ID   RPB1_IIV3               Reviewed;        1377 AA.
AC   Q196X0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable DNA-directed RNA polymerase II subunit RPB1 homolog;
DE            EC=2.7.7.6;
GN   ORFNames=IIV3-090L;
OS   Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX   NCBI_TaxID=345201;
OH   NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH   NCBI_TaxID=42431; Culex territans.
OH   NCBI_TaxID=332058; Culiseta annulata.
OH   NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH   NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH   NCBI_TaxID=7183; Psorophora ferox.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA   Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA   Kutish G.F., Rock D.L.;
RT   "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT   virus).";
RL   J. Virol. 80:8439-8449(2006).
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}.
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DR   EMBL; DQ643392; ABF82120.1; -; Genomic_DNA.
DR   RefSeq; YP_654662.1; NC_008187.1.
DR   SMR; Q196X0; -.
DR   PRIDE; Q196X0; -.
DR   GeneID; 4156234; -.
DR   KEGG; vg:4156234; -.
DR   Proteomes; UP000001358; 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..1377
FT                   /note="Probable DNA-directed RNA polymerase II subunit RPB1
FT                   homolog"
FT                   /id="PRO_0000377494"
FT   REGION          1343..1377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1343..1362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         495
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1377 AA;  155906 MW;  9D48D10DAA84FF8B CRC64;
     MTFQPEIADI AKISFGVLSP EEILKMSCCK VTSVKVSDKG ENIYSKFMGT IENGENCKTC
     DRDVWECPGH FGHFHLEVPV VNPIFINDAC NILRCICFNC YKFIVSVDHL KLENLVRRFQ
     DILLYVKNIK HCYNCESEKL PLSVVNEIIV DEDKNPLDTR KLLRVLENVD DETVRFLGFN
     PTMSHPKNFI FTVFPILPPC CRPYVMSEEN CCDDDLTYQL IEIIKNNQYL GDEFLKKAEL
     KRKKSLLQSS LPPTTDIKQK HLTNLWFRIS TYFNNSKKKA KHAATAKPIT GLKERIAGKE
     GQIRHNLLGK RCDQSGRTVV GPDPTLRLNE LCVPKEMAEI LTIPVHVTPF NRDALTQLVN
     SNKANFLIKA ANPKRSINLK NVINYRGTLL YFGDIIERDG TRITITDTKF VLQPGDTIIR
     NGKALKEIRY PERKQIELEV GDVIKRQLMD GDYVLLNRQP TLHKASMMAF KVVIKPVKTL
     KINLAITKPF NCDFDGDEMN IHVPQSYEAI AELKELSCAS KCIMSVQNGK PNVAIVQDSL
     IGLWFLSRDQ WFCQTLKRSQ FFNLLLTIDK AQNFLTRMDQ ICHVLKSKFP SKGNWEGSGL
     DGDGRVSPKV GRMVFNGRGL LSFLFPYDFD YCGGDGLSIE SGVFLEGTLE KNVVNTLIKY
     IYKDYGETVV ADFVDNIQFL TNHYLVDRGF TINASDCLKN ESIAPEIVSL TRATFSKATT
     VRDVTINPFI QEQKTLAILN SCTDQCMKLS KECLSSDNNF CVTTESGSKG SIFNICQITS
     LLGQQTIDGK RVYGLLHPQD NEFQDRGFIA NSFVEGLSPR EFLHHAMAGR KGVIDTALLT
     SVSGYGQRQG VKLNEDIKIY PDYTVRDVNG RLYQYIFGEA GYDPSQTIVV DGHQTICNVY
     RLVNRLNRSY DSSALRPLTE DEIEWMVDFI QPRREYEYIP PDVEQRICSI RRDPIVGQLR
     RIQTVDALVP ILKSHLEKCF YQTLMSPGEC VGIIGAQSMG EFSTQATLNT FHVAGSTTTG
     AVTNCLTRFQ EINNATKNPK NITCKVYFTK GNGTIEEIRR RGKDVKHIVF RDVVEKWTVE
     PATAEWWYAT FKQLYAAPIA ESGTVTKRVR FHLKRDIVFA YRISPQEIKQ SLESKFDVSC
     IFSPFDEGLI LDVFGKIEPH KLEAFVALML PTYISGLEGI KAISYHKCDE LKIWYIQTSG
     GTLSDFYTLD DIDVEHTTTN NIWDIYHTLG IEAAREFRIK ELVEIIGTGV DLSHIKLRAD
     RLTFTGTIQS LTRYTMRGEK PFSKVGFEEI MENFYKTARD AEVDDLTGVS ASIMCGKRAK
     VGTSMFDIKL NLDAILCPPS TSPLLTTEDG TTSATTPIAA TTPEQEDDEA FVDYDYT