POL1_BRAV
ID POL1_BRAV Reviewed; 2094 AA.
AC Q8V5E0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=Protein X1;
DE Contains:
DE RecName: Full=Protein X2;
DE Contains:
DE RecName: Full=Putative ATP-dependent 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 Short=PRO;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=POL;
DE EC=2.7.7.48;
OS Blackcurrant reversion association virus (BRAV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=65743;
OH NCBI_TaxID=78511; Ribes nigrum (European black currant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11551655; DOI=10.1016/s0168-1702(01)00342-2;
RA Pacot-Hiriart C., Latvala-Kilby S., Lehto K.;
RT "Nucleotide sequence of black currant reversion associated nepovirus
RT RNA1.";
RL Virus Res. 79:145-152(2001).
CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves
CC at Gln-|-Gly or Gln-|-Ser sites in the P1 and P2 polyproteins.
CC {ECO:0000250}.
CC -!- FUNCTION: The VPg-NTB polyprotein may act as a membrane-anchor for the
CC replication complex. {ECO:0000250}.
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: [Viral genome-linked protein]: Host endoplasmic
CC reticulum lumen {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=The NTB-VPg polyprotein is associated with
CC endoplasmic-derived membranes that are active in viral replication.
CC {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC yield mature proteins. Picornain 3C-like protease is autocatalytically
CC processed. NTB exists as NTB-VPg polyprotein as well as NTB mature
CC protein (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nepoviruses RNA1 polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AF368272; AAL36026.1; -; Genomic_RNA.
DR RefSeq; NP_612604.1; NC_003509.1.
DR SMR; Q8V5E0; -.
DR PRIDE; Q8V5E0; -.
DR GeneID; 993416; -.
DR KEGG; vg:993416; -.
DR Proteomes; UP000007614; Genome.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; 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:UniProtKB-KW.
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; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 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; Glycoprotein; Helicase;
KW Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..336
FT /note="Protein X1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037080"
FT CHAIN 337..523
FT /note="Protein X2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037081"
FT CHAIN 524..1105
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037082"
FT CHAIN 1106..1132
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037083"
FT CHAIN 1133..1369
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037084"
FT CHAIN 1370..2094
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037085"
FT TOPO_DOM 524..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1075..1105
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 672..838
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1136..1366
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1655..1780
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1176
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1217
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1323
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 699..706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 1341
FT /note="Involved in the cleavage site specificity"
FT /evidence="ECO:0000250"
FT CARBOHYD 1129
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2094 AA; 233298 MW; 70585D86AC9EEADB CRC64;
MVKIGSDTLA PKQLVLENKY IAACLSKPAN FALSFLAQGA SLKPSVVARA AINGVIACDT
TTFQLLAMDG TPLSFAAAAV VVRQFQLAHN RFVKIGLRQF YKECTRRCNA FNLQKAARQS
RERRAACKRI LASLDADLPC SRSSRRAIVT AHYAGVATAA RKSALFRQMR ADKRASRALA
AAMQPLVLAP PTCARIPYVC PLSSSVEESV SRRSLERCSK RVPREHASPR VASEMQPFAD
RPRLFSRVLL LPLSEITRAF FSRVFVPGSA MYDCATDLAH VVLDWWSITP MAHYLAMLDN
FLGTPTEESV RQASTNLLEE VEAMRALCRD HRANGVFAWV TETAGTIGST LKTAAVAPFH
GAGVALKAVL TPCASATLAW GEKFFQTLKS KFFEFLKPYI QHAIYASAEI EKYWAFIHGW
ATKMWNNVGV ELQALGDAAW WAIGITMVCG IVTLVEKLLV YLGALNAGGI LCSLMLTGLL
GAAGLLATGK FAEASSTLVG AMRSLIFTLF GSWKPTEASD GLTCNANALD FPLKVLETVG
TGLISAPLGT LQYIGKYGQA MDQIRKGKDA IKEFVGFCMD RVADAWDYMT GRKDSFLREI
ASAAKVDIVY WIKQTQSVLL QAQTIAVTDI VLLDTVTHLL YKGQILQLTL AKASRTTSLD
YARIVSTLIG ELTKIRATCA RAGSFDGRRP EPFWCYIYGK SHCGKSLFME DVSRALLKEN
GHAPNDIYAK NARDSFWSGY LQHACVQVDD LSACVTRPSL ESEFLQLVGS KMYSLNMAAV
EDKGMSFNSS IIVTTANVYT APTSAEITDK DAYGNRRNVV VQCRAAPDVE FDPRNPSASC
EARLVHRTDE SPLGNGQWRN CSAVLEDIIH HAAIHRNKEN LLMENYRERS DTQHPVFVGA
KSFIHRLAKE KNFAHIVCDD VLYYHDSYID STRVSEGTIN IGMEDACIQS VVQWSELVGG
VKDLGLLYAF VHAFTEGPCH VDSVEALNSE ATSCQRDFFQ SLSLLERIYM RLVQKQLDRI
RANPDFLFSV DIKTRILQSF RHGYDEMITH GGKVLAIFAA LLLVLLLYSS FFALYQTFVA
GTSSALVSAG MITQLSANAG SVCTSASNPS GAASYVSSNI PIHHRWRSNY SERSYALNSN
LEDKYLLDLL VWLQIPGDSI ISCIRFKGRS LLLTKHQALA IPEGARVYCN YYGRGRAVQT
IPLSWSYKKV REFADTEAVL FLDAQLSTMP AGREHYFNVP VERLPSVFDM NGVVMKQKRY
MTDSDDSLAA FTPNQPVVNT WENSRAKLNC ERQGINTFAY GGNYRNELPR SISSNCNTSP
EDCGAIMTMI FEGRRVVVGM HVASGKNPQG RYMSTACLLP DYHEDLSLNS MLQYTPYDGI
CKEGYRQIGN IENIGARPYT SGKTAFVAVP QHLLYSPPVL QEKLPGSAQP VTIQVEVKQP
AILSKDDPRI PEGTSYDPLI DGMAKFSHPM AVLDENVCNE VAQDIVESWH DCFQDLQDVS
DEIAINGSTE MDYEPFNLQS SEGYPYVTQR KPGESGKIRF FEMDPYTGLK SLIPNTLPAM
RYEALQRDCF TSVPEMVCIE TPKDECLPLR KICIKPKTRL FSILPLEFNL LLRKKFLHFS
SSLQMHRDTL PTQVGVNPYS REWGELLQRL RAQSSVAINC DYASFDGLLT GQILEKIGTM
INKMYIGSEA SKIQRLNLLM SIVNRKSICG ARVYEVRAGI PSGCALTVLL NSIFNEFLIR
FVWRTTIIGV PRERFSQYVT LLIYGDDNLI AVHPDYLPHF NGEIIRTRLA DVNVIITDGS
DKTAEKIEEK PLVQLDFLKR RFRKLNDGTV YAPLDLASVY TSLQNVTMGA GSIHIALQNN
VHNALLELYL HGNETWFNHL RDFYRKSHAW VNLPSWREAF AFHQGQISGV TPWTPYQMFD
VPVDGGRLRA MMANQGEAAF STHLGREIYI CGPKWCVSDP EHQFVVSTTP LRSADRGSGI
HRAIEYPCNG VGRLPSQDWV TKFKSSAHRV TAEIRKAHAS GKAIYFRDDP PYVANWCAAI
GFAQGLGYDY KSMINLYHDV SVPGSDALYF YFEQRARRAL PEPYIPPHLR TRVR
