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Database: UniProt
Entry: U4L239_PYROM
LinkDB: U4L239_PYROM
Original site: U4L239_PYROM 
ID   U4L239_PYROM            Unreviewed;      1391 AA.
AC   U4L239;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=PCON_08583 {ECO:0000313|EMBL:CCX08990.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX08990.1};
RN   [1] {ECO:0000313|EMBL:CCX08990.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX08990.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX08990.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935440; CCX08990.1; -; Genomic_DNA.
DR   STRING; 1076935.U4L239; -.
DR   eggNOG; KOG0988; Eukaryota.
DR   OrthoDB; 2735303at2759; -.
DR   Proteomes; UP000018144; 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   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..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1391 AA;  159145 MW;  4F0A975FE8F9E9C4 CRC64;
     MASRAAVAPS FQTPRRHPIP EKPEVETPSS QESNYFMSDD EFFSADESST NVRTATSRNA
     RRPPTGPSRP ARTPREPRRG PRTPQSRGHD NTRNNFPRDV QPNSTSQRNL PPREIPTHLT
     STERPSPYID QHRKNPQNYV SGRAPRVQGR GGFKDNRNRR MPQEPMKEEK FDENYMVQFR
     GNEGTRYPKP LVVGLDGSPL PTRRGRGHGG KPKLKQYMLE QAQEQFGVEG DHHLPRRYSR
     GSSVDSFPHA NFDRSSTPSI VATSVDSFPF TPTKPNFSRF NSPRPGQVLS DNSTDEDEGK
     TWYNDERSPW RSNDRISRPN PCPIKVEGIE VIELTDSDEE EHIVLDDIAR EAAESAALEN
     LKKEFGLDDQ SDDYDQYDVT ESLAGDLAEL DLVDEKFDSQ TNTHQSFETF RFLLQYEITR
     VALAVGLSSE ESATRIPAVV EGLSQEFRSA KTRKELWTVM TSFARQISNG KPFVMPEPLT
     DEIWLLINGN TPWSNEIKLS ATATLSHRSD KFNLAINLNP PNTKGGGNIF AQRFGSDRFL
     CLKISSNFFK SKPRYRGFSE AGLRAETARW LDQKELSLLN RRWRCFFVKS ETKKNRHRKE
     DEFEFGPELL NPDRAKGVSD SYFLAYFFAE SGVGLGDEAC YRTKDQLGFI KEIKSGRDEM
     IRSEMTRDDL IRWHMPLEKL MDADFAKTWD RIRLGLSTSV PTVIFQPDKI RFVEDIRSPK
     GIVMNDGCSV CSPKVMRMIR EWLKLDETPV AIQGRIGGAK GMWFTDPEAD IYSEEISITI
     TASQRKFPPH DVDADSDTMD WARRTLFVLN HSKAPAPATL NLQFVPILAA QGVPFPAFQQ
     FLEQHLEEDL QELLEAASDP ISLRSWLSSG AMRQRRQYGH IPSYISGTPQ LNDEQICMLL
     DAGFDPLKCG FLMDKLNMIV KNECNDILDG LHIRVPSSTT VFMLADPTGT LKEGEVSLQF
     SQGFLDTTLQ IRRDCIEGDV LVGRNPAHLP TDIRKVRAVC TSHPGLRMLK DVIVFSTQGD
     VPLADMLSGG DYDGDKAWVC WDRRIVEPFR NNPSFVAFKK WKSDDWVEKT YPDSRLLKDL
     GPDPNTPEFF KMFFSRGLQS MLEQDSLLGM CTEILSRYVY ANFRNIKGID RTILDLANLC
     GLLVDAPKQG IQPTPRTIDL LHALNRTLTR KPGYKTPKDK ENYPMDDPSQ WYILDQLVLY
     VGNNKVQEKQ KQFEVLINRQ GKWTDQHLTK RYHTFNELAN QDESLRRVRG YLNDELEGIQ
     RLWRKRMSPK GKDPTTYSFR AELETVYDAY IAIKPPPNVL NNPLVESWAA DSDRTFGEWR
     LLKASMLYWM NHGHQKLPWW LVMPELCHMK AEESAIETRY PAPRTITADM FMVLKPATRR
     FNDGFEPDHD N
//
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