ID   A0A139H5D4_9PEZI        Unreviewed;      1702 AA.
AC   A0A139H5D4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012494};
DE            EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494};
GN   ORFNames=AC578_5741 {ECO:0000313|EMBL:KXS97622.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS97622.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS97622.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS97622.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-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   -!- SIMILARITY: Belongs to the RdRP family.
CC       {ECO:0000256|ARBA:ARBA00005762}.
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:KXS97622.1}.
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DR   EMBL; LFZN01000138; KXS97622.1; -; Genomic_DNA.
DR   EMBL; LFZN01000138; KXS97626.1; -; Genomic_DNA.
DR   STRING; 321146.A0A139H5D4; -.
DR   OrthoDB; 2905532at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
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; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR   PANTHER; PTHR23079:SF55; RNA-DIRECTED RNA POLYMERASE; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF05183; RdRP; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022484};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1298..1540
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   1702 AA;  190747 MW;  459C8ED342EAC86C CRC64;
     MASLKSFTHI LQDGIAPTDN LWHYHVPNLP SSSKTDSAHL VKSITFVSNA NKQVVSLQMV
     PAPFNRVIKD DPLHLFLLLS VADFRLQLPA KTNGGGPQLA PARDTADYIA RLVKTGIVLN
     GVAYHFFGHS NSQLKSRSCF MFGASKELIQ RKVEALGDFS NMQSVSKKAK RLGLLFSSAE
     HALELQPERC SDIDDVKLGE FVFTDGCGMI AVQLAKLIAQ RKRIIYRNKK YLPSVLQIRY
     RGYKGVLMID PTLRGKTQVL FRHSMKKLKD VKDLSFSVVE HSKPYTFGFL NDEIVVLLNA
     LGVSTDTILG KQREYMRFLD RAYNGEPRAA FQFLSYQNEL DLAEQLLIEG FHSVRKSLRN
     LVRTEHSRML NKYEEQRCRI MLTQSRLLFG VCDPTGRDGS VSKLPPGTCF VRITLDGDGE
     PRTLINTEVL ITRNPCLHPG DLQKLRAVDV PEFSHLVDCI VFPIRGNRPS ADLMSGGDLD
     GDKFFVTWDP DVIPKKIAQA AVYPGVKERH HFGQITDDDR ADYFARYTST SLGRIKNLYL
     KWARLKGAMS PECQQLNRLF SQCVDGNRVK VPTVLEDPPE TPPDALPFVL DVLHGDATAA
     ITKNTPLVFD SESRSADILE LILHRDSVAI SEFELIQFVL RSCSKTGEDF SSFADLFNYA
     ALNDEQKAWV IGRLPPSRHM PCLIKNGLVQ SDLILPSELR KFELHHSGLH WQPVFLSSVD
     RMARFLPSVC RALDVFHKKL IVLRADERLT LMIYVPQKIP RASEVQVDAS VRVFAIPRSS
     DTASPSCKVM PTKVTYRLYC DDTVFQLYES KRANTFVFLT KGPVDSSSYR DTTMRGEQRR
     QKQKTLDDGV NFECRASIAL QKISAQVQKH VGRLNRAGVL AAEIYVISNR DVQSMRYLDR
     WLHFIDTEEK LPNFEPISQE YRIPTVSDIE RSTIPEKIAR IVWDQDFQAV EQLTTAGEVT
     RTLQLLYSTA QMSTLQFTYS RLIESVTGKD GPAQLCMLRS LLNFLPTAAF LTQSLLDSEL
     WKTHRQSLED ESSAIALELL PEFARLSHHL SAFVKLPFQL VLRNIKQLSV QQLTDLCEII
     ALTVPDVELA LDLLLESLEP EISRILIGRP LEISQCIKQL IGITIEHVEE ANSNKKFLDS
     HLRLVHDGSS DGFAVVKTLL RIDSPSTTLK TGDHIRLVVT EPPSNAPLKQ PHTMDAVVLH
     TEQGSARLRC IHQPPAYVQD CAWKYRHCGS FVTSKAMFEA VARFYGSKEA CCSLYKQLIG
     LPLSVDEQDS NSNNHDSTET NASMLNDSQN KALQAAMQHR LLFLWGPPGT GKTHTIAIIL
     QNLLVKFPDA RILATAPTHN AVDNMLQKFL DNNKNKSQAF DSCNPLRVAT NLSKVSPALR
     AFTCDAFIGQ DLTSSHSGRR KAQDRVTQSR LIFTTCIGAG LGLLRNETFD IVLIDEASQQ
     TEPETLVPLT KTCKKALLVG DHVQLRATVA KNSVVSGFDV SLFERHYTTS SPSPSSSAKI
     MLDTQYRMHP EICVFSSQEF YQRGLYSDPA NSSIQLPRSA FPWGGARKVF VQCSASEDLG
     HRSKSNEGQV AVCRKICKLL LEHDAMGSTR IAVLTPYSRQ RERLSGKLPG GVEISSIDGF
     QGREAEVVVL VTVRCNVHYE IGFLRDLRRL NVAMTRARAG VIIIGDRQTL TSCDENDADA
     EVKLTWKRLL DQCVEVLVGS DG
//