ID K0H8C1_9POTV Unreviewed; 3381 AA.
AC K0H8C1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Onion yellow dwarf virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=43130 {ECO:0000313|EMBL:AFU35736.1};
RN [1] {ECO:0000313|EMBL:AFU35736.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OYDV-Se {ECO:0000313|EMBL:AFU35736.1};
RX PubMed=23397330; DOI=10.1007/s00705-012-1597-z;
RA Celli M.G., Torrico A.K., Kiehr M., Conci V.C.;
RT "Striking differences in the biological and molecular properties of onion
RT and garlic isolates of onion yellow dwarf virus.";
RL Arch. Virol. 158:1377-1382(2013).
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=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; JX433019; AFU35736.1; -; 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; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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};
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 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 294..437
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 775..897
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1550..1702
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1718..1882
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2365..2583
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2848..2972
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 180..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 783
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 856
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3381 AA; 383712 MW; DEA2DD8E0D136247 CRC64;
MMKQYDRSGL NTKLTPKQRR RACYCDGDNL AHYHCTQCDN ICASLTMARP VNHNCDGEPF
ITYDDDPVPY TPTIPSKDFL SGFDINHPVN ENSTHSDEPS NNVKVDETHE SKFDVVEVTR
METYGLTGKE KTRASIKCGP RYKNRATETT LTKDVKAEVC GKQFVQFGSF EPVELKTHAL
NETPSKETHP TFQQDAERTN NGSVELPELT NDRQDEQDIN SKNSQTRAPR AKPKIEMTRN
NSKKMWVRKN KSEPNTSCSA DKVPPDEVIE TESKPNKVWY KRRDICKNKP LDDDKIIVTA
SELCNRLIHM AYEWNLPLVI IGKKKHEFRT TELNGKRYYK IVTKHEKGVL DCLDVNNNRE
TLSLIRLFLS KNPDDLVDEF DICKGHSGII INPYNIIGRE PLTYKTDVMV VRGRLHGRIV
DSLLPINARD IPDIEHYASD TTTASEIFKG FERTFMAIRD PVQHVCTRDI NLQECGEMCG
ILVQMMFPMW KVTCNQCANL IAERKPEQVL IDASRIKVAE MYEQMVSTGR FKHVQTVINS
LKTFEDTTQE SVKLFGEIDS ASLNKSTSQL SQINAIARIL VKGQAMTSND QEVALQNLKD
LMLWYRHKLE AQQAGDLSTF RNKVSAKTHI NLALMCDNQL DVNGMFQWGE RGYHAKRFFE
NYFTRIDNGD QYETFTTRKH IRGSRQLAIQ NLIVTTDIDR MTQSMQGTPV TDIPLGEHCV
SRCDKNFVYP CCCVTHDSGR VMCSEFKFPT KNHLVIGNSG DDKSVELPAR EDGHMYIVKD
GYCYILIFLA MMINVRESDA KAFTKRVRDF VITKLGKWPS MKELAVLCRY ISAFYPEVLT
AEIPKILIDH EHKTFHVMDS FGSKSTNYHI LKANTVQQLC RFGDINLNSE MKDYNVGGRK
RLVNLRVDSP YGYKYMTANI EDTEGYGSWR VVNGEIWDVN CSDSGVNYAS GANAHEYRGG
