RDRP_SSDRV
ID RDRP_SSDRV Reviewed; 1700 AA.
AC Q6YI57;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=RNA replication protein;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE Includes:
DE RecName: Full=Helicase;
DE EC=3.6.4.13;
OS Sclerotinia sclerotiorum debilitation-associated virus (isolate
OS Sclerotinia/China/Xie/-) (SsDRV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Sclerodarnavirus.
OX NCBI_TaxID=686987;
OH NCBI_TaxID=5180; Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16361437; DOI=10.1099/vir.0.81522-0;
RA Xie J., Wei D., Jiang D., Fu Y., Li G., Ghabrial S., Peng Y.;
RT "Characterization of debilitation-associated mycovirus infecting the plant-
RT pathogenic fungus Sclerotinia sclerotiorum.";
RL J. Gen. Virol. 87:241-249(2006).
CC -!- FUNCTION: RNA replication. The protein possibly functions as an ATP-
CC binding helicase (Probable). {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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- MISCELLANEOUS: The sclerotinia sclerotiorum debilitation-associated
CC virus contains only a single ORF.
CC -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; AY147260; AAN64332.2; -; Genomic_RNA.
DR RefSeq; YP_325662.1; NC_007415.1.
DR GeneID; 5075997; -.
DR KEGG; vg:5075997; -.
DR Proteomes; UP000000395; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..1700
FT /note="RNA replication protein"
FT /id="PRO_0000401072"
FT DOMAIN 299..462
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 842..991
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 992..1128
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1369..1480
FT /note="RdRp catalytic"
FT BINDING 868..875
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1700 AA; 193148 MW; 959C8A5DB1F64140 CRC64;
MKLRNPKAPI RNDRKAQRSF HKMLSLKAQA KLALTIQDRL ELGLLSNNFI RKKLQFVDGY
CYLKFLRCAE RKTAARNLGS DPSLGLMKRK LVPSQYHSWQ SNYTLLVTKS SKLTFAHVNR
ALGGQKLAEV PANCCIGSTI CPFLSVPGDH SSYLVNQLPY MNGYCYLKLI RRTCRFNAVV
TLGPWPLATD FFDYIIHRNL NKDLGLFKCN LENTINGSFC HIVEADPGSQ NCIFPLPQDC
RIGGSISEVV KTLGPDKEMI ERDAVTEIKK EIAIVRKYNP YHHSSKQQSA LESYGIGSDP
YAVRSHTHAA EKAIENKLLD IVGMNLRRRS VITMLWQKRN KAHLMGRSNC KDVYVNTIME
AKDLVRYDQF SFGLPSVATS TAFIGDALHH MTPESVFDLF ERSPNLMVLH ATIVIPPETL
LKCRSSNPEL YSLRYYDDKF VYIPEGHAGG SYVHEVKNSN WLAISHIQRG GKFLTVKRLE
TLAAHHYFVI VKGKVETDSI RVFQSPSQVE LLDIFADRQS NVRCSLDHAF AIKMERYVHS
LKRLELADVT AKTRQLLSSE ELLQYSPTDL VKIDNYFYFL AHTSRFNSSE ELIGSGFFES
LVSPLKQWFS EICEKFLGKS NFHKTLEALE WKVINYDVKT VIYDMSKPWE KLHWKSENNL
LSFDLDSNDN PTSLVDNTDC EASYSESTKF DYELVQVEDD FIDIRIPGID IPIYDSEYLA
SEEPVEVEES PIPEVLPEIE DNLSDSMSID GWMSQSLKTF LPEHDDKVLS ILEKFGVSKY
GQVVGKNLIL PITDFKSVQF EKIGQDEFTE SLQDRGFGFV SYTPDAERVA VAATDLEHGQ
GVLITSDEAG ELFKKAMPMS VYTCVILGAG GAGKTTFVEK FVKDNPKSFT VVTPLSVLKK
EWQRKGAKNV FTYETALKRS LKKPANEYVI LDDFTRFPAG WIELYMSLNT KSKYIVIGDS
RQADSHSMSG AFANALVPAI DLFAPLSPFY LNWTWRMTRP VANALGHVSW KLPESGKPIL
SVSSEVPKDC VVLAPSTTLK VGVETVNDKA FTYTSAQGAT FDKVAILIDD NITRVCGDKA
VYTALSRSKG EIVFVSTVTG PDTFEKVKCT PFLRTFVELV REYELNQPKV REPEEDFVDD
VTPVTSQPKV SEEFLIEELN KNSVEKFDRE IFRADLGHTD AVKEIGRVTE QIPRQQRSDE
ALNLVTLDKR VHHATVEENL DELARKKALG NILWTNFKEQ YYSGLESVMV DQDLLVSCRA
EITKTYLSKT EALLKGGQLR QSPDFDKFKI ADFLKTQWVR KTEKYGLPIK AGQTVTSFMQ
ETVMATGTLS RYMRRMFDKL CTNPNVYLHR EKTEQDFSTW VKNGWNFSGH ATINDCEAFD
ASQDGAFVEF ERLHAEFLGV PRELIDFYVD TKIKSYIWRG TISVMRLSGE GPTYDFNTWA
NMAFMATKYS IPSVAMTAYS GDDFACDQVL SVKPAFKELE CRFKLKEKRF LKSQGRGSYA
DFCGMIITPN GVIKNPRKLY LSLKSHDEIG TIDKAIVNYY NDLRTLISLG DNIFSALDAT
ETEFFAGCLN VVHDYILRGS NYEGHQNLTL FKKPRTIKWR VERDETRDCL IHMIIQDRKF
IRNLLEGVEQ TCDNKPNSNL IFRGMTNGYQ KRAKFNQLLN RQDEYLDKVL HKSAGQNALR
RLTATLDDTQ DSTVAEQSAV