ID   RPB1_FRG3G              Reviewed;        1293 AA.
AC   Q6GZW7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative DNA-directed RNA polymerase 008R;
DE            EC=2.7.7.6;
GN   ORFNames=FV3-008R;
OS   Frog virus 3 (isolate Goorha) (FV-3).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX   NCBI_TaxID=654924;
OH   NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH   NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH   NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH   NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA   Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT   "Comparative genomic analyses of frog virus 3, type species of the genus
RT   Ranavirus (family Iridoviridae).";
RL   Virology 323:70-84(2004).
CC   -!- FUNCTION: Component of the DNA-dependent RNA polymerase that catalyzes
CC       the transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Largest and catalytic component of RNA
CC       polymerase II which synthesizes mRNA precursors and many functional
CC       non-coding RNAs. Forms the polymerase active center together with the
CC       second largest subunit (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   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY548484; AAT09667.1; -; Genomic_DNA.
DR   RefSeq; YP_031586.1; NC_005946.1.
DR   SMR; Q6GZW7; -.
DR   PRIDE; Q6GZW7; -.
DR   GeneID; 2947780; -.
DR   KEGG; vg:2947780; -.
DR   Proteomes; UP000008770; Genome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
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   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   DNA-binding; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1293
FT                   /note="Putative DNA-directed RNA polymerase 008R"
FT                   /id="PRO_0000410577"
FT   DNA_BIND        270..339
FT                   /evidence="ECO:0000250"
FT   REGION          354..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..734
FT                   /note="Alpha-amanitin binding"
FT                   /evidence="ECO:0000250"
FT   REGION          776..788
FT                   /note="Bridging helix"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        354..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with RPB2"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with RPB2"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1293 AA;  140807 MW;  3429056386B93EF4 CRC64;
     MEMFASKSLQ VEGLLFGVCS PEEILATSVV EVTKSCLKAE TGSVYDPRMG SAGVDDDDAL
     CPTCENTGRE CPGHFGHIEL AKPVVLFYKE TVAWLKRCCH VCGTVGNEPR PFFFAPYSAC
     NACGAQRPLV RLVDAHDPCA IRVTVRRKDG EPETMPPELI LATLDRVRDS DVDRVLGRGK
     GSHVRFHPRR LVMTRMPVLP PCCRPNARQW PDGAMQDDNL SVFVSQIVKV NQRIKALEPD
     NPAVEGLVAQ LRLKTLCFVD NTKGKVMHAT NRKPMAGIKE RIGKKGGLLR QNIMGKRRNQ
     TGRSVVGPDG TLEVDEVGVP EAIADNLTVP VMVTPFNVSS LEAMMRDGRV SSVEMRDGTV
     HRPSEWRPSH GDHMETADGS PLGRVTRPSY DARDPSVVLR SWKTGETVTR PPPFSWPKLE
     PGMTVTRCLV DGDPVALNRQ PTLHRNSMLG MRVKRLPGKT IRLNLSVTSG FNMDFDGDEG
     NLYLPQGPQA RSETMLLMNP KSVIMSARGP HAEVSLVQDG VLGCHLMSLN SEIPCPPEEL
     ATCLMEVHGC EGWDVRDVEK GATPRDLLSS VLPSTLTVDC GGGCRIESGK IVSGHLTKSA
     VKKIVRAVCL ENGGDAAGKL VDKLQFLTNA WLSHRPFSVG YSDCLTERPE ETVRMVADAV
     CSKILEAEAA DDEDGVSVAL CGARDRGQAV TCAALTPDNR MAVMSRAQSK GDMFNLTQIA
     GLLGQQYVGG SRPGKEIDGG RRSLPHYPRV WDLEQTTLKY ESRGFVRSSF LKGLNPREVF
     FHAKSGREGM ISTSQMTGVT GYAERKMVKL NEDLVSAYDG TVRDAMGNVV QFVYGGHGMD
     PQRCWSDGCP VNFKTLAEEC SSQECSSQIS GLRSPAVTSV EEASLLVPVG LCPGAPDPVR
     ESLFLKHASV ILKGAEEHPC EDHSAWRERV ARSYAAAVLC PGEAVGVLCA QSIGAKQTQQ
     TLDTFHKAGV WLDDAGSVPF GELLGLSQKP MRRQCVVPLK VDPSTPGDEV RDLVGCSFVR
     RDLLDLLAVR PSTATVGKTA SLELDPVKCF ELRISPADVA YAVAEKFPPP HFDVSVSSFG
     VTLSWSVNYP VDNLFTGLFS VQVGGTPGVE SYRLLRGRDG GWVAVTKGTN LGAFLCHPLA
     DWERVRTDDV WDVYETLGLA AAKKRLYELM FSCVGDNLYP AHIKLLTDRM MRRGRPTPID
     RYTMRTCEVG PLSRAAFEES LDILTGAGCT AETEHCAGAG ARVAAGLPVR AGTGYMGLLC
     GKGFFDEPVV KVPDADGREY VDYSYSDDES FEW