ID E3UR63_TUMVJ Unreviewed; 3152 AA.
AC E3UR63;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Turnip mosaic virus (strain Japanese) (TuMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12230 {ECO:0000313|EMBL:ADP00834.1};
OH NCBI_TaxID=126270; Alliaria petiolata (Garlic mustard) (Arabis petiolata).
OH NCBI_TaxID=3705; Brassica.
OH NCBI_TaxID=38206; Calanthe.
OH NCBI_TaxID=3719; Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris).
OH NCBI_TaxID=264418; Hesperis matronalis.
OH NCBI_TaxID=13274; Stellaria media (Common chickweed) (Alsine media).
OH NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
RN [1] {ECO:0000313|EMBL:ADP00834.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BRS1 {ECO:0000313|EMBL:ADP00834.1};
RA Iram S., Schenk P.;
RT "A novel Turnip mosaic virus isolate characterized from Brisbane,
RT Australia.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; HM544042; ADP00834.1; -; Genomic_RNA.
DR MEROPS; C04.001; -.
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:0008236; F:serine-type peptidase 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; PTHR43519; ATP-DEPENDENT RNA HELICASE HRPB; 1.
DR PANTHER; PTHR43519:SF1; ATP-DEPENDENT RNA HELICASE HRPB; 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; 2.
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 219..361
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 693..814
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1295..1447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1448..1625
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2109..2327
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2591..2715
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2874..2915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 701
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 773
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3152 AA; 357500 MW; C360DCB98B69581D CRC64;
MAAVTFVSAI TNTTTNKPAL TGMVKFGSFS PVPLRSTTVT TVATPVAQPK LYTVQFGSLD
PIIVKGVAGS SAKETRRQLN VKEDVNLRET AALEVAKPQS SIVVRMHEEA NRERAIFLDL
ENSLKRRPYG IAENEKIIMT ARGVSKIVTR SVRAMKHKRA RERRRSQQPI VLKRENKLSE
FSIGGGPSAN IIEKEEARAK WPLHKTPSMK KRMVHRTCKM NTQSIEMLTR SLIKIFKAKS
ANIEFTEKKT IKVDFVKKER LKFARIQSTL TWKEREARLV SGASENQFID ILSNYSGSTK
AIQPGVVCAG WSGIVVRSGT LTHKPSRSPS HAFVIRGEHE GKLYDARVKI TRTMSHKIVH
FIAAGANFWK GFDRCFLAYR SSDREHTCYT RLDVTECGGG GGLIYLASSL GKITCLIVSR
IVNVASQASA FNININSPMR EIIKSSYPRF KHAVQILGRY EQSLHGENTN YQDLQKFKAD
DGMEKAAFPH ANKLNAILIK GATATGEEYA QATKHLLEIT RYMKNRTENI EKGSLKSFRN
KISQKAHINP TLMCDNQLDK NGNFIWGERG YHAKRFFSNY FEIIDPKKGY TQYETRIVPN
GSRKLAIGKL IVPTNFEVLR EQMRGEPVEP HPITVECVSK SQGDFVYACC CVTTESGEPV
SSEIKMPTKH HLVIGNSGDP KYVDLPEIEE NKMYIAKEGY CYINIFLAML VNVKESQAKE
