GenomeNet

Database: UniProt
Entry: Q65730
LinkDB: Q65730
Original site: Q65730 
ID   POLG_BSTV1              Reviewed;        3093 AA.
AC   Q65730;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-a;
DE              Short=NIa;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Coat protein;
DE              Short=CP;
OS   Brome streak virus (strain 11-Cal) (BStV) (Brome streak mosaic rymovirus).
OC   Viruses; Riboviria; Potyviridae; Tritimovirus.
OX   NCBI_TaxID=117138;
OH   NCBI_TaxID=4501; Bromus.
OH   NCBI_TaxID=97361; Hordeum murinum (Mouse barley) (Critesion murinum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7636484; DOI=10.1099/0022-1317-76-8-2035;
RA   Goetz R., Maiss E.;
RT   "The complete nucleotide sequence and genome organization of the mite-
RT   transmitted brome streak mosaic rymovirus in comparison with those of
RT   potyviruses.";
RL   J. Gen. Virol. 76:2035-2042(1995).
RN   [2]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: [Coat protein]: involved in aphid transmission, cell-to-cell
CC       and systemis movement, encapsidation of the viral RNA and in the
CC       regulation of viral RNA amplification. {ECO:0000250}.
CC   -!- FUNCTION: [Nuclear inclusion protein B]: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC       {ECO:0000250}.
CC   -!- FUNCTION: [Helper component proteinase]: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC       dipeptide at its own C-terminus. Interacts with virions and aphid
CC       stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC       known as post-transcriptional gene silencing (PTGS), a mechanism of
CC       plant viral defense that limits the accumulation of viral RNAs. May
CC       have RNA-binding activity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Cytoplasmic inclusion protein]: has helicase activity. It
CC       may be involved in replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus replication.
CC       {ECO:0000250}.
CC   -!- FUNCTION: [Nuclear inclusion protein A]: has RNA-binding and
CC       proteolytic activities. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that vary
CC         with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC         Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC         the viral polyprotein, but other proteins and oligopeptides
CC         containing the appropriate consensus sequence are also cleaved.;
CC         EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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   -!- SUBCELLULAR LOCATION: [Coat protein]: Virion {ECO:0000305}.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC       to the 5'-end of the genomic RNA. This uridylylated form acts as a
CC       nucleotide-peptide primer for the polymerase (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Genome polyprotein of potyviruses undergoes post-translational
CC       proteolytic processing by the main proteinase NIa-pro resulting in the
CC       production of at least ten individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini autocatalytically.
CC       6K1 is essential for proper proteolytic separation of P3 from CI (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; Z48506; CAA88417.1; -; Genomic_RNA.
DR   RefSeq; NP_612585.1; NC_003501.1.
DR   MINT; Q65730; -.
DR   PRIDE; Q65730; -.
DR   GeneID; 935897; -.
DR   KEGG; vg:935897; -.
DR   Proteomes; UP000000521; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025910; P1_Ser_Pept_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF13611; Peptidase_S76; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW   Helical capsid protein; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   RNA-directed RNA polymerase; Serine protease; Suppressor of RNA silencing;
