ID   POLG_MDMV               Reviewed;         380 AA.
AC   P32652;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Genome polyprotein;
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   Maize dwarf mosaic virus (MDMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12203;
OH   NCBI_TaxID=4560; Sorghum halepense (Johnson grass) (Holcus halepensis).
OH   NCBI_TaxID=4577; Zea mays (Maize).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B;
RX   PubMed=1993866; DOI=10.1099/0022-1317-72-2-237;
RA   Frenkel M.J., Jilka J.M., McKern N.M., Strike P.M., Clark J.M. Jr.,
RA   Shukla D.D., Ward C.W.;
RT   "Unexpected sequence diversity in the amino-terminal ends of the coat
RT   proteins of strains of sugarcane mosaic virus.";
RL   J. Gen. Virol. 72:237-242(1991).
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: [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=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   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; D00949; BAA00797.1; -; mRNA.
DR   PIR; PH0208; GNVSMB.
DR   SMR; P32652; -.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001592; Poty_coat.
DR   Pfam; PF00767; Poty_coat; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Virion.
FT   CHAIN           <1..52
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040289"
FT   CHAIN           1..380
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000420001"
FT   CHAIN           53..380
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040290"
FT   REGION          54..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            52..53
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   380 AA;  41120 MW;  B8ABF2AA45E1CB82 CRC64;
     KEGLAPYIAE TALRNLYLGT GIKEEEIEKY LKQFIKDLPG YIEDYNEDVF HQSGTVDAGA
     QGGSGSQGTT PPATGSGAKP ATSGAGSGSG TGAGTGVTGG QARTGSGTGT GSGATGGQSG
     SGSGTEQVNT GSAGTNATGG QRDRDVDAGS TGKISVPKLK AMSKKMRLPK AKAKDVLHLD
     FLLTYKPQQQ DISNTRATKE EFDRWYDAYK KEYEIDDTQM TVVMSGLMVW CIENGCSPNI
     NGNWTMMDKD EQRVFPLKPV IENASPTFRQ IMHHFSDAAE AYIEYRNSTE RYMPRYGLQR
     NISDYSLARY AFDFYEMTSR TPARAKEAHM QMKAAAVRGS NTRLFGLDGN VGETQENTER
     HTAGDVSRNM HSLLGVQQHH