ID E7CQR7_9POTV Unreviewed; 3184 AA.
AC E7CQR7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Apium virus Y.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=168135 {ECO:0000313|EMBL:ADT71770.1, ECO:0000313|Proteomes:UP000201179};
RN [1] {ECO:0000313|EMBL:ADT71770.1, ECO:0000313|Proteomes:UP000201179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ce {ECO:0000313|EMBL:ADT71770.1};
RX PubMed=20833213; DOI=10.1016/j.virusres.2010.09.002;
RA Xu D., Liu H.Y., Koike S.T., Li F., Li R.;
RT "Biological characterization and complete genomic sequence of Apium virus Y
RT infecting celery.";
RL Virus Res. 155:76-82(2011).
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; HM363516; ADT71770.1; -; Genomic_RNA.
DR RefSeq; YP_004123951.1; NC_014905.1.
DR GeneID; 10100606; -.
DR KEGG; vg:10100606; -.
DR Proteomes; UP000201179; Genome.
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:0016020; C:membrane; IEA:UniProtKB-KW.
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 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}; Membrane {ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 1114..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..409
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 744..867
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1343..1495
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1515..1674
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2152..2370
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2636..2760
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2919..2954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 752
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 826
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3184 AA; 362348 MW; 1B97D520BD43B4B8 CRC64;
MEALLMINNS LTLRRYNECN GTQFNMNHVR RALAAKKRNL RYDAEDDVYH CLDCDETFDT
VEQFRMEHDC EGSVERAEAE FAEIQAYIRN MVKKSKEVNE DKPKQVMPKI QFGTVGILET
SDNSPVKADE EKPKQVLSTI KFGTIGVVDT SVNPLVEIPT TKGNVWGNLE KSLESKFARR
TDKVIVKRRD GCWVYGNTVR KTPPTKKVEA KPHFEFKLAQ YDVTTISIGV GLKPSAMEST
DQHKVKCATS VRTKKRVKTP TCKLNSSQLD MLFRQLSVIM KKRNLQFEVV GSGRTKRATC
GFKKVGNCKT VYVKTLHESG IRRRIDLKLN EFQRMCLKKI YKSSIRMVPL NASRIKKGDS
GALILQEHMV GKFGRAIDEM FIVRGRYDGE VLNSLSKQTF TNAFKMIHYS TSDKFFKPFS
EAFVANIPQK LDHICESNFN IEDCGTVAAL ITQTIFRFGK ITCKHCAANY ANLSDAEMKE
WIREELDDTL ENVEKKFSDF KHVIRFLKDL RRLLYLVNTN VTTFSDTQQL IGSYENEPFT
SLKILNETLI KGNLMTPEEL NHATTLVNKL ARFQKNRTDN IRSGDLTHFR NKMSGKTTMN
FSLMCDNQLD KNGNFLWGQR GYHAKRFFSN YFEIINPVEG YDKYQMRKHP YGERTLAIKN
LIVSTNLEVL REQLKGEFRQ QPGLTDQCVS RVNGDFAYVC SCVTTESGKP IESQFLKPTK
NHLVIGNTGD SKFVDLPSEV SEKMYIAKEG YCYVNIFLAM LVNVNEESAK DFTKMVRDMV