KW   Thiol protease; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..3093
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000419992"
FT   CHAIN           1..403
FT                   /note="P1 proteinase"
FT                   /id="PRO_0000040233"
FT   CHAIN           404..809
FT                   /note="Helper component proteinase"
FT                   /id="PRO_0000040234"
FT   CHAIN           810..1087
FT                   /note="Protein P3"
FT                   /id="PRO_0000040235"
FT   CHAIN           1088..1138
FT                   /note="6 kDa protein 1"
FT                   /id="PRO_0000040236"
FT   CHAIN           1139..1783
FT                   /note="Cytoplasmic inclusion protein"
FT                   /id="PRO_0000040237"
FT   CHAIN           1784..1834
FT                   /note="6 kDa protein 2"
FT                   /id="PRO_0000040238"
FT   CHAIN           1835..2040
FT                   /note="Viral genome-linked protein"
FT                   /id="PRO_0000040239"
FT   CHAIN           2041..2275
FT                   /note="Nuclear inclusion protein A"
FT                   /id="PRO_0000040240"
FT   CHAIN           2276..2773
FT                   /note="Nuclear inclusion protein B"
FT                   /id="PRO_0000040241"
FT   CHAIN           2774..3093
FT                   /note="Coat protein"
FT                   /id="PRO_0000040242"
FT   DOMAIN          255..403
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          690..809
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   DOMAIN          1215..1366
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1367..1546
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2041..2257
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   DOMAIN          2516..2639
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1228..1235
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           1316..1319
FT                   /note="DEVH box"
FT   MOTIF           1883..1895
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        311
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        323
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        355
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        698
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        769
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        2082
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2121
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   ACT_SITE        2193
FT                   /note="For nuclear inclusion protein A activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT   SITE            403..404
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            809..810
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            1087..1088
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1138..1139
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1783..1784
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            1834..1835
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2040..2041
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2275..2276
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   SITE            2773..2774
FT                   /note="Cleavage; by NIa-pro"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1915
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   3093 AA;  348106 MW;  50F775CEF7ABCCB4 CRC64;
     MQQTHVKQVW RPKTASSKVK TSNMVYLAEE SSPLAKTELK EDAVVAADMS VINADDAVYG
