ID G0YWB2_9POTV Unreviewed; 3143 AA.
AC G0YWB2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Plum pox virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12211 {ECO:0000313|EMBL:AEK27124.1};
RN [1] {ECO:0000313|EMBL:AEK27124.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BY181 {ECO:0000313|EMBL:AEK27124.1};
RA Malinowski T., Klekowicka M., Rapinska A., Solovey A.V., Kukharchyk N.V.;
RT "Molecular characterization of Plum pox virus (PPV) isolates found in
RT Belarus.";
RL Submitted (DEC-2010) 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; HQ840518; AEK27124.1; -; mRNA.
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 2: Evidence at transcript level;
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 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 644..766
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1240..1392
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1411..1570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2050..2269
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2535..2659
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
SQ SEQUENCE 3143 AA; 355419 MW; AE1E5D473C89CA91 CRC64;
MSTIVFGSFT CHLDAAIHQD NADRVAKAWA RPENRQISNV HLLCRRTAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTITKRKGLR CFKASSEQVI ERKLKQQYKE ERERFQWING
PENVVTHIEP VTEGAPTWVP FPDIPKRPLS KTPSMKRHII FDKVRMSETT LQLFMRKVAN
NAKANGQKVE IIGTKHVVGN YIRKSQLTYF RTHVRHLDGL KPRYDITLDE ATKKIVQIFA
NTSGFKHVHG KGEITPGMSG FVINPRNISD PMQIHDTDLF IVRGKHNSIL VDARCPVSKE
HSNELVHYSD PGKKFWVGFT NSFAQCKLRE TDHQCTSDLD VQECGYVAAL VCQAIIPCGK
ITCLQCAEKY AYMSQQEIRD RFSTVIEQHE KTVMDSYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGERKEAPFS HINKINELII KGGMMTVQDY SEASDRLREL ARYQKNRTEN
IQSGSIKAFR NKISAKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFNVIDTSEG
YRRHIVRENP RGTRKLAIGN LVMSTNLAAL RKQLLGEECT RFEVSKECTS KRGANFVYQC
CCVTHEDGTP LESEIISPTK NHLVIGNSGD SKYVDLPKTE GGGMYIAKAG YCYINIFLAM
LVNVNEGEAK SFTKTVRDTL VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
SKIFHVVDSY GSLSTGMHIL KANTVNQLIS FASDTLDSSM KMYLVGGLEV DRCDEFKNVK
LLIRSIYKPE LMQQVLTEEP YLLIMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIV
SMLSALAAKV SLAQTLNAQM NVIDEHASVL HDSVFNGTKP YASYIMAIKT LERMKARTES
DHTLHDLGFS VLRNATPHLV EKSYLQELEQ AWKELSWSER FSAMLESQRW RRHIPRPFVP
AASADLGGRY DISLRSLLGS QYKRLKGGIR RRKDSVVCYA HQSMGKLFCK AVGLSTNFLP
KAFKMIDMLI VISLLLTIGA TCKSMINEHQ QLKQMAVDRE NNKRFKRLQL LYARVTDKLG
YMPTAEEFLE YVQGENPELV KYAEDLIGEG QVVVHQSKRE SQANLERVVA FVALVMMLFD
SERSDGVYKI LTKLKGIMGS IDQTVHHQSL DDIEDILDEK KLTVDFVLQS NEVAPTVPFD
STFEKWWTNQ LETGNVIPHY RTEGHFMEFT RENAAHVANE VMHGPHMDIL IRGAVGSGKS
TGLPFHLSKK GHVLLLEPTR PLAENVCKQL RGQPFNVNPT LRMRGLSTFG STPITVMTSG
YALHFLANNP VYLDNYKCII FDECHVHDAS AMAVRCLLSE YSYPGKILKV SATPPGHEVD
FKTQKEVKVI VEESLSFQQF VSNLGSGCNS DILKYGANIL VYVASYNEVD TLGKLLTDRN
FKVSKVDGRT MKVGSVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDV
DNRLVRYKKT SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPMIA TEAAFLCFTY
GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVAMVR FDGTMHQEIF RLLKSYRLRD
SEVILNKLAI PNGNVGGWMS VRDYKRQGCN LDLDDNVRIP FYVKDLPELL HEQIWQAVEN
YKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTVKIIDVLL EQERTKQAHF RAMTSQSCSS
SNFSLSSITS AIRSKYAKDH TEENIGVLQM AKAQLLEFQN LNIDPSYPEL VRNFGALECV
HHQTKEGVSN TLKLKGHWNK QLVTRDATLM LGVLGGGAWM IYSYLKDSFK EEVAHQGFNR
RQRQKLKFRQ ARDNRMAREV YGDDSTMEEY FGSAYSKKGK SKGRTRGMGT KTRKFVNMYG
YDPTDYNFVR FVDPLTGHTL DENPLMDIGL VQEHFSIIRN EQIGDDKITP QHIMANPGLV
AYYVKDATQK ALKIDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGQPTFV EPSAVPKANE
VESEEVDHES KSLFRGLRDY NPIASSICQL TNSSGARNSE MFGLGFGGVI ITNQHLFKRN
DGELTIRSHH GEFVVRDTKT LKLLPCKGRD IVIIRLPKDF PPFPKRLQFR TPTTEDRVCL
IGSNFQTRSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC GLPIVSTRDG NILGLHSLAN
STNTQNFYAA FPENFEVDYY LSNNDAANWI KQWRYNPDEV CWGSLQLKRD VPQSPFKICK
LLTDLEGDTV YTQSKTTHWL RDKLEGNLKA VGACPGQLVT KHVVKGKCTL FETYLLTHPD
ERAFFRPLMG AYQKSALNKD AYVKDLMKYS KPIVVGTVDC EQFERAVNAV ISMLISKGFE
ECCYVTDPDD IFAALNMKAA VGALYSGKKR DYFENVSEDE KYEFVRASCK RLFMGQKGVW
NGSLKAELRP KEKVEANKTR SFTAAPIDTL LGGKVCVDDF NNQFYSLNLH CPWSVGMTKF
RGGWDKLLRS LPDGWIYCDA DGSQFDSSLS PYLINAVLNI RLAFMEKWDI GEQMLSNLYT
EIVYTPIATP DGTIVKKFKG NNSGQPSTVV DNTLMVILAM TYSLLKLGYH PDTHDCICKY
FVNGDDLVIA VHPSHEHIYD ELQELFSQLG LNYTFTAKTE NKEELWFMSH KGVLHDGMYI
PKLEPERIVS ILEWDRSHEP IHRLEAICAS MVEAWGYGDL LREIRKFYSW VLEQAPYNAL
SKDGKAPYIA ETALKKLYTD EEASETEIEK YLEAFYNNAG DELDSNIVVH QTKEGGDDDV
TLVDAGKSTI TTAASTPAVT SSQFPPPPFP NLQSTAPMFD PIFTPATTQP NVRPIASVVT
SPFSYGVIGN QNVTPSSSNA LVNTRKDRDV DAGTIGTFSV PRLKSMTSKL SLPKVRGKAI
MNLNHLAHYN PAQTDLSNTR APQSCFQTWY EGVKRDYDVS DDEMSIILNG LMVWCIENGT
SPNINGMWVM MDGETQVEYP IKPLLDHAKP TFRQIMAHFS NVAEAYIEKR NYEKAYMPRY
GIQRNLTDYS LARYAFDFYE MTSTTPVRAR EAHIQMKAAA LRNVQNRLFG LDGNVGTQEE
DTERHTAGDV NRNMHNLLGV RGV
//
