ID   S3CCL9_GLAL2            Unreviewed;      1483 AA.
AC   S3CCL9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=GLAREA_08123 {ECO:0000313|EMBL:EPE24272.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE24272.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE24272.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(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; KE145373; EPE24272.1; -; Genomic_DNA.
DR   RefSeq; XP_008088360.1; XM_008090169.1.
DR   GeneID; 19467173; -.
DR   KEGG; glz:GLAREA_08123; -.
DR   eggNOG; KOG0988; Eukaryota.
DR   HOGENOM; CLU_001366_0_1_1; -.
DR   OMA; DDYLVIW; -.
DR   OrthoDB; 5477883at2759; -.
DR   Proteomes; UP000016922; 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|RuleBase:RU363098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
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..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1320..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1380..1412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1483 AA;  168275 MW;  F69A750A9EEEE075 CRC64;
     MSTATHLSYP SHGQPTAHRS HMMQSPTQRS PAPQSYNLGR RERPIIQRPA SRRPNANAST
     RYNTTAGSRQ ALNKLPPMRR KKEEPWANWP QVQVILSGLR PNETTWNIHR NFSKYGNIVF
     IDIFELSEGL RNGRGKIKFS TGVECFWQSK TYQMIAVDDS SYNVRVDLVN ERGRDFMMTS
     PVKHHIRYPQ VMPLLPTKMR FGVMVKPDIM MSQHTIYRTR CLKDLKFSVD AFRKKLTVEF
     VVKNLDPRHG PGSTFVGTHP VGELDRINKY MFQIPFDQLK VIHEVPAKGN TFQLAISLSS
     PPQFNRKREE DPQCHSSDAL QWSDFDDGWY RQTDIVYDPY LLGSAPIALQ KDRPVIDIGR
     WTSYVFDFTT DLKHTTLYSN MKQALEDHNV DIVPLNELNI ISGRPASLWT MINPPQFGQS
     AADHLAEDSS IISLPFEVRY QLEVCISREL LNEYNLDREF IEKLAELAKS DASTARNILE
     YVAENDKRIY EPLHLFNSPE ALAFSVKTDI PHYCAYSRKA TITPSTILFS SPTVETTNRV
     LRHYSRENHD GRFLRVQFTD ESFEGKINSC VKQRNDEIFT RVYRTLANGI RIGDRHYKFL
     AFGNSQFREN GAYFFCEDEH LTCNDIRDWM GNFTHINVPA KYAARLGQCF STTRAINGLS
     APTIVTIPDI EHGKYTYSDG VGKISPFLAQ MITAELGLHV AHEPSAFQFR LGGCKGILVT
     WPDAKDREVH IRKSQQKFTA VYNGLEIIRC SQYSCATLNR QTITLLSNLG VGDGVFLKMM
     KEQLSGYQNA MENDNLAIEL LCRFIDDNRM TINIAKMISS DIKDPFVSSL LHLWRSWSIK
     LLKEKAKIVV EKGAFVFGCV DETHTLRGYK APSTEGDAIP EEQLPQIFIQ VPVHGCDPKN
     PVYNVIEGIC LVGRNPSLHP GDLRICQAID VPALHHLRDV VVFPSCGDRD VPSMCSGGDL
     DGDDYFVIWD KDLQPHEWNC SPMDYDAPPA KSQRNPVAVK DLMQHFVRYM KNDSLPQIAH
     AHLAQADQLP GGAKNPKCIQ LAHLHSKAVD YVKSGHAAEM PKDLQPRRWP HFMEKRHKRK
     DQLYESTTIL GQLYNQVERI NFLPQWKVPF DRRILTAYKF EDAALKKARQ LKSKYDVHMR
     RIMAQQEIKT EFEVWSTFVL SKPRVGSDYK LGEEMGRISE GLKEQFRALV IEYAGKEFST
     LGPFVAGMYK VTKEELDCAL AECASTKLVG GRDVPARKME SETMPLISFP WLFENVLTRI
     ATGKDDEENQ VDLSEQFVSK VDKARNRMPV ADDVIRQENG LVVHRGEVLD LFRPEVLIDD
     HSDDGEHDEA SEQLGDLDND DMDLNSGSGK GSPAPRSSYS ESGSDSFIAQ PHIDGFTTKP
     HSKAVQTTLP DETSTSIQKT EVTPSSLTPS GSLIDLDEGE PGYVSPEKAS SPALRCTSPS
     RSLLDSDNEE EILEEETFEE EIVSLDIEET PIDKLAKMMA TTL
//