ID O89525_9POTY Unreviewed; 3086 AA.
AC O89525;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Ryegrass mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Rymovirus.
OX NCBI_TaxID=40666 {ECO:0000313|EMBL:AAC25028.1};
RN [1] {ECO:0000313|EMBL:AAC25028.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RGMV-AV {ECO:0000313|EMBL:AAC25028.1};
RA Gibbs A.J., Mackenzie A.M., Keese P.;
RT "The complete nucleotide sequence of an Australian isolate of ryegrass
RT mosaic virus.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An RNA-dependent RNA polymerase that plays an essential role
CC in the virus replication. {ECO:0000256|ARBA:ARBA00029404}.
CC -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC {ECO:0000256|ARBA:ARBA00029399}.
CC -!- FUNCTION: Has helicase activity. It may be involved in replication.
CC {ECO:0000256|ARBA:ARBA00029422}.
CC -!- FUNCTION: Indispensable for virus replication.
CC {ECO:0000256|ARBA:ARBA00034080}.
CC -!- FUNCTION: Involved in aphid transmission, cell-to-cell and systemis
CC movement, encapsidation of the viral RNA and in the regulation of viral
CC RNA amplification. {ECO:0000256|ARBA:ARBA00029405}.
CC -!- FUNCTION: Mediates the cap-independent, EIF4E-dependent translation of
CC viral genomic RNAs (By similarity). Binds to the cap-binding site of
CC host EIF4E and thus interferes with the host EIF4E-dependent mRNA
CC export and translation (By similarity). VPg-RNA directly binds EIF4E
CC and is a template for transcription (By similarity). Also forms
CC trimeric complexes with EIF4E-EIF4G, which are templates for
CC translation. {ECO:0000256|ARBA:ARBA00037225}.
CC -!- FUNCTION: Required for aphid transmission and also has proteolytic
CC activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus.
CC Interacts with virions and aphid stylets. Acts as a suppressor of RNA-
CC mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. May have RNA-binding activity.
CC {ECO:0000256|ARBA:ARBA00029420}.
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 Evidence={ECO:0000256|ARBA:ARBA00001848};
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; Evidence={ECO:0000256|ARBA:ARBA00000785};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00034108}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000256|ARBA:ARBA00006064}.
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DR EMBL; AF035818; AAC25028.1; -; Genomic_RNA.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.90.70.150; Helper component proteinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR002540; Pept_S30_P1_potyvir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Helical capsid protein {ECO:0000256|ARBA:ARBA00022497};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022463};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022463};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT DOMAIN 122..256
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 590..711
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1189..1341
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1360..1519
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2000..2217
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2482..2606
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2762..2853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2762..2829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2830..2853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 598
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 670
