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 22-FEB-2023, entry version 88. 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}. 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; 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:DNA-templated transcription; IEA:InterPro. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 2. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF7; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2; 1. 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. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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 //