IENRLGKWPT LMDVATACHL LTVFHPETSN AELPRILVDH NTKTMHVIDS YGSKTTGYHV
LKANTVSQLI KFADLSLKSE MKFYAVGGTA VHDIATQGVS FSMLIKALYR PKMMELILRD
EPYMLVLSVL SPSILMALFN SGSLEHATHM WIRKDQNIAQ IATMLSALAG KVTLARTINE
QLSIINRHGS SMLENVFRGT RPNVSYIQAI NVLTMIESRG SANEVLEMHG FQIFPVDLYE
TMEKIYQKEL DTSWSDLSLC GKLRAMRYSR QWRKYSLKTS NLQETRDTKG KYSISLESLR
GGTQKFVSTK SAAICQRWNL ITSTLKQKVF SKSLSLFVGL LPKIFNVVNT LIVMNLLLSI
ITQSRRMIYE HRESKQKLAN SDFDKRVDIL EEIYDTYIAV NKVQPTCEEF VEYVQKVNPD
IVEFAKQVLL NEEESVKHEA KRVSEARLEQ AMAFVALILM AIDSERSDCV HKVLNKLKSL
MSIADADVYH QSIDEIKSEI DEKKLTIDFA LDDTFTPSIR EHDATFADWW TNQINNTNVL
THYRTEGKFY EFTRQNASEV AYKISSDTSS DFLLRGAVGS GKSTGLPYEL SQRGNVLLIE
PTRPLAENVH RQLQGPPFMT NSTLRMRGLS SFGSARVTIM TSGFALHYFA NNTDQIADYD
FVLFDECHVL DSCAMAYRCL LHDNRFKGKI IKVSATPPGR ECEFKTQFPV EIRVEETLSF
QSFAQGQGTG CNYDVTGDGY NNILVYVASY NEVDSLSKLL LDKGYLVTKI DGRTMKLGNV
EIVTNGSEKK KHFLVATNII ENGVTLDIDV VVDFGTKVTP LLDVDTRMVT YNKGSISYGE
RIQRLGRVGR NKRGLALRIS QTQKGLVEVP PIIATEAAFL CFAYGLPVMT HNVSTSLLNQ
CTVKQARVML NFELSPFYMV NLVRYDGCMH PGIHNVLKKF KLRDSEITLN SVALPTRSLD
TWMSVKSYNK CGARLSMDDS VKIPFLLKDI PEKTHEQIWS VMIEHKKDNC FQRISSASAC
KIAYTLQTDI HAIPRTIAII DNLIEQERTK ESHYSSMKAN SATIGSVNIV GIVNSIRSRF
SQNYAQENIE KLQRAKSQLL EYANLDIDTS FPELVRNFQS LECVTHQSTH GISKVLQLQG
RWNKSVITKD LIVVGGILLG GSYMIYTWFR ESFAMEVYHQ GYNKRARQKL KFRNTRDARM
AREVFGDDEV IADYFGESYT KKGKQSGRTK GMGSKNRKFV NMYSYDADDF SFVRYVDPLT
GYTFDESPMT DMRLVAEKVM EGRQYELSNG DLDWQLVTAK PGIKAFYQKG GAKEAVMIDL
EPHNPLEVCN TGTIAGYPER ADEFRQTGKP TVVKVSEIPQ ANELREETTH EGLSMYKGLR
DYNSIASCIC KLTNESDGFS ESLYGIGFGC VIITNQHLFE RNNGKLKIQT HHGEFTVPNT
TMLQMSPCGN RDIVIIKLPK DLPPFPQKLK FRAPKTNERI CMVGTNFQEQ STRSTVSETS
VTYPKEGSTF WKHWISTKDG YCGLPLVATE DGKIVGIHSL SNVSNTQNYF TDFPENFGKD
TLESLNDLTW TKHWRYNSNN IGYGSLMLHK SQPDGIFKPI KLIQDLSDES VYSQSLNNTW
LFDKLNGNLK AIGKSNAQLV TKHVVKGKCL LFESYLNTHP EACEKFRPLM GAYNKSKLNK
DAYVKDLFKY TSPIEVGVLD VDTFEKSLEI VIHNMESAGF EQCEYVTDAQ AIFRALNMKA
AVGALYQGKK RDYFKEYTDE MKDEIVEQSC RRLYEGKMGV WNGSLKAELR PIEKVQENKT
RSFTAAPIDT LLAGKVCVDD FNNQFYAMHF KCPWSVGMTK FYGGWDKLLS ILPDGWTYYD
ADGSQFDSSL SPYLINAVLQ IRLHFMEAFD IGEQMLSNLY TEIVYTPILT PDGTIVKKFK
GNNSGQPSTV VDNTLMVVLA MTYSLSKLGY VGEDQANVCR YLVNGDDLLI ALHPEHEHIA
EKLSELFRQL GLKYTFESKT KDKSELWFMS HRGIQIDGLY IPKLEEERIV SILEWDRSSE
PEHRLEAICA AMVESWGYEW LTHEIRKFYN WVLDQEPYNE IARQGKAPYI AEMALKKLYT
SKDVSDSELM HFVSEFLKME NLYDEDLCVY HQGDNVLDAG NGKQDKDKKS IVPSGSGTEK
GQIQPAPDKD INTGTSGIYT VPKLKAISNK MRVPKYKNKN SMNLDFLLTY LPDQIDISNR
RATHSQYDAW FEGVKKDYDV SDAEMEILLS GLMVWCLENG TSPDLSGTWT MMDGEEQKEY
PIKPLIEHAK PTFRQIMHHF SDVAVAYIEM RNTKGPYMPG YGLKRNLRDR SLACYAFDFY
EMTSKSPERA KEAHLQMKAA SLKNSRTKVF GLDGSVSSKE ENTERHTVED VNRDMHTLLG
MKGI
//
