ID B2REG2_9POTV Unreviewed; 3340 AA.
AC B2REG2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Shallot yellow stripe virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=62059 {ECO:0000313|EMBL:CAK26091.1};
RN [1] {ECO:0000313|EMBL:CAK26091.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Onion {ECO:0000313|EMBL:CAK26091.1};
RA Adams M.J.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAK26091.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Onion {ECO:0000313|EMBL:CAK26091.1};
RA Lin L., Luo Z.;
RT "Characterisation of the onion isolate of Shallot yellow stripe virus.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An RNA-dependent RNA polymerase that plays an essential role
CC in the virus replication. {ECO:0000256|ARBA:ARBA00029404}.
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 -!- FUNCTION: Mediates the cap-independent, EIF4E-dependent translation of
CC viral genomic RNAs (By similarity). Binds to the cap-binding site of
CC host EIF4E and thus interferes with the host EIF4E-dependent mRNA
CC export and translation (By similarity). VPg-RNA directly binds EIF4E
CC and is a template for transcription (By similarity). Also forms
CC trimeric complexes with EIF4E-EIF4G, which are templates for
CC translation. {ECO:0000256|ARBA:ARBA00037225}.
CC -!- FUNCTION: Required for aphid transmission and also has proteolytic
CC activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus.
CC Interacts with virions and aphid stylets. Acts as a suppressor of RNA-
CC mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. May have RNA-binding activity.
CC {ECO:0000256|ARBA:ARBA00029420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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; AM267479; CAK26091.1; -; 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: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; PTHR18934:SF237; ATP-DEPENDENT DNA_RNA HELICASE DHX36; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 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 Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
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 1288..1309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 265..408
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 745..867
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1501..1653
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1659..1833
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2323..2541
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2806..2930
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 948..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
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 3340 AA; 379690 MW; A4C86223802A0B6A CRC64;
MLKQKNHTCY DSFEDAHISV KVSDTQIKDL STMGRYRNVG SNAQKDTRKA ISPTKKVVFK
QFDDVEPIAT GWDINNDLQK EQMTEDATHT VVGNLPKATP KQNNVDGETD DIIKQIVFGQ
FGNNDTKTTE HIVTANHKFG HNLDGTQHIT FGTLPSVEVL TTPNISYKTS DQCKETEVIG
NSVTSVEGAV ELNNTLPFES CKKVARRPIA LKPLTILCTE ILSGQHVSPC EVEDNIKVEL
EVNNNLNKQV MKTTRKQPQI RYQVQAKDMQ SDEIINNIIK VAYERKLKIE VTERNKHTFT
PYKVQDHYFY KIGTEHEKGR LSRKDVKCTQ MVMKVMKQLL DMTPSVEIDS TQIQKGSSGL
IIRPNQIINC KKMNARSDVM VIRGRKNGSL VDSLLTLKHD DLKDVDHYSD SEIALKLFGG
