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Genome polyprotein

 Q4VU86_9POTV            Unreviewed;      3176 AA.
Q4VU86;
05-JUL-2005, integrated into UniProtKB/TrEMBL.
21-AUG-2007, sequence version 2.
25-OCT-2017, entry version 89.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Zantedeschia mild mosaic virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Potyviridae; Potyvirus.
NCBI_TaxID=270478 {ECO:0000313|EMBL:AAV54595.4, ECO:0000313|Proteomes:UP000202900};
[1] {ECO:0000313|EMBL:AAV54595.4, ECO:0000313|Proteomes:UP000202900}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW {ECO:0000313|EMBL:AAV54595.4,
ECO:0000313|Proteomes:UP000202900};
PubMed=15703845; DOI=10.1007/s00705-004-0488-3;
Huang C.H., Chang Y.C.;
"Identification and molecular characterization of Zantedeschia mild
mosaic virus, a new calla lily-infecting potyvirus.";
Arch. Virol. 150:1221-1230(2005).
[2] {ECO:0000313|EMBL:AAV54595.4, ECO:0000313|Proteomes:UP000202900}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW {ECO:0000313|EMBL:AAV54595.4,
ECO:0000313|Proteomes:UP000202900};
AGRICOLA=IND43868865; DOI=10.1111/j.1365-3059.2006.01485.x;
Huang C.-H., Hu W.-C., Yang T.-C., Chang Y.-C.;
"Zantedeschia mild mosaic virus, a new widespread virus in calla lily,
detected by ELISA, dot-blot hybridization and IC-RT-PCR.";
Plant Pathol. 56:183-189(2007).
-!- FUNCTION: Helper component proteinase: required for aphid
transmission and also has proteolytic activity. Only cleaves a
Gly-Gly dipeptide at its own C-terminus. Interacts with virions
and aphid stylets. Acts as a suppressor of RNA-mediated gene
silencing, also known as post-transcriptional gene silencing
(PTGS), a mechanism of plant viral defense that limits the
accumulation of viral RNAs. May have RNA-binding activity.
{ECO:0000256|SAAS:SAAS00890155}.
-!- CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-
terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
processing of the potyviral polyprotein.
{ECO:0000256|SAAS:SAAS00336250}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00560857}.
-!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
{ECO:0000256|RuleBase:RU003351}.
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EMBL; AY626825; AAV54595.4; -; Genomic_RNA.
RefSeq; YP_002308580.1; NC_011560.1.
ProteinModelPortal; Q4VU86; -.
GeneID; 7043116; -.
KEGG; vg:7043116; -.
Proteomes; UP000202900; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00079; HELICc; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR001456; HC-pro.
InterPro; IPR031159; HC_PRO_CPD_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR002540; Pept_S30_P1_potyvir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001592; Poty_coat.
InterPro; IPR001730; Potyv_NIa-pro_dom.
InterPro; IPR013648; PP_Potyviridae.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00863; Peptidase_C4; 1.
Pfam; PF00851; Peptidase_C6; 1.
Pfam; PF01577; Peptidase_S30; 1.
Pfam; PF00767; Poty_coat; 1.
Pfam; PF08440; Poty_PP; 1.
Pfam; PF00680; RdRP_1; 1.
PRINTS; PR00966; NIAPOTYPTASE.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51744; HC_PRO_CPD; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00057850};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000202900};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Hydrolase {ECO:0000256|SAAS:SAAS00058020,
ECO:0000256|SAAS:SAAS00494788}; Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00494788};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Suppressor of RNA silencing {ECO:0000256|SAAS:SAAS00890154};
Transferase {ECO:0000256|SAAS:SAAS00510600};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00057850}.
TRANSMEM 849 866 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1071 1089 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 698 820 Peptidase C6.
{ECO:0000259|PROSITE:PS51744}.
DOMAIN 1289 1441 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1460 1619 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2094 2312 Peptidase C4.
{ECO:0000259|PROSITE:PS51436}.
DOMAIN 2578 2702 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
COILED 2854 2900 {ECO:0000256|SAM:Coils}.
