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Links from Protein

Items: 7

1.

Activating protease CtpB N-terminal domain

This domain is found N-terminal in Carboxy-terminal processing protease CtpB and related proteins. This enzyme is involved in signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. This domain contains auto-cleavage site at which it is proteolytically cleaved. The remaining part in the mature enzyme is involved in dimerisation [1]. Paper describing PDB structure 4c2c. [1]. 24243021. CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis. Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T;. Cell. 2013;155:647-658. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046799.1
Method:
HMM
2.

PDZ domain-containing protein

This entry represents the PDZ domain from a wide variety of proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF036497.5
Method:
HMM
3.

PDZ domain-containing protein

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Date:
2024-08-14
Family Accession:
NF024578.5
Method:
HMM
4.

S41 family peptidase

The serine endopeptidases in this family include C-terminal processing proteases such as the periplasmic protease Prc from Escherichia coli, involved in processing penicillin-binding protein (PBP) 3, and carboxyl-terminal processing protease CtpA from Pseudomonas aeruginosa.

GO Terms:
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
serine-type peptidase activity (GO:0008236)
Date:
2024-08-14
Family Accession:
NF015531.5
Method:
HMM
5.

PDZ domain-containing protein

PDZ domains are found in diverse signaling proteins. Review article. [1]. 9204764. PDZ domains: targeting signalling molecules to sub-membranous sites. Ponting CP, Phillips C, Davies KE, Blake DJ. Bioessays 1997;19:469-479. [2]. 8674113. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R;. Cell. 1996;85:1067-1076. Extension of PDZ family. [3]. 9041651. Evidence for PDZ domains in bacteria, yeast, and plants. Ponting CP;. Protein Sci 1997;6:464-468. [4]. 19738200. Rapid evolution of functional complexity in a domain family. Ernst A, Sazinsky SL, Hui S, Currell B, Dharsee M, Seshagiri S, Bader GD, Sidhu SS;. Sci Signal. 2009;2:ra50. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Date:
2024-10-16
Family Accession:
NF012803.5
Method:
HMM
6.

S41 family peptidase

S41 family peptidase is a serine endopeptidase similar to Bartonella bacilliformis carboxy-terminal-processing protease that shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, and cleaves at a variable distance from the C-terminus

Date:
2024-07-10
Family Accession:
11435057
Method:
Sparcle
7.

C-terminal processing peptidase

Carboxy-terminal processing proteases (EC 3.4.21.102) have paralogs in some species, and different gene symbols in different lineages, such as prc in Escherichia coli K-12, ctpA, ctpB, and ctpC in Synechocystis sp. PCC 6803, and cptA and ctpB in Bacillus subtilis.

GO Terms:
Molecular Function:
serine-type endopeptidase activity (GO:0004252)
Biological Process:
proteolysis (GO:0006508)
Date:
2023-10-20
Family Accession:
TIGR00225.1
Method:
HMM
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