ID RPB1_IIV6 Reviewed; 1026 AA. AC O55766; Q89506; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 22-FEB-2023, entry version 96. DE RecName: Full=Probable DNA-directed RNA polymerase II subunit RPB1 homolog; DE EC=2.7.7.6; GN ORFNames=IIV6-176R; 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 [GENOMIC DNA]. RX PubMed=7698884; DOI=10.1159/000150390; RA Sonntag K.-C., Schnitzler P., Janssen W., Darai G.; RT "Identification of the primary structure and the coding capacity of the RT genome of insect iridescent virus type 6 between the genome coordinates RT 0.310 and 0.347 (7990 bp)."; RL Intervirology 37:287-297(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8021587; DOI=10.1099/0022-1317-75-7-1557; RA Schnitzler P., Sonntag K.-C., Muller M., Janssen W., Bugert J.J., RA Koonin E.V., Darai G.; RT "Insect iridescent virus type 6 encodes a polypeptide related to the RT largest subunit of eukaryotic RNA polymerase II."; RL J. Gen. Virol. 75:1557-1567(1994). RN [3] 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 [4] 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. 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 -!- SEQUENCE CAUTION: CC Sequence=AAB33907.1; Type=Frameshift; Evidence={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; S75674; AAB33907.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF303741; AAB94477.1; -; Genomic_DNA. DR PIR; T03179; T03179. DR RefSeq; NP_149639.1; NC_003038.1. DR SMR; O55766; -. DR GeneID; 1733004; -. DR KEGG; vg:1733004; -. 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:0006351; P:DNA-templated transcription; IEA:InterPro. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 2.40.40.20; -; 2. DR Gene3D; 6.10.250.2940; -; 1. DR Gene3D; 6.20.50.80; -; 1. DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. 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. 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. FT CHAIN 1..1026 FT /note="Probable DNA-directed RNA polymerase II subunit RPB1 FT homolog" FT /id="PRO_0000377495" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" 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 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 588 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 590 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 592 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT CONFLICT 452 FT /note="I -> N (in Ref. 1 and 2; AAB33907)" FT /evidence="ECO:0000305" FT CONFLICT 651..652 FT /note="LT -> N (in Ref. 1 and 2; AAB33907)" FT /evidence="ECO:0000305" SQ SEQUENCE 1026 AA; 116963 MW; C66698CBCE18BC7B CRC64; MSANNNMESE IKEIESISFG MMSSEDIRQM SSFEVKTAKI SSTNLLETVH DPKSGPIGSA PCETCHQNEW DCPGHFGHIE LNVPIIHPLF INHVVNILKI FCWKCNEFLL TKDHLELNNI LKLEKEKKFN AVLEKIKKCD RCVHCTTPRA DYKLVLNDIT YKTIYRTFSY QGGAVKTARD KKLNESREIV SAEMVKKIFD NIKLEYVEML GISHPKDFCL EVFPVIPSCC RPHEVQDGNI NDDDLTYQLM EIVKNNSMIG AIKLEKESME KQYPECLKVK EILLLSNVEK QKKEIDDFLK KPIKNGLKTK KKINKEEITP LDQYLKLHDK YVKYVNNLKF RIETYCNNSQ GKATHATTGR AIKGLRERLT GKEGQIRNNL LGKRCEMSAR TVIGPDPTLK IDEVIVPKEI AQSLTFPDFV NKHNIDRLTK LVNSGNAIRL VKKNESGQEI KINLAAAINN HGTPLQHDDI IKRPKITNNH EEKHNYEEKH NFDTFETIVI KDPKNFVLKE GDILFRNNFQ QKVVLPSKKF IKLEEGWIVH RYLQNGDILV LNRQPTLHKA SMMALRVKIM DVKTFKFNLA CTKPYNADFD GDEMNAHAPQ SEESKAELFT LSTPKQCIMS CQSGKPNLTI VQDSLTGAYL MSKENNNDAT LTNGEFNDIL MVLTQNDEYN GDVVDYFLKR KEDVSNTLKK LGFSGTVLNG KGLLSLLFPN DLYINEEDLK INRGVIYDGC LTKKYLSSTE SSLIKILYKE YGVETCATFL NNIQFLTNRW LMISSFSIHA GDCIKQKEVL GTVEQCLMES EKIKMTTQNP FIREQKIMQT LSNAKDVGMK IAKDALKRDN VNLHAQNNFL TTVESGSKGD HLNIAQITSL LGQQITEGQR VKPLLSNGKR TLPHYILKEE NNDTEHFHDL LEEYESQGFI SSSFAQGLNP KEFFFHCMAG RQGVCDTAMS TATSGYIMRR NVKLTEDIKV AYDGTVQDTR GRRFQMAYGE LGYDPSKLVK VNGKPEVCNI ARLVNKLNCN FEDNIK //