ID Q85265_9POTV Unreviewed; 3061 AA.
AC Q85265;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 151.
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:CAA66472.1};
RN [1] {ECO:0000313|EMBL:CAA66472.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:CAA66472.1};
RX PubMed=9400962;
RA Jakab G., Droz E., Brigneti G., Baulcombe D., Malnoe P.;
RT "Infectious in vivo and in vitro transcripts from a full-length cDNA clone
RT of PVY-N605, a Swiss necrotic isolate of potato virus Y.";
RL J. Gen. Virol. 78:3141-3145(1997).
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; X97895; CAA66472.1; -; Genomic_RNA.
DR PIR; A60366; A60366.
DR PIR; A60678; A60678.
DR PIR; JA0073; JA0073.
DR PIR; JC1527; JC1527.
DR PIR; T01408; T01408.
DR MEROPS; C06.001; -.
DR Proteomes; UP000241299; 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:0042025; C:host cell nucleus; 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: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:CAA66472.1};
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 791..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 2517..2641
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2795..2835
FT /note="Disordered"
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 3061 AA; 347501 MW; C2E713776B181A20 CRC64;
MAIYTSTIQF GSIECKLPYS PAPFGLVAGK REVSTTTDPF ASLEMQLSAR LRRQEFATIR
TSKNGTCMYR YKTDVQIARI QKKREERERE EYNFQMAASS VVSKITIAGG EPPSKLESQV
RRGVIHTTPR MRTAKTYHTP KLTEGQMNHL IKQVKQIMST KGGSVQLISK KSTHVHYKEV
LGSHRAVVCT AHMRGLRKRV DFRCDKWTVV RLQHLARTDK WTNQVRATDL RKGDSGVILS
NTNLKGNFGR SSEGLFIVRG SHEGKIYDAR SKVTQGVMDS MVQFSSAESF WKGLDGNWAQ
MRYPTDHTCV AGLPVEDCGR VAAIMTHSIL PCYKITCPTC AQQYANLPAS DLLKILHKHA
SDGLNRLGAD KDRFVHVKKF LTILEHLTEP VDLSLEIFNE VFKSIGEKQQ SPFKNLNILN
NFFLKGKENT AREWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
NQLDKNASFL WGQREYHAKR FFSNYFEEID PAKGYSAYEN RLHPNGTRKL AIGNLIVPLD
LAEFRRKMKG DYKRQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAVESTFY PPTKKHLVIG
NSGDQKYVDL PKGNSEMLYI ARQGFCYINI FLAMLINISE EDAKDFTKKV RDMCVPKLGT
WPTMMDLATT CAQMKIFYPD VHDAELPRIL VDHETQTCHV VDSFGSQTTG YHILKASSVS
QLILFANDEL ESDIKHYRVG GIPGACPELG STISPFREGG IIMSESAALK LLLKGIFRPK
VMKQLLLDEP YLLILSILSP GILMAMYNNG IFELAVKLWI NEKQSIAMIA SLLSALALRV
SAAETLVAQR IIIDTAATDL LDATCDGFNL NLTYPTALMV LQVVKNRNEC DDTLFKAGFS
HYNMSVVQIM EKNYLSLLGD AWKDLTWREK LSATWHSYKA KRSITQFIKP IGKADLKGLY
