C45 family peptidase similar to Penicillium chrysogenum isopenicillin-N N-acyltransferase that catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
12-324
1.41e-80
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
The actual alignment was detected with superfamily member NF040521:
Pssm-ID: 468523 [Multi-domain] Cd Length: 312 Bit Score: 249.13 E-value: 1.41e-80
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
12-324
1.41e-80
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
Pssm-ID: 468523 [Multi-domain] Cd Length: 312 Bit Score: 249.13 E-value: 1.41e-80
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
92-329
1.70e-33
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.
Pssm-ID: 238910 Cd Length: 229 Bit Score: 124.39 E-value: 1.70e-33
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
12-324
1.41e-80
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
Pssm-ID: 468523 [Multi-domain] Cd Length: 312 Bit Score: 249.13 E-value: 1.41e-80
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
92-329
1.70e-33
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.
Pssm-ID: 238910 Cd Length: 229 Bit Score: 124.39 E-value: 1.70e-33
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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