POL1_CPSMV
ID POL1_CPSMV Reviewed; 1858 AA.
AC P36312;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Cowpea severe mosaic virus (strain DG) (CPSMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=31716;
OH NCBI_TaxID=132433; Calopogonium mucunoides.
OH NCBI_TaxID=3823; Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
OH NCBI_TaxID=185703; Centrosema pubescens.
OH NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp).
OH NCBI_TaxID=53866; Desmodium.
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=260885; Macroptilium lathyroides.
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3891; Psophocarpus tetragonolobus (Winged bean) (Dolichos tetragonolobus).
OH NCBI_TaxID=157791; Vigna radiata (Mung bean).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1448917; DOI=10.1016/0042-6822(92)90236-i;
RA Chen X., Bruening G.;
RT "Cloned DNA copies of cowpea severe mosaic virus genomic RNAs: infectious
RT transcripts and complete nucleotide sequence of RNA 1.";
RL Virology 191:607-618(1992).
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; M83830; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; A44214; A44214.
DR SMR; P36312; -.
DR MEROPS; C03.003; -.
DR Proteomes; UP000008566; 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; 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..1858
FT /note="RNA1 polyprotein"
FT /id="PRO_0000445835"
FT CHAIN 1..313
FT /note="Protease cofactor"
FT /id="PRO_0000037011"
FT CHAIN 314..908
FT /note="Putative helicase"
FT /id="PRO_0000037012"
FT CHAIN 909..936
FT /note="Viral genome-linked protein"
FT /id="PRO_0000037013"
FT CHAIN 937..1146
FT /note="Picornain 3C-like protease"
FT /id="PRO_0000037014"
FT CHAIN 1147..1858
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037015"
FT TRANSMEM 885..905
FT /note="Helical"
FT DOMAIN 450..621
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 936..1141
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1419..1549
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 976
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1013
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1104
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 482..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 313..314
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT SITE 908..909
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 1146..1147
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03600"
FT MOD_RES 909
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000250|UniProtKB:P03600"
SQ SEQUENCE 1858 AA; 208862 MW; E18F0F090B6FEFB3 CRC64;
MKFFAGQTVM DVLQHVSSPT TNLRLLSYCN LKKEEDGKMM LAIKEQRHRR LLTLSYGAMC
FQFSNSVGDE GIEVDDDELM FEIFDALLRT KISNSKGMTH LYSWMRGVYL STFKVEVQCD
DYNSNLLEKD LAGEAQGLSQ FVSGLADWIP SRVKTLAGYA AEGIIEAFKK HFDKLLVEYC
PMAVAACSWI TTVWTTIKEW VQSAMDAMSW IMAGCTELIS WGMCVIAGSC ALSLLEKALV
AMGLISSSFD LAGIFVRSAV VGAFCLTVVN KRSRNCAELL QLVSLAVGAV SSATSSCFQS
PVGQATDVSA ESQSGGVEML ESLAKNLTNF CDGTLVSIGK TCNAVNSINT AAGTIKNLVG
RLLSMLSNFA YKLLGLESTF LRDASVVFSE NVDGWLKQIS WCQDQFLAKA YINQDELMVL
RSLITRGEVM QREMIMGGMK VSPTVCGLIN KGCTDLAKLM AGAVMHGTSG TRKIPFVVYA
HGASRVGKTM VINRLIEDFR KELELGEDCV YPRNVVDDYW SGYKRQPIVV IDDFGAVSSD
PSAEAQLIPL ISSAPYPLNM ADLSEKGMHF DSAIVMCSSN FIECSPESKV RDEMAFRNRR
HVLFTVSLDP NIPYDGDDIT KNQIYEIKTW FHDSYHVEAT FTSYGDLLAY CKNKWVEHNT
EQEANLKQLG VKKESVAFQQ FRSILDLAVF VNQDAENFKQ RLETPDGRCH FVSCYDKSGI
LRHYTIDATG DVQEMEKVDS SLDDILLEKT NKMVLAAYKM IKYHKDTNLV IKTQLADLVD
PTKYTADFQF DGVIGSPLFS SQVMPSVKAL PLWQRMVLYT VGQNLGRTHS SWYEGIKDKC
MLALSKAYST EIKDWPVALK IVVGVILATV AGKAFWRFYA SMADAGNGGH FVGAVASAFA
GSQAVVAQSR KPNRFDVAQY RYRNIPLRKR NWAEGQMSLD QSTMLIMEKC KANFVFSNIS
CQIVMLPGRQ FLCYKHVFAS LNSPMYVDIY TANKKYKLYY KPQNRVYFET DSEIMLYKDA
SLEDIPASCW DLFCFDAEKS LPRGSFPAEI LSCKLDRTTN QHIPEWADIS ARTVNQKLDV
EFGEYQTIFY SYLQYDVSTK AEDCGSLIIA TIDGRKKIIG IHTAGRANRS GFASYMPQVE
IPVQAQAAEK FFDFLEKEQH VTEGIGKVGN LKKGVWVPLP TKTNLVETPK EWHLGTEKTK
EPSILSSTDL RLGDKQYDPF VGGIQKYAEP MGILDDEVLR HVATDIVEEW FDCVDPQEDT
FEEVDLQVAI NGLEGMEYME RVPMATSEGF PHILTRKSGE KGKGRFVYGD GEIFDLIPGT
SVHEAYLTLE ETCADTVPAL VGIECPKDEK LPLRKIYEKP KTRCFTVLPM EYNLVVRRKF
LKFVVFIMKN RHRLSCQVGI NPYGMEWSRL AMSLLEKGNN ILCCDYSSFD GLLTKQVMHL
MSEMINELCG GSSRLKQQRT NLLMACCSRY ALCKGEVWRV ECGIPSGFPL TVICNSIFNE
LLVRYSYIKI CQQARVPATI TYGFSTFVKM VTYGDDNLLS VQSAITHVFD GTKLKEFLKL
NGITITDGKD KTSPVLNFRN LEDCDFLKRG FKKESDVVWV GPEEKESLWA QLHYVTTNNL
EKHEAYLVNV VNVIRELYLH DPREAAELRR KAIQNVDFLK ENPKDLPTMA AIKEFYNMQR
QQQFVDSNDN LDSLLNPDFL FVAPHRKMHE AEMELVPKWY LRDLGKAPIN VLTGEADRIC
VLVNASIPDH LLPEKVVNIS WPYGPGRGGL PTHGWAQANL YNPNSAVVKK LRTLVNQNPD
DRVDICFRHD AVPVAIATII FLVHLGKVKG RSANEYLTKI IDSAKSLKFL PKECDIIF