ACT_SITE 706 706 For helper component proteinase activity.
{ECO:0000256|PROSITE-ProRule:PRU01080}.
ACT_SITE 779 779 For helper component proteinase activity.
{ECO:0000256|PROSITE-ProRule:PRU01080}.
SEQUENCE 3176 AA; 359491 MW; 5F053AB9D5BE9284 CRC64;
MAGVCFAFPR ALSWESMQFG SIPSNYFGVE GEQEQEAPLL NAPTMQVAPQ VMAPASKMAP
TFRDHHKVIV QRGEKLIALY DEQMHNCFAA LDARAAKPAE PIHYTHALLR KCTNMGYKKR
CDFLRKQRVA ELKEAKVHAF DAVGTVYTTG HVFDKHGMLQ TTGTSIGGGI LPSLVKGERI
ATTATSLGVR SPYERASKQN LGLRSPYYKR TPKLQRVPKK QIPRAIGESE FVTDAVLIIA
AQRGLPIEFI GKRKHALKAH YVRVRDQIVA KVELPHERGT YLSQELSYPE YINELNVLYK
HADCPLISAA ELGPGSSGFC FDKNHPITKE CTTYPFMVVR GRRYGELINA LSVENWIGEI
HHYSPNLELQ FMQGWLKYQQ LMKPKGSTHA CVFDFNNHRC GEFAAAICQT TFPLRQIACK
QCRLELGQMS KDEFKEYLDQ HMKYCDQFTI REFQGGDLGT LQDFMQQATT SVTNFKTCAE
ISKLVQGYTS THMLQIQDIN KALLKGSMVT QLELDQACKQ LLEMTQWWKK HMNLTGEDAL
KTFRNKRASK ALVNPTLMCD NQLDKNGNFV WGARGYHSKR FFTNFFEKVD PSNGYGGYIF
RKGPNGVREL AIGSLIVPLN IERARVALKG KSVDKKPLTQ ACTSKQDGNF VYACCCVTQE
DGTPVYSELK SPTKRHLVVG TSGEPKFIDL PTSDDEPMYI AREGYCYLNI FLAMLVNVNE
GDAKEFTKMV RDVLIPLLGT WPKLTDLATA VYILTVFHPE TRSAELPRIL VDHEHQTMHV
IDSFGSLSTG YHVLKTGTVS QLIHFGADDL VSEMKEYRVG GTSAMSTETA LIKSIFKPKI
MLQILNEEPY LVLMGIISPT ILIHMYRMQH FEKGIEIWIQ RDQSIAKIFI ILEQLTKKVA
VSELLSQQLE IINGQVEQLQ TVLGECPREF NSHKGAKGML DIFVERMSTN KELVSNGYFD
MNYQLYIERE KIFVQGLQQA WRELKLSEKF LLILQSKKFS PVMADTSIRK VKDAKGESSG
SLVSAYFTTG ISNLKSLKQF GFRKVERLWF SCVKAFVNIV CRMLRSCYRD FFYAFNLCLI
FCVFVQMIGT VKSIMESIKA DKALAYAAQM DKHERTLIHM YDIYKESSQG TPVFEEFRKH
VEMVRPDLVD VLSYMAANDE VVSTQAKTAA QLQLEKVVAF FAILTMCFDT ERSDAVFKVL
NKLRAVFLTL GEGVRVQSLD EILSLEGDKG LTVDFDLEVP ESSTSTALDV RFGSWWQSQL
QRNLVVPHYR TSGIFMEFTR EGAARLTNEI ILSSDSEFLI RGAVGSGKST GLPHHLPKKG
GVLLLEPTRP LAENVSKQLA KDPFYQHVTL RMRGLSRFGS SNISVMTTGY AFHYYANNPH
QLTNFDFVII DECHVHDANA IAFNCLLKNY SFGGKLLKVS ATPPGRECEF TTQHAVHLKT
EDVLSFQSFV QAQGTCANAD VVQYGHNILV YVASYTEVDM LSRLLVDKQY RVTKVDGRSM
