POL1_BRSV
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 03-AUG-2022, entry version 115.
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.
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}.
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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: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; 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
