POL1_BBWV2
ID POL1_BBWV2 Reviewed; 1870 AA.
AC Q9WNW0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
OS Broad bean wilt virus 2 (BBWV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Fabavirus.
OX NCBI_TaxID=76875;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=B935;
RX PubMed=10949946; DOI=10.1023/a:1008132310111;
RA Qi Y., Zhou X., Li D.;
RT "Complete nucleotide sequence and infectious cDNA clone of the RNA1 of a
RT Chinese isolate of broad bean wilt virus 2.";
RL Virus Genes 20:201-207(2000).
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; AF149425; AAD39217.1; -; Genomic_RNA.
DR SMR; Q9WNW0; -.
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 RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..1870
FT /note="RNA1 polyprotein"
FT /id="PRO_0000445857"
FT CHAIN 1..346
FT /note="Protease cofactor"
FT /id="PRO_0000445858"
FT CHAIN 347..936
FT /note="Putative helicase"
FT /id="PRO_0000445859"
FT CHAIN 937..962
FT /note="Viral genome-linked protein"
FT /id="PRO_0000445860"
FT CHAIN 963..1171
FT /note="Picornain 3C-like protease"
FT /id="PRO_0000445861"
FT CHAIN 1172..1870
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000445862"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 486..654
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 963..1165
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1445..1572
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1003
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1039
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1128
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 346..347
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 936..937
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 962..963
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 1171..1172
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT MOD_RES 937
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000250|UniProtKB:P03600"
SQ SEQUENCE 1870 AA; 210038 MW; A66967E55AC8B7AB CRC64;
MDFSTMQVVV GFLKTSMGLQ SIRDIVQKAK VDEKDKTLLH IHLCFFHANE MARDLNEGMD
VSQIHSSAAI KYRAAIVTRH VKMNVETGGY DRKRMVEYNN ETCVNWFSCE FKEEKEESQE
LPVDEDCVEE IVENFLENCG ISDQNDQIST TSNANYAFGQ GLYEYATRVS DAIVAVISGS
IKKGIDEFLD KVYAAMSQIF AAWMPKIRAA FQWFENIKEV VKNWARTMHE KINCILVGME
DCLYMGAGLV AATCIVTLLE KFMVVTKILP APCGAATLFL TTAMATISAA YVCTKAVEKS
VMLTNVLHFV TTNCQIVLNA LFNHDATKKE LGANQNEGEA PTGVGQFGIS TMLQDVANLM
STWSTNSVTE IGRTFGAISQ IKNGILALRD MVYFVFEKLS DLAHKVLGFE SQVLADLTIL
LGENVADWLS ECDCMVSYML EFNSRNREIF DRLSQLIEKG RLIRTGVLRT GHRGSSQVMA
LVTKALEKLI ELHNSVVMSG SNTTRKAPFM VFFTGASGTG KTSVVQRVAI NWLQEEQLGT
NEIYSRNGQD PFWSGYKRHA VVTYDDFGAV PGTTSNEAEI INVISRNPYA TVMAGLAEKG
MYFDSRLVLA SRNFLAANPE SGVHDSEAYE RRRHAVIRVS LKPGVPYNAD DPCANQTYTL
LDSKTPFREI QTFETYAELW SYLYTSFKEH EVQEELYLKS LPILDSDKKE ALEGLVGLTV
IATSFAPKAV MQYGMEKFPG HHFLVSDGEK CYFWHGDGSV ESASVEQMQL SKQDVAQLKQ
QGLSTAMMYK DLAKAFPTLN SLAVLYAKNI VVKRWVGPDL EPTKTCEDVY MREQIGNLPK
WQRAYLYVLS KYLTTQSPRG WFMECLEETK KNLRATYLWE YKQWPLPLKL ALGSLIAIMA
GGAIWYSLQS LWCMSGDASF VAGAATVFSV SSFAGQSDIP NRDNSERSFR NRKVRARTWQ
GQSSCFGDSA LWIAETCMAT LTFSNVRTQV CLAPGRGFFG VNHCLAAIPA GVMVKMDSSI
GVTYFVWGKE KLLQFDGNEI ALYMTSTLPK TVDSLLGRIH FDVETLPKTF SAVFFSYKYD
PMIQQMVPEL GSVTCKVHNK AYTLAHGEYR REIPQSLSYE ASTVAGDCGS LILAEIEGKF
KLVGMHVAFN GREGSASFMP YHASLDQKVG QGDFMLKYQE WAEPKILGPG CRAMGLIDPE
HALAASGKTT FVETPEEWHL DYPCDKLPSV LARGDPRLAG TVHADYDPFA SGMSKYAKEA
GPFDAASLKQ VCSGIVEIWE DASADFPMDE VDLDTAINGL ENVEFFDALV LGTSEGFPYR
LDRGPGDKGK SRYVSGESGS LKITDEGVLS DIAWFEEVSK TQVPDLYCIE CVKDERLPIR
KVLHEPKSRL FTVLPMSYNI VIRKKFLNFV RFFMKRRDVL TAQVGINPYS REWTRMANKL
LSKGNNILCC DYSRFDGFLP KCIMNEIGNM IARLMKTDEV SRTQIKNLML ACTSRYAMCN
RVLYRVENGI PSGFPLTVIV NSILNEILVK YAYWHCFEDN PSVQSNFDAH VSMVVYGDDN
LISVSDAISS RFDGNFLVSF MEGLGIKVTD GIDKTKVGIE FRRLENCDFL KRSFKMSPDG
TWRSPMSKES LWPQLHFVKA KKLEMAEAYI NNCNNILREL WLHDVKEAEE FRNKVLRNLR
WIGHEQLLNM QQLAVFHSEQ MNGVSDFLST CVTVDSIPLM DPLVPGMLPV KTSEIIPRVF
VAAEKHFEGN FNDFFTISIT TSRKFEEDKG FVLLFPYGAG RGGLPTTQFM RENVIRKGCS
IQKKFRQAYE KGNNILFISQ SSVVPSYVFA VMLLHSIGAI SRLSSNKALT QAMQTCKRLE
YLPKEYEEFF