QLGNVEITTQ GTSTKPHFIV ATNIIENGVT IDIDCVVDFG VKVVATLDSD NRCMRYSKCA
VTYGERIQRL GRVGRCKPGH ALRIGHTEKG IEEVPESIAT EAAFLCFAYS LPVTTNSVST
NILSRCTVKQ AKNALNFELT PFFTVHFIRH DGSMHPEIHK LLKPYKLKES EMHLNKLAIP
HQYTSQWITS AEYERLGVHI ECSPHTRAPF HANGIPDKLI EALWSVVCEF KSDAGFGSVS
SACAAKISYT LSTEPGAIPR TLAFIEHLLT EEMTKRNHFD TIGSAITGYS FSLAGIANSF
RKRYLRDYSA QNIATLQQAK AQLLEFDSKH IDFKNIQDLS DIGILNTVHL QSKGEISKFL
KLEGKWDGKS FMNDLLVGVI TIFGGGWMLW EFFIKSWKES VTTQGKKRRN QKLHFRDAYD
RKMGRMIVAD DNTMEQTFGE AYTKRGKVKG SKHTKGMGRK TRNFVHIYGV EPDEYSFIRF
VDPITGHTMD ESPRVDIRIV QDEMQDVRIK MLENDDIAPQ QIYRHPGISA YLVATNAEKA
LKIDLTPHLP TLLQRNTNAI AGFPEYEGEL RQTGAPLVID RASAPAANQV NLESKSVYKG
LRDYNNIATV ICRLENASDG HNEVMYGVGY GSYILTNGHL FRRNNGSLTI KTWHGEFKIA
NTTQIFVHFV AGKDLILLKM PKDFPPFCKM SIFRAPIREE RVCMVGTNFQ EKSLRATISE
SSIILPEGKG SFWVHWISTK DGDCGLPMVA TSDGCITGIH GLASNQTEKN FFVPFNDTIE
KDLLISADEL EWNKHWLWQP DKIAWGSLSL VANQPGSEFK VSKLITDLFS NAVQTQSKIE
KWIYTALEGN LRACGETESA LITKHTVKGR CRFFSEYLAT NPEAEKFFRP LMGAYAPSKL
NKDAFKRDFF KYNKPIELNK VQIGVFQQAL QSVINLLQEK GFKECVYVTD TTEIFDSLNL
KSAVGAQYRG KKGEYIENLD VSARDELLKQ SCERLFLGKK GIWNGSLKAE LRPMEKIRAN
KTRTFTAAPI DTLLGAKVCV DDFNNQFYSL NMECPWTVGM TKFYGGWDKL MRKLPEKWVH
CHADGSQFDS SLTPLLLNAV LTLRLCFMEE WFVGQEMLQN LYAEIVYTPI LTPDGTICKK
FRGNNSGQPS TVVDNTLMVV ISVYYACHKL GWSANEIQDR LVFFANGDDI ILSLPEEHLH
ALDTFQTSFE ELGLNYDFSE RTRDRSDLWF MSHQGKLVDG MYIPKLEEER VVSILEWDRS
KEILHRTEAI CAAMIEAWGH PELLREIRLF YLWLLHKSEF KELAAMGKTP YIAETALQKL
YTDVNATDLE LQRYVEVLTY DEDEGCGEDV VLQADDQQQQ QQQKQQQQQD QQQQQQQQQN
QQQQQQQQQN QQQQQQQNQN KTVDAGNNQN KQKSPASGGE VSDPIIPPQG GQLTTQGQRD
LDVNVGTKGK QVPRLQKMSS NMKLPMVRGK RILDLAHLIE YQPQQSDLFN TRASQTQFNN
WYDAIKNEYG VDDSQMQRIM NGFMVWCLEN GTSPNINGVW VMMDGDEQVE FPLKPMVENA
KPTLRQIMHH FSDAAEAYID LRNAAAPYMP RYGLLRNLRD RGLARFAFDF YEVTSKTPDR
AREAVAQMKA AALNNVSTRM FGLDGNIATA TENTERHTAK DVSPSMHSLL GISALQ


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