POL2_BAYMG
ID POL2_BAYMG Reviewed; 890 AA.
AC Q01365;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 (isolate Germany) (BaYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=31728;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2016598; DOI=10.1099/0022-1317-72-4-989;
RA Davidson A.D., Proels M., Schell J., Steinbiss H.H.;
RT "The nucleotide sequence of RNA 2 of barley yellow mosaic virus.";
RL J. Gen. Virol. 72:989-993(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; D01099; BAA00884.1; -; Genomic_RNA.
DR PIR; JQ1947; JQ1947.
DR SMR; Q01365; -.
DR MEROPS; C06.002; -.
DR Proteomes; UP000007446; 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_0000040554"
FT CHAIN 256..890
FT /note="70 kDa protein"
FT /id="PRO_0000040555"
FT DOMAIN 135..255
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT REGION 508..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; 98204 MW; 753AB79EABAD3640 CRC64;
MSTSSSRLFF DCGSLDWPNK SLFGDPTTRD VMDEHISSTW NAVIRRHMLA PNADAETILG
RDGLPSAQFD AYGAMLPSFI QALNAPTTRL RISAPLSTAE SILCADASHA PWLYMANSVC
AYEATHLQPV QTFIAFNFAH GYCYLSLFIP LSFRITPENA RSFSRFLEQL PDILGAYPTL
ASLYKTMLFA VRLFPEVLQA PIPIIAKRPG VLQFHVSDAR GLPPSWFPMK CGSVASFIAL
ITNNLNSDLL NGIVGSNGDG EHYTNWNSGH NHWIVNRFIT VKDLHSSLKS ALEVDLDTEG
GRNAVLDLLL DLGVTNLVRR EKRFPAYFQG AESVYLLLSC ERVGNELVAV QDALQEPLAN
YTGKDLRALI INLGGLPSRH PEICYTRNIF ENDNHLVWNF EFYRIASITK NAQIDRDVLS
SSMANLFSDF VSESSNGEYR VKEPRPVTQY RVEHDEPVAS GAPSAWWQVL VGITTAILGA
IIFFLWRCFL RAKRVKFQAK DSFPWFTTSG DDDLPPPPGD SPSRPPGRSP DRVLPRTVVR
DLSFNDDDDL HSVDLNEAGS RFGEVVSLIA RGNLRELAGA IPESLSNLTL LQTSASGSGF
YTMVALYLAT LGDAITAFHE HNDASPATIQ SLRTLELQLE ARGLRFNEAG TPANLIQRGV
KSSVGRALVR LTQSALLATG ENFRTRMAAT LERIAAERLN TLTAYDQRVI EMTTELLAAI
KTALEVERSE LTPHLANAEA LLQVYNNLFS TDYASASLLA LRREMILRSA EGRVGEQPTS
ASDAANEELV QRSMTKLDKE IELFQAQIDS QRRAVTITEA SNLRENILQP INTVANIAMA
GAFLRGGARH RMPGIPDVAA PMSNPFRAFS GRGHSLTTTR GAGLFRRPRV