ID C9WKC6_9POTV Unreviewed; 3066 AA.
AC C9WKC6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Soybean mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12222 {ECO:0000313|EMBL:ACU98958.1};
RN [1] {ECO:0000313|EMBL:ACU98958.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WS162 {ECO:0000313|EMBL:ACU98958.1};
RX PubMed=19716150; DOI=10.1016/j.virol.2009.07.007;
RA Seo J.K., Ohshima K., Lee H.G., Son M., Choi H.S., Lee S.H., Sohn S.H.,
RA Kim K.H.;
RT "Molecular variability and genetic structure of the population of soybean
RT mosaic virus based on the analysis of complete genome sequences.";
RL Virology 393:91-103(2009).
RN [2] {ECO:0000313|EMBL:ACU98958.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WS162 {ECO:0000313|EMBL:ACU98958.1};
RA Seo J.-K., Lee H.-G., Son M.-I., Choi H.-S., Lee S.-H., Kim K.-H.;
RT "Molecular characterization of Soybean mosaic virus isolates.";
RL Submitted (JAN-2009) 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}. 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; FJ640973; ACU98958.1; -; 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 Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
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 168..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 643..765
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1236..1388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1407..1566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2042..2260
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2526..2650
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2800..2836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2800..2818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2819..2835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 651
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 724
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3066 AA; 349785 MW; 2D7CB33CEE2983B8 CRC64;
MATIMIGSMA ISVPNTHVSC ASNSVMPVQA VQMAKQVPSA RGVLYTLKRE GSTQVHKHEE
ALRKFQEAFD QDVGIQRRLL VSKHSSIQST KKNGLTLRRL TLEQARAKEA AIARRKQEEE
DFLNGKYEQQ FYAGVSATKF MKFEGGSVGF RTKYWRPTPK KTKERRATSQ CREPTYVLEE
VLSIASKSGK LVEFITGKGK RVKVCYVRKH GAILPKFSLP HEEGKYIHQE LQYASTYEFL
PYICMFAKYK SINADDITYG DSGLLFDERS SLTTNHTKLP YFVVRGRRNG KLVNALEVVE
NMEDIQHYSQ NPEAQFFRGW KKVFDKMSPH VENHECTIDF TNEQCGELAA AISQSFFPVK
KLSCKQCRQH IKHLSWEEYK QFLLAHMGGH GAEWETFQEI DGMRYVKRVI ETSTAENASL
QTSLEIVRLT QNYKSTHMLQ IQDINKALMK GPSVTQSELE QASKQLLAMT QWWKNHMALT
DEDALKVFRN KRSSKALLNP SLLCDNQLDK NGNFVWGERG RHSKRFFANY FEEVVPSEGY
SKYVIRKNPN GQRELAIGSL IVPLDFERAR MALQGKSVTR EPITMSCISR QDGNFVYPCC
CVTHDDGKAF YPELKSPTKR HLVIGTSGDP KYIDLPATDA DRMYIAKEGF CYLNIFLAML
