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Database: UniProt
Entry: U4L921_PYROM
LinkDB: U4L921_PYROM
Original site: U4L921_PYROM 
ID   U4L921_PYROM            Unreviewed;      1644 AA.
AC   U4L921;
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-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012494};
DE            EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494};
GN   ORFNames=PCON_09614 {ECO:0000313|EMBL:CCX10021.1};
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:CCX10021.1};
RN   [1] {ECO:0000313|EMBL:CCX10021.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX10021.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX10021.1};
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   -!- SIMILARITY: Belongs to the RdRP family.
CC       {ECO:0000256|ARBA:ARBA00005762}.
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DR   EMBL; HF935502; CCX10021.1; -; Genomic_DNA.
DR   STRING; 1076935.U4L921; -.
DR   eggNOG; KOG0988; Eukaryota.
DR   OMA; HTTHTEN; -.
DR   OrthoDB; 5477883at2759; -.
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   CDD; cd00590; RRM_SF; 1.
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|ARBA:ARBA00022484,
KW   ECO:0000313|EMBL:CCX10021.1}; RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW   ECO:0000313|EMBL:CCX10021.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1559..1590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..187
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1567..1583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1644 AA;  185559 MW;  C4D554B5DF12EF89 CRC64;
     MTVPSSQNSG PTRSGYGGRG GRGGRGGRGG GGGHRGGRGN GYGNRTPATD LEFVLPPRPA
     PTGPPSKIQR TISVPNPGPR SGPVPQSNPS LRPSASAPLA MDRKPSPVPG PRPAPTGSLA
     QIKRLSLVSS PGPGSGPGVT LSERPSAAAP TGPPAKNKRP SPVPSPGPTS GPRAESTIPP
     RPSASAPPAM EKKPSSGLGS RQGSISGSDS GGSRRGTPAN EQRATVNGQQ GIANGQQGAV
     NDQQGKRRAK QFAEALQKGG FEPDTPHTQE AGGRALQLVQ RAIRDMARGE TMGSVPTGSR
     SKDGINTSAS QPQMAQKQQE PQMVPEAIGG WTRERKPKIA PYRGLKDEEY KKYHEVPVHV
     GPGLKNESVM DIFISLQKYG PIESIRLLTN NTGSFIGKAI VIFKSVRYPF WQEEEGIEFG
     FGKVAVRWNR PTKTPYVPSK INRSKLHVGK MEFNVRSLEF GFMVKPEEFM VMYSSEPHIT
     NIIWEVNLFK RRIEITYTMK KTQEQPKVAD SDPDQAKNPS QDDTSKFMIE IPFSHLKGLL
     TPADEDPDAD IRTFVVPLPN PPKCFRQLID WSKTMNEIGQ MVWNIQDTWA RQTDVEYDMK
     ARMEEPVSLR HKKPIIDLGR WTTYRLEFKL KTPEKKAEFK AMMSALKEYN IQAQPLTNFN
     VNRENFALTT VWDFLDTDPS FGDYNLSYPV RYQLESCISH GFINEHNITQ QFLEELRRLP
     ERTSVILLET VAEAKKRMYD PMEIFNLPRD RRLAMGRALP EFCVYMQRAT VTPTGIHFHT
     PSVEISNRVI RQYNYCSNRF IRISFSDEEH IGRLRPSDRI TSNELYNRIW RTLANGIVIG
     DRKFEFLAFG NSQLREHGAY FFASDGKITC DTIREWMGDF SDIPYIAKYA ARLGQCFSTT
     KPFKLKKYTP ERIDDVERNG YRFTDGVGKI SPLLATLITQ TMQKNRPTDS YQSCCFQFRL
     GGCKGVLVSW PDLPKYKLQI RNTQIKFWSE HAELEIIRCS QFSAASLNRQ LIIVLSNLGA
     PDQYFRDRLR NVLTDYNEAI HKPSKALEIL TKYVDPNYMT LRIADLVRGG FMKSQEPFVI
     SVLHLWRAWT MKYLKEKAKI VLEHGAFLLG CTDETQTLRG WYEDDKEDDL AQIFCQIWDH
     HSKPPGPRII TGRCVVARNP SLHPGDVRIV EAIDVPALHH LIDVVVFPQT GDRDVPNMLS
     GGDLDGDDYV VIWDEELVKP GVVKNEPPAN YTSNDARKAD GPVTITDVMK FFIDYLKNDR
     LGSIANAHLA HADHQEDGVK SSICLELAQL HSDAVDFPKS GVKASMTKKH RVQEWPHFME
     KPEEEGQRIS DKILGQLYQM VERVEFVPQY NLEPNEAIMT AFNLTEKEMQ WAKDIKTSYD
     KDMRRIMSQH SINTEFEVWS TFVMSHSGGN DYKFHETIGE HSATLMDRYR EMILNSCGDR
     AQELPRKVAA LYVYTQNHIE EGKKYLLNLR VETTPKLKGK ELNSNWSKME LAVMPLMSCP
     WLFADILIYI SKGQLNVQKD YELGKPPVFQ NWRDDEDDVE RITIEDLAKL GKDMGGLVVT
     EETDDEDEEE KKRKAKGKAV DVGSFDDDDD DEDIEVVQLV DVSVPPPQKK RNEHMGFNAA
     GNDVDYQAIE EKLKEMEFKW EDLE
//
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