ID   POLG_BSTVG              Reviewed;         942 AA.
AC   Q65729;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
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     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   Brome streak virus (strain German) (BStV) (Brome streak mosaic rymovirus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Tritimovirus.
OX   NCBI_TaxID=117139;
OH   NCBI_TaxID=4501; Bromus.
OH   NCBI_TaxID=97361; Hordeum murinum (Mouse barley) (Critesion murinum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   AGRICOLA=IND20484543; DOI=10.1007/BF01874758;
RA   Schubert J., Rabenstein F.;
RT   "Sequence of the 3'-terminal region of the RNA of a mite transmitted
RT   potyvirus from Hordeum murinum L.";
RL   Eur. J. Plant Pathol. 101:123-132(1995).
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 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=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   -!- 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   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
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; X78485; CAA55237.1; -; mRNA.
DR   SMR; Q65729; -.
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; -; 1.
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   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN           <1..108
FT                   /note="Nuclear inclusion protein A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040243"
FT   CHAIN           1..942
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000419993"
FT   CHAIN           109..606
FT                   /note="Nuclear inclusion protein B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040244"
FT   CHAIN           607..942
FT                   /note="Capsid protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040245"
FT   DOMAIN          1..90
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          349..472
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          633..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        26
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            108..109
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            606..607
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   942 AA;  105547 MW;  1AF1509108F2504D CRC64;
     ETEITPYGEN EELLWRHRIT TEVGDCGATM VALSDQKIVG FHSLGGISMN YFVPVTQELL
     DFLNSKTEKP LVPWRFSEDQ VDVGGLYIHN DFDKFPFVKT IQKLVGFQNG HMIKYCGEGF
     TPVARSENRL SRQHVISGQR ESFIHFVEAS AKWRPIVTPM LGRLQPSALN REAYYKDVLK
     YDKPIRLGTV HEEAFQSAVI NVIRILENAG FERGGVKACF DYGKIFNDLN LDAAMGALYA
     GKKKDYFVEA TDEEIEEMFL RSAGKICANG HGVWSALLKA ELRPAEKVAA NKTRTFTSAP
     IDILFGAKAV VDDFNKQFYK RHLLGPWTVG INKFNKGWDL LARSLMRYEW FIDADGSQFD
     SSITPLLMNA VLTIRLYFME RDDITELMLR NLYTQIISTC MLAEDGLIVQ KHRGNNSGQP
     STVVDNTLCL MIAMEYARQR AISDGHLNMQ MRYVCNGDDL LINANEEAKE VVQNKYEQYI
     KELELNYCFD DAFQSIEGVE FMSHKFMLRN GIYIPKLARH RIVAILEWQR SAEPQAIKSA
     ILAACVEAFG YDDSTELIRE YAISLEPVWG SFLPTDGEIE QLYLEGIAKQ EVARCLAGVD
     DVCKFESAAP GTNEAVDEML KAAGDDEALA RANATSTSDT IPPARNVGAD TTTPAKANPP
     SGRRPSSRSL IDNSIGGNGV QDVADRTSGI VFPVPTRKST SLYLTPKVKL RATTEELRKY
     ESTSLNPQQI DLRYSTQQEL NDWIKASADG LGQTEEAFID NILPGWIVHC IVNTTSSENR
     KAGSWRCVTN AGTADEEQVL YDIEPMYSAA NPTMRAIMRH FSDLAGLVIA ESFKQGRPLI
     PKGYIKAGVL DASSAARACD FVVRDRHDTA TFVQVQNQVL VNRVSGITNW LFAQQCLALV
     LTRTWRAMTL RCRRGHPQPR LSASFLEVST SCRARRRLGV QR