RDRP_GFKVM
ID RDRP_GFKVM Reviewed; 1949 AA.
AC Q8UZB6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
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;
DE Includes:
DE RecName: Full=Methyltransferase;
DE EC=2.1.1.-;
OS Grapevine fleck virus (isolate Italy/MT48) (GFkV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Tymoviridae; Maculavirus.
OX NCBI_TaxID=652668;
OH NCBI_TaxID=29760; Vitis vinifera (Grape).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11458008; DOI=10.1099/0022-1317-82-8-2009;
RA Sabanadzovic S., Ghanem-Sabanadzovic N.A., Saldarelli P., Martelli G.P.;
RT "Complete nucleotide sequence and genome organization of Grapevine fleck
RT virus.";
RL J. Gen. Virol. 82:2009-2015(2001).
CC -!- FUNCTION: RNA replication protein replicates the viral genomic RNA. The
CC central part of this protein possibly functions as an ATP-binding
CC helicase and/or methyltransferase (Probable). {ECO:0000305}.
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 -!- 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:0000255|PROSITE-ProRule:PRU00539};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ309022; CAC84400.1; -; Genomic_RNA.
DR RefSeq; NP_542612.1; NC_003347.1.
DR MEROPS; C21.001; -.
DR GeneID; 929660; -.
DR KEGG; vg:929660; -.
DR Proteomes; UP000000399; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.90.70.100; -; 1.
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; IPR008043; Peptidase_C21.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR043629; Salyut_dom.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR InterPro; IPR043181; TYMV_endopept_dom.
DR Pfam; PF05381; Peptidase_C21; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF19227; Salyut; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51738; PEPTIDASE_C21; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
KW ATP-binding; Hydrolase; Methyltransferase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1949
FT /note="RNA replication protein"
FT /id="PRO_0000402500"
FT DOMAIN 171..341
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 762..922
FT /note="Peptidase C21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT DOMAIN 1017..1175
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1176..1308
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1682..1788
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 77..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 814
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT ACT_SITE 900
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT BINDING 1048..1055
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1949 AA; 215590 MW; 980657CBE3536119 CRC64;
MVLTLCFHSD RDHHFLSTLP LAEIRRLAPG GFSVFVPEDL LPHLSPSPSC PTPPLPRELT
WSAACNPTNF PHLFRHHRPP PPCTRLTPRP PPPTPAPPSA STLPRVFHGG APPAAFQPAI
DFLHNTIQKD TIASSIIAAL NPSLTSSLTL YPYALPPRWP SALNQAGIPA TSYGHQSHPH
PIHKTIETHL LHEHWANRAT LPSTVMFMKR SKFDKLRVSN AALVKSASNF LHLLNPILTA
RDADRYTHLP LPDTLPSTPL YFMHHSLMYF SPSQIAGLFL AAPFLERLYA SLVLPAESTI
GSHPFFPSLY RYRTTGEHLH YVLEGNPSSS YTQPLTATQW LTTSSITAGD LHLTVTVLES
WFSVHSILIT RGVRPLELPR DIISLPSPDA VLLPNPSAFD IPLRSRLVPR DVCESLFVYV
RAVRTLRTTD PAGFIRTQSN KAEFDWVTAE AWDHLAQFAL LTAPVRPNTY FLPLLSPLAV
VRHWLFRKQR PIFATLTLLS ASTAAAIPIA IARLRTHSVT QLTILGHHFT PPKILARLPV
ALKRLIPKRL LPHLPSHLRP PPSWSPVFTL TFSELPKARF LTFPISGQTH TLLRQLHVPA
ILFAPQRPSR PLIFAGLLIG TVPVLYGAYR WFVSRFDPQT VYNRYSDLLH RPTWHLTFER
EPLSCFPTPF LPHPSSHPRR ARRLPPLPPA PPLPPQPPPP PPPQPSPHPP LFPASIPSPP
PRPSSPPPPA TSPASTPALT PIPAPKTAPP LTFPSPTLVA EPDAPVTARP SPLPLAPSRP
FSELYPGHYA DHSGSFFLQQ PLVASSVPYP ALDCLLVSCS AASGIPKEDL WATLCHIFPP
SDLVSDLGLS TNHLTALAFT YQWLVTLRSG ELVQRHGLLS APFAFEITHT PPVPPATVGH
FALSAPLTPT SACLTGGAPS PVISGPKASA SLPRARFGPR PEAPRPPLTP PGFTPITEPT
PATSPFALAA LRFRLNRQPL PIRQVHAYSI ALPRAKNLVS NLKNGFDGLV SSLPASDRTN
LLPLIQALDH TADFPPARPP VGLIHIAGFA GCGKSYPIQQ LLATQTFRHF RVVTPTTELR
HEWKRALKLE GPSSWRVSTW ETALAKRASV LVIDEVYKLP RGYLDLALLA DPTVEFVIIL
GDPLQGSYNP TNPDSSNHRL IPEEDHLRPF IDFYCLWTRR LPRLVADFFG VPTTNPTRGH
LAFASLNTTQ SPLLVPSDSM ARALTAGGHR AITYAASQGS TYPAPVHIFL DRNSNLVTNH
VALVALTRSR SGVHFRPRAQ DLPRHPQHLF TAFYKYAIDL LAHEADPSKP RPTPVDVTLL
FQQQLRGLTI LRDPSFSRIT GGATHAFLAH APLFTNLHGL RPTTFPDNLP TAPTYLARSL
PYHQTESYPT SALPHRVFPA STTDWSAADD HPRVNPTFVA ETRLPLQSEL APTLPSQPEP
SPTYHSPATF ETVYPGVDGE ALARTFLAAT DPLELEIFFR NNWSNQFPFI NRPDTVACNP
LTLVAPTHNQ KQDPTLLHAS LAKRLRFRDS TAPYTITAKD QALGYILYHS LQRAYCRSPE
PVPFDPVLFA SCIAENDFAQ LTSKTQATIQ ANAFRSDPDW RHTFVRIFSK TQHKVNENSL
FTSWKACQTL ALMHDYLILV LGPVKKYQRI LDSRDRPAHL YIHAGQTPHQ LSEWCQNHLT
PSVHLANDYT AFDQSQHGEA VVLEAWKMRR ASIPEPFITL HVHVKTNIEC QFGPLTCMRI
TGEPGTYDDN TDYNLAILYT QYLLHRTPVL VSGDDSLVDR VPPMNPSWPA LAPLFALKPK
PETSPFGLFC GYFVGPAGAV RAPRALFAKL AIALEDGSLP EKIASYVAEF SVGQSLGDSL
WSLIPPELVI YQSACFDLIC RHASPQLKLA LRLGEVPDWG SLLSQLKLRF LTRPLFALLD
AHTRVMVRTH KAHLLPSGHA LHPSTEPFY
