M24 family metallopeptidase cleaves amido-, imido-, or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
259-468
1.02e-17
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
The actual alignment was detected with superfamily member cd01087:
Pssm-ID: 469704 [Multi-domain] Cd Length: 243 Bit Score: 82.62 E-value: 1.02e-17
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
106-223
1.01e-15
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
The actual alignment was detected with superfamily member smart01011:
Pssm-ID: 198079 Cd Length: 135 Bit Score: 73.81 E-value: 1.01e-15
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
259-468
1.02e-17
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.
Pssm-ID: 238520 [Multi-domain] Cd Length: 243 Bit Score: 82.62 E-value: 1.02e-17
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
106-223
1.01e-15
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
Pssm-ID: 198079 Cd Length: 135 Bit Score: 73.81 E-value: 1.01e-15
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
123-173
3.69e-10
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.
Pssm-ID: 461581 [Multi-domain] Cd Length: 121 Bit Score: 57.52 E-value: 3.69e-10
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
259-468
1.02e-17
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.
Pssm-ID: 238520 [Multi-domain] Cd Length: 243 Bit Score: 82.62 E-value: 1.02e-17
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
106-223
1.01e-15
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
Pssm-ID: 198079 Cd Length: 135 Bit Score: 73.81 E-value: 1.01e-15
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
269-481
8.25e-12
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 64.40 E-value: 8.25e-12
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
123-173
3.69e-10
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.
Pssm-ID: 461581 [Multi-domain] Cd Length: 121 Bit Score: 57.52 E-value: 3.69e-10
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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