ID K4HFX2_9POTV Unreviewed; 3064 AA.
AC K4HFX2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Potato virus Y.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12216 {ECO:0000313|EMBL:AFR11769.1};
RN [1] {ECO:0000313|EMBL:AFR11769.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wilga {ECO:0000313|EMBL:AFR11769.1};
RA Visser J.C., Bellstedt D.U.;
RT "The molecular and biological characterization of South African isolates of
RT PVYNTN: implications for pathogenicity determinants.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; JN936435; AFR11769.1; -; 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: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; 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 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 141..284
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 618..740
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1229..1381
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1400..1559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2032..2250
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2520..2644
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2803..2842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2813..2842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 626
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 699
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3064 AA; 346135 MW; B43F157C87A8AC9A CRC64;
MATYMSTICF GSFECKLPYS PASCGHIVKE REVLASVDPF ADLETQLSAR LLKQEYATVR
VLKNGTLTYR YKTDAQITHI QKKLERKDRE EYHFQMAAPS IVSKITIAGG EPPSKLESQV
RRGVIHTTPR MRTAKTYHTP KLTEGQMNHL IKQVKQIMST KGGSVQLISK KSTHVHYKEV
LGSHRAVVCT AHMRGLRQRV DFRCDKWTVV RLQHLARTDK WNNQVRATDL RKGDSGVILS
NTNLKGSFGR SSEGIFIVRG SHERKIYDAR SKVTQGVMDS MVQFSSAESF WKGLDGNWAQ
MRYPTDHTCV AGLPVEDCGR VAAIMTHSIL PCYKITCPTC AQQYANLPAS DLLKILHKHA
SDGLNRLGAD KDRFVHVKKF LTILEHLTEP VDLSLEIFNE VFKSIGDKQQ SPFKNLNILN
NFFLKGKENT AREWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
NQLDKNANFL WGQREYHAKR FFSNYFEEID PAKGYSAYEN RLHPNGTRKL AIGNLIVPLD
LAEFRRKMNG DYKRQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAVESTFY PPTKKHLVIG
NSGDQKYVDL PKGNSEMLYI ARQGFCYINI FLAMLINISE EDAKDFTKKV RDVCVPKLGT
WPTMMDLATT CAQMKIFYPD VHDAELPRIL VDHETQTCHV VDSFGSQTTG YHILKASSVS
QLILFANDEL ESDIKHYRVG GVPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPK
VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
SAAETLVAQR IIIDAAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP
SYNTSVVQIM EKNYLNLLDD AWKDLTWXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XFSDWWDRQI
QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSVAG
SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS SPISVMTSGF ALHYFANNRS
QLAQFNFVIF DECHVLDPSA MAFRSLLSVY HQACKVLKVS ATPVGREVEF TTQQPVKLIV
EDTLSFQSFV DAQGSKTNAD VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM
KHGCLEIVTK GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS
VSYGERISRL GRVGRFKKGV ALRIGHTERA IIELPSMIAT EAALACFAYN LPVMTGGVST
SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD ILKKYKLRDC MTPLCDQSIP
YRASSTWLSV SEYERLGVAL EIPKQVKIAF HIKEIPPKLH EMLWETVVKY KDVCLFPSIR
ASSISKIAYT LRTDLFAIPR TLILVERLLE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL
RARYAKDYTA ENIQKLEKVR SQLKEFSNLD GSACEENLIK RYESLQFVHH QAATSLAXDL
KLKGTWKKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR
DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFINMYGFD PTEYSFIQFV
DPLTGAQIEE NVYADIRDIQ ERFSEVRKKM VENDDIEMQA LGSNTTIHAY FRKDWSDKAL
KIDLMPHNPL KVCDKTNGIA KFPERELELR QTGPAVEVDV KDIPAQEVEH EAKSLMRGLR
DFNPIAQTVC RLKVSVEYGT SEMYGFGFGA YIIANHHLFR SYNGSMEVRS MHGTFRVKNL
HSLSVLPIKG RDIILIKMPK DFPVFPQKLH FRAPTQNERV CLVGTNFQEK YASSIITETS
TTYNIPGSTF WKHWIETDNG HCGLPVVSTT DGCLVGIHSL ANNKHTTNYY SAFDEDFESK
YLRTNEHNEW VKSWIYNPDT VLWGPLKLKD STPKGLFKTT KLVQDLIDHD VVVEQAKHSA
WMFEALTGNL QAVATMKSQL VTKHVVKGEC RHFKEFLTVD AEAEAXXFFR PLMDAYGKSL
LNRDAYIKDI MKYSKPIDVG IVDCDAFEEA INRVIIYLQV HGFKKCAYVT DEQEIFKALN
MKAAVGAMYG GKKKDYFEHF TDADKEEIVM QSCLRLYKGL LGIWNGSLKA ELRCKEKILA
NKTRTFTAAP LDTLLGGKVC VDDFNNQFYS KNIECCWTVG MTKFYGGWDK LLRRLPENXX
VYCDADGSQF DSSLTPYLIN AVLTIRSTYM EDWDVGLQML RNLYTEIVYT PISTPDGTIV
KKFRGNNSGQ PSTVVDNSLM VVLAMHYALI KECIEFEEID STCVFFVNGD DLLIAVNPDK
EGILDRLSQH FSDLGLNYDF SSRTRNKEEL WFMSHRGLLI EGMYVPKLEX ERIVSILQWD
RADLAEHRLE AICAAMIESW GYSELTHQIR RFYSWLLQQQ PFATIAQEGK APYIASMALR
KLYMDRAVDE EELRAFTEMM VALDDEFEFD SYEVYHQAND TIDAGGSSKK DARPEQGSIQ
SNPNKGKDKD VNAGTSGTHT VPRIKAITSK MRMPKSKGAT VLNLEHLLEY APQQIDISNT
RATQSQFDTW YEAVRMAYDI GETEMPTVMN GLMVWCIENG TSPNVNGVWV MMDGDEQVEY
PLKPIVENAK PTLRQIMAHF SDVAEAYIEM RNKKEPYMPR YGLIRNLRDV GLARYAFDFY
EVTSRTPVRA REAHIQMKAA ALKSAQPRLF GLDGGISTQE ENTERHTTED VSPSMHTLLG
VKNM
//
