P08490 (POLG_ECHO9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 2 chains: Protein 3B Short name=P3B Alternative name(s): VPg Picornain 3C EC=3.4.22.28 Alternative name(s): Protease 3C Short name=P3C
Organism	Echo 9 virus (EV-9) (Coxsackievirus A23)
Taxonomic identifier	12060 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Human enterovirus B
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	205 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	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. Picornain 3C: Host cytoplasm Potential.
Post-translational modification	Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced By similarity. VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Sequence similarities	Belongs to the picornaviruses polyprotein family. Contains 1 peptidase C3 domain.

Ontologies

Keywords
Biological process	Host-virus interaction Initiation of viral infection Viral attachment to host cell
Cellular component	Host cytoplasm Virion
Ligand	RNA-binding
Molecular function	Hydrolase Protease Thiol protease
PTM	Covalent protein-RNA linkage Phosphoprotein
Gene Ontology (GO)
Biological process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase 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 – 22	22	Protein 3B Potential		PRO_0000039547
	Chain	23 – 205	183	Picornain 3C Potential		PRO_0000039548
Sites
	Active site	62	1	For picornain 3C activity Potential
	Active site	93	1	For picornain 3C activity Potential
	Active site	169	1	For picornain 3C activity Potential
	Site	22 – 23	2	Cleavage; by picornain 3C Potential
Amino acid modifications
	Modified residue	3	1	O-(5'-phospho-RNA)-tyrosine By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	205	1

Sequences

	Sequence		Length	Mass (Da)
	P08490 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 6C3F0490E5DAC78E	FASTA	205	22,716
	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

References

[1]

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12165 Genomic RNA. Translation: AAA42979.1. M12167 Genomic RNA. Translation: AAA42978.1.
3D structure databases
ProteinModelPortal	P08490.
SMR	P08490. Positions 23-205.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR009003. Pept_cys/ser_Trypsin-like. IPR000199. Peptidase_C3A/C3B_picornavir. [Graphical view]
Pfam	PF00548. Peptidase_C3. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
ProtoNet	Search...

Entry information

Entry name

POLG_ECHO9

Accession

Primary (citable) accession number: P08490

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program