ID   POL2_BAMMU              Reviewed;         894 AA.
AC   Q65657;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
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;
GN   Name=RNA2;
OS   Barley mild mosaic virus (strain UK-F) (BaMMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Bymovirus.
OX   NCBI_TaxID=103901;
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8725111; DOI=10.1016/0168-1702(95)01267-2;
RA   Peerenboom E., Jacobi V., Antoniw J.F., Schlichter U., Cartwright E.J.,
RA   Steinbiss H.H., Adams M.J.;
RT   "The complete nucleotide sequence of RNA-2 of a fungally-transmitted UK
RT   isolate of barley mild mosaic bymovirus and identification of amino acid
RT   combinations possibly involved in fungus transmission.";
RL   Virus Res. 40:149-159(1996).
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; X90904; CAA62412.1; -; Genomic_RNA.
DR   RefSeq; NP_604490.1; NC_003482.1.
DR   SMR; Q65657; -.
DR   MEROPS; C06.002; -.
DR   GeneID; 963864; -.
DR   KEGG; vg:963864; -.
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   Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..229
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040562"
FT   CHAIN           230..894
FT                   /note="70 kDa protein"
FT                   /id="PRO_0000040563"
FT   DOMAIN          109..229
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   REGION          502..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        117
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        189
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            229..230
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
SQ   SEQUENCE   894 AA;  98349 MW;  05A3B3B371E76243 CRC64;
     MMMNSTIRQG WQQVLRRFSI PASGDRLIVS NSTDQPIGLF GAFDTSLQTL SQVTNDPEIL
     KQKSNIPTHL DIASVLETSP RSFPWVFLTN SFCTFGGSIH AQNLQAFATA EFKSGFCYMN
     LLIPLSFDII DAHADSFRGF VEQLPDTLGA YPSLSMVLNV MLHAATRFPE IVASPVPTIA
     FDAESLQFHV TDKRGVPGMW NILKACRVYE LLSLAADGIG CEYMLYPVGA APQYSFWKKS
     MDHFISDRFV EFLAMQGLLA SALEQDYKTH DARDALLTAL QNAGYTNVVA RERRFPNGHD
     PSTVWLNLNE APISEKLTEL KRYLLVGHRS DEIADITHNV HQHVFEVLKT MSVQFSKTTN
     AYNRARFEVN HEVIWNAEYG RSSQQNAELE ALVLFLNRQS LEIENILRRT TSPVVVTNWQ
     PDVPPAAPEI SEGEPTHAVA TPITEAPTHA TPVEVVNLPP TRSYWAETLV GVLTAILGTI
     FALLTRALIR PKRLRRKSTF PWVSLDSGDE DDDHSGGGGG SPQTPGGQPP ASPAPGTHQS
     RFSVQDIASD TSLLSVDLDE DTLSQYDETF QTIRRALFEN SFGDILQNSA RWISTLEAMA
     LADGNAPYTL LAQYLNGIEE AYTNFRNTGH ISRATLSGFF VLEDSLRAAG IAFGGTTPTQ
     TIQNQSADSP ARRWKTRFEQ IACELGDASI KSLADLADII DTERERGDLT QFDVLAASSI
     SSLCRAVRII SDTTDPNTQL ALVENATAMQ NNINAILGTN VSIPFLSATR RLLITRRIQE
     AGAESRSGAT PDTIQQLADA ELAEIVSEAN MFNEMAASQR DIANATREAT IREHVLSPVN
     ALANVGMAAA FFRSGGLRSR AFHPTMPTMP GSPAAIGRPM FQAFRGRGHR LNRR