ID   E3S4P5_PYRTT            Unreviewed;      1458 AA.
AC   E3S4P5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=PTT_17559 {ECO:0000313|EMBL:EFQ87064.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ87064.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ87064.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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=2.7.7.48; Evidence={ECO:0000256|ARBA:ARBA00024517,
CC         ECO:0000256|RuleBase:RU363098};
CC   -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000256|ARBA:ARBA00005762,
CC       ECO:0000256|RuleBase:RU363098}.
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DR   EMBL; GL537176; EFQ87064.1; -; Genomic_DNA.
DR   RefSeq; XP_003304850.1; XM_003304802.1.
DR   STRING; 861557.E3S4P5; -.
DR   EnsemblFungi; EFQ87064; EFQ87064; PTT_17559.
DR   KEGG; pte:PTT_17559; -.
DR   eggNOG; KOG0988; Eukaryota.
DR   HOGENOM; CLU_001366_0_2_1; -.
DR   OrthoDB; 5477883at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProt.
DR   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR   PANTHER; PTHR23079:SF55; RNA-DIRECTED RNA POLYMERASE; 1.
DR   Pfam; PF05183; RdRP; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU363098};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW   ECO:0000256|RuleBase:RU363098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363098}.
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1381..1410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1458 AA;  164519 MW;  CEFA0E5251E4A63F CRC64;
     MHRGNHRGGR GGSRGGGQNS RAYSNSSGSS NGQHNPNRPT FKRPSIPSTS QASQPLQAPR
     PVGLFAAPAQ QQSYVDSNGH SINETYIERS STSSDSPTKK LSVKGPSRLP NQASPRHGHP
     HQRYSPGGQN NSPKPTLKDG SQHWFYNQEE KIKILDIPKA YWTKDIYESM SSFGAVFRID
     IEIGAHTNNA YVVFRPPPIK TLPPQLQLGT TLVRYETRQS LLTTVPSPVN TAKRYFEYNI
     LPAKSIEFGT RISDQTMICM YTVQSPKGIQ MGLDLNRKEL DIQFPLYLFN EVRKYRFRLP
     IALLSHVYRV NDKTTGQPTL IIPFDSPPQF YVQKKEGEGL GDGRTHTSFS NKEKAWNDWN
     TWFRETDIVS AKDKKKLKQL PLMNHKDATI IDIGKYLVLW QQNHQLTREL GRWTNYRLEF
     DAAVLTGPKF KDFSDALADY GVAIEHIDQY AIKSKVTSPL WSLLQEEIST THPHLESTPN
     PNQSSFDDLL ASQMNLDFTV RYQLEACLSN GYLKEHSITS EFLEKLHSDS RRAICLLEKV
     VDKQHIYYDP MDIFSIRIKS LEKKIPSYCT LQRSVVITPT MMHVASPVME TSNRIIRKYA
     ADSDRFIRVK FSDEKTEGQL RSMPNGKSEA VFDRVRRAMR HGIVVAGRYY EFLAFGNSQF
     REHGAYFYAP TSSKSADDIR LSLGDFTQIK TVAKFGARLG QCFSTTRAMR EKVKITPIPD
     IERNGHTFTD GVGKLSPFVA KMAAKELGLS NAFDDPPSLF QFRLGGCKGV LALDLNITGT
     EVHIRPSQQK FHAKFMGLEI IRSSALATPF FNRQIIVVLS HLGVPDHVII KKQQEMVNDY
     ETAMTDESIA LQKLRKHIDM NQSTLTMAAM VLDGFMKIQD PFMMSLLKLW RACTIKNLKE
     KARIAIEDGA FVLGCVDETA KLKGHMNDPQ SRLDATRDEK LATLPEIFLQ VDDTDKKGHY
     KIIEGVCILA RNPSLHPGDL RVVRAVNIPE LRHLKNVVVL PQTGDRDLAN MCSGGDLDGD
     DYMVLWDAAL IPKTINVPPM DFTPEKPEEI DGPISAADIG EFFVTYMKND TLGQIAHAHL
     AQADFRADGV NDETCLALAE LHSKAVDFPK SGLPAEMDRE LRPRKWPHFM EKKHISQYKI
     YRSTKILGML YDQVQLVDFK PQWENPFDKR VLDAFDLDAT MKAKAAEIKS SYDDSLRRLM
     AKHGIRTEFE AWSVFVLAHN HESRDYKFSE EFGRTVGILK AHYRGECRIA AGLGDELSDW
     SLLGPFVAAM YTVTAQEMET ALVECHTTKT VGGQKAPVRA MDPEHMPLIS FPWLFPSELG
     KIATGSKVIR QLPTEYTQGI SHRHKKPVDL ARGLEVEVAT VETDTGVTHY GELLNLDFGR
     TKPEIETNEE SVEKQETSEE KVDKKSSLGK HQEGCGLLEH GIATTRSLSL SSSSLSLPTM
     DSYVWKRDVE SKERLEKA
//