     HALEGKYSER KALPARSNET IVSFASGEDG LFLDRAACGS IFKTRTGKDT PIATAIRAAT
     RRGLAYDIAA QLYMCPKCCS ASDKVLYFDT NHNDSCQWYL DNCRAVINKD WTLDVIETYN
     VFPVLVTEEE ERRTLEAVDI ALKPLGTVPV HDVVQVYDQK IGEHKEVERN QEAAHGSEPA
     IITTTPVLRR QCIEKRLLRH VHQANKVIAN TVEIYDLMTE TSQICAEKAI PLVFVDYEKK
     KRIRPRVPLR HVLESNNVDP SDDLYADVVP FLKHYGTCGR PVGVINPRDI KPGWSGVVLL
     QDELPESLHQ ECVDGVFVVQ GIGPDGQLKN ALKTTTGERI EYYSSKRRMA VNAHVPKAHS
     FCKYSSLTET LMELDYLRVI SALADVHDPQ CVECHKERNE RSFIENLKYT QQGAQNLFNA
     GTGMGLAFVA SIASGQLMIQ RQQPQSSSSI VDQTPRTNED GSLSHNINLL LTPEVVDIWR
     SMKQMVHLPN RKLYMASFND QFGNFDFIPN STLQGVFPDF TMPVTIALND DDKVETNYRH
     VDKNSTIETC VEGLYTQFDA AYWTKKAAQV HKIQPIDQCG MEIGNIALKL CHWEGDVALF
     SPIIRPTPGH LMFGSTDRLL RIPDMTNARH YVPKVGYCYL YLFALAMNFC DGENRVTVDA
     YINKTCRELG AWPKFGEVLR ALDRMATYYG CYDAVVPVML VDHVQRTIHV PSPFGIVQSG
     MHMIQINNLG DLIKLDTMGA SELKEYEIGG FRETYKSITK CVKSKSAFME KLNQDNEWLV
     DMICNPSTLF VLSQLMDTHG LILKDVENSF DRLAALLALK ELGSALGPLL TTRKRVALYM
     QSLSKVDELV PHLGMPTGAM NLLKSEIELI QNAIVEEQDM AEIDRVEGKK SILERRDEMF
     APCVYNEFIN SFGYVSLPGI AYRLTYTGVG ARIGRGCEHL KTVWSGSWIP EIHLPENLRS
     NTWSAIKKYT VYSGGTAWRY MKLKIVESAT QILVAAVITA IGSWLLKKLL KFIRHEKGRL
     NEVVVFQSKQ EELFISKFMA VCFVISTFFS LDMSNAIYSS LTKFRAIFSI LSVGSIYQSG
     ALEKLEEQLG HVDTFHEFKL YDHDATHANI APSVQSFGTW LDTRVLAGQQ GCDPLEGRHT
     KFEMNKNTRD AIAARVLADK DNEFLVMGHV GCGKSTYFPV ALSKQARVLI CEPTRVLVTN
     LHDSMMHTCQ VAPSVMMRNH RCITGSSIMV QTYGFALHYL VNNPENLQQY DFVLFDEVHH
     TCAEKVVLYN WLKGRDWGGK IVKLTATDRS PSAEIKAQKS LDIMTLPTMT PLDFVKEQGL
     STKADASKHG KVILVFLTSF REVDSCYDEL KRKENFDAIK ADSRNLRNKT SLADLISECK
     KEFIYIFATN ILQTGINIEA DVVVDFGYKI VPTYDVDNRM LTTTRKPVNK ADRIQRLGRV
     ARMKAGVAMK IGATIDPEAY DDEVTATEAA LLSFAMQVPP VLRNVNLQIF QRITREQVVT
     AARFEHQLSY MVWMVNKDGS MPTKLYDLFS PLLLSQGNMR LSPYYSSLYD SDTFMTVKNY
     VDIGYLKHDR TTNQRLPFHC HDVSTTFAMK VADRFEDSRA PSTYSIRVPA VNLRHTAVKL
     STDPAQVGMI LVVIGEALVH QKNILEQLKS TRTQLDNYNS CILVPNWNVR GKLDDAINRV
     ERNVSILENQ KNSVEKMSVA RGYDELKELL EENHAVAAHV MYQKGPQKFI DDVLLQKRDF
     SWMPYISVGA ACLMAGCAWY MLYRQRAKHE AKFEGKASRV KASKQKAFDD KMARADNYTY
     YETTDELHNH AREWNDYPTD WVDKVRKKAN VHAMQFGREA PRRDVRNDRP FFNFYGIDEK
     LYDTVTFHDM AASFSVEQPI TAMEVEEAFE KIYLNRQEDE AFFDHPMPKK ILAEFKGKDG
     KVINVEMEPH NPRKANRRGL PVGYADHRGE FRQAKPAEEG PIKFERKALN PKATPYAVFE
     SKALYGGPRC YEHITNNQVL LAGPSGYLNG LITGSKLLAP YHFVKDISSD SQDPSRMIAR
     FGTYNLGNIL NLQVVKFTMI DLIGLDLPVE FQPRRTLKCF RVPVIGEKAV LVLSRYSKEG
     WKSCVSAETE ITPYGENEEL LWRHRITTEV GDCGATMVAL SDQKIVGFHS LGGISMNYFV
     PVTQELLDFL SSKTEKPLVP WRFSEDQVDV GGLYIHNDFD KFPFVKTIQK LVGFQNGHMI
     KYCGEGFTPV ARSENRLSRQ HVISGQRESF IHFVEASSKW RPLITPMLGR LQPSALNREA
     YYKDVLKYDK PIRLGTVHEE AFQSAVINVI RILENAGFER GGVKACFDYG KIFNDLNLDA
     AMGALYAGKK KDYFVEATDE EIEEMFLRSA GKICANGHGV WSALLKAELR PAEKVAANKT
     RTFTSAPIDI LFGAKAVVDD FNKQFYKRHL LGPWTVGINK FNKGWDLLAR SLMRYEWFID
     ADGSQFDSSI TPLLMNAVLT IRLYFMERDD ITELMLRNLY TQIISTCMLA EDGLIVQKHR
     GNNSGQPSTV VDNTLCLMIA MEYARQRAIS DGHLNMQMRY VCNGDDLLIN ANEEAKDVVQ
     GKYEQYIKEL ELNYCFDDAF QSIEGVEFMS HKFMLRNGIY IPKLARHRIV AILEWQRSAE
     PQAIKSAILA ACVEAFGYDD LTELIREYAI SLEPVWGSFL PTDGEIEQLY FEGIAKQEVA
     RCLAGVDDVC KFESAASGTN EAVDEVLKAA GDDEALARAN AAATSGATTP AQNVGAGTTT
     PAKATPQSGR RPSFGSLIDN PIGGNGVQDV ADRTSGIVFP VPTRKSTSLY LPPKVKLRAT
     PERIEKVRKY LPDPQQIDLR YSTQQELNDW IKASADGLGQ TEEAFIDNIL PGWIVHCIVN
     TTSSENRKAG SWRCVTNAGT ADEEQVLYDI EPMYSAANPT MRAIMRHFSD LARLVIAESF
     KQGRPLIPKG YIKAGVLDAS SAAAACDFVV RDRHDTATFV QVQNQVLVNR VSGITNRLFA
     QAMPSAGANE DMARHDAQDA AEGIHNLGGA RAF
//
DBGET integrated database retrieval system