NISPQAFLGQ GVQRVKGTAS GLNERLNNYI NTKCVNISSF FIRRIFRRLP TFVTFINSLL
VISMLTSVVA VCQAIILDQR KYRKEIELMQ IEKNEIVCME LYASLQRKLE REFTWDEYME
YLKSVNPQIV QFAQAQMEEY NVRHQRSTPG VKNLEQVVAF ITLIIMMFDA ERSDCVFKTL
NKFKGIVSSM DHEVKHQSLD DVIKNFDERN EVIDFELNED TIKTSSVLDT KFSDWWDRQI
QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST GLPVHLSAAG
SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSVFGS SPISIMTSGF ALHYYANNRS
QLTQFNFIIF DECHVLDPSA MAFRSLLSVY HQTCKVLKVS ATPVGREVEF TTQQPVKLVV
EDTLSFQSFV DAQGSKTNAD VVQHGSNILV YVSSYNEVDT LAKLLTDRNM VVSKVDGRTM
KHGCLEIVTK GTSAKPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKIS
VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIEIPSMIAS EAALACFAYN LPVMTGGVST
SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD ILKKYKLRDC MTPLCDQSIP
YRASSTWLSV SEYERLGVVL DIPKQIKIAF HIKDIPPKLH EMLWETVIKY KDVCLFPSIR
ASSISKIAYT LRTDLFAIPR TLILVERLIE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL
RARYAKDYTA ENIQKLEKVR SQLKEFSNLN GSACEENLMK RYESLQFVHH QATTSLAKDL
KLKGVWKKSL VVQDLLIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR IQALKFRHAR
DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS RRFVNMYGFD PTEYSFIQFV
DPLTGAQIEE NVYADIRDIQ ERFSDVRKKM VEDDEIELQA LGSNTTIHAY FRKDWSDKAL
KIDLMPHNPL KICDKSNGIA KFPERELELR QTGPAIEVDV KDIPKQEVEH EAKSLMRGLR
DFNPIAQTVC RVKVSVEYGT SEMYGFGFGA YIIVNHHLFK SFNGSMEVRS MHGTFRVKNL
HSLSVLPIKG RDIIIIKMPK DFPVFPQKLH FRAPVQNERI CLVGTNFQEK HASSIITETS
TTYNVPGSTF WKHWIETNDG HCGLPVVSTA DGCLVGIHSL ANNVQTTNYY SAFDEDFESK
YLRTNEHNEW TKSWVYNPDT VLWGPLKLKE STPKGLFKTT KLVQDLIDHD VVVEQAKHSA
WMYEALTGNL QAVATMKSQL VTKHVVKGEC RHFKEFLTVD SEAEAFFRPL MDAYGKSLLN
REAYIKDIMK YSKPIDVGIV DCDAFEEAIN RVIIYLQVHG FQKCNYITDE QEIFKALNMK
AAVGAMYGGK KKDYFEHFTE ADKEEIVMQS CFRLYKGSLG IWNGSLKAEL RCKEKILANK
TRTFTAAPLD TLLGGKVCVD DFNNQFYSKN IECCWTVGMT KFYGGWDKLL RRLPENWVYC
DADGSQFDSS LTPYLINAVL IIRSTYMEDW DLGLQMLRNL YTEIIYTPIS TPDGTIVKKF
RGNNSGQPST VVDNSLMVVL AMHYALIKEC VEFEEIDSTC VFFVNGDDLL IAVNPEKESI
LDRMSQHFSD LGLNYDFSSR TRRKEELWFM SHRGLLIEDM YVPKLEEERI VSILQWDRAD
LPEHRLEAIC AAMIESWGYF ELTHQIRRFY SWLLQQQPFS TIAQEGKAPY IASMALKKLY
MNRTVDEEEL KAFTEMMVAL DDEFECDTYE VHHQGNDTID AGGSTKKDAK QEQGSIQPNL
NKEKEKDVNV GTSGTHTVPR IKAITSKMKM PKSKGATVLN LEHLLEYAPQ QIDISNTRAT
QSQFDTWYEA VQLAYDIGET EMPTVMNGLM VWCIENGTSP NINGVWVMMD GNEQVEYPLK
PIVENAKPTL RQIMAHFSDV AEAYIEMRNK KEPYMPRYGL VRNLRDGSLA RYAFDFYEVT
SRTPVRAREA HIQMKAAALK SAQSRLFGLD GGISTQEENT ERHTTEDVSP SMHTLLGVKN
M
//
