POL1_BBWVS
ID POL1_BBWVS Reviewed; 1842 AA.
AC Q76L40;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=Genome polyprotein B;
DE Contains:
DE RecName: Full=Protease cofactor;
DE Contains:
DE RecName: Full=Putative helicase;
DE EC=3.6.4.-;
DE AltName: Full=Membrane-binding protein;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P03600};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
GN Name=RNA1;
OS Broad bean wilt virus 1 (strain Spinach/United States/ATCC PV-132/1963)
OS (BBWV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Fabavirus.
OX NCBI_TaxID=649895;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=13163; Myzus.
OH NCBI_TaxID=4101; Petunia.
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Kobayashi Y.O., Kobayashi A., Nakano M., Hagiwara K., Honda Y., Omura T.;
RT "Analysis of genetic relations between Broad bean wilt virus 1 and Broad
RT bean wilt virus 2.";
RL J. Gen. Plant Pathol. 69:320-326(2003).
CC -!- FUNCTION: [Picornain 3C-like protease]: Thiol protease that cleaves the
CC RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}.
CC -!- FUNCTION: [Viral genome-linked protein]: Plays a role in RNA
CC replication. It is covalently linked to the 5'terminus of both viral
CC single-stranded RNA1 and RNA2 molecules.
CC {ECO:0000250|UniProtKB:P03600}.
CC -!- FUNCTION: [Protease cofactor]: Down-regulates the RNA1 polyprotein
CC processing and enhances trans-cleavage of RNA2 polyproteins. The
CC protease cofactor and the putative helicase seem to target the
CC replication complexes to ER membranes. Their physical association
CC causes the membrane rearrangement of host ER that may result in
CC formation of the small membranous vesicles that are the site of viral
CC RNA synthesis. {ECO:0000250|UniProtKB:P03600}.
CC -!- FUNCTION: [Putative helicase]: The protease cofactor and the putative
CC helicase seem to target the replication complexes to ER membranes.
CC Their physical association causes the membrane rearrangement of host ER
CC that may result in formation of the small membranous vesicles that are
CC the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome.
CC {ECO:0000250|UniProtKB:P03600}.
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 -!- SUBCELLULAR LOCATION: [Putative helicase]: Host membrane
CC {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P03600}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P03600}.
CC -!- SUBCELLULAR LOCATION: [Protease cofactor]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P03600}.
CC -!- PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC like protease in vivo yield mature proteins. Picornain 3C-like protease
CC is autocatalytically processed. {ECO:0000250|UniProtKB:P03600}.
CC -!- PTM: [Viral genome-linked protein]: Uridylylated by the polymerase and
CC is covalently linked to the 5'-end of genomic RNA. This uridylylated
CC form acts as a nucleotide-peptide primer for the polymerase.
CC {ECO:0000250|UniProtKB:P03600}.
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DR EMBL; AB084450; BAD00183.1; -; Genomic_RNA.
DR RefSeq; NP_945134.1; NC_005289.1.
DR SMR; Q76L40; -.
DR PRIDE; Q76L40; -.
DR GeneID; 2658942; -.
DR KEGG; vg:2658942; -.
