ID E6Y7B5_9POTY Unreviewed; 2404 AA.
AC E6Y7B5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:ACP28863.1};
OS Wheat yellow mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=75746 {ECO:0000313|EMBL:ACP28863.1};
RN [1] {ECO:0000313|EMBL:ACP28863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Zhumadian {ECO:0000313|EMBL:ACP28863.1};
RA Xu J., Zhang Z., Han C., Li D., Yu J.;
RT "Sequence analysis of Wheat yellow mosaic virus isolated from Zhumadian.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC {ECO:0000256|ARBA:ARBA00029399}.
CC -!- FUNCTION: Indispensable for virus replication.
CC {ECO:0000256|ARBA:ARBA00034080}.
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}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; FJ361766; ACP28863.1; -; 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: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:0008234; F:cysteine-type peptidase 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:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
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; 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; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW 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 RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 264..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 473..615
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1360..1575
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 1854..1978
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2404 AA; 269191 MW; 5BD4A6C39310D7D6 CRC64;
MEQTAAQAAA RHATHTNSAQ EQPPVSPMNL SANFVAPELF YASNVEKIKS IMRMRSTTRI
IDAISRDFEL VAFLILSPAH LMQLETTLRC EMKSSIVPIA NSDAGFETCA VLKTALDGMK
YHFGTTTLEQ GWTSMMKHAD SCLQESSSSA VAMLQTQVQK VGSLLISGKN RVESCELYVL
HLTARAFRTE YGLKGTCFGE HCALLHDLKA CVCGTVPKEF LWAKTKKRSM FTIPEWIART
PTDCFMLCLR AIPIFHRCTM AMSLLYWSCV ATVNFPSIMA FLFKRQFTKY IAHSFAKHSI
YFLMLGIVAL LWAFRTYASK NPKIALQARS ANEKEKKLMM LLASAVGITY LFDYDIAEAL
GNSLHKISRL SSYLMDDHQG IASRMFSASY GLQAGDNTED AVTTIISDLL SVTFQIVDED
ATAGVLEEVS DTTFSSWVSV NTLAGRNMSR PLQYPVNQTY PLTPMNVLLQ AQAMVDSDNC
WSMVVGHTGS GKSTYLPVQY SNYLAKKTDR RQQILVCEPT QAATENVCSG IAANLGRAVY
GRHEGWSRMG DHCIQVMTYG SALQCHAMDP GFISTFDAIF LDEAHDVKEH SLVFESICNN
FKSVRKFYVS ATPRDGSSCP DATRKFPLTV QQSVCDSYKK FIAAQGGDDL LDVTRYDTVL
VFLAGRPECV KAANAWNANI TGEKRAFSLS SDNFATDFAM LTERLKTHKT IIFTTNIIET
GVTLSVDCVV DFGYTMRPSL DLNHKTLRLE RRRVTANERK QRIGRAGRLK EGHAIVCGDE
DRSVNVVSPD VLYGAALLSF KHNVPFYMND TFESSWLEGV TKSQADTMTI FKLPIFLTRD
LVNSDGSVAK EFLNILKKHQ FTTSDIKQAP HSIARHLFPT WASYFALFQS INYGEEKDEI
PSNLRHARVP FSISTLSKFD WNALALACEQ HRPTVTSSFQ SLDQPARVVT LQTNSANILG
SIAHLCNMRN NYKALIDSNN HVKQSMATNV MFKWFSSSRI TADLDRNLSR CLANLSVVET
TISSLKQISA GNSQVMASPT LQSHLENIIE LQSNDMLTDE TLSNALGIFN PKTNLFLLLA
TKGFKLVYVI CLLILINLIY RLLSHWRAWL KNKNDTVNPD ALTNTMTVQE GSEILKEVLK
MTPAMRREVT KDMKVAVADN DSTFSFVFPY EHIDLEGKGN KYRPREDARL MYSTRDDATF
DTWNEKAKEK RKKISDRAEP EMKQPYQKRP YYNFYDLQTD SNILEAIFYT TEGDEFFRTA
NPNKDMHSVA EKLKAFLDTK PIIGRHQRQL LEETAQVVIK DDKGTAHRMD ISTHNPNTLK
NNGSGRVGYD EHRGDFRQDS PALESPYELE AEFGNSKDEV MLEASTGILL SQVSVDVATR
IGRISIGTFN VNCFLYSDWI LAPAHFQDRN GAVTIEFPDQ TVSTTTDNLN AHGVKRFYGL
DLIAIRRPPS LRPEKKLVKA FAITEPVIAQ MVFIDSQGIR KFSQSDWIRR EAGSNRWSHK
ISTQNGMCGC PVLDVGKNRL IGIHVATNRT TGRNEFQPFS REAVDFINGP GNKVPFSPWT
FNRPACGYRQ GEATFDSRTI QNQASDTLSK INNSILGFGS DLKGQLVQPV TPALRTRFEA
LFGGGSFELV GTMNKGLIDK HIIVGENDNV HDFMREHPTF AWLQGFMDEY APSVLNYSAY
YKDLCKYNRK KHQLSFNPHE LRSATAGMIR MLEDAGLTQG DVRTPQQVVS DMQWNTSAGP
SYQGKKRDVC AHLSEQEVLR LAETSRQQFL ACNSIGIWNG SLKAELRAIE KVEAEKTRVF
TASPITSLFA MKFYVDDFNK KFYATNLKAP HTVGINKFSR GWEMLHDKLN RPGWLHGSGD
GSRFDSSIDP FFFDIIKEIR KHFLPVEHHR AIDLIYDEIL NTNICLANGM VIRKNVGNNS
GQPSTVVDNT LVLMVSFLYA YIHKTGDHML KKLNDRFVFV CNGDDNKFAI SPEFDAEFGH
DFSPELTELG LTYEFDDITD DICANPYMSL TMVRTPFGIG FSLPVERIVA IMQWAKKGGV
LHSYLAGISA IYESFNTPKL FKSVYAYLLW LTEEHGSDIL AAMTGTATAL PIPSMLDVYR
LHYGDSSIEL QAADTQTDAQ KEEARLAAAT KKAADDADAA RLRKVEADRV EAARVKKASD
DKKARDLTAT KVDDGKIVAD AGTKRTNAAT KEKWSLPETK PVNAGLKLRI SMDKLKSAPK
SIVEHDNSIA LDSEVKKWSD AVRTSLGITT DEAWINALIP FLGWCANSGA SDKHAENQTM
QVDNGTGALT EMSLSPFIVH ARLNGGLRRI LRAYSDETVL LLQEHKIVTK WAMKHGAFAH
AAYAFDFFVP RPWMNPQDME VAKQARLAAL GTGTYNTMLT SDTTNLRKTT NRRVLDTDGH
PELT
//
