RDRP_PVXHB
ID RDRP_PVXHB Reviewed; 1456 AA.
AC Q07630;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 HB) (PVX).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=73488;
OH NCBI_TaxID=3711; Brassica campestris (Field mustard).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8409947; DOI=10.1099/0022-1317-74-10-2251;
RA Querci M., van der Vlugt R., Goldbach R., Salazar L.F.;
RT "RNA sequence of potato virus X strain HB.";
RL J. Gen. Virol. 74:2251-2255(1993).
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; X72214; CAA51012.1; -; Genomic_RNA.
DR PIR; JQ2294; JQ2294.
DR Proteomes; UP000006842; 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 GO; GO:0039694; P:viral RNA genome replication; 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_0000222555"
FT DOMAIN 59..225
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 474..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..542
FT /note="Basic and acidic residues"
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; 165138 MW; 10730A1EADA4FAB4 CRC64;
MAKVREVYQS FTDSTTKTLI QDEAYRNIRP IMEKHKLSNP YAQTVEAAND LEGFGIATNP
YSIELHTHAA AKTIENKLLE VLGSLLPQEP VTFMFLKPRK LNFMRRNPRI KDIFHNVAIE
PRDVARYPKE TIIHKLAEIK TDTAYISDTL HFLDPSYIVE TFQNCPKLQT LYATLVLPVE
AAFKMESTHP NIYSLKYFGD GFQYIPGNHG GGAYHHEFSH LQSVKVGKIK WRDPKDGLLG
HLNYTHEQVD THTVTVQLQE SFAANHLYCI RRGNMMTPEV RTFGQPDRYV LPPQIFLPKV
HNCKKPILKK TMMQLFLYVR TVKVAKNCDI FAKIRQLIKS SDLDKFSAVE LVYLVSYMEF
LAALQATTCF SDTLSGGLLT KTLAPVRAWI QEKKMQLCGL EDYAKLVKAV DWRPVDFSFK
VETWDFRFNP LGMWKAFQPS ELSDVEEMNN FFDDGDLLDC FTRMPAYAVN AEEDLAGMRG
DNQGETSTAP REPEGDKKEY VNPAETFLDK LTRKHNRETK SRAAKKAKRL AEIQDSINRD
QTEEESQGAP NMGEAPSNAE LPGTNGAGAG TTFPTLKALP QKWEDASFTD SSMTDQMEIM
PGKEAVEVAT QKVVDELPWK HWLPQLNAVG FKALEIQRDR NGTMIMPITE MVFELDKEEF
PEGTPEALAR ELKAMNRSPT TIPLDLLRAR DYGSDVKNKR IGAITKTQAA SWGEYLTGKI
ESLPERKVAA CVIHGAGGSG KSHAIQKALR EIGKGSDITV VLPTNELRLD WSKKVPNTEP
YMFKTYEKAL IGGTGSIVIF DDYSKLPPGY IEALVSFSTK IKLIILTGDS RQSVYHETSD
DASIRHLGPA TEVFAKYCRY YLNATHRNKK DLANMLGVYS ERTGTTEISM SSEFLEGVPT
LVPSDEKRKL YMGTGRNDTF TYAGCQGLTK PKVQIVLDHN TQVCSANVMY TALSRATDRI
HFINTSANSS AFWEKLDSTP YLKTFLSVVR EQALREYEPV EAEPIREPEP QTHMCVENEE
SVLEEYKEEL LEKFDREIHS EAHGHSNCVQ TEDTTVQLFS HQQAKDETLL WATIDARLKT
SNQESNFREF LSKRDIGDVL FLNYQRAMGL PKEPIPFSQE VWEACAHEVQ SKYLSKSKCN
LINGTVRQSP DFDENKIMVF LKSQWVTKVE KLGLPKIKPG QTIAAFYQQT VMLFGTMARY
MRWFRQAFQP KEVFINCETT PEDMSAWALS NWNFTRPSLA NDYTAFDQSQ DGAMLQFEVL
KAKHHCIPEE IIQAYIDIKT NAQIFLGTLS IMRLTGEGPT FDANTECNIA FTHTKFDIPA
GTAQVYAGDD SALDCVPEIK QSFHRLEDKL LLKSKPVITQ QKKGSWPEFC GWLITPKGVM
KDPIKLHVSL KLAEAKGELK KCQDSYEIDL SYAYDHKDSL HDLFDEKQCQ AHTLTCRTLI
KSGRGTVSLP RLRNFL
