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Database: UniProt
Entry: F2NZ18_9VIRU
LinkDB: F2NZ18_9VIRU
Original site: F2NZ18_9VIRU 
ID   F2NZ18_9VIRU            Unreviewed;       873 AA.
AC   F2NZ18;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS   Diadromus pulchellus ascovirus 4a.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Toursvirus; Toursvirus dptv1a.
OX   NCBI_TaxID=158683 {ECO:0000313|EMBL:CCA61446.1, ECO:0000313|Proteomes:UP000203898};
RN   [1] {ECO:0000313|EMBL:CCA61446.1, ECO:0000313|Proteomes:UP000203898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19636425; DOI=10.1371/journal.pone.0006397;
RA   Bigot Y., Renault S., Nicolas J., Moundras C., Demattei M.V., Samain S.,
RA   Bideshi D.K., Federici B.A.;
RT   "Symbiotic virus at the evolutionary intersection of three types of large
RT   DNA viruses; iridoviruses, ascoviruses, and ichnoviruses.";
RL   PLoS ONE 4:e6397-e6397(2009).
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; CU469068; CCA61446.1; -; Genomic_DNA.
DR   RefSeq; YP_009220717.1; NC_011335.1.
DR   Proteomes; UP000203898; 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; 2.40.40.20; -; 1.
DR   Gene3D; 6.10.250.2940; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000203898};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          188..526
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   873 AA;  98716 MW;  1E51F0B8C963649A CRC64;
     MSYVRELKSI SFAVSSPEDI RNKSVYEVKS IKLGDSKYNT IYDPRGGALF GKACETCKQH
     EQACTGHFGH IELNAPVVHP LFFNHVFNIL KVVCSSCSRL LVSRQHLEFS GILKYDGERR
     LAEIINKVKK FKECFHCGVL KREYTIKKDP LLNIIQCDGV DVSDIEIKAV FDDIDAETLD
     MLNISHPRNC CLEVFPVIPP CCRPYEIVCN TLKEDDLSRQ LVEIVKANLQ LKDNETNEAL
     IHNLKLKIET YCRSPKKKGK LVTCNGEQPV GIRERLTGKT GQMRDNLMGK RTEMSSRTVI
     GPDPTLRVDE VGVPEEIVNN TTFPEIVYPH NIEYLKQLVK TEKIEKIKRN DKIIRIDLQI
     YEDVASFLEI GDVVVRRDGG RFTTSSAKFD LEPTDRILRC GVDVTPENVP VPKEPDVRVG
     DSVLRKIRNG DWVLMNRQPT LWKGSMMAFK CRIHKSRTFT FNLAVCKAFN ADFDGDEQNG
     HFPQSIEAVV ELMSLSTPKH CLLSSTNGTP VIVVLQDALL GAYLITDDDG FVIDRDDYND
     LIMHLTKGYD GVMRRRRQIR ATLKSRGLPC AERDLRRGKN IVSLLFEESF NFKHDDFEID
     RGVVVSGRLS KAYLGSSHNS IMSMLVSQYS PDVCMDFLND IQFMTNKWML SRSFSINLSD
     FRSVDGVRGV VDDKLAEAKV VEETIINKKL KEAKINGVLP NAKDLGMKIS TQIENNNMVT
     TILSGSKGDY FNLGQVKGLL GQQIINSKRI PTKIDNGTRS LPHYPRNELS DRDRYESRGF
     IMNGFYDGLN VKEFFFHAMS GRQGVCDTAM TTFMSGYNMR KLVKLTEDIK IQNDRVVADS
     SGCVYDFSYG PLGFNPENGV PDVDAVINKI VNS
//
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