ID V5RQW9_9POTV Unreviewed; 3145 AA.
AC V5RQW9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Leek yellow stripe virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=42004 {ECO:0000313|EMBL:AHB39218.1};
RN [1] {ECO:0000313|EMBL:AHB39218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SW8 {ECO:0000313|EMBL:AHB39218.1};
RA Wylie S.;
RT "Viruses of garlic.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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; KF597283; AHB39218.1; -; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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 213..355
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 689..811
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1294..1446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1461..1624
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2103..2320
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2586..2708
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2862..2911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 907..934
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2862..2898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 697
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 770
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3145 AA; 356146 MW; 309ABD36D0E73EE6 CRC64;
MAKILASVNY VEYGQGSGQD MAVGREEILR RVLARILSNT HNSSYVFGAT GYGKVQNSKA
LCAQRMGARY NWEDDVYECT TCNGAFQTKI DFKEHDCDEE NEDLKLIPED FSLKLEEFPT
LSESTTCEAK TENGTTYFGD FGTPTLLESV PTCGVVFSVD ARQQEQLGNV DGNSVHICTL
DNNNETPITK HTIPDPSLVS LQSRQRTTHA SDKMNGINTS TLIHHLTRIV HDRQLDVHFV
GKRRLDGRCV RVDGKSYLQL QTKHTSGLRR RVDCHIPKGL ESVIHALAKG SGYKSRVHVS
KIKKGWSGFV LKPQNIIGQV GKCKHDFFVV RGSLKGKLVD ACARIDLGKS ELEHYSAGQI
IWKNFEDEFV KLRPNLQHKC TSDIDVSKCG KLAAVLIQLF HPCGKITCAE CIADATNKTP
AEYITELLAR MPLARERIEE LDAFPHISNL LTLLEAKFEK STSNSEIYAQ VLQSIGHIKT
QPFDKLNNMN SLLVGHCGSV PNSVVQKLQE DLLEVVRYTK KRTDSINRGE IQHYRNKIAS
KAHFNLDLMC DNQLDKNGNF IWGERGYHAR RFFLNYFDVI DPTANYSNHI IRHNPNGSRK
LATGRLIVST NFEVFRENLR GDKVHAHQIT EECISRDERN FVYSCSCVTH EDGSALESRI
ILPTKNHLVI GNSGDPKYID LPIDTELTLY IAKEGYCYIN IFLAMLVNVR ESQAKTFTKM
VRDVLVEKLG KWPTMMDVAT ACSFLTVFYP DTITAELPRI LVDHNCKSLH VIDSYGSLDT
GFHILKANTV NQILHFASID LTSELKHYRV GGRTADFQYV NVAPKLDMTT RTLYMLITSI
YKPSRFSQII EQEPFTLVLS VLSPAIMRAM LNNESFERSI SFWIHRDRSI TQIMALLQTL
AKRIPVSNNL QDQMQFLENN VETLHRLLEK TNHTMHSKVL ASNVISALYN KSLTDKSLLE
