POL1_BPMV
ID POL1_BPMV Reviewed; 1850 AA.
AC Q9YJU5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=Genome polyprotein B;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=Protease cofactor;
DE AltName: Full=32 kDa protein;
DE Contains:
DE RecName: Full=Putative helicase;
DE EC=3.6.4.-;
DE AltName: Full=58 kDa protein;
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 AltName: Full=24 kDa protein;
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};
DE AltName: Full=87 kDa protein;
OS Bean-pod mottle virus (strain Kentucky G7) (BPMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=31715;
OH NCBI_TaxID=53866; Desmodium.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10403699; DOI=10.1023/a:1008012502470;
RA Di R., Hu C.-C., Ghabrial S.A.;
RT "Complete nucleotide sequence of bean pod mottle virus RNA1: sequence
RT comparisons and evolutionary relationships to other comoviruses.";
RL Virus Genes 18:129-137(1999).
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}.
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; U70866; AAD09629.1; -; Genomic_RNA.
DR RefSeq; NP_612349.1; NC_003496.1.
DR SMR; Q9YJU5; -.
DR MEROPS; C03.003; -.
DR PRIDE; Q9YJU5; -.
DR GeneID; 956617; -.
DR KEGG; vg:956617; -.
DR Proteomes; UP000007610; 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; 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; 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 RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..308
FT /note="Protease cofactor"
FT /id="PRO_0000037001"
FT CHAIN 309..904
FT /note="Putative helicase"
FT /id="PRO_0000037002"
FT CHAIN 905..932
FT /note="Viral genome-linked protein"
FT /id="PRO_0000037003"
FT CHAIN 933..1140
FT /note="Picornain 3C-like protease"
FT /id="PRO_0000037004"
FT CHAIN 1141..1850
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037005"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 449..614
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 930..1136
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1414..1544
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 972
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1008
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1098
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 475..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 308..309
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 904..905
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 932..933
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 1140..1141
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT MOD_RES 905
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000250|UniProtKB:P03600"
SQ SEQUENCE 1850 AA; 209918 MW; 232F3AAFCFA3AA40 CRC64;
MKFYPGQNIS EIVYHFQSNE TANRLDAYFA CGCEEDTEVL ARLKQCNPRL LHLSYAAFCL
EMGSHSIEEM EYDDGELIFS YFQNFLLSIV SNSSKTTKLR AYIRSAFAYH FQHFVEFDQY
TNDSLNTVDT SVSAQGIADL ALSMVRWIPT QIKKVVNFGV GSVIESFSEH FNKLLMQYCP
IVFQAFSWVN NIWTMVKEWI EEAAKEISWF LQGCKELHAW GMCILASSCA LGLVEKCLIS
LGMISESFDL VGLFVRSAIV GAFCVSIKTG KFVTNSELIT CATIAVSTIA TVMSQAFKPS
EEIKGQFQAL SVLEGLATQL TSFCDTSLVA MGKTCTAFNQ ICTAGKNVKV IAGRLLEVVS
NFVRKLLGLD SAFLRDAALI FSQDVDGWLR NISWCQEQFL LKAYMSQDDL IVLRSLVVKG
ERMREQMLEG EVKVSPSVCN LIVKGCEEAN KLMRESRLHC SKTIRKIPFV IFAHGESRVG
KSLLVDRLIT DFCDHLEIGE DAVYSRNPSD PFWSGYRRQP IVTIDDFAAV VSEPSAEAQL
IPLVSSAPYP INMAGLEEKG MHFDSQIMMC SSNFLEPSPE AKIRDDMAFR NRRHVLITVE
LKPGVEYDES DFTKNQRYLL KTWFHYHYVV DQTFESYADL LAHCFTKWER HVKEQESNLS
QIKGKKSESG HFYNFQQLMD LAVSWNLNAD IMKNRIKAER NDMVYVFSAG RKDKILHCFL
NKEGECTVRP DSIDDPEAQA LLKASETMLM KAYAFLKYNN ATNLIVRTHL AELVNEDFYD
EKFNFIGTIG TPAFHRQIAA HLEKMPLWQK AILCGMGHCL SRKSKETWYT GMKEKFVQMM
KSIYETEVTD WPVPLKIISG TILATILGTT FWKLFSFLRD AGNGGVFVGN VASAFTTSSV
LEAQSRKPNR YEVSQYRYRN VPIKRRAWVE GQMSFDQSVV AIMSKCKASM RMGNTDAQIL
MVPGRRFIAH GHFFKNLTQK VRVQIVTSEK SYWHVYDPDK FQMFDNSEIG LYTNPTLEDI
PHSAWDLFCW DSEKTLPNNF SAELLSCKLD TVTGQYYPRM APINCRVHRQ PIHITEGNYV
RKQDVSIEYD ACTIPNDCGS LVVAKVGNHK QIVGFHVAGS KGRLGYASLI PYVEPVVQAQ
SAEVYFDFFP VEVDSQEGVA HIGELKSGVY VPLPTKTNLV ETPKEWQLDL PCDKIPSVLT
TTDERLVGTE HEDMTHSWWY SKYATPMMPL DEEILSKVAQ DMVEEWFDCV DEEDTFEEVS
LSAALNGVEG LDYMERIPLA TSEGFPHVLS RKNGEKGKRR FVTGDGEEMS LIPGTSVEEA
YNKLTVELEK CVPTLVGIEC PKDEKLPRRK IFDKPKTRCF TILPMEFNLV VRQKFLNFVR
FIMKKRDKLS CQVGINPYSM EWTGLANRLL SKGNDILCCD YASFSGLITK QVMSKMAEMI
NSLCGGDEKL MRERTHLLLA CCSRMAICKK DIWRVECGIP SGFPLTVICN SIFNEMLIRY
SYEKLLRQAK APSMFLQSFR NFISLCVYGD DNLISVHEYV KPYFSGSKLK SFLASHNITI
TDGIDKTSAT LQFRKLSECD FLKRNFKQMS NVLWVAPEDK ASLWSQLHYV SCNNLEMQEA
YLVNLVNVLR ELYLHSPEEA RRLRRKALSC IEWLQKADVP TIAQIEEFHS MQRIMNAPDS
NDNIDLLLSI DLLGLQGAAR PSQIRLWFDD KLVLANTQEF FDGNFPADSW LPIFVNCLYP
VSQLPAEAVI VNVVCGSGRG GLPTTAWISS AVNNRSSDIN KKIRTALGKG KKIVFLTRVD
PFPVALLAVL FGVKNEILSS NATNPMLTRL LENCKSLKYL VDECPFAFVN
