aminopeptidase P family protein (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 ...
372-536
2.89e-92
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 cd01085:
Pssm-ID: 469704 [Multi-domain] Cd Length: 224 Bit Score: 283.30 E-value: 2.89e-92
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
53-197
1.71e-09
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.
The actual alignment was detected with superfamily member pfam01321:
Pssm-ID: 480631 Cd Length: 128 Bit Score: 56.16 E-value: 1.71e-09
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
372-536
2.89e-92
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: 283.30 E-value: 2.89e-92
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
371-529
1.49e-35
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: 132.75 E-value: 1.49e-35
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
53-197
1.71e-09
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.
Pssm-ID: 460159 Cd Length: 128 Bit Score: 56.16 E-value: 1.71e-09
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
372-536
2.89e-92
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: 283.30 E-value: 2.89e-92
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
371-529
1.49e-35
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: 132.75 E-value: 1.49e-35
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
371-529
4.93e-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.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 80.19 E-value: 4.93e-17
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
376-527
7.16e-17
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: 79.48 E-value: 7.16e-17
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
53-197
1.71e-09
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.
Pssm-ID: 460159 Cd Length: 128 Bit Score: 56.16 E-value: 1.71e-09
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
411-503
3.22e-07
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: 51.80 E-value: 3.22e-07
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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