GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ADE02:PRO

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2). (10515)
Gene Name(s) No Information Provided.
Protein Name(s) Protease

Adenain Adenovirus protease AVP Adenovirus proteinase Endoprotease

External Links
UniProt P03252
EMBL J01917
PIR A03823
RefSeq AP_000176.1
NP_040526.1
PDB 1AVP
1NLN
4EKF
4PID
4PIE
PDBsum 1AVP
1NLN
4EKF
4PID
4PIE
ProteinModelPortal P03252
SMR P03252
MEROPS C05.001
GeneID 2652998
EvolutionaryTrace P03252
Proteomes UP000008167
GO GO:0042025
GO:0019012
GO:0004197
GO:0008234
GO:0003677
Gene3D 3.40.395.10
InterPro IPR000855
Pfam PF00770
PIRSF PIRSF001218
PRINTS PR00703
ProDom PD003705

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008234

cysteine-type peptidase activity

PMID:12758141[1]

ECO:0000314

F

As seen in figure 5, AVP activity exhibited a complex sensitivity to carboxamidomethylation as a function of pH. One cysteine had a pKa of about 4.3. The most likely candidate for the low pKa is the conserved residue Cys122.

Since five of the eight cysteines of AVP are buried in the interior of the molecule, the most likely candidate to be alkylated was one of the three cysteines found on the surface. Cys199 is only found in human adenovirus serotypes 2 and 5; it is located in a region of the molecule distant from either the pVIc binding site or the active site groove. Furthermore, mutation of Cys199 to Ser199 had no effect on enzyme activity (Brown and Mangel, unpublished). In the AVP–pVIc complex, Cys104 forms a disulfide bond with Cys10 of pVIc. Thus, there is now considerable evidence that Cys122 is the active site nucleophile of human adenovirus serotype 2 proteinase; this amino acid residue is conserved in all adenovirus serotypes.

complete
CACAO 6541

enables

GO:0008234

cysteine-type peptidase activity

PMID:12758141[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004197

cysteine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000855

F

Seeded From UniProt

complete

GO:0097282

immunoglobulin-mediated neutralization

PMID:22623776[2]

ECO:0000314

P

fig 4 shows neutralization

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000855

P

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000523799

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000523799

F

Seeded From UniProt

complete

enables

GO:0004197

cysteine-type endopeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000523799

F

Seeded From UniProt

complete

enables

GO:0008234

cysteine-type peptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000523799

F

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000523799

C

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0946
UniProtKB-SubCell:SL-0274

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008234

cysteine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0788

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1048
UniProtKB-SubCell:SL-0414

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 McGrath, WJ et al. (2003) Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold. Biochim. Biophys. Acta 1648 1-11 PubMed GONUTS page
  2. Qiu, H et al. (2012) Serotype-specific neutralizing antibody epitopes of human adenovirus type 3 (HAdV-3) and HAdV-7 reside in multiple hexon hypervariable regions. J. Virol. 86 7964-75 PubMed GONUTS page