ID Q6Q098_9POTV Unreviewed; 3063 AA.
AC Q6Q098;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Sugarcane mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12224 {ECO:0000313|EMBL:AAS76887.1};
RN [1] {ECO:0000313|EMBL:AAS76887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCMV-SX {ECO:0000313|EMBL:AAS76887.1};
RX PubMed=15744565; DOI=10.1007/s11262-004-4584-y;
RA Zhong Y., Guo A., Li C., Zhuang B., Lai M., Wei C., Luo J., Li Y.;
RT "Identification of a naturally occurring recombinant isolate of Sugarcane
RT mosaic virus causing maize dwarf mosaic disease.";
RL Virus Genes 30:75-83(2005).
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 -!- SUBUNIT: Interacts with host eIF4E protein (via cap-binding region);
CC this interaction mediates the translation of the VPg-viral RNA
CC conjugates (By similarity). Part of a complex that comprises VPg, RNA,
CC host EIF4E and EIF4G; this interaction mediates the translation of the
CC VPg-viral RNA conjugates. {ECO:0000256|ARBA:ARBA00044023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00034108}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. 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, ECO:0000256|RuleBase:RU003351}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY569692; AAS76887.1; -; 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:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 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 nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022463}; Membrane {ECO:0000256|SAM:Phobius};
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 Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 948..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..233
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 571..693
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1182..1334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1353..1512
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1988..2206
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2472..2596
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2752..2850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3033..3063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2756..2819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3063 AA; 346129 MW; CB6F94AFD439CF62 CRC64;
MAGSWTHVTY KWQPDVNNAR DVKRVMEMFA AKHQHYTEEQ RLAHNSKLLR KACVTSAEFI
EPAQKPKCHQ TWVEKCDHNP TEHFVYQRST PEKKVLSTKP KTTSVTKLIR DVLEISKGSG
IKIELIGKRI KRKTQLSIRQ HNGKDFLHCK TRHENGLFKR KDIDINVKWL PTIEAIAKCY
STVNAEELQS LNRGSSGLTF MQNDELFIVR GRMHGEIVNS LHENKHVMEI EHYADPQANS
FWKGYTDAYV GNRNISTTHT EHTPTINLEE CGKRMALLEI LFHSTFKITC KTCNIDDLEL
SDDEFGAKLY SNLQRIEERQ REYLAKDQKL LRMIHFVKDR CNPKFSHLPL LWQVAETVGH
YTDNQSKQII DISEALIKVN TLTPDDAVKA SVALLEVARW YKNRKESLKT DTLDSFRNKI
SPKSTINAAL MCDNQLDKNA NFVWGNREYH AKRFFANYFE AVDPTDAYEK HVTRFNPNGQ
