ID   POLG_OMV                Reviewed;        1136 AA.
AC   P20234;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
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     AltName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
DE   Flags: Fragment;
OS   Ornithogalum mosaic virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12204;
OH   NCBI_TaxID=81765; Lachenalia.
OH   NCBI_TaxID=51466; Ornithogalum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Burger J.T., Brand R.J., Rybicki E.P.;
RL   Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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: [Viral genome-linked protein]: Mediates the cap-independent,
CC       EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC       Binds to the cap-binding site of host EIF4E and thus interferes with
CC       the host EIF4E-dependent mRNA export and translation (By similarity).
CC       VPg-RNA directly binds EIF4E and is a template for transcription (By
CC       similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC       templates for translation (By similarity).
CC       {ECO:0000250|UniProtKB:P18247}.
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   -!- SUBUNIT: [Viral genome-linked protein]: Interacts with host eIF4E
CC       protein (via cap-binding region); this interaction mediates the
CC       translation of the VPg-viral RNA conjugates (By similarity). Part of a
CC       complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC       mediates the translation of the VPg-viral RNA conjugates (By
CC       similarity). {ECO:0000250|UniProtKB:P18247}.
CC   -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC       {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins
CC       in the host nucleus. {ECO:0000250|UniProtKB:P21231}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC   -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC       polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC       This uridylylated form acts as a nucleotide-peptide primer for the
CC       polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC   -!- PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes
CC       post-translational proteolytic processing by the main proteinase NIa-
CC       pro resulting in the production of at least ten individual proteins.
CC       The P1 proteinase and the HC-pro cleave only their respective C-termini
CC       autocatalytically. 6K1 is essential for proper proteolytic separation
CC       of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
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; D00615; BAA00490.1; -; Genomic_RNA.
DR   PIR; JQ0494; JQ0494.
DR   MEROPS; C04.005; -.
DR   PRIDE; P20234; -.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; 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; -; 2.
DR   Gene3D; 3.30.70.270; -; 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; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Viral RNA replication; Virion.
FT   CHAIN           <1..122
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040291"
FT   CHAIN           1..1136
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420002"
FT   CHAIN           123..365
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040292"
FT   CHAIN           366..883
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040293"
FT   CHAIN           884..1136
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040294"
FT   DOMAIN          123..341
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          607..731
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        168
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        203
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        273
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            122..123
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            365..366
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            883..884
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   1136 AA;  128915 MW;  0A7AE0527743FD61 CRC64;
     EYTIVRYVDP LTGATQDENP LMAIDLVQEY FAKIRSQLVS EEKLETQNII ANPGIQAYYM
     KNRGDAALKV DLTPHNPLLV TKTGTIAGFP ENEFILRQTG KAVNVKMSEV PVENELEEVE
     HEGKNLNRGL RDYNVVSNVV CRLTNESDGH SASLFGLGYG GYIITNRHLF KNNNGTLKVQ
     SQHGDFIVKN TTQLKMVPVG KTDILIIRMP KDFPVLPQKL RFRAPANEDK VCLIASNFQE
     RYVSSLVSET SSVYPVGNGE FWQHWISTKD GHCGLPLTST KDGFIVGIHS LSTITNSKNF
     FASIPANFEE QYLAKLDQQD WTANWKYNPN EVSWNGLRLQ ENKPGRIFQA VKEVSALFSD
     AVYEQGQEVG WLFRELKDNL KAVAVLPNQL VTKHVVKGPC QCFIQYLNES PEASAFFKPL
     MGQYGKSILS KEAFVKDIMK YSKPIVLGEV DFIKFEEGYN NVLRMFHDIG FEKCEYVTDS
     MEVYKNLNLK AAVGAMYTGK KQQYFEGMSE DEIHQLVIAS CFRLWSGKFG VWNGSLKAEL
     RPLEKVQACK TRTFTAAPLD TLLGAKVCVD DFNAQFYDKH LTAPWTVGIC KYYKGWDTFM
     NKLPEGWLYC DADGSQFDSS LTPFLINSVL RLRLEFMEDW DIGARMLSNL YTEIIYTPIA
     TPDGTVVKKF RGNNSGQPST VVDNTLMVVL AMNYALAKLS IPYEEMDSRI RYFANGDDLL
     VAVEPTKGGE ILDSLQASFS ELGLIYDFND RTFDKTQLSF MSHQALWDGD MFIPKIKQER
     VVSILEWDRS TQPEHRIEAV CAAMIEAWGY PELLQEIRKF YAFMVTQEPY SAIHAQGKTR
     YISERALVTL YKDEKVVLSD IGPYIQKLAE MSLGCVDEVV MHQADSMDAG GSSRPPAPLV
     RQQDQDVNVG TFSVARVKAL SDKMMLPKVR GKTVLNLQHL VQYNPEQTEI SNTRATRTQF
     NNWYDRVRDS YGVTDDQMAV ILNGLMVWCI ENGTSPNLNG NWTMMDGDEQ IEYPLQPVLE
     NAQPTFRQIM AHFSNAAEAY IEKRNSEQRY MPRYGSQRNL NDYSLARYAF DFYEMTSRTA
     NRAREAHIQM KAAALRNTKT KLFGLDGKVG TEEEDTERHV ASDVNRNMHS LLGVNM