RDRP_PVXX3
ID RDRP_PVXX3 Reviewed; 1456 AA.
AC P17779;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RNA replication protein;
DE AltName: Full=165 kDa protein;
DE AltName: Full=ORF1 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 Potato virus X (strain X3) (PVX).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12185;
OH NCBI_TaxID=3711; Brassica campestris (Field mustard).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3404114; DOI=10.1099/0022-1317-69-8-1789;
RA Huisman M.J., Linthorst H.J.M., Bol J.F., Cornelissen B.J.C.;
RT "The complete nucleotide sequence of potato virus X and its homologies at
RT the amino acid level with various plus-stranded RNA viruses.";
RL J. Gen. Virol. 69:1789-1798(1988).
CC -!- FUNCTION: RNA replication. The central part of this protein possibly
CC functions as an ATP-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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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 -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; D00344; BAA00249.1; -; Genomic_RNA.
DR PIR; JA0102; WMWGPV.
DR RefSeq; YP_002332929.1; NC_011620.1.
DR PRIDE; P17779; -.
DR GeneID; 7065759; -.
DR KEGG; vg:7065759; -.
DR Proteomes; UP000008687; 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:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
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; -; 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; IPR007094; RNA-dir_pol_PSvirus.
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.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 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..1456
FT /note="RNA replication protein"
FT /id="PRO_0000222556"
FT DOMAIN 59..224
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 695..862
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 863..997
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1236..1343
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 536..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 735..742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1456 AA; 165606 MW; E06E3FF2AB48E97B CRC64;
MAKVREVYQS FTDSTTKTLI QDEAYRNIRP IMEKHKLANP YAQTVEAAND LEGFGIATNP
YSIELHTHAA AKTIENKLLE VLGSILPQEP VTFMFLKPRK LNYMRRNPRI KDIFHNVAIE
PRDVARYPKE TIIDKLTEIT TETAYISDTL HFLDPSYIVE TFQNCPKLQT LYATLVLPVE
AAFKMESTHP NIYSLKYFGD GFQYIPGNHG GGAYHHEFAH LQWLKVGKIK WRDPKDSFLG
HLNYTTEQVE MHTVTVQLQE SFAANHLYCI RRGDLLTPEV RTFGQPDRYV IPPQIFLPKV
HNCKKPILKK TMMQLFLYVR TVKVAKNCDI FAKVRQLIKS SDLDKYSAVE LVYLVSYMEF
LADLQATTCF SDTLSGGLLT KTLAPVRAWI QEKKMQLFGL EDYAKLVKAV DFHPVDFSFK
VETWDFRFHP LQAWKAFRPR EVSDVEEMES LFSDGDLLDC FTRMPAYAVN AEEDLATIRK
TPEMDVGQEV KEPAGDRNQY SNPAETFLNK LHRKHSREVK HQAVKKAKRL AEIQESMRAE
GEAEPNETSG GMGAIPSNAE LPGTSDARQE LTLPTTKPVP ARWEDASFTD SSVEEEQVRL
LGEEAVKTAT QQVIEGLPWK HWIPQLNAVG FKALLIQRDR SGTMIMPITE MVSGLEKEDF
PEGTPKELAR ELLVMNRSPA TIPLDLLRAR DYGSDVKNKR IGAITKTQAT SWGEYLTGKI
ESLTERKVAT CVIHGAGGSG KSHAIQKALR EIGKGSDITV VLPTNELRLD WSKKVPNTEP
YMFKTYEKAL IGGTGSIVIF DDYSKLPPGY IEALVCFYSK IKLIILTGDS RQSVYHETAE
DASIRHLGPA TEYFSKYCRY YLNATHRNKK DLANMLGVYS ERTGVTEISM SAEFLEGIPT
LVPSDEKRKL YMGTGRNDTF TYAGCQGLTK PKVQIVLDHN TQVCSANVMY TALSRATDRI
HFVNTSANSS AFWEKLDSTP YLKTFLSVVR EQALREYEPA EAEPIQEPEP QTHMCVENEE
SVLEEYKEEL LEKFDREIHS ESHGHSNCVQ TEDTTIQLFS HQQAKDETLL WATIDARLKT
SNQEANFREF LSKKDIGDVL FLNYQKAMGL PKERIPFSQE VWEACAHEVQ SKYLSKSKCN
LINGTVRQSP DFDENKIMVF LKSQWVTKVE KLGLPKIKPG QTIAAFYQQT VMLFGTMARY
MRWFRQAFQP KEVFINCETT PEDMSVWALN NWNFSRPSLA NDYTAFDQSQ DGAMLQFEVL
KAKHHCIPEE IIQAYIDIKT NAQIFLGTLS IMRLTGEGPT FDANTECNIA YTHTKFDIPA
GTAQVYAGDD SALDCVPEVK HSFHRLEDKL LLKSKPVITQ QKKGSWPEFC GWLITPKGVM
KDPIKLHVSL KLAEAKGELK KCQDSYEIDL SYAYDHKDSL HDLFDEKQCQ AHTLTCRTLI
KSGRGTVSLP RLRNFL