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Database: UniProt
Entry: A0A1L3IZI7_9POXV
LinkDB: A0A1L3IZI7_9POXV
Original site: A0A1L3IZI7_9POXV 
ID   A0A1L3IZI7_9POXV        Unreviewed;      1288 AA.
AC   A0A1L3IZI7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA-directed RNA polymerase 147 kDa polypeptide {ECO:0000256|ARBA:ARBA00021673};
DE            EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
GN   ORFNames=BAV00105 {ECO:0000313|EMBL:APG58288.1};
OS   BeAn 58058 virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Oryzopoxvirus.
OX   NCBI_TaxID=67082 {ECO:0000313|EMBL:APG58288.1};
RN   [1] {ECO:0000313|EMBL:APG58288.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BeAn58058 {ECO:0000313|EMBL:APG58288.1};
RA   Wanzeller A.L.M., Souza A.L.P., Azevedo R.S.S., Junior E.C.S.,
RA   Filho L.C.F., Oliveira R.S., Lemos P.S., Junior J.V., Vasconcelos P.F.C.;
RT   "The Complete Genome Sequence of BeAn58058 Virus Isolated from Oryzomys sp.
RT   Rodents in Amazon Region-Brazll.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 147
CC       kDa subunit family. {ECO:0000256|ARBA:ARBA00006884}.
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DR   EMBL; KY094066; APG58288.1; -; Genomic_DNA.
DR   RefSeq; YP_009329703.1; NC_032111.1.
DR   GeneID; 30524344; -.
DR   KEGG; vg:30524344; -.
DR   Proteomes; UP000202017; 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; 3.30.1490.180; RNA polymerase ii; 1.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 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; 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; 1.
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:0000313|EMBL:APG58288.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000202017};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          186..467
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
SQ   SEQUENCE   1288 AA;  147896 MW;  6762ED97AA62D892 CRC64;
     MAVIAKVSYS LYNQEEINAT DILINHNKND DDIGTVKDGR LGATDGSLCK TCEKTELKCF
     GHWGKVRLYE THVLKPEYIG EVTRILNHIC IRCGFLRSRE VYTEDLSKLS SYELKKLKEK
     LLSKKKSCWN SKCMQPYHKI TFSKKKVCFV NKSDDVQVPN ALIYQKITSI YRKFWPLLEI
     YQKPENLFYK NFFPIPPLII RPAISFWIDS IPKETNEITY SLGMIVKYCN INADEQVIQK
     AIIEYEDNKI ISNNTTSINL SYITSGKNNM IRSYIVARRK DQTARSVIGP DTNLTINDVG
     IPGYIRNTLT EKIFINAFTI EEVKKLFTEN KIKFYFNKRL NQLTRIKQGK FIKNKIHMLV
     GDWVEVALKE NTSIIFGRQP SLHRYNVIAS TIKYTDGDTI KIPPGIANSQ NADFDGDEEW
     DIIEQNPKSV IEQSILMYPT TLLKHDIHGA PVYGSIQDEI VAAYSLYRMI DLSLDEVMNL
     LGKYGLDFLS KNNNKKTYTG KDIYEYLIGE PVNYGNILRN GKLITDSVGS DLVVAMRQMS
     LAGLISDYKS NVEGVDFIIK SSYVFKRFLT IYGFCVTFKE LRPSPEFTNR LDALNAEKIE
     LIKDAYNRYL KDVDSGKILP LSKNMEIDAI DSMLSNLTNL NIKEIENYMI ETLQSNPENN
     LLKMARAGYK VNPTELMYIL GTYGQQRIEG DLPETKIMGR ILPYYLPDTK DPEGRGYILN
     SLAKGLTGSQ YYFSMLVARS QSTDIVCETS RTGTLARKII KKMEDVVVDG YGQIVYNNIL
     IKYAANYTKI AASDCKTVEL IYPDESMVWF LEISAIWERI KNGFIYSQKQ KVSKKTLAPF
     NFLVFIEPVK SNETIINTKE LYDMIQNVIE HVKENYYFTI SNIDFIEYIF LTHLNPSRVK
     ISKDTAINIF KNFYNKLNYS LGGGTPIGII SAQVLSEKFT QQALSSFHTT EKSGAVKHKL
     GFNEFNNLTN LSKSRTEIIT LISEDIDKLQ NIKINFEFVC LGELNPTISV KEIDNTYFIY
     IDINRLFIKR ADITELIVEY IIERFVSFSV LIKEWGLDTT LLDANNIRIT IAAIFVEPQK
     LSLNKFMMIL TGAANKGKIS KYKIPINEST YYDNFNKHKK VYKITIELLN LKELGSFDLE
     NVNVYPGVWN TFDIFGIETT RSYLCEALLN TYGEGFDYLY QPCDLLSSIL CMNYEPESVN
     RFKFGSISAL KRATFGDNKS LLTAALHNKT EYVNDNSSCH FFSKVPKIGT GYYKYFINLE
     MLTRLERKIS VKLSEKMIDD VINITEDF
//
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