POL2_BAMMA
ID POL2_BAMMA Reviewed; 893 AA.
AC Q65329;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 ASL) (BaMMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=103899;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX AGRICOLA=IND20480706; DOI=10.1007/BF01876238;
RA Timpe U., Kuehne T.;
RT "The complete nucleotide sequence of RNA2 of barley mild mosaic virus
RT (BaMMV).";
RL Eur. J. Plant Pathol. 100:233-241(1994).
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; X75933; CAA53537.1; -; Genomic_RNA.
DR SMR; Q65329; -.
DR MEROPS; C06.002; -.
DR PRIDE; Q65329; -.
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_0000040558"
FT CHAIN 230..893
FT /note="70 kDa protein"
FT /id="PRO_0000040559"
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 893 AA; 98329 MW; D6EB74D9D6CF6407 CRC64;
MMMNSMIRQG WQQVLRRFSI PTSGDRLIVS NSTDQPIGLF GAFDTSLQTL SQVTNDPEVL
KQKSNIPTHL DVASVLEASP RSFPWVFLTN SFCTFGGSIH AQNLQAFATA EFKSGFCYMN
LLIPLSFDII DAHADSFRGF VEQLPDTLGA YPSLSMVLNV MLHAATRFPE IVASPIPTIA
FDAESLQFHV TDKRGVPGMW NILKACRVYE LLSLAADGIG CEYMLYPVGA APQYSFWKKS
MDHFTSDRFV EFLAMQDLLA SALEQDYATH DARDALLSAL QNAGYTNVVA RERRFPNGHD
PSIVWLNLSE APISEKLTEL KRYLLVGHRS DDTADITHNV HQHVFEVLKT MSVQFSKTTN
AYNRARFEVN HKVIWNAEYG RGPQQNAELE ALVLFLNRQS LEIENILHRT TSPVVVTSWK
PDVPPAAPEI KEEEPTHAIA TPITEAPSHV TPVEVVNLPP TRSYWAETLV GILTAILGTV
FAFLTRALIR AKRLRRKSTF PWVTLNSGDD DDDQSGGGGG GPQTPGGQPP VPHTRGTHQS
RFSVQDIASD TSLLSVDLDE DTLSQYDETF QKIRRALFET SFADILQNSA RWISTLEAMA
LADGNAPYTL LAQYLNGIEE AYTNFRNTGH ISRATLSGFF ALEDNLRAAG IAFGTTTPTQ
TIQNQFADSP ARRWKTRFEQ IACELGDASI KSLADLADII DTERERGDLT QFDVLAASSI
SSLCRAVRII SDTTDPNAQL ALVENATAMQ NNINAILGTN VSIPFLSATR RLLITRRVQE
AGAESRSGAT PETVQQLADA ELAKIVSEAN MYNEMAASQR DIANATREAT IREHVLSPVN
ALANVGMAAA FFRSGGLRSR AFNPAMPTMP GGPAAAGRPM FQAFRGRGHR LNR