ID G0T5J3_IRV9 Unreviewed; 1342 AA.
AC G0T5J3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Wiseana iridescent virus (WIV) (Insect iridescent virus type 9).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus;
OC Invertebrate iridescent virus 9.
OX NCBI_TaxID=68347 {ECO:0000313|EMBL:ADO00511.1, ECO:0000313|Proteomes:UP000112896};
OH NCBI_TaxID=107013; Wiseana cervinata.
RN [1] {ECO:0000313|EMBL:ADO00511.1, ECO:0000313|Proteomes:UP000112896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21632757; DOI=10.1128/JVI.00645-11;
RA Wong C.K., Young V.L., Kleffmann T., Ward V.K.;
RT "Genomic and proteomic analysis of invertebrate iridovirus type 9.";
RL J. Virol. 85:7900-7911(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
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; Evidence={ECO:0000256|ARBA:ARBA00024550,
CC ECO:0000256|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; GQ918152; ADO00511.1; -; Genomic_DNA.
DR RefSeq; YP_004732950.1; NC_015780.1.
DR GeneID; 10963889; -.
DR KEGG; vg:10963889; -.
DR Proteomes; UP000112896; 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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 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 {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 187..547
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1342 AA; 152975 MW; 475F965DDA49C8C8 CRC64;
MEIVEEISNL GKISFGILSP EEIIKMSCCN ITAVKVSDKG ENIYSKFMGT IENGENCKTC
DKDVWECSGH FGHFNLEHPV VNPIFINDVV NVLKCICFKC YKFILSEDHL KLENMVYKFS
NILEWVKTIN YCYNCETEKT SLSVVNETIV DEDKTPIDTR KILRILENLD AKTVKILGFN
PDMSHPKNFI FTVFPVLPPC CRPYVMSDEN CCDDDLTYQL TEIIKNNQYL SEEYLTKTEL
KRKKSVLQSS LLPTLDIQQK HFTNLKFRIS TYFNNSKKKA KHAATARPIT GLKERIAGKE
GQIRHNLLGK RCDQSGRTVI GPDPTLKLNE LGVPAEMAKI LTIPVHVTPF NIDELTDIVN
SGKANFLIKG SDPKRSINLK NIINFRGTLL YFGDIIERDG ERIVIKDTKF ELKVGDSIIR
NGKKLKDVRY PENKKIKLDI GDIIKRQLRN GDWVLLNRQP TLHKPSMQAF IVVIIDGKTL
RMNLAMAKAY NADFDGDEMN LHVPQSYEAT AELMELSSSS KCIMSSQNGK PNACIVQDSL
IGLFYLSKEE WTVQTLEKEQ FFDLLMVLQS ISQDFSTRIE KIYSTVVLHG IKNPCIFNGK
GILSFLFPTD FDFVNAGVTI KNGVFISGTL EKNVVNNQLI KIIYKDYGEV VVASFIDNIQ
FITNKYLIER GFTINAADCL KNGNNEEIKE LTRSTFVKAT TLKEVTINPF IREQKILGAF
SSLTDQSMKK SKDSLEPFNN FKITEESGSK GSIFNICQIT SMLGQQTIDG KRVYGLIHPQ
DNEFKNKGFI ENSFVEGLRP REFLHHAMAG RKGVIDTALL TSVSGYGQRQ GVKLNEDIKI
YPDYTVRDVN GRLYQYIFGE VGYDPAQTII VDGVQCICDI VRLVQRLKKP LEPENKKFRK
LDEDELENMV DFIIPRRGIP ADVEERICKL RKDPILKQLK KVEICDELVP ILKKELEVRY
YQTLMSPGEC VGIIGAQSMG EFSTQATLNT FHVAGSTTTG TVTNCLTRFQ EINNATKNPK
NIIGKIYFTS NNSTIEEIRN LGIRVKHVIF QNVIQGEWNI ENIKNEEWWY STFKKIYTVN
LSDVKTKIRF TLNKEILYAY RVTCEMIKEA LEEKLGVICI FSPLLTDEIY FDVFCGIENH
KLDLFVEGML YPTYICGIEG VKGVSYRECE KLKVWYIQTE GGTLKDFYAL EGVDVENTTT
NNVWDIYNTL GIEAAREFRI KEMVEIMGSG VDISHIKLRA DRLTFTGTIQ SLTRYTMRGE
KPFSKVGFEE IMENFYRTAR DAEVDDLTGV SASIMCGKRA KVGTSMFDVK LDMERILNNG
KLDPIQDEEE VDEGAFVDYD YY
//
