ID M5AC89_TUMVJ Unreviewed; 3164 AA.
AC M5AC89;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:BAM99234.1};
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:BAM99234.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GBR57 {ECO:0000313|EMBL:BAM99234.1};
RA Nguyen H.D., Tomitaka Y., Ho S.Y.W., Duchene S., Vetten H.-J., Lesemann D.,
RA Walsh J.A., Gibbs A.J., Ohshima K.;
RT "Turnip Mosaic Potyvirus Probably First Spread to Eurasian Brassica Crops
RT from Wild Orchids about 1000 Years Ago.";
RL PLoS ONE 8:e55336-e55336(2013).
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; AB701716; BAM99234.1; -; 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: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..2935
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; 357709 MW; 4F5574122A807AEC CRC64;
MAAVTFASAI TNAITNKPAS TGMVQFGSFP PMPLRSATVT TVATPVAQPK LYTVQFGNLD
PVVVKGGAGS LAKATRQQPN VEIDVSLSEA AALEVAKPKP NAVLRMHEEA NKERALFLDW
EAGLKKRSYG VAENEKVVMT TRGVSKVVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSE
FSIGGGLSAS AIEAEEVRTK WPLHKTPSMK RRKMHKMCRM NEQGIDMLMR SLIKIFKAKS
ADIEYTGKKS IKIDFVEKKR TKFARVQVAH LLGKRAQRDL STGVEENHFI DTLSSFSGSK
RSIKPGVVCA GWSGVIVRGG VLTQKQSRSP SEAFVIRGEH EGKLYDARIK VTKTMSHKIV
HFSAAGANFW KGFDRCFLAY RSDNRDHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
IQSISDGMEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
KSFRNKVSQK SHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RVVPNGSRKL AIGKLIVPTD FEVLREQMRG EPVEPYPVTT ECVSKSQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWEDAHGV DNIDNPQWCI
KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
LVVLKSLAQK VSTSQSVLAQ LQIIERSLPE LIEAKANVKG PDDAATRACN RFMGMLLHMA
EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWL ERCAIRYYSS KQSIFTQKDL
PMQSEVDLGG RYSASVISSY EWSKQQAKGV KSSVVNKLRS GMSWTNDKVS NSVCRTINYL
VPDVFKFMNV LVCISLLIKM TAEANHMVTT QRRLKLDMEE TERRKIEWEL AFHHAILTQS
ANQHPTLDEF IAYIAEKAPH LSEHIDPEER VVVHQAKRQS EQELERIIAF VALVLMMFDA
ERSDCVTKIL NKLKGLVATV EPSVYHQTLN EIEDDLSERN LFVDFELSSD GEMLQQLPAE
KTFASWWSHQ LSRGFTIPHY RTEGKFTTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTTFG SAPISVMTSG
FALNYFANNR SRIEEFDFVI FDECHVHDAN AMAMRCLLHE CDYSGKIIKV SATPPGREVE
FSTQYPVSIS TEDTLSFKDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
FKVTKVDGRT MKVGNIEITT SGTPSKKHFI VATNIIEKGV TLDIDVVADF GTKVLPYLDT
DSRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEV TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLNKLAI PNRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLDMWDVIVK
FKGDAGFGRL SSASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SNFSLQSITN AIKSRMMKDH TCENISVLEG AKSQLLEFRN LNSDHSFVTK ADGISRHFMS
GYGALEAVHH QSTNEMSKFL KLKGKWNKTL ITRDVLVICG VLGGGIWMVI QHLRSRISEP
VTHEAKGKRQ RQKLKFRNAR DNKMGREVYG DDDTIEHFFG DAYTKKGKSK GRTRGIGHKN
RKFINMYGFD PEDFSAVRFV DPLTGATLDD NPFTDITLVQ KHFGDIRMDL LGEDELDPNE
IRVNKTIQAY YTNNKTGKAL KVDLTPHMPL KVCDLHATIA GFPERENELR QTGKAQPINI
DEVPKANNEL VPVDHESNSM FRGLRDYNPV SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LVIKSRHGEF VIKNTTQLHL LPIPDRDLLL IRLPKDIPPF PQKLGFRQPE
KGERICMVGS NFQTKSITSI VSETSSIMPV ENSHFWKHWI STKDGQCGSP MVSTKDGKIL
GLHSLANFQN SINYFAAFPD DFVEKYLHTI ETHEWVKHWK YNTSAISWGS LNIQASQPAG
LFKVSKLISD LDSTAVYAQT QQNRWMFEQL TGNLKAIAHC PSQLVTKHTV KGKCQMFDLY
LKLHDEAREY FQPMLGQYQK SRLNREAYAK DLLKYATPIE AGNIDCDLFE KTVEIVTSDL
RGYGFETCNY VTDENDIFEA LNMKSAVGAL YKGKKKDYFA EFTPEMKEEI LKQSCERLFL
GKMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLRAPWS
VGMTKFYCGW DRLLESLPDG WVYCDADGSQ FDSSLSPYLI NAVLNIRLEF MEEWDIGEVM
LRNLYTEIVY TPISTPDGTL VKKFKGNNSG QPSTVVDNTL MVILAVNYSL KKSGIPRELR
DSLIRFFVNG DDLLLSVHPE YEYVLDTMAD NFRELGLKYT FDSRTREKGD LWFMSHQGHR
REGIWIPKLE PERIVSILEW DRSKEPCHRL EAICAAMIES WGYDKLTHEI RKFYAWMIEQ
APFSSLAQEG KAPYIAETAL RKLYLDKEPA QEDLTQYLQA IFEDYEDGAE VCVYHQAGET
LDAGLTEEQK QAEKEKKERE KAEKERERQK QLALKKGKDV AQEEGKRDKE VNAGTSGTFS
VPRLKSLTSK MRVPKYEKRV ALNLDHLILY TPEQTDLSNT RSTRKQFDTW FEGVMADYEL
TEDKMQIILN GLMVWCIENG TSPNINGMWV MMDGDDQVEF PIKPLIDHAK PTFRQIMAHF
SDVAEAYIEK RNQDRPYMPR YGLQRNLTDM SLARYAFDFY EMTSRTPIRA REAHIQMKAA
ALRGANNNLF GLDGNVGTTV ENTERHTTED VNRNMHNLLG VQGL
//
