ID POL1_BRSV Reviewed; 2264 AA. AC P18522; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 08-NOV-2023, entry version 120. DE RecName: Full=RNA1 polyprotein; DE AltName: Full=P1; DE Contains: DE RecName: Full=P1A protein; DE Short=1A; DE AltName: Full=Protease cofactor; DE Contains: DE RecName: Full=Putative ATP-dependent helicase; DE EC=3.6.4.-; DE AltName: Full=1B; 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=1C-VPg; DE Contains: DE RecName: Full=Picornain 3C-like protease; DE Short=3C-like protease; DE EC=3.4.22.-; DE AltName: Full=1D-PRO; DE Contains: DE RecName: Full=RNA-directed RNA polymerase; DE EC=2.7.7.48; DE AltName: Full=1E-POL; OS Beet ringspot virus (BRSV) (Tomato black ring virus (strain S)). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Secoviridae; Comovirinae; Nepovirus; Nepovirus betae. OX NCBI_TaxID=191547; OH NCBI_TaxID=4681; Allium porrum (Leek) (Allium ampeloprasum var. porrum). OH NCBI_TaxID=4045; Apium graveolens (Celery). OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet). OH NCBI_TaxID=38871; Fraxinus (ash trees). OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce). OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil). OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean). OH NCBI_TaxID=35938; Robinia pseudoacacia (Black locust). OH NCBI_TaxID=23216; Rubus (bramble). OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OH NCBI_TaxID=4113; Solanum tuberosum (Potato). OH NCBI_TaxID=13305; Tulipa. OH NCBI_TaxID=3603; Vitis. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Greif C., Hemmer O., Fritsch C.; RT "Nucleotide sequence of tomato black ring virus RNA-1."; RL J. Gen. Virol. 69:1517-1529(1988). CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves CC the P1 and P2 polyproteins. {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}. CC -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo CC yield mature proteins. Picornain 3C-like protease is autocatalytically CC processed (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}. 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; D00322; BAA00234.1; -; Genomic_RNA. DR PIR; JQ0009; GNVVTB. DR RefSeq; NP_620112.1; NC_003693.1. DR SMR; P18522; -. DR MEROPS; C03.025; -. DR GeneID; 988049; -. DR KEGG; vg:988049; -. DR Proteomes; UP000007615; 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:0016020; C: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-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR Gene3D; 1.20.960.20; -; 1. 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; DNA/RNA polymerases; 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; 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..565 FT /note="P1A protein" FT /evidence="ECO:0000255" FT /id="PRO_0000037060" FT CHAIN 566..1203 FT /note="Putative ATP-dependent helicase" FT /evidence="ECO:0000255" FT /id="PRO_0000037061" FT CHAIN 1204..1230 FT /note="Viral genome-linked protein" FT /evidence="ECO:0000250" FT /id="PRO_0000037062" FT CHAIN 1231..1440 FT /note="Picornain 3C-like protease" FT /evidence="ECO:0000255" FT /id="PRO_0000037063" FT CHAIN 1441..2264 FT /note="RNA-directed RNA polymerase" FT /evidence="ECO:0000255" FT /id="PRO_0000037064" FT TOPO_DOM 566..1156 