P20234 (POLG_OMV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 4 chains: Viral genome-linked protein Alternative name(s): VPg 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 Nuclear inclusion protein B Short name=NI-B Short name=NIB Alternative name(s): RNA-directed RNA polymerase EC=2.7.7.48 Capsid protein Short name=CP Alternative name(s): Coat protein
Organism	Ornithogalum mosaic virus
Taxonomic identifier	12204 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Potyviridae › Potyvirus
Virus host	Lachenalia [TaxID: 81765] Ornithogalum [TaxID: 51466]

Protein attributes

Sequence length	1136 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Capsid protein: 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: 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	Capsid 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. Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI By similarity.
Sequence similarities	Belongs to the potyviridae genome polyprotein family. Contains 1 peptidase C4 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	Viral RNA replication
Cellular component	Virion
Ligand	Nucleotide-binding
Molecular function	Capsid protein Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro 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 – 122	›122	Viral genome-linked protein By similarity		PRO_0000040291
	Chain	1 – 1136	1136	Genome polyprotein		PRO_0000420002
	Chain	123 – 365	243	Nuclear inclusion protein A By similarity		PRO_0000040292
	Chain	366 – 883	518	Nuclear inclusion protein B By similarity		PRO_0000040293
	Chain	884 – 1136	253	Capsid protein By similarity		PRO_0000040294
Regions
	Domain	123 – 341	219	Peptidase C4
	Domain	607 – 731	125	RdRp catalytic
Sites
	Active site	168	1	For nuclear inclusion protein A activity By similarity
	Active site	203	1	For nuclear inclusion protein A activity By similarity
	Active site	273	1	For nuclear inclusion protein A activity By similarity
	Site	122 – 123	2	Cleavage; by NIa-pro By similarity
	Site	365 – 366	2	Cleavage; by NIa-pro By similarity
	Site	883 – 884	2	Cleavage; by NIa-pro By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P20234 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 0A7AE0527743FD61	FASTA	1,136	128,915
	10 20 30 40 50 60 EYTIVRYVDP LTGATQDENP LMAIDLVQEY FAKIRSQLVS EEKLETQNII ANPGIQAYYM 70 80 90 100 110 120 KNRGDAALKV DLTPHNPLLV TKTGTIAGFP ENEFILRQTG KAVNVKMSEV PVENELEEVE 130 140 150 160 170 180 HEGKNLNRGL RDYNVVSNVV CRLTNESDGH SASLFGLGYG GYIITNRHLF KNNNGTLKVQ 190 200 210 220 230 240 SQHGDFIVKN TTQLKMVPVG KTDILIIRMP KDFPVLPQKL RFRAPANEDK VCLIASNFQE 250 260 270 280 290 300 RYVSSLVSET SSVYPVGNGE FWQHWISTKD GHCGLPLTST KDGFIVGIHS LSTITNSKNF 310 320 330 340 350 360 FASIPANFEE QYLAKLDQQD WTANWKYNPN EVSWNGLRLQ ENKPGRIFQA VKEVSALFSD 370 380 390 400 410 420 AVYEQGQEVG WLFRELKDNL KAVAVLPNQL VTKHVVKGPC QCFIQYLNES PEASAFFKPL 430 440 450 460 470 480 MGQYGKSILS KEAFVKDIMK YSKPIVLGEV DFIKFEEGYN NVLRMFHDIG FEKCEYVTDS 490 500 510 520 530 540 MEVYKNLNLK AAVGAMYTGK KQQYFEGMSE DEIHQLVIAS CFRLWSGKFG VWNGSLKAEL 550 560 570 580 590 600 RPLEKVQACK TRTFTAAPLD TLLGAKVCVD DFNAQFYDKH LTAPWTVGIC KYYKGWDTFM 610 620 630 640 650 660 NKLPEGWLYC DADGSQFDSS LTPFLINSVL RLRLEFMEDW DIGARMLSNL YTEIIYTPIA 670 680 690 700 710 720 TPDGTVVKKF RGNNSGQPST VVDNTLMVVL AMNYALAKLS IPYEEMDSRI RYFANGDDLL 730 740 750 760 770 780 VAVEPTKGGE ILDSLQASFS ELGLIYDFND RTFDKTQLSF MSHQALWDGD MFIPKIKQER 790 800 810 820 830 840 VVSILEWDRS TQPEHRIEAV CAAMIEAWGY PELLQEIRKF YAFMVTQEPY SAIHAQGKTR 850 860 870 880 890 900 YISERALVTL YKDEKVVLSD IGPYIQKLAE MSLGCVDEVV MHQADSMDAG GSSRPPAPLV 910 920 930 940 950 960 RQQDQDVNVG TFSVARVKAL SDKMMLPKVR GKTVLNLQHL VQYNPEQTEI SNTRATRTQF 970 980 990 1000 1010 1020 NNWYDRVRDS YGVTDDQMAV ILNGLMVWCI ENGTSPNLNG NWTMMDGDEQ IEYPLQPVLE 1030 1040 1050 1060 1070 1080 NAQPTFRQIM AHFSNAAEAY IEKRNSEQRY MPRYGSQRNL NDYSLARYAF DFYEMTSRTA 1090 1100 1110 1120 1130 NRAREAHIQM KAAALRNTKT KLFGLDGKVG TEEEDTERHV ASDVNRNMHS LLGVNM

References

[1]	Burger J.T., Brand R.J., Rybicki E.P. Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Potyvirus proteins: a wealth of functions." Urcuqui-Inchima S., Haenni A.L., Bernardi F. Virus Res. 74:157-175(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00615 Genomic RNA. Translation: BAA00490.1.
PIR	JQ0494.
3D structure databases
ProteinModelPortal	P20234.
SMR	P20234. Positions 131-344.
ModBase	Search...
Protein family/group databases
MEROPS	C04.005.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001592. Poty_coat. IPR001730. Potyv_NIa-pro_dom. IPR001205. RNA-dir_pol_C. IPR007094. RNA-dir_pol_PSvirus. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00863. Peptidase_C4. 1 hit. PF00767. Poty_coat. 1 hit. PF00680. RdRP_1. 1 hit. [Graphical view]
PRINTS	PR00966. NIAPOTYPTASE.
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS51436. POTYVIRUS_NIA_PRO. 1 hit. PS50507. RDRP_SSRNA_POS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_OMV

Accession

Primary (citable) accession number: P20234

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program