ID Q5TLC4_TUMVJ Unreviewed; 3164 AA.
AC Q5TLC4;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Turnip mosaic virus (isolate UK1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus;
OC Turnip mosaic virus (strain Japanese).
OX NCBI_TaxID=300942 {ECO:0000313|EMBL:BAD69811.1};
RN [1] {ECO:0000313|EMBL:BAD69811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UK1 {ECO:0000313|EMBL:BAD69811.1};
RX PubMed=15659771; DOI=10.1099/vir.0.80540-0;
RA Tan Z., Gibbs A.J., Tomitaka Y., Sanchez F., Ponz F., Ohshima K.;
RT "Mutations in Turnip mosaic virus genomes that have adapted to Raphanus
RT sativus.";
RL J. Gen. Virol. 86:501-510(2005).
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; AB194790; BAD69811.1; -; 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..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; 357407 MW; D62807AC659D8EB0 CRC64;
MAAVTFASAI TNAITSKPAL TGMVQFGSFP PMPLRSTTVT TVATSVAQPK LYTVQFGSLD
PVVVKSGAGS LAKATRQQPN VEIDVSLSEA AALEVAKPRS NAVLRMHEEA NKERALFLDW
EASLKRSSYG IAEDEKVVMT THGVSKIVPR SSRAMKLKRA RERRRAQQPI ILKWEPKLSG
ISIGGGLSAS VIEAEEVCTK WPLHKTPSMK KRTVHRICKM NDQGVDMLTR SLVKIFKTKS
ANIEYIGKKS IKVDFIRKER TKFARIQVAH LLGKRAQRDL LTGMEENHFI DILSKYSGNK
TTINPGVVCA GWSGIVVGNG ILTQKRSRSP SEAFVIRGEH EGKLYDARIK VTRTMSHKIV
HFSAAGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
IQSISDGVEK AAFPHVNKLN AILIKGATVT GEEFSQATKH LLEIARYLKN RTENIEKGSL
KSFRNKISQK AHINPTLMCD NQLDRNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RAVPNGSRKL AIGKLIVPTN FEVLREQMKG EPVEPYPVTV ECVSKLQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWEDTHGS SNIDNPQWCI
KRLIKGVYKP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRVDSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANVNG PDDAATRACN RFMGMLLHMA
EPDWELADGG YTILRDHSIS ILEKSYLQIL DEAWNELSWS ERCAIRYYSS KQAIFTQKDL
PMKSEADLGG RYSVSVMSSY ERSKQCMKSV HSSIGNRLRS SMSWTSSKVS NSVCRTINYL
VPDVFKFMNV LVCISLLIKI TAEANHIVTT QRRLKLDIEE TERRKIEWEL AFHHAILTQS
AGQHPTIDEF RAYIADKAPH LSEHIEPEEK AVVHQAKRQS EQELERIIAF VALVLMMFDA
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN DIEDDLSERN LFVDFELSSD GDMLQQLPAE
KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK IAHESDKDIL LMGAVGSGKS
TGLPYHLSRK GNVLLLEPTR PLAENVHKQL SQAPFHQNTT LRMRGLTAFG SAPISVMTSG
FALNYFANNR MRIEEFDFVI FDECHVHDAN AMAMRCLLHE CDYSGKIIKV SATPPGREVE
FSTQYPVSIS TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD ALSKLLIERD
FKVTKVDGRT MKVGNIEITT SGTPSKKHFI VATNIIENGV TLDIDVVADF GTKVLPYLDT
DSRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTEK GLSEVPSCIA TEAALKCFTY
GLPVITNNVS TSILGNVTVK QARTMSVFEI TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD
SEIVLNKLAI PHRGVNAWLT ASEYARLGAN VEDRRDVRIP FMCRDIPEKL HLDMWDVIVK
FKGDAGFGRL SSASASKVAY TLQTDVNSIQ RTVTIIDTLI AEERRKQEYF KTVTSNCVSS
SNFSLQSITN AIKSRMMKDH TCENISVLEG AKSQLLEFRN LNADHSFATK TDGISRHFMS
EYGALEAVHH QNTSDMSKFL KLKGKWNKTL ITRDVLVLCG VLGGGLWMVI QHLRSKMSEP
VTHEAKGKRQ RQKLKFRNAR DNKMGREVYG DDDTIEHFFG DAYTKKGKSK GRTRGIGHKN
RKFINMYGFD PEDFSAVRFV DPLTGATLDD NPLTDITLVQ EHFGNIRMDL LGEDELDSNE
IRVNKTIQAY YMNNKTGKAL KVDLTPHIPL KVCBLHATIA GFPERENELR QTGKAQPINI
DEVPRANNEP VPVDHESNSM FRGLRDYNPI SNNICHLTNV SDGASNSLYG VGFGPLILTN
RHLFERNNGE LVIKSRHGEF VIKNTTQLHL LPIPDRDLLL IRLPKDVPPF PQKLGFRQPE
KGERICMVGS NFQTKSITSI VSETSTIMPV ENSQFWKHWI STKDGQCGSP MVSTKDGKIL
GLHSLANFQN SINYFAAFPD DFAEKYLHTI EAHEWVKHWK YNTSAISWGS LNIQASQPSG
LFKVSKLISD LDSTAVYAQT QQNRWMFEQL NGNLKAIAHC PSQLVTKHTV KGKCQMFDLY
LKLHDEAREY FQPMLGQYQK SKLNREAYAK DLLKYATPIE AGNIDCDLFE KTVEIVVSDL
RGYGFETCNY VTDENDIFEA LNMKSAVGAL YKGKKKDYFA EFTPEMKEEI LKQSCERLFL
GKMGVWNGSL KAELRPLEKV EANKTRTFTA APLDTLLGGK VCVDDFNNQF YDHNLRAPWS
VGMTKFYCGW DRLLESLPDG WVYCDADGSQ FDSSLSPYLI NAVLNIRLGF MEEWDIGEVM
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 QLALKKGKDV AQEEGKRDKE VNAGTSGTFS
VPRLKSLTSK MRVPRYEKRV ALNLDHLILY TPEQTDLSNT RSTRKQFDTW FEGVMADYEL
TEDKMQIILN GLMVWCIENG TSPNINGMWV MMDGDDQVEF PIKPLIDHAK PTFRQIMAHF
SDVAEAYIEK RNQDRPYMPR YGLQRNLTDM SLARYAFDFY EMTSRTPIRA REAHIQMKAA
ALRGANNNLF GLDGNVGTTV ENTERHTTED VNRNMHNLLG VQGL
//
