in the core particle (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; AF198100; AAF44533.1; -; Genomic_DNA.
DR RefSeq; NP_039152.1; NC_002188.1.
DR SMR; Q9J544; -.
DR GeneID; 1486761; -.
DR KEGG; vg:1486761; -.
DR Proteomes; UP000008597; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
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 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; IPR024390; RNA_pol_132_poxvirus.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR Pfam; PF12415; rpo132; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Virion.
FT CHAIN 1..1161
FT /note="DNA-directed RNA polymerase 132 kDa polypeptide"
FT /id="PRO_0000048067"
SQ SEQUENCE 1161 AA; 133469 MW; 334C2FC5DD63584F CRC64;
MDQKLGNKFL EPDPKQNVFY RPLHFQYVSY ENFISYRLKE ILSVNRTLLS FKNDTEKIVL
RINNIKIIPP DYSPIIASIK GKSYDALVTF TVDIRKEVMT KDGLHVSTIS SYEGNDSQLI
KIPLLIGYGN KNPLDNSKFV SPNIIGGVFI NKQSIEKVGI NIVEKTTTWP KFKIVKPNAY
TFSFSSISPV NILPTKYRHY KITMDLSQLE NCYISSAKTF ITVNVIVLIK FLINQDLNYI
KNNLTYGMPL ETIYLINAII ESSKTILEAE DFNINDYIES LIESEFQKQR SITSIDDFRY
DLMYNFLPHM VNSSDQLKGF YLLGLLRKFI YCIYHTSRYP DRDSMVCHRV LTYGRYFEIL
ANDELENYIT NIKNDITNSH KNKGVCNVSI HVLTTPGFNH AFSGLLSGKF KKTDGSYRTH
PHYSWMQNIS IPRSVGYYPD QVKISKMFSV RKYHPSQYAF FCPSDVPERG PQVGLISQLS
VLTSVSNIRT TEYIDLKNAI MKYIYTYDKN DISYFQTGHI ITIENDLVAA INPELVDKFV
DDFKFRKRVN YFDNLEIGIS NVKDHMNEIR INIGSGRLIR PFLVVYKGEL VMDTIGEELE
KRIDTITFSD IQKEYPHVIE MLDLEQFVFS NVCESVSKFR ELSDEDKKLY DYCDFPNEFR
DGYVASTLVG INHNSGPRAI LGCAQAKQAI SCLSSDLRNK IDNGIHLLYP ERPIVLSKAT
ETSKIAINCF GQHVLVALMS YKGMNQEDGI VVKREFIERG GLDIVTAKKH QVEIPIENFK
NRERINSTAY SKLDINGLVR LNAFLEPGDA IAKNISSRTL DDDFVADNQI SFDISEKYTD
MYMSRVERVQ VDLTDKVKVR VLTMKERRPI MGDKFTSRTS QKGTIAYIAS ESELPYDKNG
VTPDIIINST SIYSRKTISM LIEMILTSAY SVKPYNNNGK NRPICFPSSN ETDIEYYIEF
ARKCYQSAIP DLDKDELENE VYCESILYDP ETDKPYKTKV FMGPLYYLRL RHLTQDKATV
RCRGKKTKLI RQANEGRKRG GGIKFGEMER DCLIAHGAAN TITEILKDSE EDYQDVYVCE
NCGDIATKKN NNVYCIRCTK LNLYTVLTKI DTTHVSKVFL TQMNARGIKI NLTFNEQNPL
FYKPMKQIDL SPTILKNHDL S