ID   RDRP_PCVC               Reviewed;        1117 AA.
AC   Q8JVC2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   29-SEP-2021, entry version 54.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
GN   Name=p1;
OS   Penicillium chrysogenum virus (isolate Caston/2003) (PcV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC   Ghabrivirales; Chrysoviridae; Alphachrysovirus.
OX   NCBI_TaxID=654932;
OH   NCBI_TaxID=5076; Penicillium chrysogenum (Penicillium notatum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12888349; DOI=10.1016/s0022-2836(03)00695-8;
RA   Caston J.R., Ghabrial S.A., Jiang D., Rivas G., Alfonso C., Roca R.,
RA   Luque D., Carrascosa J.L.;
RT   "Three-dimensional structure of penicillium chrysogenum virus: a double-
RT   stranded RNA virus with a genuine T=1 capsid.";
RL   J. Mol. Biol. 331:417-431(2003).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC       genome. {ECO:0000305}.
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;
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DR   EMBL; AF296439; AAM95601.1; -; Genomic_RNA.
DR   RefSeq; YP_392482.1; NC_007539.1.
DR   GeneID; 5075912; -.
DR   KEGG; vg:5075912; -.
DR   Proteomes; UP000006714; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   Pfam; PF02123; RdRP_4; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   4: Predicted;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase.
FT   CHAIN           1..1117
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000404268"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  128548 MW;  0A59F9B85F5943B3 CRC64;
     MTVSGRSSWQ NGKTTNAMRA GKLATERDLE SANYGSRSVE KLRHERAVGN LNKGRFLGMN
     KWSDEQLKHS MARYEDLAAT RHNLFAVIMP SGCGKTSLAR TYGMVDVDEL VSRAEHDQYV
     EMRNEIVCGR GDWHDHNTLW FARLNQTLAL LDYSVPVVIF VHTEETALEI GARPVACLTL
     ETTAHEMNIS GRGPKFREFS RESLRSCKPS NRVPNQYRFK SNKELEAFFL EVMNVSGLPV
     GAPFKYSTSI WNSSYSRDVP GWILRGERAG TQQVSINELR LLFEQGKIPK ECVDYYVRAS
     YVPTQFDFGV TMFEWSQALG QLPGCYNSRR DFDTLTDLMG VFPPHSPKEV TRSNVTLRTL
     CHTFDILSMP DAKEIASYHV GEGHTLVTNL LANWKGITQF TTVSHLVFPW FKVCERDWSD
     KMKTLHSLVR CSKFFMNTRI TEKDRQALMY MDLLVGRGEY TVDEMAEVEL RTDDTYNTKH
     LSYDPNRQVF TNQQYKKDFI TSVEEAYVRL KIEPKPVNVD GFIDFYHRRA SWLTKGGLVY
     NKLPPEMKKF GGQVFDAIYN TCREIQGRHN KKSLFEVYEL AEVLQGANEN NFNLTKTQIK
     YEVGKKDRTL LPGTLVHFVV FTYVLYLAEK QGQIGSVRLN TDSEVDIRYF DKKMCTGVFH
     VLYDWADFNE QHSAWEMGVV VDYLKHLIVA PRDYAVFVEA IVAGMYNMGL HDRDGNVHKI
     WRGLYSGWRG TTWINTVLNF CYVHIALQNV ERLFGVRVVL YVDHGGDDID LGLSEPAVMP
     WFLEVMDAML FKANKWKQMF GTRSEFFRNT ICDGRVYASP TRALASFVAG DWEGAGRATV
     KERVVSLLDQ IAKLRRRGCS EELCQGLTIA TISHWCRIKD GEDWLSLPAE IIHGHPDDGG
     LGVPDRDNNF WRLEEKVPEI NEEWYKVVVP DYKASRDYVN VLARDVEKFS LVIEEREKLA
     RKLSEDSYDI EKSVDHERWK HLLNFRTRVI AKELAVEPME DSVVFEGFLE YEVEEGTEKK
     FDLASRYQEF VSYLSLNGRA ITKEELLDLM SDGEVCLEAI EFQGDIYYAR LVPEFIAYRA
     TMFCKEAINK GVCDAISAQL FFRTICWMSA SVFEHAI