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3086 AA; 348437 MW; C4659D0D9271838D CRC64;
MMNFGSLNVG LKQVDGTWVP RVFEEKEMAR LLAEKQHARV MRATQEMMRA PNPFAEFDDM
HQRGNPFAGI VKKCETREPK SAQKPIVTVN TIPVVIHTDV IWPENGKVHA LSRRRAPHKH
ARRSKILACD LLTQVLNISK RSGKSVEVIG KRRCCLKPRR RDGKSCFGVI TKHHKGVLSS
RDMVKDLFVD SIIEHIAYTG HTPLIDAAGI KPGDSGLIYR EKRDGYITRV VRGRHGGEII
DARDYVRADI HTIKHYSDDE KPLVKYAPYC QPSHHTYGHM CRVAWSDTEI LQFREMLSQA
IMPQRDPRCD ICAEVAGQRT KDEILQQART SQMMQMLEFG KEDERWKAPR RVMETLLEES
NWPSMDYSTS SDITTICCGN NDEPFRRIYS IMTVLAEPNL ADVSAWQEAN CSLLQLARYM
KNREMSVQAG NSATFTNPFP PTVHTYGPTN NGTDIVQSPW DSWGDKQPIA FAFFEKHFDK
WQVNEFSVDR RVRKHIRGTR KLALLDLNQS RSIKDLEDHV QEEEIPYERK TDSCITMYKD
QYLYSCSCVT ARDGKPYLSM RYLQATGLIP VTRGADVQHI PNPDSVAGIL LCRTRRYCYI
NIFLPMLALA PHYRVGKLSE LIGKLIKVLG KWPKLKDVAL ACLYITEYHT YAQNALLPPI
LVHHSTRTMH VVDTLGSLSI GYHVLKAGTV KHLVNLASRL ATGEMLDYNV GGSQIGINAY
DLLIRGTFDH KLLERALEAD PYYILYSALS PTVLKQMYTS RSYANALRVF VRSNQSLFQV
VCTLENLARR MTRAQSIEQQ IVQLQSLYPQ LLDMLGENTP DSPLSWLSHH VTTDSMQRAI
ELNNCDIELA RGGYASVNTS WRRKKEQYYA DLIEEYYNAL SLQERYSYRV RTLDICTPLR
HYLRSAKKIS FETASNICTQ AYSHTIGRGI SIVSSGGRKG RTWLTARGDS FYKTMISRAI
KLYTPEVSAV IGVATVVGIL LSTMTTLHTY LVKNKQTAQK TNEKFEELMY DKVALYIPKY
DAEHSHLQGK DLDFEHFARW LMTRDKKLSN FVQSHLIDTV THQAKDDTNV WIEKCIATIV
LMMMAIDSNK SDKLYQILCK LRTVFSTMGQ TVVTHQSIDE ILDIDESKRT TIDFERVEVM
QPAQPILKTT FESFWDMQIQ MGRTVVHYRT TGRLVELTRE NIAEVVATIS SDTANAEFIV
RGGVGTGKST SLPTALCERG RVLMLEPTRP LTENVAQQLR GEPHFKSPSV HMRGLNTFGS
SRITIMTSGY ALHYYANNRQ LLRDFEFIIF DECHVMDSSA MAFYSLCNDA KVAAKLLKVS
ATPAGRECDF KPIFPVRVSE AAQLSFESFV TAQGSKSTYD IIQYGNNILV YVASYNEVDK
LATMLLEKRF RVTKVDGRTM KLNTHGIELH GTAQVKHFIV ATNIIENGVT LEIDCLVDFG
TKVVAQLDTE GRRIMYMKVP ISYGERIQRL GRVGRTKPGA ALKVGHTMRG IVEIPEVIAT
EAAFQCFMYD LPVMTGQVQV SLLSKCTREQ ARTMAAFELS PFTMSNLVAF DGTMHPAIHD
LLKKFKLRDS TVVLRRTALP LRASASWYTV REYETIIGDL HIENKDVRIP FVANDLSNSL
LEGLWDAIQC NRSDVSTTKL TTVSANKIAY TLKTDTSSIQ RTISIIDDLL AGERKKQEMF
THHLSTTSGG YTFGLNAIAM CIKSRYAKGY CIENIATLTN VRNQLTEFSG MSEDQYTSEI
IQNYPDLTLV HHQSKQEIIR NLKLKAKYDQ TLIASDLLLG TAVLIGGGAM LYKTFMTATN
TRVHLEGDGK RQRQKLQYRA ARDSKQDYEV YADEREIQEN YGEAYTKHGR KGPAHEKGMG
SKTREFTNFY GFDPAEYDTV RLVDPITGKT CDKAVRDLLR MRDVADTFAE IREAMDEDMI
LQPGVNFAPA LIEAYFMNNR TNAARRVDLV PHNPMQVGRL SNNIAGFPTH DGELRQSRPS
RPLQKDQVPA ANEYSVQHES KSIAKGLRDY HPVSSNLCAL EYYCGDMRTS IYGVCYGPYI
LTTAHLIKEK GGWLKIRTKH GLFKLEAMDR VQIRELCGSD IIVIKGPKDM PPAPMRLKFR
APKSGERSVL VGFVDDNLDR QLISDSSAVY RRENTGFWKH WITTKYGNCG LPMVSVDTMD
IIGLHSLGAQ NSNENYFAAL TDDFSKQFFE PETDVPWQRK WSYNADKVNY GTMDLTSNQP
SGAFRTTKLL EDLLEAVSHQ SQEYTWLTKY CGANLLVIGK CPGNLITKHV IKGKSPTFDL
FLSVDTQASE FFKPLMGDYA PSRLNREAFV KDITKYDTEI PIGNLSITDF ENAVEDTYYI
LKDSGIEQCN YITDAIPIFD SMNMKAATGA LYGGKKKDYF ENYTDDMKQN ILKESYIRLR
EGKMGIWNGS LKAELRSKEK VEANKTRVFT AAPLDTLLAG KGCVDDFNNQ FYAAHLKGPW
TVGITKFFGR WNDFLSELPP GWDYFDADGS RFDSSLTPFL LNAVLNIRKK FMINWAFGQR
CLENLYTEII YTPIATPDGS VVKKMRGNNS GQPSTVVDNT IMVIIAMQYA ISKAEFPAGR
LRDQIRYFAN GDDLVVAVEP SLSDKISSFS ASFAELGLSY DFSNKVNDRS ELQFMSHTGK
LIDGIYIPKL ERERICAILE WSRSDEPQFQ LDAISAAMIE AWGDDELLYQ IRRYYSWLLE
QEPYKSIAEL GHAPYLAEAA LKALYTGKDP DAELIAIYER AMLNTPPTED RPTKVVHEAN
VTAASSAATQ TSTTSPTVTS TSGASTSTSS GTTSAPLAST TPPASATTTP SAGTTAPTTP
AVRAANLRTS QDTERQRRMR ESQLNVRGEN DDEDVPAASE FALPRLPTLG AKIRVPKFKG
AIVLNKDHLI KYTPDQRDLS NTRATQEQFE KWYSGVRNEV EKTDEEMALL LNGFMVWCME
NGTSPDLSGS WTMMEGEEQI CYPLEPFCRH AQPTLRSIMA HFSDAATAYV VLRNQKSRYM
PRYGLKRGLN DYSLAPYAFD FYEITSTSPL RAREAHAQMK AAAIRGKASR MFGLDGNVSA
QSENTERHTV EDVNTRVHSL SGANML
//
