Reviewed, UniProtKB/Swiss-Prot P18478 (POLG_WMV2U)

Names and origin

Protein names	Recommended name:     Genome polyprotein Cleaved into the following 3 chains:     1- 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     2- Recommended name:             Nuclear inclusion protein B                 Short name=NI-B                 Short name=NIB               EC=2.7.7.48         Alternative name(s):             RNA-directed RNA polymerase     3- Recommended name:             Coat protein                 Short name=CP
Organism	Watermelon mosaic virus II (isolate USA)
Taxonomic identifier	148360 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus
Virus host	Citrullus lanatus (Watermelon) (Citrullus vulgaris) [TaxID: 3654] Cucumis melo (Muskmelon) [TaxID: 3656] Cucumis sativus (Cucumber) [TaxID: 3659] Cucurbita pepo (Vegetable marrow) (Summer squash) [TaxID: 3663]

Protein attributes

Sequence length	1017 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nuclear inclusion protein B is a RNA-dependent RNA polymerase that plays an essential role in the virus 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	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.
Biotechnological use	The gene for the coat protein is introduced by genetic manipulation and expressed in squash so as to obtain virus resistant plants.
Miscellaneous	Readthrough of a terminator codon TGA occurs between codons for Ala-267 and Gln-269.
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
Technical term	Genetically modified food
Gene Ontology (GO)
Biological process	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 nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 219	›219	Nuclear inclusion protein A By similarity		PRO_0000040497
	Chain	220 – 736	517	Nuclear inclusion protein B By similarity		PRO_0000040498
	Chain	737 – 1017	281	Coat protein By similarity		PRO_0000040499
Regions
	Domain	461 – 585	125	RdRp catalytic
Sites
	Active site	57	1	For nuclear inclusion protein A activity By similarity
	Active site	127	1	For nuclear inclusion protein A activity By similarity
	Site	219 – 220	2	Cleavage; by NIa-pro By similarity
	Site	736 – 737	2	Cleavage; by NIa-pro By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P18478-1 [UniParc]. Last modified September 5, 2006. Version 3. Checksum: 8853B6411C871E2E	FASTA	1,017	115,489
	10 20 30 40 50 60 LSVTRKQCLE LGMVLSLSPM GTYLEGTMGC LQLKHGHGGF VIHNTTQLRI HFIQGKDAIL 70 80 90 100 110 120 IRMPKIFLRL QSATSLDNQN VRNEFAWLEQ TFKRRAYGQQ SQSSSIILPE GKGSFWIHWI 130 140 150 160 170 180 TTQDGFCGLP LVSVNDGHVV GIHGLTSNDS EKNFFVPFTD GFEKEYLDNA DNLSWDKHWF 190 200 210 220 230 240 WEPSKIAWGP LNLVEEQPKE EFKISKLVSD LFGNTVAVQS RKERWVLDAM EGNLVACGQA 250 260 270 280 290 300 DSALVTKHVV KGKCPYFAQY LSLHDGAXQF FEPLMGAYQP SRLNKDAFKK DFFKYNKPVV 310 320 330 340 350 360 LNEVDFNAFE KAVEGVITMM VDFEFAECLF VTDPDEIYGS LNMKAAVGAQ YKGKKQDYFS 370 380 390 400 410 420 GMDSFDKERL LYLSCERLFN GEKGIWNGSL KAELRPIEKV QANKTRTFTA APLDTLLGAK 430 440 450 460 470 480 VCVDDFNNQF YSFNLKCPWT VGMTKFYGGW DKLMRSLPDG WTYCHADGSQ FDSSLTPLLL 490 500 510 520 530 540 NAVLSIRCCF MEDWWVGREM LENLYAEIVY TPILAPDGTI FKKFRGNNSG QPSTVVDNTL 550 560 570 580 590 600 MVVIAMYYSC CKQGWSEEDI ERRLVFFANG DDIILAVKDE DVWLYDTLSA SFAELGLNYN 610 620 630 640 650 660 FDERTKKREE LWFMSHQAML VDGIYIPKLE PERIVSILEW DRSKELMHRT EAICAAMIEA 670 680 690 700 710 720 WGYTELLQEI RKFYLWLLSK DEFKELAASG KAPYIAETAL RKLYTDVNTQ PSELQRYLEV 730 740 750 760 770 780 LDFNHIDGCC ESVSLQSGKE TVENLDAGKE SKKDASDKGN KPQNSQVGQG SKEPTKTGTV 790 800 810 820 830 840 SKDVNVGSKG KEVPRLQKIT KKMNLPTVGG KIILSLDHLL EYKPSQVDLF NTRATKTQFE 850 860 870 880 890 900 SWYSAVKVEY DLNDEQMGVI MNGFMVWCID NGTSPDVNGV WVMMDGEEQV EYPLKPIVEN 910 920 930 940 950 960 AKPTLRQIMH HFSDAAEAYI EMRNSESPYM PRYGLLRNLR DRELARYAFD FYEVTSKTPN 970 980 990 1000 1010 RAREAIAQMK AAALAGVNSR LFGLDGNIST NSENTGRHTA RDVNQNMHTL LGMGPPQ

References

[1]	Slightom J.L. Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Watermelon mosaic virus II and zucchini yellow mosaic virus: cloning of 3'-terminal regions, nucleotide sequences, and phylogenetic comparisons." Quemada H., Sieu L.C., Siemieniak D.R., Gonsalves D., Slightom J.L. J. Gen. Virol. 71:1451-1460(1990) [PubMed: 2374006] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 736-1016.
[3]	"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
EMBLGenBankDDBJ	D13913 Genomic RNA. Translation: BAA03009.2.
PIR	JQ0498.
3D structure databases
HSSP	HSSP built from PDB template 1LVM based on UniProtKB P04517.
ModBase	Search...
Family and domain databases
InterPro	IPR001730. Peptidase_C4. IPR001592. Poty_coat. IPR001205. RNA-dir_pol_picornavirus. IPR007094. RNA-dir_pol_PSvirus. [Graphical view]
Pfam	PF00863. Peptidase_C4. 1 hit. PF00767. Poty_coat. 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_WMV2U

Accession

Primary (citable) accession number: P18478

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	September 5, 2006
Last modified:	October 13, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)