ID Q1KN84_9POTV Unreviewed; 3140 AA.
AC Q1KN84;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
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:ABE97923.1};
RN [1] {ECO:0000313|EMBL:ABE97923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Penn4 {ECO:0000313|EMBL:ABE97923.1};
RX PubMed=17872538; DOI=10.1099/vir.0.82814-0;
RA Wallis C.M., Stone A.L., Sherman D.J., Damsteegt V.D., Gildow F.E.,
RA Schneider W.L.;
RT "Adaptation of plum pox virus to a herbaceous host (Pisum sativum)
RT following serial passages.";
RL J. Gen. Virol. 88:2839-2845(2007).
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; DQ465243; ABE97923.1; -; Genomic_RNA.
DR MEROPS; C06.001; -.
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: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 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..2268
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2534..2658
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 3140 AA; 355615 MW; 2D5561E9DD043258 CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLRKQYQE ERERFQFLNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF ATPSMKKKVV FTKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGN YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTNGFHHVHK KGEVTPGMSG FVVNPMNLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKE
QSNEIIHYSD PGKQFWDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL VCQAIIPCGK
ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGERKEAPFS HLNKINELII KGGMMSAQDY IEASDHLREL ARYQKNRTEN
IRSGSIKAFR NKISSKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG
YRRHIVRENP RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
LININEDEAK SFTKTVRDTL VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSNM KTYLVGGLEV DKCDEFKNVK
LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIT
SMLSALAAKV SLASTLNAQM SVIDEHAAVL CDSVFDGTKP YASYMMAVKT LERMKARTES
DHTLNDLGFS VLRQATPHLV EKSYLQELEQ AWKELSWSEK FSAILESQRW RKHIPKPFIP
KDGADLGGRY DISVRSLLGN QYKRLRDVVR RKRDDVVCYT HQSMGKLFCK AIGISTSFLP
STLKMLDMLI VFGLLLSIGA TCNSMINEHK HLKQLAADRE DKKRFKRLQV LYTRLSEKVG
CTPTADEFLE YVGGENPDLL KHAEDLIGDG QVVVHQSKRD SQANLERVVA FVALVMMLFD
SERSDGVYKI LNKLKGIMGS VDQAVHHQSL DDIEDILDEK KLTVDFVLQS NEVAPTVPFD
STFEKWWTNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL IRGAVGSGKS
TGLPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPHNVNPT LRMRGMSTFG STPITVMTSG
YALHFLANNP TYLDNYKCII FDECHVHDAS AMAFRCLLSE YSYPGKILKV SATPPGHEVD
FKTQKEVKVI VEESLSFQQF VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS
FKVSKVDGRT MKIGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDI
DNRLVRYTKK SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPIIA TEAAFLCFTY
GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR FDGTMHQEIF RLLKSYRLRD
SEVILNKLAI PNSNVCGWMS VRDYKRQGCN LDLDENIRVP FYVKDIPETL HERIWQAVET
HKSDAGFGRI CSSSACKIAY TLQTDIHSIP RTIKIIDALL EQERTKQAHF RAMTSQSCSS
SNFSLSSITS AIRSKYAKDH TEENIGVLQM AKSQLLEFKN LNIDPSYPEL VRNFGALECV
HHQTKEGVSK ALQLKGHWNK RLITRDATLM LGVLGGGAWM IFSYLRDSFK EEVVHQGFNR
RQRQKLKFRQ ARDNRMAREV YGDDSTMEDY FGSAYSKKGK SKGKTRGMGT KTRKFVNMYG
YDPTDYNFVR FVDPLTGHTL DENPLMDINL VQEHFSQICN DYIGDDKITM QHIMSNPGIV
AYYIKDATQK ALKVDLTPHN PLRVCDKTAT IAGFPEREFE LRQTGHPVFV EPNAIPKINE
EGDEEVDHES KSLFRGLRDY NPIASSICQL NNSSGARQSE MFGLGFGGLI VTNQHLFKRN
DGELTIRSHH GEFVVKDTKT LKLLPCKGRD IVIIRLPKDF PPFPKRLQFR TPTTEDRVCL
IGSNFQTKSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC GLPIVSTRDG SILGLHSLAN
STNTQNFYAA FPDNFETTYL SNQDNDNWIK QWRYNPDEVC WGSLQLKRDI PQSPFTICKL
LTDLDGEFVY TQSKTTHWLR DRLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE
HEFFRPLMGA YQKSALNKDA YVKDLMKYSK PIVVGAVDCD QFERAVDVVI SMLISKGFEE
CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFKNVSDQDK ESFVRASCKR LFMGKKGVWN
GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN NQFYSLNLHC PWSVGMTKFR
GGWDKLLRAL PEGWIYCDAD GSQFDSSLSP YLINAVLNIR LAFMEEWDIG EQMLSNLYTE
IVYTPIATPD GTIVKKFKGN NSGQPSTVVD NTLMVILAMT YSLLKLGYHP DTHDCICRYF
VNGDDLVLAV HPAYESIYDE LQEHFSQLGL NYTFATKTEN KEELWFMSHK GVLYDDMYIP
KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV LEQAPYNALS
KDGKAPYIAE TALKKLYTDT EASETEIERY LEAFYDDIND DGESNVVVHQ ADEREDEEEV
DAGKPIVVTA PAATSPILQP PPVIQPAPRT TAPMFNPIFT PATTQPATKP ISQVSGPQLQ
TFGTYGNEDA SPSNSNALVN TNRDRDVDAG SIGTFTVPRL KAMTSKLSLP KVKGKAIMNL
NHLAHYSPAQ VDLSNTRAPQ SCFQTWYEGV KRDYDVTDDE MSIILNGLMV WCIENGTSPN
INGMWVMMDG ETQVEYPIKP LLDHAKPTFR QIMAHFSNVA EAYIEKRNYE KAYMPRYGIQ
RNLTDYSLAR YAFDFYEMTS TTPVRAREAH IQMKAAALRN VQNRLFGLDG NVGTQEEDTE
RHTAGDVNRN MHNLLGVRGV
//
