POL2_BAYMJ
ID POL2_BAYMJ Reviewed; 890 AA.
AC Q01207;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 yellow mosaic virus (strain Japanese II-1) (BaYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=31729;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2016599; DOI=10.1099/0022-1317-72-4-995;
RA Kashiwazaki S., Minobe Y., Hibino H.;
RT "Nucleotide sequence of barley yellow mosaic virus RNA 2.";
RL J. Gen. Virol. 72:995-999(1991).
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; D01092; BAA00876.1; -; Genomic_RNA.
DR SMR; Q01207; -.
DR MEROPS; C06.002; -.
DR Proteomes; UP000007447; 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 Hydrolase; Protease; Thiol protease.
FT CHAIN 1..255
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040556"
FT CHAIN 256..890
FT /note="70 kDa protein"
FT /id="PRO_0000040557"
FT DOMAIN 135..255
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT REGION 507..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 98464 MW; 5D0C70CE2AEFD5D0 CRC64;
MSASSSRQLF DCGSLDWPNK SLFGDPTTRD VMHEHISSTW NAVIRRHMLA PNADAETILG
RDGLPSAQFD AYGAMLPSFI QALNAPTTRL RITHRCPTAE SILCADASHA PWLYMANNVC
AYEATHLKPV QTFIAFDFAH GYCYLSLFIP LSFRITFENA RSFSRFLEQL PDILGAYPTL
AAIYKTMLFA IRLFPEVLQA PIPIIAKRPG VLQFHVSDAR GLPPSWFPMK CGSVRSFVAL
ITNNLNSDLL DGIVGSNGDG EHYTNWNSGH DHWIVNRFIT VRDLHSSLKS ALDVDLDTEG
GRNAVLDLLL DLGVTNLVRR EKRFPAHFQG AESVYLLLSC ERVGNELVAV QDALQEPLAN
HSGLDLRALI INLGGLPSRH SDICYTRNIF ENDNHLVWNF EFYRIASITR NAQIDRDMLS
SSMANLFSNF VSESSNGQYR VKEPRPIAQY RVEHDEPVAS GAPSAWWQVL IGITTAILGA
IIFFLWRCFL RAKRVKFQAK DSFPWFTTSG DDDSPPPPGD SPSHPPGRSP DRVLPRTVVR
DLSFNDDDDL HSVDLDEAGS RFGEVVSLIA RGNLRELAGA IPESLSNLTL LQTSASGSGF
YTMVALYLAT LGDAITAFHE HNDASPTTTQ SLRTVELQLE ARGLRFNEAG TPANLIQRGV
NSSVGRALVR LTQSALLATG EKFRTRMATT LERIAAERLN TLTAYDQRVI EMTTELLAAI
KTALEVERSE LTPHLANAEA LLQVYNNLFS TDYASASLLA LRREMILRSA EGRVGEQPTS
ASDAANEELV QRSMTKLDKE IELFQAQIDS QRRAVTITEA SNLRENILQP INTVANIAMA
GAFLRGGARH RMPGMPDVAA PMPNPFRAFS GRGHSLTTTR SGGLFRRPRV