Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682715    60 SNVKVILNGGQKI--TFLRPDGYFTFHEVPAGTHLIEVSAMGYFFSPVRVDVS-ARHRGKVQATLTETRRS--------- 127
Cdd:pfam09430   7 SNTRVTLDGGLHHfeVPVRRDGSFVFRDVPEGSYVLDVESPGYRFEPYRVDVTgKGKANAVKVTYVETYEVnpvfgkgnl 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 30682715   128 -LTELVLEPLKEEQYYEIREPFNIMSIVKSPM 158
Cdd:pfam09430  87 eSYPLVIKPVGPHDYFEPREKFSITDLLKSPM 118

ER membrane protein complex subunit 7, beta-sandwich domain; This is the beta-sandwich domain found in ER membrane protein complex subunit 7 (EMC7), which is an integral membrane component of the EMC. EMC is widely conserved and involved in membrane protein biogenesis. It mediates the insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins in an energy-independent manner, both post-translational insertions of tail-anchored proteins and co-translational insertion of multipass membrane proteins. This entry includes UPF0620 protein C83.10 from S. pombe, an orthologue of animal EMC7. This domain is also found in nodal modulators, which have been identified as part of a protein complex that participates in the nodal signalling pathway during vertebrate development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682715    60 SNVKVILNGGQKI--TFLRPDGYFTFHEVPAGTHLIEVSAMGYFFSPVRVDVS-ARHRGKVQATLTETRRS--------- 127
Cdd:pfam09430   7 SNTRVTLDGGLHHfeVPVRRDGSFVFRDVPEGSYVLDVESPGYRFEPYRVDVTgKGKANAVKVTYVETYEVnpvfgkgnl 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 30682715   128 -LTELVLEPLKEEQYYEIREPFNIMSIVKSPM 158
Cdd:pfam09430  87 eSYPLVIKPVGPHDYFEPREKFSITDLLKSPM 118

ER membrane protein complex subunit 7, beta-sandwich domain; This is the beta-sandwich domain found in ER membrane protein complex subunit 7 (EMC7), which is an integral membrane component of the EMC. EMC is widely conserved and involved in membrane protein biogenesis. It mediates the insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins in an energy-independent manner, both post-translational insertions of tail-anchored proteins and co-translational insertion of multipass membrane proteins. This entry includes UPF0620 protein C83.10 from S. pombe, an orthologue of animal EMC7. This domain is also found in nodal modulators, which have been identified as part of a protein complex that participates in the nodal signalling pathway during vertebrate development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682715    60 SNVKVILNGGQKI--TFLRPDGYFTFHEVPAGTHLIEVSAMGYFFSPVRVDVS-ARHRGKVQATLTETRRS--------- 127
Cdd:pfam09430   7 SNTRVTLDGGLHHfeVPVRRDGSFVFRDVPEGSYVLDVESPGYRFEPYRVDVTgKGKANAVKVTYVETYEVnpvfgkgnl 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 30682715   128 -LTELVLEPLKEEQYYEIREPFNIMSIVKSPM 158
Cdd:pfam09430  87 eSYPLVIKPVGPHDYFEPREKFSITDLLKSPM 118

CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682715    41 ITGRVKIPPSN--VIGhiakfsnVKVILNGGQKITFLRPDGYFTFHEVPAGTHLIEVSAMGYFFSPVRVDVSARHRGKVQ 118
Cdd:pfam13715   1 ISGTVVDENTGepLPG-------ATVYVKGTTKGTVTDADGNFELKNLPAGTYTLVVSFVGYKTQEKKVTVSNDNTLDVN 73

                          90
                  ....*....|....
gi 30682715   119 ATLTETRRSLTELV 132
Cdd:pfam13715  74 FLLKEDALLLDEVV 87