DR Proteomes; UP000000409; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Helicase; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1842
FT /note="RNA1 polyprotein"
FT /id="PRO_0000402781"
FT CHAIN 1..318
FT /note="Protease cofactor"
FT /id="PRO_0000402782"
FT CHAIN 319..908
FT /note="Putative helicase"
FT /id="PRO_0000402783"
FT CHAIN 909..934
FT /note="Viral genome-linked protein"
FT /id="PRO_0000402784"
FT CHAIN 935..1143
FT /note="Picornain 3C-like protease"
FT /id="PRO_0000402785"
FT CHAIN 1144..1842
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000402786"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 458..626
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 935..1137
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1417..1544
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 975
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1011
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1100
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 487..494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 318..319
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 908..909
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 934..935
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 1143..1144
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT MOD_RES 909
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000250|UniProtKB:P03600"
SQ SEQUENCE 1842 AA; 205786 MW; 1784AEFEAFA8DEB1 CRC64;
MDSETIDMCV KFLKISFGLQ SLKNLVKELF GGSELEKLAY VHAAFFHANE MAIHWNADLP
WEEVMSSKRI KERFGYVKSH FLRNVVYNAD ASGQMIRYNT TTCEQWFCCN FNLASYSASY
NSLVPEEGGS MPINEEAEIK IGQSLLTCAQ SVTKAIYAKL STLTTRSIQG FLECLRDAIC
GAFSSWLPCI RGAFAWFGNI IEVLKHWAGA AHEKLHNFLE GIEECLYMGL GLVASTCIVA
LIEKFLVTMS VISGPCGRPT LFLTSAMAII SSTYLLSKAV EKSSAFTMLL GFVTQSCQTV
LGSLFGKSAK GSEEAQGQFG PSAMLESLAT LVSSWSSSSV TEIGRTFGAI SQIKNGIIAL
KDMALFVFSK LCEMASKVLG FESQILADLS IILGENVADW LDECDCMLAY LLEFNSNARD
IFDRLSQLIE KGKAIRMGIL RTTHRGPSQV LSLVTKALDK LTELHNSVIM SGANSTRKTP
FMLFFTGKSG VGKTSVVQRM AANWLQQEQL GSNEVYSRNG LDPFWSGYKR QAVVTYDDFG
AVPGSVSNEA EIINVVSSNP HSVMMADLKE KGMYFDSRLI IASSNFLAAN PESGVHDSEA
YERRRHVVVQ VSLKEDMAYD PGNPCANQRY TLLESKAPFA EKAVFESYEE LWSHVYNAFK
AHEEKEKLFL SSLPIPERSE KEALQALIGI CVMTTSYAPK AVIQYGIDHL VGYHYLISSA
EHVYFWHEKG EVEIVPMHLM KLDKMDKATM ASTSLKSALM CQDMAKNFPT LNPLAVLYAK
NIVIRGWVDA NLQASKKCED SYMREQIESL PKWQRAYLHV LSGHIASNET RGWFLNCLEV
TKSNSRSSYI WEYKSWPMPL KLALGSFLAI LAGSAIFCSL QSLWSISGNA SFVAGAASIF
TIGSATAQSA PPNKDGSEYT YRNKKIKIRN WEGQGPCFGD SALWIAENCM ATLVVMKDRV
QVCMAPGRSF LGVNHFLRMI PNGVMVKLET GMTETYFVWE KSKLKLFENS EIALYTSSNL
PKAPDSLVDR FHFDLETLPK TFPAQFFTYK FDKDMQQYVP ELGELLCKKA ERALCVVSGE
YRRVISHHLT YRNPTVAGDC GGLVLAIIEG KCKLVGLHVA SDGEEGAASP VPWDPDFKVA
QGQSDFLLSY DEWAVPKVLG PGCKAVGIIS PEHTVGSGGK TSFLETPIEW QLNRPCGKIP
SILVKGDVRL AGTENADYDP FAVGMTKYAK EAGPFEPNGL DRVCESIAET WHDASDGFEF
GPVDLEAALN GIENMEYFDA LVLSTSEGYP YRLDRKPGEK GKARYVEGEP GNLEITDERI
LADIHWFEEI SKTQVPDLYC IECVKDERLP VRKVIKEPKS RLFTVLPMSY NLAIRKKFLN
FVRFIMKRRD VLPCQVGINP YSRQWGKVAD RLLEKGNSIL CCDYSRFDGF LPKCIMVKIA
EMFSNIVGET GAEREQTKNL MLACCSRYAI CGRVLYRVEN GIPSGFPLTV IVNSILNEIL
IKYAYWKCFE TESLIRDHFD TYVAMVVYGD DNLISVSEAI SSKFNGNFLV NFMCNLGIKV
TDGVDKTKVG IEFRTIEDCD FLKRKFKENA DGTWSGVMAE EHLWPQLHFV KAKKVEMSEA
YISNCNNILR ELWLGSPEKA AAFRREVISK LKWVEPQRLL TISQVALFHN EQMNGEHPFV
EACHQLENLE LMAPLEPGML PIKTQEIMPG LFVASEKNFT GNFDDYFTIS ITTNRKFEDG
KGFQIIFPYG AGRGGLPSKA FMEQNVIRKG CAIQKAFKQG LEKGNKMLFI SQSSVIPAYV
FAIMLYRSVD RLPRALSNKA LTSALGICKK LSYLPKDFPD LF
