RPB1_IIV6
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 03-AUG-2022, entry version 93.
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};
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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: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; 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.
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
