ID G9FIF9_9POTV Unreviewed; 2561 AA.
AC G9FIF9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Lily virus A.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=1046301 {ECO:0000313|EMBL:AEN25474.2};
RN [1] {ECO:0000313|EMBL:AEN25474.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bate1 {ECO:0000313|EMBL:AEN25474.2};
RX PubMed=22075920; DOI=10.1007/s00705-011-1166-x;
RA Wylie S.J., Luo H., Li H., Jones M.G.;
RT "Multiple polyadenylated RNA viruses detected in pooled cultivated and wild
RT plant samples.";
RL Arch. Virol. 157:271-284(2012).
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; JN127335; AEN25474.2; -; 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; 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; 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; 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 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 144..266
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 745..883
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 883..1057
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1536..1754
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2020..2143
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2302..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2302..2321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 225
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEN25474.2"
SQ SEQUENCE 2561 AA; 290588 MW; 3387CDE5196892B6 CRC64;
LDLMCDNQLD KNGNFVWGLR GYHAKRFLAN YFEIVDTNHA YREHLVRKNP NGQRELATGK
FIVSTNFEVF RKNMEGHPVE SMPVTQSCIS QRGERFIYAC CCITNEDGTP MESTFKMPTK
NTLALGNTGD EKFVDLPPGT EERMYIAKEG YCYINIFFAM LINVREQQAK AFTKMVRDRL
VPELGTWPTM LDVATACHTL TVFFPDTLSA ELPRILVDHT TKTMHVIDSY GSVSTGYHQL
KANTVSQLIL FASDTLKSEM KHYVVGGRPE RLDVEFNALK LLMKGIYRPK LMRTLLEGRP
YLMCMAMCSP GILMALHNSG SLELAAKHWI VRKREVSQIF TMLTMLAMKV SLAKVLADQL
TLISESAGDF LKLMDCTFET HHSVNLVQTF LAHLEEKKNA DMVLLGSGFA NMCATTHELL
EKNYLAELDA SWGALSWSEK LSQMWHLRKS RASTTIVLTP VSGADLKGRY DVSVKALSTR
TFKSARKSVC NYIHSVKNRT YQFIGKQVCN SLTRTTRLFP ELAKYVNILM AISVILKTST
MINAYSSEFV RLKHNELVCA EDARWNKLLH IYDMLERTQG AKPTYDEFIE YLSKWEPALL
EEFREVLDVS PRAAETVEFQ AKPSGERNLE RIMAFVTLIM MVVDAERSDC VYKVLNKLKS
LIGTIHQEGV KFQSIDDIKD TLSEKNMTID FELSGDDPTI DKMHGSTFEQ WWSNQLERNN
VIPHYRTEGF FMEFTRQNAA SVATEIAHNA HHDILVRGAV GSGKSTGLPF YLGKKGRVLM
LEPTKPLAAN VHKQLAGEPF CMKSITVMTS GYAFHYFANN PHQLKDHEFV LFDECHVNDS
SAMAFRCLLA EHEYKGKVIK VSATPPGREV QFPVEIVPVE RLTFQQFVSI QGTGAVGDAT
SRGDNILVYV SSYSEVDLLS KGLIEKGHKV TKVDGRTMKV GSSEIETVGT AAKKHFIVAT
NIIENGVTLD VDVVVDFGLK VVAELDVDLR LTRYTKQSIS FGERIQRLGR VGRHKPGVAV
RIGHTEKGLQ SIPVSVATEA AFLSFAYGLP VMTHNVSTNI LTNCTVLQAR TMMLFELSPF
YTVHFVRYDG SIHPAVHQLL APYKLRDSEV VLNKVAIPNR GVNQWATAKE YAFQGFRMGI
DDDVRLPFHA NDIPERLHEC MWRAVQKHKG DAGFGRISTT SACKIAYTLQ TDVASIQRTI
CILDRLIENE LRKQEYYKNI TSSSCTSSSF SLLTITNAIR ARYMKDHTIE NISVLQAAKA
QILEFRNVEY NLENIERMTE YGALECVNFQ SLEDMSRHLR LKGHWNKSVL THDVMICGAV
LVGGFWMLGS HYASKCSEVV RFQAKNKRQR QRLRFREARD NKHAYEIHGE DADLQHYFGA
AYTAKGKKKG NTVGMGAKTR KFINMYNFDP TEYSFARYVD PLTGFTLDEN SITNVDLVQD
HFGKIRRKLM EDGELEKEAV ASKARLEVYF VKNLASQILR IDMTPHNPLR VCDRRETVAG
FPEREWELRQ SGAPVMMAPN LLPASNPYEE EVDFENRSTF HGLRDYNPIA TCVCRLENNS
DGYTSSIHGL GYGSYIITNQ HLFNRNNGTL TIESHHGVFH IPNTTQLKLF PIPGRDIILV
QLPKDFPPFA KRLKFREPTA TEKVCLVGTL FQDKTTTSTV SEASIITRKD GSHFYRHWIS
TKDGQCGLPA VSTKDGCVLG IHSLTSLVND SNFFISFPED FEKEYLNKAS ELEWVKHWKL
NVDKICWGSL SLESNKPSNL FKLSKDIQSL DTEIVGLQSR EDKWLFDKLQ GNLKAVARTR
NQLVTKHVVK GKCMLFETYL NTNPQARDYF QPMMGYYQKS RLNKEAYIKD LFKYASPIVV
GEVNCEHFEE AYEDVVSLFE RANFGTCNYI TDETEIFAAL NMKAAVGALY SGKKREYFAN
YTDKDKENIV RDSCQRLFLA QMGVWNGSLK AELRAKEKVD LNKTRTFTAA PVDTLLGGKV
CVDDFNNRFY SLNIQCPWSV GMTKFYKGWD EMLRKLPDGW VYCDADGSQF DSSLSPYLIN
SVLNLRLHFM ESWDLGEQML KNLYTEIIYT PIATPDGTII KKFKGNNSGQ PSTVVDNTIM
VIMAIHYSYK NLKITTPLDD FCKYFVNGDD LLLAVRPDFE YILDHLSTTF KQLGLNYDFT
SRTHDRSELW FMSHQGILQD GLYIPKLEPE RIVSILEWDR ALEPVHRLEA ICASMIEAWG
NQPLLHEIRK FYSWVLEQAP YSALAVEGKA PYLSEMALRA LYTGRDTTQG ELEKYLSQLE
LLEELEGPEE VIFQANETLN AGATSTSRTQ PATQAGAGSS QLVTRDRDVD AGTVGTFQVP
RIQKLAARLA VPKISGRILI NLDHLINYNP EQVDISNTRA SQHQFASWYE GVKLDYGLED
AGMAIILNGF MVWCIENGTS PNINGMWVIM DGADQVEYPL RPMIEHAKPT LRQIMAHFSP
LAEAYIEKQN LERPYMPRYG LQRNLTDFGL ARYAFDFYEM NSKTPQRARE AHIQMKAAAL
RGARTKLFGL DGKVTTQDED TERHTTDDVN AKMHSLLGVN M
//
