ID Q4LCH0_9POTV Unreviewed; 3129 AA.
AC Q4LCH0;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Thunberg fritillary mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=299200 {ECO:0000313|EMBL:CAH65461.1, ECO:0000313|Proteomes:UP000203731};
RN [1] {ECO:0000313|EMBL:CAH65461.1, ECO:0000313|Proteomes:UP000203731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ningbo {ECO:0000313|EMBL:CAH65461.1};
RX PubMed=15789262; DOI=10.1007/s00705-005-0519-8;
RA Wei C.B., Chen J., Zhang Q.Y., Shi Y.H., Lin L., Zheng H.Y., Adams M.J.,
RA Chen J.P.;
RT "A new potyvirus from Thunberg fritillary (Fritillaria thunbergii Miq.) in
RT Zhejiang, China.";
RL Arch. Virol. 150:1271-1280(2005).
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; AJ851866; CAH65461.1; -; Genomic_RNA.
DR RefSeq; YP_254713.1; NC_007180.1.
DR MEROPS; C06.001; -.
DR GeneID; 5076473; -.
DR KEGG; vg:5076473; -.
DR Proteomes; UP000203731; Genome.
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; 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; 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 ECO:0000313|EMBL:CAH65461.1};
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 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 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 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 851..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1077..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..359
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 696..818
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1292..1444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1448..1622
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2102..2320
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2587..2710
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 704
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 777
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3129 AA; 354367 MW; 5D31AC077A339E01 CRC64;
MAVAMIMNTL VNNLSAPPII PSKYTLSDME KRQYASVCIF GDFGALKPIT TNAANNNAAK
AIVTEMTGRE SQGPMVLAKH MAKPSNGGSV VHVRRGPNAW VLQARAQIRS SEQQMDTAFG
RLATACAERI EKMGPQKPVK VKGRWTTRAF SQKELKAEKE RVLWLKNRRN DLTIEPNVIE
HIEVPDDGPH VSLGTLMRDT EVLKKTKKVL APVRGHCALE CDIANLLHET LKIFGSRGKP
VEVIEKGKRT RISNVRRGKR WYIRCFLPHM RGEKLAQELN RTSNLESLVR VYNRKFNRDV
EVDMRSIKPG DSGIVYNGEL LRGQRVETEH FIVRGKLNGR LIDARSYMEV EDLLSIKEFS
KDVATQFWDG LNRKFLQARN FDDDHKCESN LSVAKCGEVA GLLIQAIYPC GRITCKKCIA
RATGLTRLEY GSFIGTRVKK VKEEIRADYK DFTHIPDILT HLERATTTSN DNLDDFSAIN
TIVFDKKESP FSHIREINDV LMKSGEATNA DFEMATHHLL EVTRYLKNRT DIIAESKTAR
FRNKASAKTH FNADLMCDNR LDKNGNFLWG QRGYHAKRFL LNYFERIDPD KGYAMYVDRR
HPNGIRKLSI DKLIVSTNLE TFRQQMAGRK VHSYSITDEC VSKRGGSYVY QNCCVTHDDG