FTKVVRDKLV GELGKWPTLL DVATACYSKS LLPGRCNAEL PRMLVDHKTK IIHVVDSYGS
LSTGYHILKT NTVEQLIKFT RHNLESSLKH YRVGGTKWED AHGGTSNIDN PQWCIKRLIR
GVYRPKQLKE DMLTNPFLPL YALLSPGVIL AFYNSGSLEY LMNHYIRADS SVAVLLVVLK
SLARKVSASQ SVLAQLQIIE RSLPELVEAR ANITESDGAA AHACNKFLGM LIHMSEPNDE
LANGGYTILR DHSITILEKS YLQILDEAWS ELSWSERCAV KYYSSKQAIF SQKDLPVQSG
VDLGGRYSES VISSYEWSKQ RMKILYSSMC NKTRNSVSWV GGKVSSSVCK TINYLVPDVF
RFINVLVCIS LLITIASEAN RIVTAQRRLK LDVAETERKK IEWELAFHHS ILTHSANQHP
TLDEFIAYIS ANAPHLSEHI EFEEKSVVHQ AKRQSEQELE RIIAFIALVL MMFDAERSDC
VTKILNKLKG LVSTVEPTVY HQALNDIEDD LSERNLFVDF ELNNDGEMIQ QLPAEKTFAS
WWNHQLSRGF TIPHYRTEGK FMTFTRATAT EVAGRIAHES DRDILLMGAV GSGKSTGLPY
HLSRKGNVLL LEPTRPLAEN VHKQLSQAPF HQNTTLRMRG LTAFGSAPIS VMTSGFALNY
FANNRARIEE FDFVIFDECH VHDANAMAMR CLLHECDYSG KIIKVSATPP GREVEFSTQY
PVTISTEDVL SFQDFVNAQG SGSNCDVISK GDSILVYVAS YNEVDTLSKL LAERDFKVTK
VDGRTMKVGN IEITTSGTPS KKHFIVATNI IENGVTLDID VVADFGTKVL PYLDTDNRML
STTKTSINYG ERIQRLGRVG RHKPGHALRI GHTEKGLSEV PSCIATEAAL KCFTYGLPVI
TNNVSTSILG NVTVKQARTM AVFEITPFYT SQVVRYDGSM HPQVHALLRR FKLRDSEITL
NKLAIPNRGV NAWLTASEYA RLGANVEDRR DVKIPFMCRD IPEKLHLEMW DVIVKFKGDA
ALDVFQVPAQ VKLHIPCRQM LTPFNEQSPL SIHNREEREA EYFRTVTSNW FLFFSFLNAE
HPKCNKTSHD ERSYVEYLSA EGAKSQLLEF KNLNADHSFV TKNDGISRSF MSEYGALEAV
HHQSTNDMSK FLKLKGKWNK TLITRDVLVI CGVLGGGIWM IIQRLQSPKT EPVVHEAKGK
RQRQKLKFRN ARDNKMGREV YGDDDTIEHF FGDAYTKKGK SKGRTRGLGH KNRKFINMYG
FDPEDFSAVR FVDPLTGATL DENPFTDIAL VQQHFGDIRN NLIAEDELEP QALQVHKTIQ
AYYTNNKTGK ALKVDLTPHM PLKVCDIHAT IAGFPEREFE LRQTGKATPI SMDEVPKANT
ELVSVDHESS SMFRGLRDYN PISNNICHLT NVSDGASNSL YPKGFGPLIL TNRHLFERNN
GELLIKSRHG EFVIKNTTQL HLLPIPDRDL LLIRLPKDIP PFPQKLGFRQ PEKGERICMV
GSNFQTKSIT SVISETSTIM PVDNSQFWKH WISTKDGQCG SPMVSTKDGK ILGLHSLANF
QNSINYFAAF PNDFAEKYLH TIEAHEWVKH WKYNTSGISW GSLNIQAAQP AGLFKVSKLI
SDLDSTAVYA QTQQNRWMYE QLTGNLKAIA HCPSQLVTKH TVKGKCQMFD LYLKLHDEAR
EYFQPMLGQY QKSRLNREAY AKDLLKYATP IEAGNIDCGL FEETVEVVIS DLWGYGFETC
NYVTDEVDIF EALNMKSAVG ALYKGKKRDY FAEFTPEMKE EILKQSCKRL FLGKMGVWNG
SLKAELRPLE KWRQTRHERS QPHHWTLCSG KVCVDDSTTN STTIILKLLG ALGDKILLWL
GPLIGITTRW LDLLRRRWIT VRSSLSPYLI NAVLNIRLEF MEEWDVGEVM LRNLYTEIVY
TPISTPDGTL VKKFKGNNSG QPSTVVDNTL MVILAVNYSL KKSGVPGELR DSIIRFFVNG
DDLLLSVHPT YEYVLDTMAD NFRELGLKYT FDSRTKEKGD LWFMSHQGHK REGIWIPKLE
PERIVSILEW DRSKEPCHRL EAICAAMIES WGYDKLTHEI RKFYAWVIEQ APFNSLAQEG
KAPYIAETAL RKLYLDKEPS QEDLTQYLEA IFEDYEDDTE VCVYHQARET LDAGLTDEQK
QAEKERKDRE KRRRAGETKA ISTQKGKDQH KKKESVTRKS MLELWNFQCT RLKSLASKMR
VPKYEKKLAL NLDHLILYTP EQTDLSNTRS TQKQFNTWFE GVMADYELTE HKMQIILNGL
MVWCIENGTS PNINGMWVMM DGDDQVEFPI KPLIDHAKPT FRQIMAHFSD VAEAYIEKRN
QDRPYMPRYG LQRNLTDMSL ARYAFDFYEM TSRTPIRARE AHIQMKAAAL RGANNNLFGL
DGNVGTTVEN TERHTTEDVN RNMHNLLGVK GL
//