VNVNEDEAKD FTKMVRDVIV PRLGKWPTML DVATAAYMLT VFHPETRNAE LPRILVDHAC
QTMHVIDSFG SLTVGYHVLK AGTVNQLIQF ASNDLQSEMK FYRVGGEVQQ RMKCETALIT
SVFKPKRMVQ ILENDPYILL MGLVSPTILI HMYRMKHFEK GVELWISKEH SVAKIFIILE
QLTKRVAAND VLLEQLEMIS ETSERFMSIL EDCPRAPHSY KTAKDLLTMY IERKASNSQL
VENGFVDMND KLYMAYEKIY SDRLKQEWRA LSWLEKFSIT WQLKRFTPHT EKCLTKKVVE
ESSASSGNFA SVCFMNAQSH LRNVRNTLFQ KCDQVWTASV RAFVRFIIST LHKCYSDIVY
LVNICIIFSL LVQMTSVLQG IVNTARRDKA LIHMHKRKED EEAVIHLYEM CEKMEGGHPS
VEKFLNHVKG VRPDLLSVAM SMAGESEDVS VQAKTATQLQ LEKIVAFMAL LTMCIDNERS
DAVFKVLSKL KAFFSTMGED VKVQSLDEIQ NIDEDKKLTI DFDLETNKES SSVSFDVKFE
DWWNRQLQQN RVIPHYRSTG EFLEFTRETA AKIANLVATS SHTEFLIRGA VGSGKSTGLP
HHLSKKGKVL LLEPTRPLAE NVSKQLSLEP FYHNVTLRMR GLSKFGSSNI VVMTSGFAFH
YYVNNPQQLS DFDFIIIDEC HVQDSPTIAF NCALKEFEFG GKLLKVSATP PGRECEFTTQ
QPVKLKVEDH LSFQNFVQAQ GTGSNADMIQ HGNNLLVYVA SYNEVDQLSR LLTEKHYKVT
KVDGRTMQMG NVEIATTGTE GKPHFIVATN IIENGVTLDI DCVIDFGLKV VATLDTDNRC
VRYNKQSVSY GERIQRLGRV GRCKPGFALR IGHTGKGVEE VPEFIATEAA FLSFAYGLPV
TTQSVSTNIL SRCTVKQARV ALNFELTPFF TTNFIKYDGS MHPEIHRLLK PYKLRESEML
LTKLAIPYQF VGQWITVKEY ERQGIHLNCP EKVKIPFYVH GIPDKLYEML WDIVCKYKND
AGFGSIKSVN ATKISYTLST DPTAIPRTLA ILDHLLSEEM TKKSHFDTIG SSVTGYSFSL
AGIADGFRKR YLRDYTQHNI AILQQAKAQL LEFDCNKVDI NNLHNVEGIG ILNAVQLQSK
HEVSKFLQLK GKWDGKKFMN DAVVAIFTLV GGGWMLWDYF TRVIREPVST QGKKRQIQKL
KFRDAFDRKV GREVYADDYT MEHTFGEAYT KKGKQKGSTR TKGMGRKSRN FIHLYGVEPE
NYSMIRFVDP LTGHTMDEHP RVDIRMVQQE FEEIRKDMIG EGELDRQRVY HNPGLQAYFI
GKNTEEALKV DLTPHRPTLL CQNSNAIAGF PEREDELRQT GLPQVVSKSD VPRAKERVEM
ESKSVYKGLR DYSGISTLIC QLTNSSDGHK ETMFGVGYGS FIITNGHLFR RNNGMLTVKT
WHGEFVIHNT TQLKIHFIQG KDVILIRMPK DFPPFGKRNL FRQPKREERV CMVGTNFQEK
SLRATVSESS MILPEGKGSF WIHWITTQDG FCGLPLVSVN DGHIVGIHGL TSNDSEKNFF
VPLTDGFEKE YLENADNLSW DKHWFWEPSK IAWGSLNLVE EQPKEEFKIS KLVSDLFGNT
VTVQGKKERW VLDAMEGNLV ACGQADSALV TKHVVKGKCP YFAQYLSVNQ EAKSFFEPLM
GAYQPSRLNK DAFKRDFFKY NKPVVLNEVD FQAFEKAVAG VKLMMMEFDF KECVCVTDPD
EIYDSLNMKA AVGAQYKGKK QDYFSGMDSF DKERLRYLSC ERLFYGEKGV WNGSLKAELR
PIEKVQANKT RTFTAAPIDT LLGAKVCVDD FNNQFYSLNL TCPWTVGMTK FYRGWDKLMR
SLPDGWVYCH ADGSQFDSSL TPLLLNAVLD VRSFFMEDWW VGREMLENLY AEIVYTPILA
PDGTIFKKFK GNNSGQPSTV VDNTLMVVIA MYYSCCKQGW SEEDIQERLV FFANGDDIIL
AVSEKDTWLY DTLSTSFAEL GLNYNFEERT KKREELWFMS HQAMLVDGIY IPKLEPERIV
SILEWDRSKE LMHRTEAICA AMIEAWGYTE LLQAIRKFYL WLLNKDEFKE LASSGKAPYI
AETALRKLYT DVNAQTSELQ RYLEVLDFKH ADDCCESVSL QSGKEKEGDM DAGKDPKKST
SSSKGAGTSS KDVNVGSKGK VVPRLQKITR TMNLPMVEGK IILSLDHLLE YKPNQVDLFN
TRATRTQFEA WYNAVKDEYE LDDEQMGVVM NGFMVWCIDN GTSPDANGVW VMMDGEEQIE
YPLKPIVENA KPTLRQIMHH FSDAAEAYIE MRNSESPYMP RYGLLRNLRD RELARYAFDF
YEVTSKTPNR AREAIAQMKA AALSGVNNKL FGLDGNISTN SENTERHTAR DVNQNMHTLL
GMGPPQ
//