TPVESGFLSP TKHHLVIGNT GEAKFVDLPQ DEILQMYIAK DGYCYINIFF AMLINVREDQ
AKSFTKMVRD MIIPKLGVWP TVMDVATTCK LLTVFFPDTA NAELPRIYVD HAHKMMHVID
SYGSYDTGYH LLKSNTVSQF MNFSSIDMES ELKYYRVGGK FVASHLVMTN FNTLIKAIYR
ADLMRDILTH EPYLVMLAVL SPGVLLALFN SGSLEVATRM WIRQDQNIAQ IMTMLSILAA
KVSVSKVLLE QKRIIEMNAE HLLRATDHTF FPCKSIDTAI CALTVMDEEH KSDQALRDNG
FYAHLLNSSE ILEKSYMEDL EASWLELSLW ARLRLIFQSR KLHKKYLGFV ELENRTGTIG
RYSTSLSACL TMMKHNFTRC VKKIKSKTKT RMYNIVGRVT CAMVGNCKYL FPDLVHFMNV
LTVLGFLLTI YRSIFVHIAE YKSLKAKEQA SVDERNAKIA GAIYKELGME TKILPTIEEF
RERLGSLSPE LLTWFDGTYK LEDYIFQAKT DGERNLERVV AVSALLLMIF DAERSDVVYK
ILNKLKTLIG VVETEPMKFQ SLDDARDILE EKNLTVDFEL QGDNECLPIQ GGTTFEQWWN
HQLLHNNVIP HYRTEGHFIE FTRESAVAVA NEIAHGPHTD YLVRGAVGSG KSTGLLFHLS
AKGGVLLLEP TKPLAENVYK QLRKEPFFLN PTLRMRGTTY IGSAPVTIMT SGFALHYYAN
NIKRLEEIKH IIFDECHVHD SNAMAFRCLL SEYAFCGKIL KVSATPPGRE IEFTTQKPVE
LLIEENLSIQ QFVSNLGSKS NSDVTAKGDS ILVYVASYNE VDQLSKLLLE KNFKVTKVDG
RTMKSGRTEI ETHGTSERKH FIVATNIIEN GVTLDIDVVV DFGTKVVPEL DGDARLIRYR
KVSVSYGERI QRLGRVGRFK PGVALRIGST ERGLQAVPGV VATEAAFHSF TYGLPVMTEG
VSTSILSNCT VPQARTMMNF ELPIFFTAPL VRFDGTMHAA VHKLLIPYKL RDSDITLNRL
AIPTASQKGW NTAREYAMHG CRLNVEDEIT IPFYARDIPE KLISELHTVV VNNKSDSGFG
RVSSASAARI AYTLQTDPCS IQRTIAIIDK LIEAEQRKKA YFDSVTGISV STSNFSLSSI
INAIKTRHMT NHTAENIGVL QAAKGQLMEF RNITLDWETV DKFGQNGALE CLHFQSEVEM
SKHLRLKGHW NKSLITTDTI VAGTVFIGGV WMLYTHFKDT IKQTYSFQAK NKRQRQKLKF
RQARDNKHAI EVYGDDANLE HYFGSAYTAK GKSKGNTCGM GTKIRRFVNM YGFDVTDYSF
ARYVDPLTGA TIDENPLTDL GMVQEHFGKV RTQFISDDQL DPNQVRLNTK IEAYFVKNAA
KEVLKVDLTP HNPLQLGDIV PSISGFPERE LELRQTGKPV LIPYSQLPER NEKETESLVF
ESASNFHGLR DYNPIAMTVC SLQNTSDGVV ATLFGIGYGS VIIANQHLFR CNNGTLCVKS
HHGEFKVANT TELQLFPVNG RDIILIKLPK DFPPFPRKLK FRCVEKGERV CLVGSNFQTR
SISSTVSETS VTAPSPSEAF TKHWITTKDG QCGLPIVSTK DGKIIGLHSL SSTVSSTNMF
TNIPSEFEEK VLMCIDSLEW TKKWRLNVDK ANWGAVNIKD DLASGLFKLS KDISSIHDSE
WNFQAGFKQN WLYEQLDGNL KAIGRTPNAL VTKHVVRGKC NLFAAYLALD KQANDYFTPL
LGSYQKSRLN REAYIKDVKK YASPIIVGSV DCDAFEEAFK DVIKVFTDVG FKECAYITDH
VETFDALNKK AATGALYKGK KGEYLAGYSE SEKEEMLKES CKRLFLGKMG VWNGSLKAEL
RPIEKCIANK TRSFTAAPID TLLGGKTCVD DFNNQFYSLH FALPSSVGMT KFYGGWNDLL
CRLPDNYVYC DADGSQFDSS LSPYLINAVL NLRLHFMEDW GVGHTMLENL YTEIVYTPIA
TPDGTIIKKF KGNNSGQPST VVDNTIMVML AVNYALRVNH ITESAHDFIR YYINGDDLLI
AIRPDMEHLL DKFQESFQQL GLNYTFNSRT RNKTELWFMS HQGILRDGIF IPKLERERVV
SILEWDRAEL PEHRLEAICA AMIEAWGHDE LIHEVRRFYH WVLQQEPYNE LAAQGKAPYI
SEVALKALYT GTAATESELV RYYNTMERLN VVMDDEFCFQ ADRTEQIDAG RDQVRKRTQE
TNQGEGSQQA IVREPDVNVG SAGALTVPRL REINSKINLP MVRGKRIVNL DHLLLYTPQQ
TDIYNTRATQ TQFAAWYDGV KQDYELEDDQ MQIVLNGLMV WCIENGTSPN LNGMWVMMDE
DKQVEFPIKP LLDHAKPTFR QIMAHFSELA EAYIIKRNIT KPYMPRYALK RNLTDMSLAQ
YAFDFLEITS RTPARAREAQ AQMKAAALKN ARTRMFGLDG SVGTTEEDTE RHTTTDVNRS
MHSMLGIRM
//
