Reviewed, UniProtKB/Swiss-Prot Q01681 (POLG_PPVEA)

Names and origin

Protein names	Recommended name:     Genome polyprotein Cleaved into the following 6 chains:     1- Recommended name:             Cytoplasmic inclusion protein                 Short name=CI               EC=3.6.1.-     2- Recommended name:             6 kDa protein 2                 Short name=6K2     3- Recommended name:             Viral genome-linked protein         Alternative name(s):             VPg     4- Recommended name:             Nuclear inclusion protein A                 Short name=NI-A                 Short name=NIA               EC=3.4.22.44         Alternative name(s):             49 kDa proteinase               Short name=49 kDa-Pro     5- Recommended name:             Nuclear inclusion protein B                 Short name=NI-B                 Short name=NIB         Alternative name(s):             RNA-directed RNA polymerase             EC=2.7.7.48     6- Recommended name:             Coat protein                 Short name=CP
Organism	Plum pox potyvirus (strain El amar) (PPV)
Taxonomic identifier	31738 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus
Virus host	Prunus domestica (Garden plum) [TaxID: 3758] Prunus persica (Peach) [TaxID: 3760] Prunus cerasifera (cherry plum) [TaxID: 36595] Prunus armeniaca (Apricot) [TaxID: 36596] Prunus salicina [TaxID: 88123] Prunus glandulosa [TaxID: 105665] Prunus spinosa (Blackthorn) [TaxID: 114937]

