IPR008969
Carboxypeptidase-like, regulatory domain superfamily
InterPro entry
Short name | CarboxyPept-like_regulatory |
Overlapping entries |
Description
This domain superfamily identifies a number of eukaryotic carboxypeptidases, these include carboxypeptidase D, E (H), N, X, X2 and Z. These are metallopeptidases belong to MEROPS peptidase family M14 (clan MC), subfamily M14B.
Carboxypeptidase D (CPD) is a new B-type metallocarboxypeptidase that is membrane bound and has an acidic pH optimum. A hydrophobic region at the N terminus represents the signal peptide, and one near the C terminus that probably represents the transmembrane anchor. A regulatory domain within the protein has been identified as a β-sandwich, comprising 7 strands in 2 sheets in a greek-key topology. Some family members have an additional 1-2 strands to the common fold
[1].
The bacterial and archaeal sequences having this signature are variously annotated, examples are:
* Hypothetical/conserved/membrane/cell surface protein
* N-acetylglucosamine deacetylase
* Side tail fibre protein homologue from lambdoid prophage Rac
* Hypothetical tonB-linked outer membrane receptor
* OmpA-related protein
* Putative outer membrane protein, probably involved in nutrient binding
* TonB-dependent receptor
This entry also includes the teneurin family members, which may function as cellular signal transducers.
References
1.Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation. Haucke V, Wenk MR, Chapman ER, Farsad K, De Camilli P. EMBO J. 19, 6011-9, (2000). View articlePMID: 11080148
Cross References
Contributing Member Database Entry
- SUPERFAMILY:SSF49464