RPB2_IIV3
ID RPB2_IIV3 Reviewed; 1140 AA.
AC Q197F1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable DNA-directed RNA polymerase II subunit RPB2 homolog;
DE EC=2.7.7.6;
GN ORFNames=IIV3-009R;
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. 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; DQ643392; ABF82039.1; -; Genomic_DNA.
DR RefSeq; YP_654581.1; NC_008187.1.
DR SMR; Q197F1; -.
DR PRIDE; Q197F1; -.
DR GeneID; 4156258; -.
DR KEGG; vg:4156258; -.
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: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 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; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 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..1140
FT /note="Probable DNA-directed RNA polymerase II subunit RPB2
FT homolog"
FT /id="PRO_0000377754"
FT ZN_FING 1092..1108
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT BINDING 773
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 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1140 AA; 128256 MW; 5AF25A307D89BFB8 CRC64;
MNQLNQKTKL DKHLSSDNRA KIVADYFKTN GLVKHQIETF NHFISKGLKT IINNESSIKY
QSHDNYSLKF TNIYVEYPSI IDDDRTIRDL YPQEARNKDL SYTGNVCVNV IEMVENKEGK
PPQISEQYRV PIAKIPIMLG SDVCHLSKYT PLENEQINGH SQADQGGYFI INGKERVLIS
QVRKAYNKPV CFVKSTSQKE DVLICEMRSM CEETFHSTSV QVKMIKNKIM VSLKLKRKLI
DIPVGIVFKC LGYNPDQMGS KFRSLFNLPP EYEKYIDAIK NDCLEEFAYG IAVSAADGDN
SDSGGESGGE EEADQEEHIV KVFRNMSTSV DKDGGMAATG ITIEDVQKSL DMDLFPHLGI
TSTRKQRVDL LAFMVKKYLL TLTRKIPVDN RDDYNHKRVE TAGELYSFLF RLLYKKFQKT
CITQIRNRKP DISNFLRTSG ITTGILYSFS SGYWGVQRNT YIRTGVSQVV NPKVSLLANY
SSLRRVVIPE SKDGKEAKTS EIRQIHPSSS FLVCPVETPE GKGVGTVLNM AVFCQVTTGI
STCEIMDQID SFGVDLKCHC TIKDPNNCLL LLINGSPYGN GHANVIHRLN FLNDTNISIV
VNRALGVIEI FSDAGRFIRP IFDLDKICNF EGEIVPSFKW FLDNQLIRYI DINEAAANSI
AIELRDLSTN PNTRYNLMEL DPCGMFGIVA GIIPFPDRTQ SARNCFYSSM VKQAIGFVPC
HNLKTETVSH TLNYPQKPLV TTSFAEYNQL NEYPNGINAI VAIACYTGYN QEDSIILNKS
SIDRGLFGTI TYNTFTAQEK KNGIIEERIE IPSNAIKIRD CNYGLVGPDG IVRLRQRVKK
GDVLICKVTI KNKNQDEKLV DSSVIVQHGE EGYVDRIVDN VIDGCRIVKV VIGQMRTPEI
GDKFCSGMAQ KGTCGMIFPQ EDMPFTASGM TPDIIINPNC IPSRMTINQI ISTVMGKLYT
VNPNPRFRNG NSFQENSNTI LKELCHHLKL NGFDPSGSEV MYSGFTGERI QSTIFMGPTY
YHRLKHMVKD KMHARSHGQV TTLHRQPNCG RSQGGGLRFG EMEKDCILVH GATQFLNERM
FLNSDPFQID VCKDCGMMSS TSKKCHHCGS INVKRCNIPY SCKNLLQELN GMGIKTKIDL
