Putative endoplasmic reticulum metallopeptidase 1-A [Caenorhabditis elegans]
Protein Classification
M28 family metallopeptidase( domain architecture ID 10133732)
M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; similar to Homo sapiens endoplasmic reticulum metallopeptidase 1 that is required for the organization of somatic cells and oocytes into discrete follicular structures
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| M28_Fxna_like | cd03875 | M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
71-382 | 9.51e-141 | |||||
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown. : Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 420.07 E-value: 9.51e-141
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| Name | Accession | Description | Interval | E-value | |||||
| M28_Fxna_like | cd03875 | M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
71-382 | 9.51e-141 | |||||
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown. Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 420.07 E-value: 9.51e-141
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| Peptidase_M28 | pfam04389 | Peptidase family M28; |
153-348 | 1.18e-70 | |||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 231.41 E-value: 1.18e-70
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| Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
153-355 | 1.35e-20 | |||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 92.12 E-value: 1.35e-20
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| Name | Accession | Description | Interval | E-value | |||||
| M28_Fxna_like | cd03875 | M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
71-382 | 9.51e-141 | |||||
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown. Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 420.07 E-value: 9.51e-141
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| Peptidase_M28 | pfam04389 | Peptidase family M28; |
153-348 | 1.18e-70 | |||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 231.41 E-value: 1.18e-70
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| M28 | cd02690 | M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
151-349 | 1.65e-37 | |||||
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases. Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 139.40 E-value: 1.65e-37
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| Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
153-355 | 1.35e-20 | |||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 92.12 E-value: 1.35e-20
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
153-253 | 4.15e-08 | |||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 56.43 E-value: 4.15e-08
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| M28_SGAP_like | cd03876 | M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ... |
144-251 | 1.37e-05 | |||||
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures. Pssm-ID: 349873 [Multi-domain] Cd Length: 289 Bit Score: 48.06 E-value: 1.37e-05
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| M28_like_PA | cd05660 | M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
182-275 | 1.97e-05 | |||||
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 47.35 E-value: 1.97e-05
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| M28_QC_like | cd03880 | M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) ... |
150-225 | 1.14e-04 | |||||
M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease. Pssm-ID: 349876 [Multi-domain] Cd Length: 305 Bit Score: 45.31 E-value: 1.14e-04
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| M28_like | cd08015 | M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
153-352 | 5.82e-04 | |||||
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349937 [Multi-domain] Cd Length: 218 Bit Score: 42.20 E-value: 5.82e-04
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| M28_like | cd05640 | M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ... |
152-304 | 7.64e-04 | |||||
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349893 [Multi-domain] Cd Length: 281 Bit Score: 42.44 E-value: 7.64e-04
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| M28_like | cd03877 | M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
182-296 | 1.04e-03 | |||||
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution. Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 41.46 E-value: 1.04e-03
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| M28_like_PA_PDZ_associated | cd05663 | M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ... |
140-296 | 1.08e-03 | |||||
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution. Pssm-ID: 349913 [Multi-domain] Cd Length: 266 Bit Score: 42.06 E-value: 1.08e-03
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| M28_like_PA | cd05661 | M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ... |
153-233 | 1.63e-03 | |||||
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Pssm-ID: 349911 [Multi-domain] Cd Length: 262 Bit Score: 41.40 E-value: 1.63e-03
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| Zinc_peptidase_like | cd03873 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
153-327 | 3.89e-03 | |||||
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 39.72 E-value: 3.89e-03
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| M20_18_42 | cd18669 | M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
153-221 | 4.87e-03 | |||||
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 39.34 E-value: 4.87e-03
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| M28_like | cd05643 | M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ... |
182-355 | 5.56e-03 | |||||
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion. Pssm-ID: 349895 [Multi-domain] Cd Length: 290 Bit Score: 39.70 E-value: 5.56e-03
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