FTSDEDKLTE NSDFSSPIAI PEESNDESDQ HYVKPVRRTK TASLHTLSSD DEPHSVASHD
SELDEDQFSE VSTDLNADDE LYYSDDSSCD GDYTDVYNES TDLDVKESRS FDAALGRAAL
GLGERKDTCI SYFKLLIRAS FTRLNFKLMM IRDPYMLLFA LMTPTVMKRF LEDGSFTVAA
QIFLQQSDDL VYIATTLETL AEKLSAHKTY LAQFQEISST ARDILSRHTT FHQTKSSQQA
RSMLELLEST SMMNDELHSR GYVVNTMAMQ ETKKKCYDAI YLELWHELSL SEKCSYEWEK
LKCMRRTLNI AKLKDISAQG SNVKNCSRQC LTYISTATRA QVSGFCSITT QVKDKLISSI
SDFITACFSR VMRNIVKYIQ VTIFIAMLLE VWKTLSQIII EHKRLKMIEA ERISKLKFKK
IRALYDCLVA KLGHEPTKDE LIEYITAIDP TLKDELEMQD DVVEYQAKSK SETTLEQIVA
LCALVAMFFN TEKSDAVFKI LSKVKNVFAS TDIPVHYQAL DEPVDVNEFL GLTVNFDLAH
GQNLDINRFD TSFEDYWKKS LQNGHVCNHY RSHGLFLEFT RTTAESVCEV IKQSDQCEFL
ISGCVGSGKS TYLPSLLSTK GRILIVEPTR PLTENVYNGL SGDPFFQSVT MCMRGAHQYG
SGNISVMTTG YALHSLANNR DNISKYDYIM IDECHVLDAN AMALYCLLKD VNYKGKILKT
SATIPGRESG FKFLTQHDVT LNVEENMTFD AFVQAQGTGS NACVTTRGHN ILVYVSSYNE
VDTLSRKLVE NGHKVTKVDG RTMKLGGTRI ETNGSANKKH FIVATNIIEN GVTLDIDVVV
DFGMKVGTVL DIDTRSIRYV KQPISHGERI QRLGRVGRIK KGHALRIGTT EKGVPNIPTC
IATEAAFLCF IYGLPLITNN VVVSALGKCT SRQARTMASF ELSPFYMKDL VKYDGSMHKQ
IHSALKPFIL RDTEIQLKDS AIPLAATKDW LSAREYNQVG GHINCDDNVR IPFMINGIPE
KVHEQVWKAC VDNAHIVRLN PLSSANAQKV SYTLSSDSSS ILRTIGIIEE LIKEEKQKSM
QFQTLRNTPV GPNSFNLTYL TNMLKSKYMV DHSEENLETL YKARSQLIEF NTNYNPDMSA
DKIRDYPYTS MVNYQSTNDV AQALHLKGKY NMKNISTDII VSAIVLFGGA WMAYDMFKHS
MSSKVQYQAK NRRQIQKLRF RKSRDQKLNY AVAGDDTTIG NYFGTAYTKK GKTRGTVHGM
GKKMNRFYTM YGVDPTEYSI IRYVDPITGN TCDTSATEYT PTGIEVLNDM RMEMVNDDVI
DPQKFHKSSE SGYVAYYIKH GADKALKIDL TPHNPLMVCH HTAAIAGFPD KEGMLRRTGP
AQEIDIKDVP TPKSYSYNDH VTFEAKSACC GPRNYNAISS VICNLELQSD GHVRKTFGIG
YGPYIIANQH LFTHNNGTLK IKSQHGEFVI KNTCQLQLRP IDGIDVVIIR LPKDHPPFSS
KLRFREPEER EKVCLVSVEF NPSITAALVS ETSFTYHETG TNFWKHWITT KEGHCGLPIV
STKDGCVLGI HSLTNQEHAV NYFTTFPNNF HETFLSANNV LDWVKGWKHN TDNIAWGSLE
IRDAAPEPIF KTTKLISDLI NSVSFQSSEH TWLTKHLNNN LKVVGSCPGV LITKHIIKGR
CPMFQLYLTT NEAAKFYFQP LLGHYGKSML NKQAYVKDFT KYASIIETGV VDTDLFEASI
IDVVTILTRG GMSKCNYITE TMDIINSLNM KSAVGALYGG KKKEYFSDYQ EADFDKLLEA
SCKRLYLGKM GIWNGSLKAE IRSVEKIALN KTRSFTAAPI ETLLGGKVCV DDFNNKFYSC
NLSIPSTVGI TKFYRGWHNM LSALPENWVY CDADGSRFDS SLTPYLLNAV LAIRLEFMED
WDIGRQMLSN LYTEIIYTAI ATPDGSVVKK FKGNNSGQPS TVVDNTLMVM LSVQYALRKC
GIALNDQDEV IKYFCNGDDL LIAVHPDHEG ILDHFKQYFQ ELGLDYDFSN RSRSKEDVYF
MSHRGLLRDG VYIPKLDMER IVSILEWDRA DKPEHRMEAI CAAMIEAWGY PELLHEIRKF
YQWLLEQAPY NQIAQSGKAP YIAETALRKL FMNVDASEEE LLRYHEMYET LDNEIEVCKV
VRYQAGPGED AAAQSSTTKQ VAKQKDKDVD AGTTGKFSVP RIKALSDKMR FPKVGKNVVL
NAEHLLTYKP EQIELYNTRA TLRQFENWYM AIKKEYDVDD EQMKIILNGL MVWCIENGTS
PNLTGNWTMM DGEEQVEYPL APVLDNAKPT FRQIMAHFSD AAEAYIEYRN ATEKYMPRYG
LQRNLTELSL ARYAFDFYEM TSKTPTRAKE AHMQMKAAAV RGAANRLFGL DGNINTTEED
TERHTAADVN KHQHTLLGIK M
//
