ID D6RRC2_TUMVJ Unreviewed; 3164 AA.
AC D6RRC2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:BAJ08151.1};
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:BAJ08151.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IRN TRa6 {ECO:0000313|EMBL:BAJ08151.1};
RX AGRICOLA=IND44187316; DOI=10.1007/s10658-008-9390-2;
RA Farzadfar S., Tomitaka Y., Ikematsu M., Golnaraghi A.R., Pourrahim R.,
RA Ohshima K.;
RT "Molecular characterisation of Turnip mosaic virus isolates from
RT Brassicaceae weeds.";
RL Eur. J. Plant Pathol. 124:45-55(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB440238; BAJ08151.1; -; 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: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..2936
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; 357996 MW; 6FC516386279ED0F CRC64;
MAAVTFASAT TNAVTNKLAS TGMVQFGNFP PVPLRSTIVT TVVTPVAQPK LYTVQFGSLD
PVVVKGVAGS SAKETRQQLN VKEDVNLRGT AALEVAKPQP SIEERMQEEA RKERAIFQEL
ENKLGRRPYG IAENEKIIMT ARGFSKIVPR SKKEMKHKRT KERRNLQQSV VLEWDSTVSK
ISIGGGPSAN AMEAEAVRIK RPLHKTPSMK KKTVHKVCRM NGQGTDMLIR SLIKIFKAKN
ASIEYTGRKS IKIDFVKKER VKFARVQVAH LLGKRAQRDL STGVEENRFI DILSEYSGGK
RAINPGVVCA GWSGIIISGG ALTQKQSRSP SKAFVVRGEH EGKLYDARIK VTKMMSHKIV
HFSAAGANFW KGFDRCFLAY RSDNREHTCY TGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSMKNRL LQLREVIKSS YPRFKHAVQI LDRYEQSLNS ANENYQDFAE
IQSLTDGMEK AAFPHANKLN AILIKGATAT SEEFAQATKY LLEITRYMKN RTENIEKGSL
KSFRNKISQK AHINPTLMCD NQLDRNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RIVPNGARKL AIGKLIVPTN FEVLREQMRG EPVEPHPITV ECVSKSQGDF VYACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYVDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHILKTNTVE QLIKFTRHNL ESSLKHYRVG GTKWEDVHGA KNIDDPQWCI
KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRVDSNVAVL
LVVLKSLAKK VSVSQSVLAQ LQIIERSLPE LVEARANIAE SDGAAAQACN RFLGMLIHRS
EPNNELLDGG YTTLRDHSIA ILEKSYLQIL DEAWSELSWL ERCAVRYYSS KQAIFSQRDL
PMQSGVDLGG RYSESVVSSY EWSKQRMKKL YSSMCSKTRN SMSCVSRKVS SSICRTINYL
VPDIFRFINV LICISLLLTI ASETNRIVTA QRKLKLDVVE AERKKIEWEL AFHHSILTHS
ANQHPTFDEF VEYINAKAPH LSEYIEPEEK AVVHQAKRQS EQELERIIAF IALVLMMFDA
ERSDCVTKIL NKLKGLVSTV EPTVYHQALN DIEDDLSERN LFVDFELNND GELIQQLPAE
KTFASWWNHQ LSRGYTIPHY RTEGKFMTFT RATATEIAGR IAHESDKDIL LMGAVGSGKS
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG
FALNYFANNR ARIEEFDFII FDECHVHDAS AMAMRCLLHD CDYSGKIIKV SATPPGREVE
FSTQYPVTIS TEDTLSFQNF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLAEKD
FKVTKVDGRT MKVGNIEITT SGTPSKKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ELLKRFKLRD
SEIVLNKLAI PNRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLEMWDVIVK
FKGDAGFGRL SSASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SSFSLQSITN AIKSRMMKDH TCENISILEG AKSQLLEFRN LNADHSFTTK TDGISRHFMS
EYGALEAVHH QSTNDMSKFL KLKGKWNKTL ITRDVLVICG VLGGGIWMIL QRLQSGVTEP
VIHEAKGKRQ RQKLKFRNAR DNKMGREVYG DDDTIEHFFG DAYTKKGKSK GRTRGLGHKN
RKFVNMYGFD PEDFSAVRFV DPLTGATLDE SPFTDITLIQ KHFGDIRNDL LEEDELEPQA
IQYHKTIQAY YTNNKTGKAL KVDLTPHIPL KVCDLHATIA GFPEREFELR QTGKAQPISI
DEVPKANTEL VPVDHESSSM FRGLRDYNPI SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LLIKSRHGEF VIRNTTQLHL LPIPDRDLLL IRLPKDIPPF PQKLGFRQPE
KGERICMVGS NFQTKSITSV VSETSTVMPV ENSQFWKHWI STKDGQCGSP MVSTKDGKIL
GLHSLANFQN SINYFAAFPD DFAEKYLYTI ETHEWVKHWK YNTSGISWGS LNIQAAQPAG
LFKVSKLISD LDSTAVYAQT QQNRWMYEQL TGNLKAIAHC PSQLVTKHTV KGKCQMFDLY
LKLHDEAREY FQPMLGQYQK SRLNREAYAK DLLKYATPIE AGNIDCDLFE KTVEIVISDL
WGYGFETCNY VTDETDIFEA LNMKSAVGAL YKGKKKDYFA EFTPEMKEEI LKQSCERLFL
GKMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLSAPWS
VGMTKFYCGW NRLLESLPDN WIYCDADGSQ FDSSLSPYLI NAVLNIRLEF MEEWDVGEVM
LRNLYTEIVY TPISTPDGTL VKKFKGNNSG QPSTVVDNTL MVILAVNYSL KKSGIPSELR
DSIVRFFVNG DDLLLSVHPK YEYILDTMAD NFRELGLKYT FDSRTKEKSD LWFMSHQGHK
REGIWIPKLE PERIVSILEW DRSKEPCHRL EAICAAMIES WGYDKLTHEI RKFYAWVIEQ
APFNSLAQEG KAPYIAETAL RKLYLDKEPS QEDLTQYLEA IFEDYEDGTE VCVYHQAGET
LDAGLTEEQK QAEKERKERE KAEKEREKQK QLALKKGKNS SQEEGERDKE VNAGTSGTFS
VPRLKSLASK MRVPKYEKKL ALNLDHLILY TPEQTDLSNT RSTQKQFNTW FEGVMADYEL
TEDKMQIILN GLMVWCIENG TSPNINGMWV MMDGDDQVEF PIKPLIDHAK PTFRQIMAHF
SDVAEAYIEK RNQDRPYMPR YGLQRNLTDM SLARYAFDFY EMTSRTPIRA REAHIQMKAA
ALRGANNNLF GLDGNVGTTV ENTERHTTED VNRNMHNLLG VKGL
//
