ID Q6I7R6_TUMVJ Unreviewed; 3164 AA.
AC Q6I7R6;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
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:BAD24946.1};
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:BAD24946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu-2R1 {ECO:0000313|EMBL:BAD24946.1};
RX PubMed=15218194; DOI=10.1099/vir.0.79825-0;
RA Suehiro N., Natsuaki T., Watanabe T., Okuda S.;
RT "An important determinant of the ability of Turnip mosaic virus to infect
RT Brassica spp. and/or Raphanus sativus is in its P3 protein.";
RL J. Gen. Virol. 85:2087-2098(2004).
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; AB105135; BAD24946.1; -; 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 2884..2938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2886..2931
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; 357802 MW; E93A45416849B8F3 CRC64;
MAAVTFASAI TNAITNKPAL TGMVQFGSFP PVPLRSTTAI TATTSVAQPK LYTVQFGSLD
SVVVKGGAGS FAKATRQQPN VEIDVSLSEA AALEVAKPRS NAVLRMHEEA NKERAIFLDW
EASLRKSSYG IAENEKVVMT TRGVSKIVPR SSRAMKHKRA RERRIAQQPI ILKWEPKLSE
ISIGGGLSAS AIEVEEVRTK RPLHKTPSMK KRMVHKTCKM NDQGIDMLTR SLVKIFKTKS
ANIEYIGKKS IKVDFIRKER TKFARIQVAH LLGKRAQRDL STGMEENHFI DILSGYSGNK
TTINPGVVCA GWSGIVVRNE ILTQKRSRSP SEAFVIRGEH EGKLYDARVK VTRTMSHKIV
HFSAAGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSMKHRL VQLRDVIKSS YPRFKHAVQI LDRYEQSLRS ANENYQDFAE
IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
KSFRNKISQK AHINPTLMCD NQLDRNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RVVPNGSRKL AIGKLIVPTN FEVLREQMKG EPVESYPVTV ECVSKLQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWEDTHGF NNIDDPQWCI
KRLIKGVYRP KKLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRVDSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIDRSLPE LVEAKANINA SDDAASNACN RFMGMLLHMS
EPNWELADGG YTILRDHSIS ILEKSYLQIL DEAWNELSWS ERCAIRYYSS KQAIFTQKDL
PMRSEVDLGG RYSASVMSSY ERSKQRMKSV YSSIGSRLRS GVSWTSSKVS NSVCRTINYL
VPDVFKFINV LVCISLLVTI TAEANRIVTT QRRLRLDVEE TERKKIEWEL VFHHAILTQS
AGQHPTIDEF RAYIADKAPH LGEHIEPEEK VVVHQAKRQS EQELERIIAF VALVLMMFDA
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN DIEDDLSERN LFVDFELSND GDMLQQLPAE
KTFASWWNHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDRDIL LMGAVGSGKS
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG
FALNYFANNR MRIEEFDFVI FDECHVHDAN AMAMRCLLHE CDYSGKIIKV SATPPGREVE
FSTQYPVSIN TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD SLSKLLIERG
FKVTKVDGRT MKVGNIEITT SGTPSKKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLNKLAI PNRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLDMWDVIVK
FKGDAGFGRL TGASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SNFSLQSITN AIKSRMMKDH TCENISVLEG AKSQLLEFRN LNADHSFATK TDGISRHFMS
EYGALEAVHH QNTSDMSKFL KLKGKWNKTL ITRDVLVLCG VLGGGLWMVI QHLRSKISEP
VTHEAKGKRQ RQKLKFRNAR DNKMGREVYG DDDTIEHFFG DAYTKKGKSK GRTRGLGHKN
RKFINMYGFD PEDFSAVRFV DPLTGATLDD NPLTDITLVQ EHFGNIRMDL LGEDELDSNE
IRVNRTIQAY YMNNKTGKAL KVDLTPHIPL KVCDLHATIA GFPEREHELR QTGKAQPINI
DEVPRANNKL VPVDHESNSM FRGLRDYNPI SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LVIKSRHGEF VIKNTTQLHL LPIPDRDLLL IRLPKDIPPF PQKLGFRQPE
KGERICMVGS NFQTKSITSI VSETSTIMPV ENSQFWKHWI STKDGQCGSP MVSTKDGKIL
GLHSLANFQN SINYFAAFPD DFAEKYLHTI EAHEWVKHWK YNTSAISWGS LNIQASQPSG
LFKVSKLISD LDSTAVYAQT QQNRWMFEQL NGNLKAIAHC PSQLVTKHTV KGKCQMFDLY
LKLHDEAREY FQPMLGQYQK SKLNREAYAK DLLKYATPIE AGNIDCDLFE KTVEIVISDL
QGYGFETCNY VTDENDIFEA LNMKSAVGAL YKGKKKDYFA EYTPEMKEEI LKQSCERLFL
GKMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLRAPWS
VGMTKFYCGW DRLLESLPDG WVYCDADGSQ FDSSLSPYLI NAVLNIRLEF MEEWDVGEVM
LRNLYTEIVY TPISTPDGTL VKKFKGNNSG QPSTVVDNTL MVILAVNYSL KKSGIPSELR
DSIIRFFVNG DDLLLSVHPE YEYILDTMAD NFRELGLKYT FDSRTREKGD LWFMSHQGHK
REGIWIPKLE PERIVSILEW DRSKEPCHRL EAICAAMIES WGYDKLTHEI RKFYAWMIEQ
APFSSLAQEG KAPYIAETAL RKLYLDKEPA QEDLTHYLQA IFEDYEDGAE ACVYHQAGET
LDAGLTDEQK QAEKEKKERE KAEKERERQK QLALKKGKNA AQEEGERDKE VNAGTSGTFS
VPRLKSLTSK MRVPRYEQRV ALNLDHLILY TPEQTDLSNT RSTRKQFDTW FEGVMADYEL
TEDKMQIILN GLMVWCIENG TSPNINGMWV MMDGDDQVEF PIKPLIDHAK PTFRQIMAHF
SDVAEAYIEK RNQDRPYMPR YGLQRNLTDM SLARYAFDFY EMTSRTPIRA REAHIQMKAA
ALRGANNNLF GLDGNVGTTV ENTERHTTED VNRNMHNLLG VKGL
//
