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Database: UniProt
Entry: A0A0W0FJX2_9AGAR
LinkDB: A0A0W0FJX2_9AGAR
Original site: A0A0W0FJX2_9AGAR 
ID   A0A0W0FJX2_9AGAR        Unreviewed;      1184 AA.
AC   A0A0W0FJX2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=WG66_10854 {ECO:0000313|EMBL:KTB36643.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB36643.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB36643.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB36643.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) 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=2.7.7.48; 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTB36643.1}.
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DR   EMBL; LATX01001892; KTB36643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0FJX2; -.
DR   eggNOG; KOG0988; Eukaryota.
DR   Proteomes; UP000054988; 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:SF14; RNA-DEPENDENT 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:UP000054988};
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          15..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..651
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  133784 MW;  BC3FCEED2FD12A51 CRC64;
     MTEVIRKGSS QLLWDQLPDP IDWNGPLDGI DDESGSKEDL ARGAEARGEE GEGAEEDIEE
     QYDSYIAMMS QAKHLGIRSY SQEYDDIDID PEDDISGLIA AYDEGPGVPT QPIPPLSTNV
     TLNSEDTLAV PTNSECGGLG KRDSSTSTCI DPRPLKNARF DSPDDQSKPS VSSIDTPYYI
     TRRPLNKWKL PIGVLWEIDR LMASGKITED SLKSECLSKL QCLGNNVRAA PMVEKMLTGK
     DAGGELVKVS NRPDPFAKER STKFPYDELD KEEEQFREGQ EFGCLGFNKN SDWYGGKVHL
     RAKVKNVANK YSKDPDFRVL LDRAELGPSF RFSRRFGSAS FVRMKIPKAL WGSAFIEPLM
     SFLLRPFVFC GSVYRAFYEK DKTVFLFRTN EMSVGNSISS TRVVPGRLSL TDFLEFHNPL
     EPNSKQTVAK WASRFALGLS TSAPGLKLKA ENIHEIEDIM SVEGEDMTDG SGFINQAALR
     LLQSKFKWDE WPTAIQCRVA GAKGMLLQHP NNENHEPEVW IRPSQTKIRY SNNDEDECRL
     IIDVLRSCHS RSSCVLGTET IINMAENGVP AKRFFKLLDE GFNRLITSLT TWEGEDAMYN
     LWATVARLGG VRAARAARVQ AGLARVLGYS EGDAQDDEDE DGLDEQESED SSVAWWGDEI
     SGQPSSLEET VMRLLDAGFN PYICSVLREK LSAIVTTHIQ NYGAKYRVEV PMSCMTFIQP
     GEFFLTRHLP SVDNLSGFTD PLGVLEEGQI FYKSARRDLP TLDGHLTDTI IGPVLVTRHP
     CKLPTDVQKW DAVDCPQLRD QTGIIFFSIK GRRRAADYLG GGDYDGDKSL LIYDPSIVDP
     FVNADIRFAD PRNDIEEKCF VKGTKKLPEL VAEHIPTKEN PLARVRALQD FLLGGLRNIS
     RVGQYSNMHD YCTVTKGYTH EDTIRMAHMF CRTLDGAKTG LTVREDVFTA DRKSYNRGVM
     KWKKPAVKSS MKSQYVSDDG GMKVERPKHL GPFIMDSLVK YSLHRAATFE RQFKERMLKH
     KKHIIDEHLV EPWRKAEKYA QQKKEKGCPL DMQALDEIRS HVKKVYEKHR EQVKKMRPKR
     NGGHFTDLPI EIRQNQLRDL SKEFASYPNP DDLMLDEGIV SRLRASYAYL HDCEANKYTD
     KGWTRFPWDV AMSELCLIKG KAIGGSKTVV AGFYDRFFLT KTRQ
//
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