aminopeptidase family protein P (metallopeptidase M24) 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 ...
190-429
2.67e-85
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: 261.35 E-value: 2.67e-85
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
20-151
2.92e-22
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: 91.42 E-value: 2.92e-22
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
190-429
2.67e-85
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: 261.35 E-value: 2.67e-85
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
193-420
8.28e-37
Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.
Pssm-ID: 459852 [Multi-domain] Cd Length: 208 Bit Score: 133.91 E-value: 8.28e-37
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
20-151
2.92e-22
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: 91.42 E-value: 2.92e-22
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
15-158
6.63e-20
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: 85.37 E-value: 6.63e-20
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
190-429
2.67e-85
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: 261.35 E-value: 2.67e-85
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
193-420
8.28e-37
Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.
Pssm-ID: 459852 [Multi-domain] Cd Length: 208 Bit Score: 133.91 E-value: 8.28e-37
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
20-151
2.92e-22
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: 91.42 E-value: 2.92e-22
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
193-422
5.53e-22
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: 93.29 E-value: 5.53e-22
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
217-422
1.66e-20
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.
Pssm-ID: 238525 [Multi-domain] Cd Length: 208 Bit Score: 89.11 E-value: 1.66e-20
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
15-158
6.63e-20
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: 85.37 E-value: 6.63e-20
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
238-312
2.05e-03
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.
Pssm-ID: 238524 [Multi-domain] Cd Length: 243 Bit Score: 39.64 E-value: 2.05e-03
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
360-422
3.80e-03
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.
Pssm-ID: 238518 [Multi-domain] Cd Length: 224 Bit Score: 38.70 E-value: 3.80e-03
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.
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