NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3512851 [NCBI, ExPASy, EBI, Israel, Japan]
Werner G., Rosenwirt B., Bauer E., Seifert J.-M., Werner F.-J., Besemer J.;
"Molecular cloning and sequence determination of the genomic regions encoding protease and genome-linked protein of three picornaviruses.";
J. Virol. 57:1084-1093(1986).

Comments

FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced (By similarity).
PTM: VPg is covalently linked to the genomic RNA (By similarity).
SIMILARITY: Belongs to the picornaviruses polyprotein family.
SIMILARITY: Contains 1 peptidase C3 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M12165; AAA42979.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12167; AAA42978.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P03300; 1L1N. [HSSP ENTRY / PDB]

ModBase

P08490.

Protein family/group databases

MEROPS

C03.011; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0019012;	Cellular component: virion (inferred from electronic annotation from UniProtKB-KW).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0018144;	Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000199; Pept_C3_picorn.
Graphical view of domain structure.

Pfam

PF00548; Peptidase_C3; 1.
Pfam graphical view of domain structure.

ProDom

PD001125; Pept_C3_picorn; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

ProtoNet

P08490.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Covalent protein-RNA linkage; Cytoplasm; Hydrolase; Phosphoprotein; Protease; RNA-binding; Thiol protease; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 22`	`22`	`Protein 3B (Potential).`	`PRO_0000039547`
`CHAIN`	`23 205`	`183`	`Picornain 3C (Potential).`	`PRO_0000039548`
`ACT_SITE`	`62 62`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`93 93`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`169 169`		`For picornain 3C activity (Potential).`
`SITE`	`22 23`	`2`	`Cleavage; by picornain 3C (Potential).`
`MOD_RES`	`3 3`		`O-(5'-phospho-RNA)-tyrosine (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`205 205`

Sequence information

Length: 205 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 22716 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 6C3F0490E5DAC78E [This is a checksum on the sequence]

        10         20         30         40         50         60 
GAYTGMPNKK PKVPTLRQAK VQGPAFEFAV AMMKRNASTV KTEYGEFTML GIYDRWAVLP 

        70         80         90        100        110        120 
RHAKPGPSIL MNDQEVGVLD AKELVDKDGI NLELTLLKLN RNEKFRDIRG FLAREEVEVN 

       130        140        150        160        170        180 
EAVLAINTSK FPNMYIPVGQ VTDYGFLNLG GTPTKRMLMY NFPTRAGQCG GVLMSTGKVL 

       190        200 
GIHVGGNGHH GFSAALLRHY FNEEQ

P08490 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools