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Database: UniProt
Entry: Q70WS7_BAYMV
LinkDB: Q70WS7_BAYMV
Original site: Q70WS7_BAYMV 
ID   Q70WS7_BAYMV            Unreviewed;      2412 AA.
AC   Q70WS7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   SubName: Full=Polyprotein 1 {ECO:0000313|EMBL:CAD56471.1};
GN   Name=1 {ECO:0000313|EMBL:CAD56471.1};
OS   Barley yellow mosaic virus (BaYMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Bymovirus.
OX   NCBI_TaxID=12465 {ECO:0000313|EMBL:CAD56471.1};
OH   NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN   [1] {ECO:0000313|EMBL:CAD56471.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1 {ECO:0000313|EMBL:CAD56471.1};
RA   Adams M.J.;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD56471.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1 {ECO:0000313|EMBL:CAD56471.1};
RX   PubMed=13679620; DOI=10.1099/vir.0.19347-0;
RA   Kuehne T., Shi N., Proeseler G., Adams M., Kanyuka K.;
RT   "The ability of a bymovirus to overcome the rym4-mediated resistance in
RT   barley correlates with a codon change in the VPg coding region on RNA1.";
RL   J. Gen. Virol. 84:2853-2859(2003).
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; AJ515479; CAD56471.1; -; mRNA.
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: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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR   Pfam; PF00270; DEAD; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561,
KW   ECO:0000313|EMBL:CAD56471.1};
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        259..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          474..632
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1359..1574
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000259|PROSITE:PS51436"
FT   DOMAIN          1858..1982
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2177..2202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2412 AA;  270802 MW;  606827FE729B375B CRC64;
     MEQTLAQAVS RKGKTNTPMA EERKHFSPMN FSANFVAPEL FYSANVRKIK NIFRERSTTR
     FLDAISSDFE LVAFLTLSPA HLMQLETTLR QEIRSSVVPI VTSDASFETV AVIKTALDGM
     RFHFGHTTLE KGWMSMMRHA ESCLQESSSS AVNDLQMQIK RVGSLLLSGK NRVESCELSV
     LNLTARRFRI EYGLNGTYFG EHVAMLLDLK RYIYGTVPKE FLWAKTKKHS LFTTPEWIKR
     TPIDCFLFCL RVIPILHRFG VAISLLYWSC VAALNFPAFM AFLFKRQFAK YLAHSCAKHS
     IYFIFLSIIA ILWSFRTFAS QKPKIVLQAR STAEKEKKLM MILASVVGIT YLFDYDIAEA
     LGNCLHKISR LSSYLLDDHQ GIASRMFGAS YGLQAGDSAE DAITTIISDL LSVTFKIVDE
     DASQGTVEDA SETTFHSWVG VNTLAGRNMS RPLQYDVNKT YALTPQNVQL QARAMADANN
     CWSMVVGHTG SGKSTYLPVQ YSNYLSTKSD RRQQILICEP TQAATENVCA GVAANLGRAV
     YGRHEGWSRM GDHCIQVMTY GSALQCHAMD PSFISTFDAI FLDEAHDIKE HSLVFESICD
     TFKSVRKFYV SATPRDGSVC PEAARKYPLH VETSVCDSYR KFIAAQGGGD LLDISKHDTA
     LVFLAGRPEC IKAANAWNAS VTGEKRAFPL SSDNFATDFS MLTERLKTHK TIIFTTNIIE
     TGVTLSVDCV VDFGHTMRPC LDLNQKSLRL DRRRVTRNER QQRIGRAGRL KDGYAIVCGD
     VDRAVNIISP DVLYGAALLS FKHNVPFYMN ETFESSWLEG VTKAQADTMT IFKLPIFLTR
     DLINADGSVA REFLDVLKRH QFTTSDIKQA PSVTAKHIFP TWASYFSLHQ ALHYGDDKDE
     IPHELRYARV PFSVTTLSKF DWPALALACE KHRASMSNVF AGIEEPARVV TLQTNPANIQ
     ASITHLTHMS KNYKTLIENN QHVRQSMMTN VMFKWFSSTR ITKDLDRNLR RCTDNLSVVE
     ATLSSLRQIL AGNTQVHATP HMQSTLEDII ELQASDTLTE ESLANALGIF VPKCNLFLLL
     ATKGFKLVYV VCILLLVNLV YTGLRKWREH LKQKGSNEIL TNTMPVSEGG EILAEVMKME
     PKMRKNIKRD MDAAVESKLC GFTFVFPDDD KIGLEGKGNK YRPREDARLM YSTREDATFD
     AWNEKAKERR KKVTDKAEPE LRRAYEKRPY FNFYDLQTDS NILEAIFYTT EGDEFFRTAD
     PNKDMNLVAD KLRSFLDTKL VVGHHQRKLL EETAHVVVKD TKGTAHKMEI SEDDPDFLKE
     NGSGKVGYPE HRGQFRQEGV AITGDYDLEA EFGADADEIT LEASTGILLS QVGVDVATRV
     GRICIGTFNM NCYFYSDWIL VPGHLQDRSG NVTIQFPDQT VQTTTDALNA NGVKRFYGLD
     VIAIRRPAIL RPRTKLVKAF AIEEPVIAQM VFVDAQGVRK FTQSDWARKE ENSGRWSHKI
     STVLGMCGCP VLDVGKNRLI GIHVATNYTK KRNEFQPFTQ EVVDFINGPG TKIPYCPWVF
     DRPACGYSSP NALFEKPTTL ADVIHMQASD GLHNINNAIE GFGSSLKGQL VSPPTESTRQ
     RFDKLFGSGS FELIGQMNKG LIDKHVIVGE NDDVYDFMRE HPTFTWLKDF MNEYAPSVLS
     YSAYYKDLCK YNRAKHVLTY NPEELHCATK GLIKMLEDAG LTQGSVRTPQ QVVSDIQWNT
     SAGPSYQGKK RDLCAHLSDD EVLHLAEVCR QQFLEGKSTG VWNGSLKAEL RTIEKVEAEK
     TRVFTASPIT SLFAMKFYVD DFNKKFYATN LKAPHTVGIN KFGRGWEKLH DKLNRPGWLH
     GSGDGSRFDS SIDPFFFDVV KTIRKHFLPS EHHKAIDLIY DEILNTTICL ANGMVIRKNV
     GNNSGQPSTV VDNTLVLMTA FLYAYIHKTG DRELALLNER FILVCNGDDN KFAISPQFDE
     EFGHDFSPEL VELGLTYEFD DITSDICENP YMSLTMVKTP FGVGFSLPVE RIIAIMQWSK
     KGGVLHSYLA GISAIYESFD TPKLFKSIYA YLLWLTEEHE AEILAAMTQS STALPIPSML
     DVYRLHYGDD EIWLQAADPL TDAQKEAAHT AAADRARLDL ADADRRRKVE ADRVEAARVK
     KAADAVLKPV NLTATRMPTE DDGKLKTPSG ARIPSSAADG NWSVPATKQV NAGLTLKIPL
     NKLKSVPKSV MEHNNSVALE SELKAWTDAV RTSLGITTDE AWIDALIPFI GWCCNNGTSD
     KHAENQVMQI DSGKGAVTEM SLSPFIVHAR MNGGLRRIMR NYSDETVLLI TNNKLVAHWS
     MKHGASANAK YAFDFFVPRS WMNPQDIEVS KQARLAALGT GTYNTMLTSD TTNLRKTTNH
     RVLDSDGHPE LT
//
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