EGFMNTIDLS REIYEKNYQE HLQEQWREQP LSQKLSSIIA TAKLYLRSVG QTKFAAPDLK
GKAHVYTTRS LGVIAKTGNA VKESAQKCCN TWYYSVVRHV FFYSLHSVRR LCPDLLTYCS
VVGVFYYMVS LFMKVKSYLD VHRSLKELKA VNEYNKKVKH LDYLYGKLCV KLNGPPSESE
FLEYISRKQP SLEQVAALET NLCVPSMEFQ AKGDFQHLEK MIALLVLLTM LFDANRSDAV
YKILNKFKGV MSSIDKEPML HQSLDDIQDI IEEKNLTVDF NLTDADPTVN RIPGATFSQW
WKNQIERNRM LPHYRSGGHF LEFTRANAGS LASIIAHEEH KEILIRGAVG SGKSTSLPFH
LHTKGSILLL EPTRPLAENV YKQLKGAPFF TNPTFKMRGL TQFGSSPITV MTSGFAFQFY
ANNINQLKDF DFIMFDECHC FDAQAMAFFC LLKEHEFEGK ILKVSATPPG REVEFTTQFP
VDVRIEGHLS HQQFVNNLGT GANSDILPCG DNILIYVASY NEVDQLSKLL MDRKFKVSKV
DGRTMKSGKI EIITEGTSTN KHFIVATNII ENGVTLDVDV VVDFATKVVP ELDEEAHMIR
YNKKSISYGE RIQRMGRVGR HKRGTVLKIG ETEKASWRVP PCIATEAAFY CFAYGLPVIS
DGVSTSILEN CTVPQARTMM QFELSIFFMF HFVKHDGSMH PAIHDRLKQY KLRDSEIVLN
KTAIPHRGLT AWPTVEEMKR HGCSINQPDE VRLPFFIKDV PDKLYGDLHE VLKKHSGDAC
FGKIRGMSAC KIAYTLQTDP ASIQRTIKIL DKLYESELQK KAYFANVTSS SCSSFNYALT
TITNAIRARH MQDYTTENLS VIQNAKSQLL EFNNIRTPKM TEDALADYGA LECMMYQSEN
EMSDFLKLKG RWNKSVIIKD IVLASVTAVG GVLMMYEYVK GKLEEPMDYQ GKNYRQRQKL
RFREAHDSKH AYEIHGDDAQ LQTYFGSAYT KKGKKSGNTV GAGKKMHRFY NVYGFEPTDY
SFARYVDPLT GATLDESTVT DLSLVQDHFG TIRNQMRQSG DLEPEQISRN TTVECYYVND
LAKKVLKIDL TPHNPLRVSG KSNNVMGFPE RTLDLRQTGA PVTVSYNQLP PSKRDVGTFE
FEGKSLLSGL RDYNPVAACV CKITNESDGV ITHIFGLGYG PYVITNQHLF RRNNGILRIH
THAGEYLVNN ACTLKMHPIP ERDIIIIRLP KDFTPFPQRL RFRPTRVGEH VCLVSSNFQT
KSISSVVSET SATAGTANKN FFKHWITTKH GQCGNPLVSV TDGCVVGIHS MASTVSSMNM
YVGFPENFVD DYLSNDLLEW TKGWKLSADR SCWDGITLVD SKAEGLFKLT KEMFTLDDGQ
WEFQSGHKDW MYNKLEGNLK AVGRTSGNLV TKHSVKGKCM LFQTYLSVEP EEAEYFTPLM
GAYSKSALNK EAYIKDLSKY SGEISVGNVD CDVFEQAFEK VVTLMRSKGF HECAYITNEH
EILAALNMKA AVGALYSGKK REYFADFSDE DKYEIVKESC KRLFLGKMGV WNGSLKAELR
PIEKVMANKT RSFTAAPLDT LLGGKVCVDD FNNQFYSRHF DLPWTVGMSK FRKGWDTLLR
KLPESWVYCD ADGSQFDSSL SPYLINAVLK LRLRFMEDWD VGETMLRNLY TEIVYTPIAT
PDGTIVKKFK GNNSGQPSTV VDNSLMVVFS MYYAMEMSNI EDIHNKCVFF VNGDDLIIAV
EPGSEVFLDS LQTLFHQLGL NYNFDNRTRD KEKLCFMSHV GLLQDGIYIP KLDKERIVSI
LEWDRAQQPE HRLEAICAAM IEAWGYPDLL NRIRKFYCWI LEQAPYSELS TVGKAPFISE
AALRNLYTDC KATESELARY LELYDSEAPT EDIFEYQAGE ELDAGTQSSK GQKNNADKSI
EQRNPVISHS SAHGRNDGGS SDLSMGKDKD VNVGTTGTFS VPRIKQIPQK GIAIPMDGGK
SILNLDHLLQ YKPSQLCITN TRATRTQFMT WKARLQDEYG VTESEMSIIL NGLMVWCIEN
GTSPNINGVW TMMDGDEQVE FPLRPVVEHA QPTLRQIMAH FSALAEAYIE MRNAEQAYMP
RYGLQRNLTD MGLARYAFDF YEVTSRTPVR AREAHAQMKA AALRNSRPKL FGLDGNVTTT
DEDTERHTAH DVNARMHHLD GAHMQ
//
