ID Q0EDF7_TUMVJ Unreviewed; 3164 AA.
AC Q0EDF7;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
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:BAF31145.1};
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:BAF31145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AKD934J {ECO:0000313|EMBL:BAF31145.1};
RX PubMed=17170463; DOI=10.1099/vir.0.82335-0;
RA Ohshima K., Tomitaka Y., Wood J.T., Minematsu Y., Kajiyama H., Tomimura K.,
RA Gibbs A.J.;
RT "Patterns of recombination in turnip mosaic virus genomic sequences
RT indicate hotspots of recombination.";
RL J. Gen. Virol. 88:298-315(2007).
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; AB252100; BAF31145.1; -; Genomic_RNA.
DR MEROPS; C06.001; -.
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:0042025; C:host cell nucleus; 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; 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 219..362
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 698..820
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1300..1452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1471..1630
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2117..2335
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2601..2725
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2883..2937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2886..2930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 706
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 779
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3164 AA; 357791 MW; 03DDC1251261A03C CRC64;
MAAVTFASAI TNATINKPTS TGMVQFGNFP PVPLRSTTIT TVATPVAQPK LYTVQFGNLD
PVVVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NRERALFLDW
ETSLKRRSHG VAENEKVMMT TRGVSKIVPR SSRAMKQKRA RERRRAHQPI ILKWEPVLSG
TSIGGGLSAS AIEAEEVRTK WPLHKTPSMK KRTVHRICKM NDQGIDMLTR SLIKIFKTKS
ANIEYIGKKS IKVDFIRKEQ TKFARVQVAH LLGKRAQRDL LTGAEENHFI DTLSTYSGNR
KIINPGVVCA GWSGIVLRNG ILTQKQSRSP SQAFVIRGEH EGKLYDARVK VTKVMSHKII
HYSAAGANFW KGFDRCFLAY RGDNREHTCY TGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSIKHKL AQLREVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
IQSISDGTDK AAFPHINKLN AILIKGATAT GEEFSQATKY LLEIARYLKN RTENIEKGSL
KSFRNKISQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RIVPNGSRKL AIGKLIVPTN FEVLREQMKG EPIEPHPITV ECVSKLQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHILKTNTVE QLIKFTRCNL ESSLKHYRVG GTAWEEAHGF KNIDSPQWCI
KRLIQGVYRP KKLREDMLTN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRADSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIDRSLPE VVEAKANITG PDEAASQACN RFLGMLIHMA
EPNNELADGG YTILRDHSIS ILEKSYLQIL DEAWSELSWS ERCAIRYYSS KQSIFSQKDL
QMRSDVDLGG RYSESVTSSY EWGKQRVKSV YSNACNKVRS SVSWTSSKVS SSVCKTINYL
VPDVFKFINV LVCISLLATI AAEANRIVTT QRRLKLDIEE TERKKIEWEL AFHHAILTQS
AGQHPTLDEF TAYIGEKAPH LSEYIEPEEK AVVHQAKRQS EQELERVIAF IALVLMMFDA
ERSDCVTKIL NKLKGLVSTV EPTVYHQTLN DIEDDLSERN LFVDFELSND GEILQQLPAE
KTFATWWNHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHENDKDIL LMGAVGSGKS
TGLPYHLSRK GSVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTSFG SAPISVMTSG
FALNYFANNR TRIEEFDFVI FDECHVHDAN AMAMRCLLHE CDYSGKVIKV SATPPGREVE
FSTQYPVTIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLVERD
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLNKLAI PNRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLEMWDVIVK
FKGDAGFGRL SSASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SNFSLQSITN AIKSRMMKDH TCENISVLEG AKSQLLEFRN LNADHSFTTK SDGISRHFMS
EYGALEAVHH QNTNDMSKFL KLKGKWNRTL ITRDVLVICG VLGGGIWMII QHLRTKISEP
VTHEAKGKRQ RQKLKFRNAR DNKMGREVYG EDDVIEHFFG DAYTKKGKSK GRTRGLGHKN
RKFINMYGFD PEDFSAVRFV DPLTGATIDE SPIMDIALVQ EHFGKIRMDL LGEDELEPDE
LRMNKTIQAY YMNNKTGKAL KVDLTPHVPL KVCDLHATIA GFPEREHELR QTGKAQPMDL
SEVPKANTEL IPVDHESSSM FRGLRDYNPI SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LVIKSRHGEF VIKNTTQLHL LPIPDRDLLL IRLPKDIPPF PQKLGFRQPE
KGERICMVGS NFQTKSITSV VSETSTIMPV ENSQFWKHWI STKDGQCGSP MVSTKDGKIL
GLHSLANFQN SINYFAAFPD DFAEKYLYTI EAHEWVKHWK YNTSAISWGS LNIQASQPAG
LFKVSKLISD LDSTAVYAQT QQNRWMYEQL NGNLKAIAHC PSQLVTKHTV KGKCQMFDLY
LKLHDEAREY FQPMLGQYQK SRLNREAYAK DLLKYATPIE AGNIDCELFE KTVETVISDL
RGYGFETCNY VTDETDIFEA LNMKSAVGAL YKGKKKDYFA EFTPEMKEEI LKQSCERLFL
GRMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLRAPWS
VGMTKFYCGW DRLLESLPDG WIYCDADGSQ FDSSLSPYLI NAVLNIRLEF MEEWDIGEVM
LRNLYTEIVY TPISTPDGTL VKKFKGNNSG QPSTVVDNTL MVILAVNYSL RKSGIPNELR
DSLIRFFVNG DDLLLGVHPK YEYVLDTMAD NFRELGLKYT FDSRTREKGD LWFMSHQGHK
REGIWIPKLE PERIVSILEW DRSKEPCHRL EAICAAMIES WGYDRLTHEI RKFYAWMIEQ
APYSSLAQEG KAPYIAETAL RKLYLDKEPA QEDLTQYLQA IFEDYEDGAE VCVYHQAGET
LDAGLTEEQK QAEKERKERE RSERERERQR QLALKKGKNA AQEEGERDNE VNAGTSGTFS
VPRLKSLTSK MRVPKYEKRV ALNLDHLILY TPEQTDLSNT RSTRKQFDTW FEGVMADYEL
TEDKMQIILN GLMVWCIENG TSPNINGMWV MMDGDDQVEF PIKPLIDHAK PTFRQIMAHF
SDVAEAYIEK RNQDRPYMPR YGLQRNLTDM SLARYAFDFY EMTSRTPIRA REAHIQMKAA
ALRGANNNLF GLDGNVGTTV ENTERHTTED VNRNMHNLLG VKGL
//