RKLSIGKLVI PLDFQKIRDS FVGLSINKQP LSKACVSKID GGYVYPCCCV TTEFGKPAYS
EIIPPTKGHI TIGNSVDPKI VDLPNTTPPS MYIAKDGYCY INIFLAAMIN VNEESAKDYT
KFLRDELVER LGKWPKLKDV ATACYALSVM FPEIKNAELP PILVDHESKS MHVIDSYGSL
SVGFHILKAS TVGQLIKFQY ESLESEMREY IVGGTLTQQT FNTLLKTLTK NMFKPNKIKQ
IIEEEPFLLM MAIASPTVLI SLYNNCYIEQ AMTYWIVKNQ GVAAIFTQLE ALAKKTSQAE
LLVLQMQILE KASNQLRLAV TGLNHVDPAK RLLWSHLEAM TTRSEMNKEL IAEGYALYDE
RLYTLMEKSY VDQLNQSWAE LSYCGKFSAI WRVFRVKKYY KPSLTVRKSV DLGAVYNISA
THLISDLVQR SRDRVSSTLT KLRNGFYDKM EKARVSAVRT VYWFIPDIFR LVHIFIILSL
LTTIANTIVT TMNDYKKLKK QQREDEYEAE INEVRKIHAN LMKEHNDNLT CDQFIEYIRQ
THPRLIEATL DLTHTGVIHE GKSSLETNLE QAMAVGTLLT MILDPQKSDA VYKVLNKMRT
VISTFEQNVS FPSINFTNIL TPPVTQQSVD VDEPLTLSTD KNLTIDFDTN QDLPADTFSN
DVTFEDWWAN QISNNRTVPH YRLGGKFVEF TRENAALVSI ELAHSNIEKE FLLRGAVGSG
KSTGLPYHLS ARGKVLLIEP TRPLAENVCR QLQGPPFNVS PTLTMRGLSS FGCTPITIMT
SGFALHMYAN NPDKISDYDF IIFDECHIME APAMAFYCLL KEYEYRGKII KVSATPPGRE
CEFTAQHPVD IHVCENLTQQ QFVRELGTGS NVDATKYGNN ILVYVASYND VDSLSHALIE
LHYSVIKVDG RTMKQNTTGI VTNGTSQKKC FVVATNIIEN GVTLDVDVVV DFGLKVTAEL
DVDNRAILYK RVSISYGERI QRLGRVGRNK PGTVVRIGKT MKGLQEIPAM IATEAAFMCF
AYGLKVITHN VSTTHLAKCT VKQARTMMQF ELSPFVMAEL VKFDGSMHPQ IHEALVKYKL
RDSVIMLRPN AIPKVNFHNW LTARDYNRMG CTVELEDHVK IPYYIRGIPD KLYGKLYDII
LQYSPTSCYG RLSSACAGKV AYTLRTDPCS LPRTIAIINA LITEEYAKRD HYRNMIANPS
SSHAFSLNGL VSMIASRYMK DHTKENIDKL VRVRDQLLEF QGTGMQFQDP SELMDIGALN
TVIHQGMDAT AACIGLQGRW NASLIQRDLM ISAGVFTGGI FMMWYLFIKW SKTEVSHQGK
NKRSRQKLRF KEARDNKYAY DVTGSEEVLG ENFGTAYVKK GKGKGTKVGL GIKQHKFHMM
YGFDPQEYNL IRFVDPLTGA TLDEQIHADI RLVQEHFSVI RDEAVANDTI ERQHIYSNPG
LQAFFIQNGS ANALRVDLTP HTPLRVVTNN NIAGFPEYEG TLRQTGTALQ IPVNQVPAAN
ETGVAHESKS MMAGLGDYTP ISQQLCLIQN DSDGIKRNVY SIGYGSYLIA PAHLFKYNNG
EITIKSSRGL YKIRNSVEIK LHPIAHRDMV IIQLPKDFPP FPMRLKFSKP SRESRVCLVG
VNFQQNYSTC IVSESSVTAP KGNGDFWKHW ISTVDGQCGL PLVDVKSKHI VGIHSLASTS
GNTNFFVAMP EDFNDYIHNL VQTNKWEKGW HYNPNLISWC GLNLVDSAPK GLFKTSKLVE
DLDMSVEEQC KVTETWLTEC IQDNLQVVAK CPGQLVTKHV VKGPCPHFQL YLSTHDEAKA
YFAPLLGKYD KSRLNRAAFI KDISKYAKPI YIGEINYDVF EKAIERVIKI LKDVGMQQCT
YVTDEDEIFQ SLNLNAAVGA LYTGKKKDYF KDFSNEDKSE IIMRSCERIY NGQLGVWNGS
LKAEIRPIEK TILNKTRTFT AAPLETLLGG KVCVDDFNNQ FYSHHLEGPW TVGITKFYGG
WNRLLEKLPD GWIYCDADGS QFDSSLTPYL INAVLHIRLQ FMEKWNLGEQ MLRNLYTEIV
YTPIATPDGS VIKKFKGNNS GQPSTVVDNT LMVILAFNYA MLSSGVKEEE IDNCCRMFAY
GDDLLLAVHP KFEHILDGFQ NHFGNLGLNF EFTSRIRDKS ELWFMSTRGI KCEGIYIPKL
GKERIVAILE WDRSNLPEHR LEAICAAMVE AWGYPDLVQE IRKFYAWLLE MQPFANLAKE
GLAPYIAETA LRNLYLGTGI KEEEIGKYFK QFAKDLPGYI EDYNEDVFHQ SGTVDAGAQG
GGSGSGTTPP ATGSGTGTRT PSTGTPAQGN TPPASGGSSG NNGGGQSGSN GTGGQAGSSG
AGGQRDKDVD AGSTGKISVP KLKAMSKKMR LPKAKGKDVL HLDFLLTYKP QQQDISNTRA
TKEEFDRWYD AIKKEYEIDD TQMTVVMSGL MVWCIENGCS PNINGNWTMM DGDEQRVFPL
KPVIENASPT FRQIMHHFSD AAEAYIEYRN STERYMPRYG LQRNLTDYSL ARYAFDFYEM
TSRTPARAKE AHMQMKAAAV RGSNTRLFGL DGNVGETQEN TERHTAGDVS RNMHSLLGVQ
QHH
//
