ID   RPB2_IIV6               Reviewed;        1193 AA.
AC   Q91F97;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable DNA-directed RNA polymerase II subunit RPB2 homolog;
DE            EC=2.7.7.6;
GN   ORFNames=IIV6-428L;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX   NCBI_TaxID=176652;
OH   NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH   NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH   NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH   NCBI_TaxID=58607; Gryllus campestris.
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA   Jakob N.J., Mueller K., Bahr U., Darai G.;
RT   "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT   coding strategy of the genome of Chilo iridescent virus.";
RL   Virology 286:182-196(2001).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA   Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT   "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT   defining the core set of iridovirus genes.";
RL   Virol. J. 4:11-11(2007).
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; AF303741; AAK82288.1; -; Genomic_DNA.
DR   RefSeq; NP_149891.1; NC_003038.1.
DR   SMR; Q91F97; -.
DR   GeneID; 1733408; -.
DR   KEGG; vg:1733408; -.
DR   Proteomes; UP000001359; 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; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
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; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 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..1193
FT                   /note="Probable DNA-directed RNA polymerase II subunit RPB2
FT                   homolog"
FT                   /id="PRO_0000377755"
FT   ZN_FING         1137..1158
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   BINDING         808
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         1137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1193 AA;  136060 MW;  A0DC39385C6C2519 CRC64;
     MNNMNLNNMN LNNMNLLKEV SEENRLMLLK DYFQTSGLVK HQLETFDHFI FHDIKTIIDD
     EASIIFNGKR SLSSQIKNGA VEEGYNRKES EKIMLKFENV FVAKPTITND DTTVRPLYPA
     EARQKMITYD SFVFVDVLEY VLRDEEEILV NKHLRVQIAK IPIMLRSSTC NLYNCTPQER
     IELGEGIEDP GGYFIINGNE RVLIGQLRNA YNRSICFRNK FSEPLTCDMR SMSEETGHSV
     LIQLRLNDSP ISQKRNLKKL DKNGTIDLII SQTKTPIPIS FVFRVLKVAT IDKLKFLIGD
     EEELDKYLIK IVEETSDGGI FDDMEIEISQ EDDFNEENEE STEKKKITQF IEQDMFPHLG
     VSSTHEEKAI LLGKMVRKLL LVNETSINAN KFAQRANDET NKTNKTNKMY YTQEDRDNYS
     NKRVETAGVL CFELFRMLYK RFIKSNINQL EKRNRVEMDV ISKNAFITTG LHFSFSTGNW
     GVQKNNYIRT GVAQIPQNKV SFGAFFSYLR RFVIPMGKEG KNTKIRQIHP SSIFFACPSE
     TPEGQFVGIT LNFSMLAEVS IRTSSVVIKE IIEASHQAFK HVHEISLEEN KQFLSKLSII
     FVNGGICGLT SKPQQLLSDV RDLKLKHCLK YDVSAVFIPE LKEVHISSDA GRFIRPVLNL
     QSIKTNGNVM WNSFQNCLEN GHVVYKDAYE IEQSQIAINL QDLSRYPTVY DSMEIHASCM
     LGVMAAQIPF AEHTQSPRLC YQSSMAKQAI GNIPSHHVKS DNTTRVMDYV QRPLVTTQIA
     EMNRFNDFPN GLNAMVAVAI YTGFNQEDSI ILNKASIDRG MFHVVTYKTI IVEERKIGVN
     EKICMPVASV RRMNNYSLLE DNPESPYFGV VKVKSFVKRN DVLVGKVITK ISKDGTRQET
     DHSTIVSISE EGKVDRIIRT SKKGILMFKI VIAQQKRPEI GDKFCSAMAQ KGTVGMILEE
     VDMPFMEDGS IPDMIINPHC LPSRMTINQI MASIMGKTCC AKNETFGDAS PFQESSLEKP
     QDKIHALCKE LEECGYNYNG TETMMCGWNG KKLRAEIFFG PVYYHRLTHM VSDKIFSRAS
     TNQKRHAITR QPLNGRANEG GLRIGEMEKD CMLVHGISKF LHEKMFDQSD KFIINLCVPC
     KSYFKVVKTQ NGFFCSGCNG IDIVKFNCPF AAKLFFQELT AMGQKLEFKV KNA