ID Q7T4H8_TUMVJ Unreviewed; 3164 AA.
AC Q7T4H8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
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:BAC79413.1};
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:BAC79413.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NDJ {ECO:0000313|EMBL:BAC79413.1};
RX PubMed=12859632; DOI=10.1046/j.1365-294X.2003.01881.x;
RA Tomimura K., Gibbs A.J., Jenner C.E., Walsh J.A., Ohshima K.;
RT "The phylogeny of Turnip mosaic virus; comparisons of 38 genomic sequences
RT reveal a Eurasian origin and a recent 'emergence' in east Asia.";
RL Mol. Ecol. 12:2099-2111(2003).
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; AB093616; BAC79413.1; -; 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..2937
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; 357347 MW; 900BD869E0C17473 CRC64;
MAAVTFATAI TNTTASRSAS TGMVQFGNFP PVPLRSTTAT TVATPVAQPK LYTVQFGSLD
PVVVKSGAGS FAKATRQQPN VEIDVSLSEA AALEVAKPRP NAVLRMHEEA NKERALFLDW
EASLKRSSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKSSG
ISIGGGLSAS AIEVEEVRTK WPLHKTPSMK RKMVHRRCKM NDQGVDMLMR SLIKIFKAKS
ANIEFIGRKS VKVDFVKKEQ TKFARVQVVH LLGKRAQRDL LTGAEENHFI DTLSTYSGNK
KIINPGVVCA GWSGIVIRNG ILTQKQSRSP SQAFVIRGEH EGKLYDARVK VTKVMSHKIL
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 NNIDDPQWCI
KRLIQGVYRP KKLREDMLTN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRADSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LVEARANIVG PDEAASQACN RFLGMLIHMA
EPNNELADGG YTILRDHSIS ILEKSYLQIL DEAWSELSWS ERCAIKYYSS KQAIFSQKDL
QMRSDVDLGG RYSESVTSSY EWGKQRVKSV YSNACNKVRS SVSWTSSKIS SSVCKTINYL
VPDVFKFINV LVCISLLVTI AAEANRIVTT QRRLKLDIEE TERKKIEWEL AFHHAILTQS
AGQHPTLDEF TAYIGEKAPH LSEHIEPEEK AVVHQAKRQS EQELERVIAF IALVLMMFDA
ERSDCVTKIL NKLKGLVSTV EPTVYHQTLN DIEDDLSERN LFVDFELSND GEILPQLPAE
KTFASWWNHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDRDIL LMGAVGSGKS
TGLPYHLSRK GSVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTSFG SAPISVMTSG
FALNYFANNR TKIEEFDFVI FDECHVHDAN AMAMRCLLHE CDYSGKVIKV SATPPGREVE
FSTQYPVTIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLNKLAI PNRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLEMWDAIVK
FKGDAGFGRL SGASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SNFSLQSITN AIKSRIMKDH TCENISVLEG AKSQLLEFRN LNADHSFTTK SDGISRHFMS
DYGALEAVHH QNTNDMSKFL KLKGKWNKTL ITRDVLVICG VLGGGIWMII QHLRMKISEP
VTHEAKGKRQ RQKLKFRNAR DNKMGREVYG EDDVIEHFFG DAYTKKGKSK GRTRGLGHKN
RKFINMYGFD PEDFSAVRFV DPLTGATIDE SPIMDIALVQ EHFGKIRMDL LGEDELEPDE
LRMNKTIQAY YMNNKTGKAL KVDLTPHIPL KVCDLHATIA GFPEREHELR QTGKAQPMNL
SEVPKANTEL IPVDHESSSM FRGLRDYNPI SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LVIKSRHGEF VVKNTTQLHL 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
RGYGFETCNY VTDENDIFEA LNMKSAVGAL YKGKKKDYFA EFTPEMKEEI LKQSCERLFL
GKMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLRAPWS
VGMTKFYCGW DRLLESLPDG WVYCDADGSQ FDSSLSPYLI NAVLNIRLGF 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
LDAGLTEEQK 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
//
