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RNA1 polyprotein (Genome polyprotein B) (P1) [Cleaved into: Protease cofactor (32 kDa protein); Putative helicase (EC 3.6.4.-) (58 kDa protein) (Membrane-binding protein) (NTP-binding protein) (NTB); Viral genome-linked protein (VPg); Picornain 3C-like protease (3C-like protease) (EC 3.4.22.-) (24 kDa protein); RNA-directed RNA polymerase (EC 2.7.7.48) (87 kDa protein)]

 POL1_CPMVS              Reviewed;        1866 AA.
P03600;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 118.
RecName: Full=RNA1 polyprotein;
AltName: Full=Genome polyprotein B;
AltName: Full=P1;
Contains:
RecName: Full=Protease cofactor;
AltName: Full=32 kDa protein;
Contains:
RecName: Full=Putative helicase;
EC=3.6.4.-;
AltName: Full=58 kDa protein;
AltName: Full=Membrane-binding protein;
AltName: Full=NTP-binding protein;
Short=NTB;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
Contains:
RecName: Full=Picornain 3C-like protease;
Short=3C-like protease;
EC=3.4.22.-;
AltName: Full=24 kDa protein;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=87 kDa protein;
Cowpea mosaic virus (strain SB) (CPMV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Secoviridae; Comovirinae; Comovirus.
NCBI_TaxID=928299;
NCBI_TaxID=3821; Cajanus cajan (Pigeon pea) (Cajanus indicus).
NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp).
NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16453487;
Lomonossoff G.P., Shanks M.;
"The nucleotide sequence of cowpea mosaic virus B RNA.";
EMBO J. 2:2253-2258(1983).
[2]
COVALENT RNA LINKAGE AT SER-920 (VPG), AND URIDYLYLATION.
Jaegle M., Wellink J., Goldbach R.;
"The genome-linked protein of cowpea mosaic virus is bound to the 5'
terminus of virus RNA by a phosphodiester linkage to serine.";
J. Gen. Virol. 68:627-632(1987).
[3]
FUNCTION OF VPG, AND MUTAGENESIS OF 920-SER--LYS-922; 928-MET-GLN-929;
934-ASN--VAL-936; 939-LYS--VAL-942; 945-ASP-ALA-946 AND GLN-947.
PubMed=11883002; DOI=10.1006/viro.2001.1137;
Carette J.E., Kujawa A., Guhl K., Verver J., Wellink J.,
Van Kammen A.;
"Mutational analysis of the genome-linked protein of cowpea mosaic
virus.";
Virology 290:21-29(2001).
-!- FUNCTION: Picornain 3C-like protease is a thiol protease that
probably cleaves the B and M polyproteins.
{ECO:0000269|PubMed:11883002}.
-!- FUNCTION: VPg plays a role in RNA replication.
{ECO:0000269|PubMed:11883002}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBCELLULAR LOCATION: Putative helicase: Host membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
-!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in
vivo yield mature proteins. Picornain 3C-like protease is
autocatalytically processed (By similarity). {ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase.
-!- SIMILARITY: Belongs to the comoviridae genome polyprotein B
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X00206; CAA25029.1; -; Genomic_RNA.
PIR; A04211; GNWE2C.
RefSeq; NP_613283.1; NC_003549.1.
ProteinModelPortal; P03600; -.
MEROPS; C03.003; -.
PRIDE; P03600; -.
GeneID; 956628; -.
KEGG; vg:956628; -.
OrthoDB; VOG0900006M; -.
PMAP-CutDB; P03600; -.
Proteomes; UP000008589; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Covalent protein-RNA linkage;
Helicase; Host membrane; Hydrolase; Membrane; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Viral RNA replication.
CHAIN 1 326 Protease cofactor. {ECO:0000255}.
/FTId=PRO_0000037006.
CHAIN 327 919 Putative helicase. {ECO:0000255}.
/FTId=PRO_0000037007.
CHAIN 920 947 Viral genome-linked protein.
{ECO:0000255}.
/FTId=PRO_0000037008.
CHAIN 948 1155 Picornain 3C-like protease.
{ECO:0000255}.
/FTId=PRO_0000037009.
CHAIN 1156 1866 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000037010.
TRANSMEM 897 917 Helical. {ECO:0000255}.
DOMAIN 462 633 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1099 1134 Peptidase C3.
DOMAIN 1429 1559 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 494 501 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 987 987 For picornain 3C-like protease activity.
{ECO:0000255}.
ACT_SITE 1023 1023 For picornain 3C-like protease activity.
{ECO:0000255}.
ACT_SITE 1113 1113 For picornain 3C-like protease activity.
{ECO:0000255}.
SITE 326 327 Cleavage. {ECO:0000255}.
SITE 919 920 Cleavage. {ECO:0000255}.
SITE 947 948 Cleavage. {ECO:0000255}.
SITE 1155 1156 Cleavage. {ECO:0000255}.
MOD_RES 920 920 O-(5'-phospho-RNA)-serine.
{ECO:0000269|Ref.2}.
MUTAGEN 920 922 SRK->GRS: Increased efficiency of
cleavage between the putative helicase
and VPg. Complete loss of infectivity.
{ECO:0000269|PubMed:11883002}.
MUTAGEN 920 921 SR->YG: Slightly decreased efficiency of
cleavage between the putative helicase
and VPg. Complete loss of infectivity.
MUTAGEN 920 920 S->T: Decreased efficiency of cleavage
between the putative helicase and VPg.
Complete loss of infectivity.