Protein attributes

Sequence length	1518 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Coat protein is involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. Nuclear inclusion protein B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Cytoplasmic inclusion protein has helicase activity. It may be involved in replication. Nuclear inclusion protein A has RNA-binding and proteolytic activities.
Catalytic activity	Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subcellular location	Coat protein: Virion Potential.
Post-translational modification	VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity. The viral RNA of potyviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins By similarity.
Sequence similarities	Belongs to the potyviruses polyprotein family. Contains 1 peptidase C4 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	RNA replication
Cellular component	Capsid protein Virion
Ligand	Nucleotide-binding
Molecular function	Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Covalent protein-RNA linkage Phosphoprotein
Gene Ontology (GO)
Biological process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 179	›179	Cytoplasmic inclusion protein By similarity		PRO_0000040325
	Chain	180 – 232	53	6 kDa protein 2 By similarity		PRO_0000040326
	Chain	233 – 425	193	Viral genome-linked protein By similarity		PRO_0000040327
	Chain	426 – 668	243	Nuclear inclusion protein A By similarity		PRO_0000040328
	Chain	669 – 1186	518	Nuclear inclusion protein B By similarity		PRO_0000040329
	Chain	1187 – 1518	332	Coat protein By similarity		PRO_0000040330
Regions
	Domain	910 – 1034	125	RdRp catalytic
	Motif	273 – 280	8	Nuclear localization signal Potential
Sites
	Active site	471	1	For nuclear inclusion protein A activity By similarity
	Active site	506	1	For nuclear inclusion protein A activity By similarity
	Active site	576	1	For nuclear inclusion protein A activity By similarity
	Site	179 – 180	2	Cleavage; by NIa-pro By similarity
	Site	232 – 233	2	Cleavage; by NIa-pro By similarity
	Site	425 – 426	2	Cleavage; by NIa-pro By similarity
	Site	668 – 669	2	Cleavage; by NIa-pro By similarity
	Site	1186 – 1187	2	Cleavage; by NIa-pro By similarity
Amino acid modifications
	Modified residue	295	1	O-(5'-phospho-RNA)-tyrosine By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q01681-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: A1268F972F5B247C	FASTA	1,518	172,033
	10 20 30 40 50 60 LNKLAIPNAN VCGWMSVRDY KRQGCNLDLD DNIRVPFYVK DLPETLHEKI WQTVEAHKAD 70 80 90 100 110 120 AGFGRICSSS ACKIAYTLQT DIHSIPRTVK ILDALLEQER TKQAHFRSMT SQSCSSSNFS 130 140 150 160 170 180 LSSITSAIRS KYAKDHTEEN IGVLQMAKAQ LLEFKNLNID PSYPELVRNF GALECVHHQT 190 200 210 220 230 240 KEGVSKALRL KGHWNKQLVT RDATLMLGVL GGGAWMIFSY LRDSFKEEVV HQGFNRRQRQ 250 260 270 280 290 300 KLKFRQARDN RMAREVYGDD STMEDYFGSA YSKKGKSKGR TRGMGTKTRK FVNMYGYDPT 310 320 330 340 350 360 DYNFVRFVDP LTGHTLDENP LMDINLVQEH FSQVRNDYLG DDKITMQHIM SNPGIVAYYI 370 380 390 400 410 420 KDATQKALKV DLTPHNPLRV CDKTATIAGF PEREFELRQT GQPVLVEPNA IPQINEEGDE 430 440 450 460 470 480 EVGHESKSLF RGLRDYNPIA SSICHLTNAS GTRQSEIYGL GFGGLIVTNQ HLFKRNDGEL 490 500 510 520 530 540 TIRSHHGEFV VKDTKTLKLL PCKGRDIIII RLPKDFPPFP RRLQFRTPTA EDRVCLIGSN 550 560 570 580 590 600 FQTKSVSSTM SETSATYPVD NSHFWKHWIS TKDGHCGLPI VSTRDGSILG LHSLANSTNT 610 620 630 640 650 660 QNFYAAFPDN FETTYLANQD NDNWIKQWRY NPDEVCWGSL QLKRDVPQSP FTICKLLTDL 670 680 690 700 710 720 DGEFVYNQAK TTHWLRDKLE GNLKAVGACP GQLVTKHVVK GKCTLFETYL LTHPEEREFF 730 740 750 760 770 780 QPLMGAYQKS ALNKDAYVKD LMKYSKSIVV GAVDCEQFER AVDVVISMLI SKGFSECSYV 790 800 810 820 830 840 TDPEEIFSAL NMKAAVGALY SGKKRDYFKD TSELEKEEFV RASCKRLFMG KKGVWNGSLK 850 860 870 880 890 900 AELRPKEKVE ANKTRSFTAA PIDTLLGGKV CVDDFNNQFY SLNLHCPWSV GMTKFRGGWD 910 920 930 940 950 960 KLLRALPDGW IYCDADGSQF DSSLSPYLIN AVLNIRLAFM EEWDIGEQML SNLYTEIVYT 970 980 990 1000 1010 1020 PIATPDGTIV KKFKGNNSGQ PSTVVDNTLM VILAMTYSLL KLGYHPDTHE CICRYFVNGD 1030 1040 1050 1060 1070 1080 DLVLAVHPAY ESIYDELQHH FSQLGLNYTF TTKTENKEDL WFMSHKGIMC EGMYIPKLEP 1090 1100 1110 1120 1130 1140 ERIVSILEWD RSSEPIHRLE AICASMVEAW GYKELLREIR KFYSWVLEQA PYNALSKDGK 1150 1160 1170 1180 1190 1200 APYIAETALK KLYTDTEASE TEIERYLEAF YSNLTDEDES NVVVHQADEK EDDEEEVDAG 1210 1220 1230 1240 1250 1260 RPLVTTTQQP IVTTTTQQTP ITSTTLQATQ AMFNPIFTPA TTEPTTRTVP HTTTTTPPSF 1270 1280 1290 1300 1310 1320 GVIGNEDTAP NASNAVVRTG RDRDVDAGSI GTFTVPRLKA MTSKLSLPKV KGKAIMNLNH 1330 1340 1350 1360 1370 1380 LAFYSPAQVD LSNTRAPQSC FQTWYEGVRR DYDVTDDEMS IILNGLMVWC IENGTSPNIN 1390 1400 1410 1420 1430 1440 GMWVMMDGET QVEYPIKPLL DHAKPTFRQI MAHFSNVAEA YIEKRNYEKA YMPRYGIQRN 1450 1460 1470 1480 1490 1500 LTDYSLARYA FDFYEMTSTT PVRAREAHIQ MKAAALRNAQ NRLFGLDGNV GTQEEDTERH 1510 TAGDVNRNMH NLLGMRGV

References

[1]	"Nucleotide sequence of the 3'-terminal region of the RNA of the El Amar strain of plum pox potyvirus." Wetzel T., Candresse T., Ravelonandro M., Delbos R.P., Mazyad H., Aboul-Ata A.E., Dunez J. J. Gen. Virol. 72:1741-1746(1991) [PubMed: 1856701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Potyvirus proteins: a wealth of functions." Urcuqui-Inchima S., Haenni A.L., Bernardi F. Virus Res. 74:157-175(2001) [PubMed: 11226583] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56258 mRNA. Translation: CAA39698.1.
PIR	PQ0221.
3D structure databases
SMR	Q01681. Positions 434-647.
ModBase	Search...
Family and domain databases
InterPro	IPR001730. Peptidase_C4. IPR001592. Poty_coat. IPR013648. PP_Potyviridae. IPR001205. RNA-dir_pol_picornavirus. IPR007094. RNA-dir_pol_PSvirus. IPR009003. Ser/Cys_Pept_Trypsin-like. [Graphical view]
Pfam	PF00863. Peptidase_C4. 1 hit. PF00767. Poty_coat. 1 hit. PF08440. Poty_PP. 1 hit. PF00680. RdRP_1. 1 hit. [Graphical view]
PRINTS	PR00966. NIAPOTYPTASE.
PROSITE	PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_PPVEA

Accession

Primary (citable) accession number: Q01681

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 19, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)