FNKTFIAIRD KPQHVCERDI ELELCGEMCG TITQMLAPMF KITCSQCATL LASRSKEQQY
MDMSRQKVFE QYERLIATGK FPHITRAIEN LNPISEVSER SLSLYTQIDS LSMNGQTSQS
RQINEIAKVI GKGPLVCTDE TEAALKQLLE LTNWYRKRLE AQMSGGLESF RNKISSKTHI
NLALMCDNQL DVNGMFQWGE RGYHAKRLFA NYFTKVTDGS QYEALAIRKH IRGNRELAIK
NLIVSKDIAK MQQSFVGNPI VAYPLGKACI SKLNNNYVYP CCCVTMDDGK PLCSELRFPT
KNHLIIGNSG DDKNVQLPPS SDGHMYIVKD GFCYVLIFLA MLINVSEGDA KGFTKKVRDD
IIPQLKQWPT MRDLAVMCRY LCAFYPAVIT AEIPKILVDH EHKTFHVMDS FGSKTTGYHI
LKANAVQQLC RFGDVDLESE MNMYNVGGRQ APIHVTRTYG DQKFEMRSNI ELSEDFEGCD
SYNYELWDFK HDIARGTQVS EAGCCSETII SDHSECWYNI NDELSNGSLH TDEISSDETD
SENPESDDNP IEDSVKARSR PASLHTIDSE SDDLSGSAYE SDEGSIQHSE SSASPSEKVV
ADLNARLARA KMNIDRSPES KDITFFRSLV KAVFSKRHFE KILREDPYIL LFSMLTPTVI
TRMLHDDLYV KASQLLIMHD DDLARIASTL QIMAERVSRH KVFVVQMRII SEAARDILGL
SEGFHNTDSS QTARHLLEML NEQDLADFDL LAQGYVASTQ KLYEMKKKCF DTIYHDYLRG
LSLCQRLGCE WRSLKYNYRM RNLDQSEERL TCTTIAKDCL VQCSSATQSY VRQHAANLYL
GATNIVRSVA RRGCYVAVRA ISSLYRDILV YINIFAVISI LLAMWNTVVG IRTNYKRLQL
EELKIQHSKQ NNQVEKLYAQ YIKEHKDKPT KEEFQEYISD HSDPLLEFFI RNYIGVEYQA
KSQSEVTLEK IVAYVALFAM LFNSEKSDGV FKILSKLKTI FSTTDVHYQA LDSPDDVEEF
LNTTVDFEVI VPNEPDINSF DMTFEEYWKK QLATNRFCAN YKTNGVLYEF TRKTAEDVAS
KIQQETHTEF LVSGAVGSGK STGLPFYLSQ KGKVLIVEPT RPLTENLFNS LSAEPFNQSV
SMCMRGNTVY GSGNITIMTT GYALHYLANN REQIKSYDYV LVDECHVMDA NAIAFYALLK
DTNFKGKIIK ASATIPGHEN RFEFKTQFET SINFEGQMTF ERFVKEQGSC SNACVVSRGN
NILVYVASYS EVDTLSKLLL EKGYKVTKVD GRTMKVGGTQ IETTGTAEKK HFIVATNIIE
NGVTLDIEVV VDFGRKVVAV LDDESRMMRY TKQEVSHGER IQRLGRVGRN KPGHILRIGS
TQKGIVETPI CVATEAAYLC FVYGLPIMPN NVSVSSISKC TTRQARTMAA FELSPFYMKD
LVRFDGSMHP EIHKILKKYI LRDTEIKITE MACPTGVTRT WNSVGEYNKM GGHILCDENI
RLPFFVNGIP EKVHEEIWNV VKQHQSKFKL TPLKTASVNK IAYTLSTDKD SLVRTVGMIE
EMIKEERYKH AQFQAIKNTP VGVGNFNLNY FSNLLKTRYM IDHSEQNIEI LQRTRSQLLE
VHAMYNSEMS TTVLRSYPLV SAVEYQTKEQ LSKGLGLQGK YEMSKISKDV IVCGLTLAGG
LFMIYKSFCD GVESKVHYQA KSRRRLRFRD AADRKQRYAL EGDDGTIEQY FGSAYTKKGR
QKGTVRGMGI KNHRFYNMYG FDPTEYSIVR FVDPLTGNTY DDAATATTYN GVSALLQMRR
DMVNDDAIEM QALHLNRAKV LEAYYIKAGA DKAVKADLER DRVLKVTLTP HDPLMVCHNF
ETIAGYPDKE GEFRRTGPIE TVTKDEVPKA QSYEPVYEVA YEAKSLCSGP RNYTAIAGII
CRLKLDSDGH TREIYGIGYG PYVITNQHLF TRNNGTLKIK SQHGNFLIKN TAQLQLYPID
KMDLVIIKLP KDHPPFSQKA NFRTPKEHEK VSMICVEFLP SSNTPSVSEP SFTFPERNSH
FWKHWISTKE GHCGLPFVSL QDGNIVGIHS LSDNGNAVNY FTGFPENFKE EYLDRAGDVE
WVKGWIHNTD NIAWGSLNLA KGAPESCFKA TKLISDIING VAFQAQDYTW LTKRLDGNLK
CVGACPGNLI TKHVVKGKCP MFQLYLNTDE RVKAFFEPLL GFYGKSCLNK EAYIKDFTKY
SSDIVVGEID TDVFEEAINN VENILLRGGM TKCNFVTDPD DIMNSLNMKA AVGALYGGKK
GAYFKDMSDK DVEHLIFMSC KRLYLGKMGI WNGSLKAEIR PIEKVQANKT RSFTAAPIET
LLGGKVCVDD FNNNFYRRNL AIPSTVGITK FYKGWNDLMC LLPDGWVYCD ADGSRFDSSL
TPYLMNAVLN IRLRFMEEWD IGQEMLKNLY TEIIYTPIAT PDGSIIKKFK GNNSGQPSTV
VDNTLMVMLS VQYTLLKNDI KFMEQDSIIR YFCNGDDLLI AIHPDHIRIL DSFAKHFADL
GLEYDFSSRT TNREELYFMS HRGLMRDGVY IPKLDKERIV SILEWDRAKE PEHRLEAICA
AMVEAWGYDE LLHEIRLFYK WVLEQAPYNL IAQTGKAPYI AETALKRLYM DEQATESELE
QYIRLYQILD DRIPTPSYVS YQVSETEDAA NVNTDKQVGK NKDKDKDVDV GTSGEFSVPK
VKMLSDKMRL PRVGKKVILN GKHLLSYKPD QVDLYNTRAT HAQFKTWYDA VKLEYELTDE
QMKIVMNGLM VWCIENGTSQ NLTGVWTMMD GENQMEYPLS PIIDNAKPTF RQIMAHFSDA
AEAYIEYRNA TEKYMPRYGL QRNLREYSLA RYAFDFYEMN SKTPIRAKEA HMQMKAAAVR
GVTNRMFGLD GNISTDDENT ERHTAADVNK DHHTLLGLRM
//
