ID POLG_WMV2U Reviewed; 1017 AA.
AC P18478;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 08-NOV-2023, entry version 124.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Nuclear inclusion protein A;
DE Short=NI-A;
DE Short=NIA;
DE EC=3.4.22.44;
DE AltName: Full=49 kDa proteinase;
DE Short=49 kDa-Pro;
DE Contains:
DE RecName: Full=Nuclear inclusion protein B;
DE Short=NI-B;
DE Short=NIB;
DE EC=2.7.7.48;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
DE Flags: Fragment;
OS Watermelon mosaic virus II (isolate USA).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus; Watermelon mosaic virus.
OX NCBI_TaxID=148360;
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Slightom J.L.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 736-1016.
RX PubMed=2374006; DOI=10.1099/0022-1317-71-7-1451;
RA Quemada H., Sieu L.C., Siemieniak D.R., Gonsalves D., Slightom J.L.;
RT "Watermelon mosaic virus II and zucchini yellow mosaic virus: cloning of
RT 3'-terminal regions, nucleotide sequences, and phylogenetic comparisons.";
RL J. Gen. Virol. 71:1451-1460(1990).
RN [3]
RP REVIEW.
RX PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT "Potyvirus proteins: a wealth of functions.";
RL Virus Res. 74:157-175(2001).
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
CC -!- FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-
CC cell and systemis movement, encapsidation of the viral RNA and in the
CC regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
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: [Capsid protein]: Virion {ECO:0000305}.
CC -!- PTM: Genome polyprotein of potyviruses undergoes post-translational
CC proteolytic processing by the main proteinase NIa-pro resulting in the
CC production of at least ten individual proteins. The P1 proteinase and
CC the HC-pro cleave only their respective C-termini autocatalytically.
CC 6K1 is essential for proper proteolytic separation of P3 from CI (By
CC similarity). {ECO:0000250}.
CC -!- BIOTECHNOLOGY: The gene for the coat protein is introduced by genetic
CC manipulation and expressed in squash so as to obtain virus resistant
CC plants.
CC -!- MISCELLANEOUS: Readthrough of a terminator codon TGA occurs between
CC codons for Ala-267 and Gln-269.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; D13913; BAA03009.2; -; Genomic_RNA.
DR PIR; JQ0498; JQ0498.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Genetically modified food; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN <1..219
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040497"
FT CHAIN 1..1017
FT /note="Genome polyprotein"
FT /id="PRO_0000420034"
FT CHAIN 220..736
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040498"
FT CHAIN 737..1017
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040499"
FT DOMAIN 1..195
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 461..585
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 741..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 127
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT SITE 219..220
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 736..737
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1017 AA; 115489 MW; 8853B6411C871E2E CRC64;
LSVTRKQCLE LGMVLSLSPM GTYLEGTMGC LQLKHGHGGF VIHNTTQLRI HFIQGKDAIL
IRMPKIFLRL QSATSLDNQN VRNEFAWLEQ TFKRRAYGQQ SQSSSIILPE GKGSFWIHWI
TTQDGFCGLP LVSVNDGHVV GIHGLTSNDS EKNFFVPFTD GFEKEYLDNA DNLSWDKHWF
WEPSKIAWGP LNLVEEQPKE EFKISKLVSD LFGNTVAVQS RKERWVLDAM EGNLVACGQA
DSALVTKHVV KGKCPYFAQY LSLHDGAXQF FEPLMGAYQP SRLNKDAFKK DFFKYNKPVV
LNEVDFNAFE KAVEGVITMM VDFEFAECLF VTDPDEIYGS LNMKAAVGAQ YKGKKQDYFS
GMDSFDKERL LYLSCERLFN GEKGIWNGSL KAELRPIEKV QANKTRTFTA APLDTLLGAK
VCVDDFNNQF YSFNLKCPWT VGMTKFYGGW DKLMRSLPDG WTYCHADGSQ FDSSLTPLLL
NAVLSIRCCF MEDWWVGREM LENLYAEIVY TPILAPDGTI FKKFRGNNSG QPSTVVDNTL
MVVIAMYYSC CKQGWSEEDI ERRLVFFANG DDIILAVKDE DVWLYDTLSA SFAELGLNYN
FDERTKKREE LWFMSHQAML VDGIYIPKLE PERIVSILEW DRSKELMHRT EAICAAMIEA
WGYTELLQEI RKFYLWLLSK DEFKELAASG KAPYIAETAL RKLYTDVNTQ PSELQRYLEV
LDFNHIDGCC ESVSLQSGKE TVENLDAGKE SKKDASDKGN KPQNSQVGQG SKEPTKTGTV
SKDVNVGSKG KEVPRLQKIT KKMNLPTVGG KIILSLDHLL EYKPSQVDLF NTRATKTQFE
SWYSAVKVEY DLNDEQMGVI MNGFMVWCID NGTSPDVNGV WVMMDGEEQV EYPLKPIVEN
AKPTLRQIMH HFSDAAEAYI EMRNSESPYM PRYGLLRNLR DRELARYAFD FYEVTSKTPN
RAREAIAQMK AAALAGVNSR LFGLDGNIST NSENTGRHTA RDVNQNMHTL LGMGPPQ
//
