Pathways & interactions
Carboxypeptidase-like, regulatory domain superfamily (IPR008969)
Short name: CarboxyPept-like_regulatory
- Peptidase S8A, bacillopeptidase F (IPR012103)
- Bacteriophage 933W, L0121, tail fibre, N-terminal (IPR013609)
- TonB-dependent outer membrane protein, SusC/RagA (IPR023996)
- Carboxypeptidase M N-terminal domain (IPR033842)
- Carboxypeptidase E, carboxypeptidase domain (IPR034232)
- Metallocarboxypeptidase Z, carboxypeptidase domain (IPR034239)
- Carboxypeptidase D, carboxypeptidase-like domain 1 (IPR034241)
- AEBP1/CPX, carboxypeptidase domain (IPR034243)
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 beta-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 [PMID: 11080148].
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.
- SSF49464 (SSF49464)