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1157..1177 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1178..1203 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 750..916 FT /note="SF3 helicase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" FT DOMAIN 1227..1436 FT /note="Peptidase C3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT DOMAIN 1713..1841 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" FT ACT_SITE 1270 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT ACT_SITE 1308 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT ACT_SITE 1400 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT BINDING 780..787 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" SQ SEQUENCE 2264 AA; 253678 MW; 65949E4B5CE8B722 CRC64; MSVTLSPSGD CFSFNHVKYN NSLNKYLFYN SNLDIVLDDF DFYFNFYVKK YNVLLSFFSD RVLSALYTSM SVSEAASLAM EDFCELALDE LKINPFHQLW EETLANWPVY PGTSLLDFCR TQYEIRREAA EASAEILRLK EVARQRAFDD EVEFLIKHGA KVHFAPSFAA QLWRAGKDQK KCRGILLGKL NKAKALGEAH RSAVARAQAK AEVLREFEPS PQQIQRALEA QIFADRLSRK YAALTARVRA KRAAARELRE KELFLETQDL LNAPLLPPME KVGIERKYRK VRPTGSNVTS TPKPNVLENL CPFMGLGAKT ADVRCQATLM AGKIHPQYPR LASAIYAWVL GPSMKFECIA PVKTFIKGLT FMVDYFPEEV LIDELNKINS EARCFEASLV LEEERAKLEA HAENANCRAN IFMKAMAGVK NMAKCAYSGF LTGCEEAGRS LSEGVCSVMI NSFRECIKMI HKELGCAMEL IEVMIKKVKD WYNSMLEKLH CGLATLGTYA MYALAILLGC GLTTLLERCI GGAGILTKLF VTGVFAAIGL HAAGGFDGLQ REMVQMCTAL AAGIFDVHHK GNGKYSPMAD ILAEQRLEDR RADNVRSIPI ISGIISAMQQ FGTGLCSMHS ISLIEIGKLG AACHSMRMGK EALKEFCATI MYYLGRISDK VTGRETVFFD ELSTLVSVDV RGWILCAQSC IRESFHTEIG NQFFRDMVAQ LVDDGQKLQV GVNGIPRKIS TDYSQLSSDT EGPNELHKRT IRAGISEGRR CEPVWIYLFG QRHCGKSNFM ATLDNALAKH FGLPNTTAYR NCKDSFFSGY SGQTFFHVDD LSSVKLDPPM EAEMINLVSC QEVPLNMADL ADKPIYFRSP FIISSSNFED VPAGCGVRDI EAYRSRKACL VEMRRKPGVL FDPDNPLLAS QARFKDPMSQ MLLEGQTEEN SWLEMEDVVT EIINISARHR AAQEKLQARY MREKSLLDPL ALAAENFLKG EVQTHILIFL VLNLKSWNPK PQGGRGLYVD GSLYLLDPTF QFEEIPITDD GYKRLWDERM RKSFLSKIQT GEYLNSKSMV VTGFLRSLVN GDCAVLSKDT LSSSASVAQQ SIFKALGIDE RIYLRTLQHQ LDLYSADIPE NPYSNSAWIK ILKAIGMGRT YLAENGCGIL MIAAALILIL VSAWGFWKLF IGLFSGSMSL GAAIVGMSAV DIKAQQKSSS QEGGYRARNI PIHHRYAYAK SQAGDGLLPA ARFVCCYLST GGGFVSAMQY KNKSVRMTRH QALRFQEGEQ LTVIFSSTGE SQLIRWHKYM MREEPGSEIV TWLAPSLPSL SPDLKDLFLE DKEVDLPNHF KTIGYVLRVD NTAFHYDLLD TYAAVDKTPL PLKGVVGNEL YLHEIPEKIT FHYESRNDDC GMIILCQIKG KMRVVGMLVA GKDKTSWADI MPPNTLAELQ SQIEYIPKFG EAYDGFFKAG YVPMADAPTL PKKTNMVPVP QSLRVPCDVP IKEPAVLTNA DKRCPAGVNP PVTALKKKFE HPMKELEQEI LDEVATDILE TWYDCEDHVL NDIPLVVAIN GIPADSEEAE LENFVMKTSP GYPYFKNNRA EKLKGKSAYF EEAEDGTLKL KEGGMAAKLH ENLVEFTKNE VPELVVIECT KDELLPERKI KVGACRLFEI MPLHYNLFLR QKTCAFTQFL QHNRHVLPCQ VGTNPYSREW GHMLNRLMRP KTNEAINCDY SGFDGLLNAQ VIECIAKMIN RLYALSGESE VQQAQRYNML MALVGRYAFV GPEVYKVNCG LPSGFALTVV VNSVFNEILI RYAYKKLAPK PERNRFNQVV CLLVYGDDNL ISVSPSIASW FTGEAIRITL AEKKVKITDG SDKDAPTIEA KSFWELDFLK RKFLKLDNGI VQAPLDRSAI FSSLYWLTPD KSKFHASQRA SDFQGTVDVV EELILNVNVA LMELYLHNDP REFSRVRDFY IKALPLATGQ FRTWAFCEAF HSAQQTGMLK YDPAKVLDHM SGLDFKKFMH VSEQGNKAHF YTEMLGVAGP HYKPQENDFI VSTEPLKMGV CGEHVPIQYG SGVGGLPTKK WVLDFGRPSQ LKNKLGYLIH PILRAQIEAG KRLVFMSPAP YVANNAALIA FGTGGKMLIQ KDALVHYRNV IPESTSGLEQ YFDAPLPTAT IGTFYFANGE TYAALCEYKE GKVLNYEGFP TLILNEAAKD RKVPCMVATQ AKTKFKVSLA CDSTMCPHHT AVCETYEKAF RHCWLAKCKT SAVKVSPWHG TKLS //