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Database: UniProt
Entry: A0A0P7B1Z1_9HYPO
LinkDB: A0A0P7B1Z1_9HYPO
Original site: A0A0P7B1Z1_9HYPO 
ID   A0A0P7B1Z1_9HYPO        Unreviewed;      1360 AA.
AC   A0A0P7B1Z1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE            EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN   ORFNames=AK830_g6098 {ECO:0000313|EMBL:KPM40471.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM40471.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM40471.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM40471.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-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:KPM40471.1}.
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DR   EMBL; LKCW01000083; KPM40471.1; -; Genomic_DNA.
DR   STRING; 78410.A0A0P7B1Z1; -.
DR   OrthoDB; 5477883at2759; -.
DR   Proteomes; UP000050424; 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; IPR035979; RBD_domain_sf.
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.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424};
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..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1218..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1310..1327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1360 AA;  154759 MW;  47753D0C814A233E CRC64;
     MTRSRPPPGH NHRQHRGGAT SRRSPTNREN VPPHRQQWRS NTSNTQPPTE WHTWPEFTVY
     LDNLPTNVTT VNLWDWFSNE GDIVYMDIFE RGSQGSMSGK IRFEPPPKRD FWSTGKYSVT
     HPDGHKYPNG LSIHVKASGE VPDGWVRSPV CPDRHHPIKI TLHPLALQFG SLVGLKKMKV
     MKSFCVPVAD ESLKVELNLK MKFLTAFFQT EVVTQHGHSK VREHKLVIDF SRMKEVHQTA
     CEDDNIAIVV PLKFAPRYYW KQDDMTSVFS DAAKSWGASE AWCRATDILK DVESRMEHPV
     ALHTEYNDPG FIDLGRWTTI RFVLGGKSKE AAVLNRQLIS ALEDFNIISQ VRDDFKAVIG
     KAPEIWGHLE HPKMLEEGNA LHLLGLSTAP ATQVSFEVRY QLEVCISRRI LNEHHISVEF
     LRELASMDPS RARLLLEYLA DQNELVQNPM SVFENPDAKS YFPHVRVPHY CALMRKAVIT
     PTTIRFNTPT VEMSNRVLRR YSHMHDRFLR VQFMDEAENS RIRINKDRND EIWKRLSRTL
     YQGIKIGDRV YEFLAFGSSQ LKQCGAYFFC PTHHTSCDDI RKWMGQFSHI KIIAKYAARL
     GQCLSTTREV RGISVPSIRP IEDIERNGHC FTDGVGKISP FIAQMIVEDI GLDVFDQPSA
     FQFRMGGCKG VLALWPDAKG TEVHVRESQE KFKAEFNGLE INRCAKFATA TLNRQTITIL
     EALGVPTSSF VDLLNHQLHI YELAMEDNKT AVEILRTFVD ENQTTLAIAE LLEADFKTEQ
     AHEPFVVNIL NLWRTWSLKL LKEKARIHVE NSAFVLGCVD ETKTLRGHSW TTEDSKDKDV
     NKLPQIFLQL TNSKDYNKTR VIKGVCLVGR NPSLHPGDIR IVEAVDEPKL HHLKDVVVFP
     ATGDRPVPSM LSGGDLDGDD FFIIWDSSLM PKTWNYPPMD YTGPKPQQLD RDVNVDDLRD
     FFVKYMQNDE LPLIAVSHLA TADNFGLMSQ KCLELAALHS KAVDYPKTGE PATMRRDQQV
     RKWPHFMEKK NIYHSKKALG VIYDRVVNKS IQFNPIWDSP FDQRIAEHDT VKPDNDMLNA
     AKKIKRDYDT SVRRILNQHD VKTEFELWTG FAMSKPPVGS DYKRQEELGR EYGVLKQRFR
     DICYEAAGGK HAEAVDRFVA AMYLVTEEEI KLALCETMDD ADCVSQSGQA EAKAMPLISF
     PWIFHWVMIR LVSSGKMSKG PTQVATDGKP SQHLEQPPID KQSESAKASH KASVVETARI
     DLGADYTHLP DGTVIHRGEP LTLFDFSETA PSESPVLEPG EEKAFRSQEV QQGDQHGPSS
     NGNGDKDQVL TEAEEKGRET EAQKESAMGR LARLIDCEGE
//
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