ID   RPB2_FRG3G              Reviewed;        1221 AA.
AC   Q6GZR3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative DNA-directed RNA polymerase II subunit RPB2 homolog;
DE            EC=2.7.7.6;
GN   ORFNames=FV3-062L;
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. Second largest component of RNA polymerase
CC       II which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Proposed to contribute to the polymerase catalytic activity and
CC       forms the polymerase active center together with the largest subunit
CC       (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}.
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DR   EMBL; AY548484; AAT09722.1; -; Genomic_DNA.
DR   RefSeq; YP_031641.1; NC_005946.1.
DR   SMR; Q6GZR3; -.
DR   PRIDE; Q6GZR3; -.
DR   GeneID; 2947762; -.
DR   KEGG; vg:2947762; -.
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: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   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 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; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
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; 2.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 2.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1221
FT                   /note="Putative DNA-directed RNA polymerase II subunit RPB2
FT                   homolog"
FT                   /id="PRO_0000410574"
FT   ZN_FING         1174..1190
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         823
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with DNA-directed RNA
FT                   polymerase largest subunit"
FT                   /evidence="ECO:0000250"
FT   BINDING         1174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1221 AA;  133260 MW;  8E96C8A2D671B948 CRC64;
     MSRGMTTEGA SLTAAASSSA STWLTESTPS TPSSSGSSYP ALSTFSSCSN SASSPDEADP
     MSEMSPKISV ASMILLKDME EFLHLYVSSA NMHPSNFVRH HIESFDDMLW NEFPAMVARE
     KPVSVKGYRV KFGTVRYEPP CPDGKPWEKL TPAMARRTDA TYHSAAVCDL TVTDPKGLET
     VYPRLELCKI PVMVGSAVCW TRTEGSPLPG ECPSDPGGYF IIKGKERVVV PHIRPAYDQP
     CVYKNGDGWL CEFRSVNRET RQTVLVQAKT DCRRKLEFSL PYIKQYVPVG LVFKALGKTA
     REAVAMCGLG SFLGDEVSCR TVHHQSMAAL LMEQHASAPE DPVADLAKHV PDGRSVYSKQ
     AEGAKQAKYA DRASVEEDRN AKGSKEDYVR HVLAGEIFLH GGDAAEHLGW MVKRMADAAS
     GIGTCTDRDD LANKRVDATG PLIAFLLDGL LKQYVKLFVK SAGCQKNLCP YTVLQNSMVM
     TNSLHMCFAT GNWTVKRLGP PSYVRVGVSQ VLSNNNYGAR VSHLRRIMHA VSFRGKNIRM
     RQLHSSHYGF LCPYETPEGE KVGIVLNMAE GAGFSLETPR EVVLATVRLG KGLPGFFEGA
     PARLAWSGAA GSASVDVDGV LCGVTGDPVG FVREARLCLP GVSVVWKKVE REIHLLGCQG
     RFVRRVLDPE GIRGSGYDSP PAPEERDIEM DPAPSSSPSD SLPCPPGVYV CAQELSVCSL
     GDGEYADPPA SEILTDAMSS VIPFYDHTQS PRNAYQSNMG KQAIGFPAVN CSDRYDATLH
     RLDYPQKSLV DSRSVKRLGF DEMAHGALPV VAIMTAGGFN QEDSVVLNAS SLDRGLFSCV
     TYRTVSCADK RRTKYDSEVV CLPDWGLRNR EWDYDLLGDD GVIDPSCAGA LARRVEGKRK
     AAKRPAGQRT GGGPAGLCDA LWIPAGTVLV GKVSHSLGPG GNPMRRDVSL TVKQSEEGYL
     DRVTVDVDSD GKKLVKVRLR TPRHPEMGDK FASFTAQKGT CGAVLTQEDM PFDKDGVVPD
     LIINPHAFPS RMTVNYLLQM CFGTAACKLG KTYDATAFER EDVVRDIAEA AKEAGIDCWD
     SVLHSGSTGR RLPTKIFMAP CPYQRLKHMV SGKMHSRTHG PTDALTRQPV AGRSREGGIK
     IGEMEQWCKI SHGASESLKE SVYDMSDKYE VPVCKECGRI SDHFEYCRMC DATDMSLVKL
     PYTTKILFQE LRSIGISIAF K