ID   POL2_BAYMY              Reviewed;         890 AA.
AC   Q9YJW2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Genome polyprotein 2;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=70 kDa protein;
OS   Barley yellow mosaic virus (isolate China/Yancheng/1998) (BaYMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Bymovirus.
OX   NCBI_TaxID=652104;
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10500279; DOI=10.1016/s0168-1702(99)00076-3;
RA   Chen J., Shi N., Chen Y., Diao A., Chen D., Wilson M.A., Antoniw J.F.,
RA   Adams M.J.;
RT   "Molecular analysis of barley yellow mosaic virus isolates from China.";
RL   Virus Res. 64:13-21(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC         the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC         potyviral polyprotein.; EC=3.4.22.45;
CC   -!- PTM: The viral RNA2 of bymoviruses is expressed as a single polyprotein
CC       which undergoes post-translational proteolytic processing resulting in
CC       the production of at least two individual proteins. The HC-pro cleaves
CC       its C-terminus autocatalytically (Potential). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bymoviruses polyprotein 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ132269; CAA10638.1; -; Genomic_RNA.
DR   RefSeq; NP_149000.1; NC_002991.1.
DR   SMR; Q9YJW2; -.
DR   MEROPS; C06.002; -.
DR   GeneID; 963862; -.
DR   KEGG; vg:963862; -.
DR   Proteomes; UP000006704; Genome.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.70; -; 1.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR036417; TMV-like_coat_sf.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   SUPFAM; SSF47195; SSF47195; 1.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..255
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000064781"
FT   CHAIN           256..890
FT                   /note="70 kDa protein"
FT                   /id="PRO_5000064782"
FT   DOMAIN          135..255
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   REGION          506..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          788..816
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        515..529
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        215
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            255..256
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
SQ   SEQUENCE   890 AA;  98247 MW;  A45ACE23FB6B76F9 CRC64;
     MSASSSRLLF DCGSLDWPNK SLFGDPTTRD VMNEHISSTW NAVIRRHMLA PNANAETILG
     RDGLPSAQFD AYGAMLPSFI QALNAPTTRL RISAPLSTAE SILCADASHA PWLYMANSVC
     AYEATHLQPV QTFIAFNFAH GYCYLSLFIP LSFRITFENA RGFSRFLEQL PDILGAYPTL
     AAIYKTMLFA IRLFPEVLQA PIPIIAKRPG VLQFHVSDAR GLPPSWFPMK CGSVASFVAL
     ITNNLNSDLL NGIVGSNGDG EHYTNWNSGH DHWIVNRFIT VKDLHSSLKS ALEVDLDTEG
     GRNAVLDLLL DLGVTNLVRR EKRFPAYFQG AESVYLLLSC ERVGNELVAV QDALQEPLAN
     YSGLDLRALI INLGGLPSRH SDICYTRNIF ENDNHLVWNF EFYRIASITK NAQIDRDVLS
     SSMANLFSDF VSESSNGQYR VKEPRPVVQY RVEHDEPVAS SAPSAWWQVL IGITTAILGA
     IIFFLWRCFL RAKRVKFQAK DSFPWFTTSG DDDSPPPPGD SPSRPPGRSP DRVLPRTVVR
     DLSFNDDDDL HSVDLNEAGS RFGEVVSLIA RGNLRELAGA IPESLSNLTL LQTSASGSGF
     YTMVALYLAT LGDAITAFHE HNDASPATIQ SLRTLELQLE ARGLRFNEAG TPANLIQRGV
     NSSVGRALVR LTQSALLATG ENFRTRMATT LERIAAERLN TLTAYDQRVI EMTTELLAAI
     KPVLEVERSE LTPHLANAEA LLQVYNNLFS TDYVSASLLA LRREMILRSA EGRVGEQPTS
     ASDAANEELV QRSMTKLDKE IELFQAQIDS QRRAVTITEA SNLRENILQP INTVANIAMA
     GAFLRGGARH RMPGMPDVAT PMPNPFRAFS GRGHSLTTTR SGGLFRRPRV