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Links from Protein

Items: 12

1.

Middle or third domain of peptidase_M16

Peptidase_M16_M is the third domain of peptidase_M16 in eukaryotes of the insulin-degrading-enzyme type. Insulin-degrading enzymes - insulysin - are zinc metallopeptidases that metabolise several bioactive peptides, including insulin and the amyloid-beta-peptide. The tertiary structure of insulin-degrading enzymes resembles a clamshell composed of four structurally similar domains arranged to enclose a large central chamber. Substrates must enter the chamber, and it is likely that a hinge-like conformational change allows substrate binding and product release. Triphosphates are found to dock between the inner surfaces of the non-catalytic domains three and four [1]. [1]. 22049080. Anion activation site of insulin-degrading enzyme. Noinaj N, Song ES, Bhasin S, Alper BJ, Schmidt WK, Hersh LB, Rodgers DW;. J Biol Chem. 2012;287:48-57. (from Pfam)

Date:
2024-10-16
Family Accession:
NF027513.5
Method:
HMM
2.

PQQ synthase PqqF-like, C-terminal lobe domain 4

This entry represents domain 4 from the C-terminal lobe of PQQ synthase PqqF, a protein required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. It consists of four structurally similar domains organised in N-terminal (domain 1 represented in Pfam: PF00675 and domain 2 in Pfam:PF22454) and C-terminal (domain 3 and domain 4) lobes [1]. This domain is also found in other Peptidase M16 members, such as Nardilysin and insulin degrading enzymes from human. [1]. 27231346. Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway. Wei Q, Ran T, Ma C, He J, Xu D, Wang W;. J Biol Chem. 2016;291:15575-15587. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046284.1
Method:
HMM
3.

insulinase family protein

Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp [1]. [1]. 11470436. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J;. Structure (Camb) 2001;9:615-625. (from Pfam)

Date:
2024-10-16
Family Accession:
NF017044.5
Method:
HMM
4.

insulinase family protein

Date:
2024-08-14
Family Accession:
NF012879.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.

insulinase family protein

insulinase family protein (peptidase M16) similar to pitrilysin is a zinc-dependent peptidase that cleaves small peptides close to a terminus, often including bonds on the amino side of basic residues such as arginine

Date:
2017-11-13
Family Accession:
11487641
Method:
Sparcle
12.

pitrilysin

Gene:
ptrA
GO Terms:
Molecular Function:
metalloendopeptidase activity (GO:0004222)
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
metal ion binding (GO:0046872)
Date:
2021-08-25
Family Accession:
NF011681.0
Method:
HMM
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