MUTAGEN 928 929 MQ->VA: No effect on infectivity.
{ECO:0000269|PubMed:11883002}.
MUTAGEN 934 936 NNV->RNI: 80% decrease of infectivity.
{ECO:0000269|PubMed:11883002}.
MUTAGEN 939 942 KRRV->RKRN: Complete loss of infectivity.
{ECO:0000269|PubMed:11883002}.
MUTAGEN 945 946 DA->EG: 50% decrease of infectivity.
Replicative proteins display a uniform
cytoplasmic distribution, instead of the
normal accumulation near the nucleus.
{ECO:0000269|PubMed:11883002}.
MUTAGEN 947 947 Q->H: Strongly decreased efficiency of
cleavage between VPg and 3C-like
protease. Complete loss of infectivity.
{ECO:0000269|PubMed:11883002}.
SEQUENCE 1866 AA; 209810 MW; 0D4CD8A11C0B2976 CRC64;
MGLPEYEADS EALLSQLTIE FTPGMTVSSL LAQVTTNDFH SAIEFFAAEK AVDIEGVHYN
AYMQQIRKNP SLLRISVVAY AFHVSDMVAE TMSYDVYEFL YKHYALFISN LVTRTLRFKE
LLLFCKQQFL EKMQASIVWA PELEQYLQVE GDAVAQGVSQ LLYKMVTWVP TFVRGAVDWS
VDAILVSFRK HFEKMVQEYV PMAHRVCSWL SQLWDKIVQW ISQASETMGW FLDGCRDLMT
WGIATLATCS ALSLVEKLLV AMGFLVEPFG LSGIFLRTGV VAAACYNYGT NSKGFAEMMA
LLSLAANCVS TVIVGGFFPG EKDNAQSSPV ILLEGLAGQM QNFCETTLVS VGKTCTAVNA
ISTCCGNLKA LAGRILGMLR DFIWKTLGFE TRFLADASLL FGEDVDGWLK AISDLRDQFI
AKSYCSQDEM MQILVLLEKG RQMRKSGLSK GGISPAIINL ILKGINDLEQ LNRSCSVQGV
RGVRKMPFTI FFQGKSRTGK SLLMSQVTKD FQDHYGLGGE TVYSRNPCDQ YWSGYRRQPF
VLMDDFAAVV TEPSAEAQMI NLISSAPYPL NMAGLEEKGI CFDSQFVFVS TNFLEVSPEA
KVRDDEAFKN RRHVIVQVSN DPAKAYDAAN FASNQIYTIL AWKDGRYNTV CVIEDYDELV
AYLLTRSQQH AEEQEKNLAN MMKSATFESH FKSLVEVLEL GSMISAGFDI IRPEKLPSEA
KEKRVLYSIP YNGEYCNALI DDNYNVTCWF GECVGNPEQL SKYSEKMLLG AYEFLLCSES
LNVVIQAHLK EMVCPHHYDK ELNFIGKIGE TYYHNQMVSN IGSMQKWHRA ILFGIGVLLG
KEKEKTWYQV QVANVKQALY DMYTKEIRDW PMPIKVTCGI VLAAIGGSAF WKVFQQLVGS
GNGPVLMGVA AGAFSAEPQS RKPNRFDMQQ YRYNNVPLKR RVWADAQMSL DQSSVAIMSK
CRANLVFGGT NLQIVMVPGR RFLACKHFFT HIKTKLRVEI VMDGRRYYHQ FDPANIYDIP
DSELVLYSHP SLEDVSHSCW DLFCWDPDKE LPSVFGADFL SCKYNKFGGF YEAQYADIKV
RTKKECLTIQ SGNYVNKVSR YLEYEAPTIP EDCGSLVIAH IGGKHKIVGV HVAGIQGKIG
CASLLPPLEP IAQAQGAEEY FDFLPAEENV SSGVAMVAGL KQGVYIPLPT KTALVETPSE
WHLDTPCDKV PSILVPTDPR IPAQHEGYDP AKSGVSKYSQ PMSALDPELL GEVANDVLEL
WHDCAVDWDD FGEVSLEEAL NGCEGVEYME RIPLATSEGF PHILSRNGKE KGKRRFVQGD
DCVVSLIPGT TVAKAYEELE ASAHRFVPAL VGIECPKDEK LPMRKVFDKP KTRCFTILPM
EYNLVVRRKF LNFVRFIMAN RHRLSCQVGI NPYSMEWSRL AARMKEKGND VLCCDYSSFD
GLLSKQVMDV IASMINELCG GEDQLKNARR NLLMACCSRL AICKNTVWRV ECGIPSGFPM
TVIVNSIFNE ILIRYHYKKL MREQQAPELM VQSFDKLIGL VTYGDDNLIS VNAVVTPYFD
GKKLKQSLAQ GGVTITDGKD KTSLELPFRR LEECDFLKRT FVQRSSTIWD APEDKASLWS
QLHYVNCNNC EKEVAYLTNV VNVLRELYMH SPREATEFRR KVLKKVSWIT SGDLPTLAQL
QEFYEYQRQQ GGADNNDTCD LLTSVDLLGP PLSFEKEAMH GCKVSEEIVT KNLAYYDFKR
KGEDEVVFLF NTLYPQSSLP DGCHSVTWSQ GSGRGGLPTQ SWMSYNISRK DSNINKIIRT
AVSSKKRVIF CARDNMVPVN IVALLCAVRN KLMPTAVSNA TLVKVMENAK AFKFLPEEFN
FAFSDV


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