ID   POLG_NIGSP              Reviewed;         293 AA.
AC   P83574;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
DE   Flags: Fragment;
OS   Nigerian sorghum potyvirus (Dawa mosaic virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=228731 {ECO:0000305};
OH   NCBI_TaxID=4558; Sorghum bicolor (Sorghum) (Sorghum vulgare).
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=15503220; DOI=10.1007/s00705-004-0411-y;
RA   Seifers D.L., Haber S., Ens W., She Y.M., Standing K.G., Salomon R.;
RT   "Characterization of a distinct Johnsongrass mosaic virus strain isolated
RT   from sorghum in Nigeria.";
RL   Arch. Virol. 150:557-576(2005).
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: [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   -!- 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   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
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DR   SMR; P83574; -.
DR   iPTMnet; P83574; -.
DR   PRIDE; P83574; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   InterPro; IPR001592; Poty_coat.
DR   Pfam; PF00767; Poty_coat; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Capsid protein; Direct protein sequencing; Virion.
FT   CHAIN           1..293
FT                   /note="Capsid protein"
FT                   /id="PRO_0000040460"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylserine; by host"
FT                   /evidence="ECO:0000269|PubMed:15503220"
FT   NON_TER         1
SQ   SEQUENCE   293 AA;  32856 MW;  C8A00F84823EB6BA CRC64;
     SGNEDAGNVK PAAGTKENKS DKEKDKPESG NAANAKATSN TKEDGGESGT KPTTANKDKD
     VDVGSTGTFV IPKLKKVSPK MRLPMVSNKA ILNLDHLIQY KPDQRDISNA RATHTQFQFW
     YNRIKKEYDV DDEQMRILMN GLMVWCIENG TSPDINGYWT MVDGNNQSEF PLKPIVENAK
     PTLRQCMMHF SDAAEAYIEM RNLDEPYMPR YGLLRNLNDK SLARYAFDFY EINSRTPNRA
     REAHAQMKAA AIRGSTNHMF GLDGNVGESS ENTERHTAAD VSRNVHTYRG AKI