POL2_BAMMN
ID POL2_BAMMN Reviewed; 891 AA.
AC P89684;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Na1) (BaMMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=103900;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8973524; DOI=10.1007/bf01718216;
RA Kashiwazaki S.;
RT "The complete nucleotide sequence and genome organization of barley mild
RT mosaic virus (Na1 strain).";
RL Arch. Virol. 141:2077-2089(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; D83409; BAA18954.1; -; Genomic_RNA.
DR SMR; P89684; -.
DR MEROPS; C06.002; -.
DR Proteomes; UP000007444; 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..229
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040560"
FT CHAIN 230..891
FT /note="70 kDa protein"
FT /id="PRO_0000040561"
FT DOMAIN 109..229
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT REGION 502..540
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 891 AA; 97943 MW; A290247196822BE2 CRC64;
MMMNSTIRQG WQQVLKRFSI PASGDRLIIS NPTDQPIGLF GAFDTSLQTL SQVGDDPEVL
KQKIHIPTHL DIASALEASP RSFPWIFLTN SFCTFGGSIH AQNLQAFATA EFKSGFCYMN
LLVPLSFDII DAHADSFRVF VEQLPDMLGA YPSLSMVLNV MLHAATRFPE IVSSPVPTIA
FDAESLQFHV TDKRGVPGMW NILKAGRVYE LLSLAADGVG CEYMLYPVGA APQYSFWKKS
MDHFTSDRFV EFLAMQNLLA SALEQDYTTH DALDALLAAL QNAGYTNVVA RERRFPNGHD
PSTVWLNLSE APISEKLTDL KRYLLVGHRS DDTADITHNV HQYVFEVLKT MSVQFSKRTN
AYNRARFEVN HKVIWNAEYG RGPQQNAELE ALVLFLNRQS LEIENILHRT TSPVVVTNWQ
PDVPTAAPEV SEGEPTHAVA TPMTEAPAHA TPVEVVNLPS TRSYWAETLV GVLTAVLGTI
FALLTRALIR AKRLRRKPTF PWVTLDSGDE DDDHSGGGGG GPQTPGGQPP ASPAHRTHQS
RLSVQDIASD TSLLSVDLDE DTLSQYDETF QRIRRALFET SFTDILQNSA RWISALEAMA
LADGNAPYTL LAQYLNGIEE AYTSFRNTGH VSRATLSSFF ALEDSLRAAG IAFGATTPTQ
TIQNQFADSP ARRWKTRFEQ IACELGDASI KSLADLADII DTERERSDLT QFDVLAASSI
SSLCRAVRII SDTTDPDAQL ALVENATAMQ NNINAILGTN VSIPFLSATR RLLVTRRIQQ
AGAENRSGAT PETIQQLADA ELIVSEANMF NEMATSQRDI ANATQEATIR EHVLSPVNAL
ANVGMAAAFF RSGGMRSRAL HPAMPTMPGV SAATGRPIFQ AFRGRGHRLN R