yippee interacting protein 3, isoform A [Drosophila melanogaster]
Protein Classification
Ntn hydrolase family protein( domain architecture ID 307)
Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Ntn_hydrolase super family | cl00467 | The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ... |
14-155 | 1.87e-09 | ||||
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences. The actual alignment was detected with superfamily member cd01906: Pssm-ID: 469781 Cd Length: 182 Bit Score: 54.42 E-value: 1.87e-09
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| Name | Accession | Description | Interval | E-value | ||||
| proteasome_protease_HslV | cd01906 | proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ... |
14-155 | 1.87e-09 | ||||
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide. Pssm-ID: 238887 Cd Length: 182 Bit Score: 54.42 E-value: 1.87e-09
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| Proteasome | pfam00227 | Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ... |
14-155 | 4.55e-08 | ||||
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH). Pssm-ID: 459721 [Multi-domain] Cd Length: 188 Bit Score: 50.64 E-value: 4.55e-08
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| Name | Accession | Description | Interval | E-value | ||||
| proteasome_protease_HslV | cd01906 | proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ... |
14-155 | 1.87e-09 | ||||
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide. Pssm-ID: 238887 Cd Length: 182 Bit Score: 54.42 E-value: 1.87e-09
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| Proteasome | pfam00227 | Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ... |
14-155 | 4.55e-08 | ||||
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH). Pssm-ID: 459721 [Multi-domain] Cd Length: 188 Bit Score: 50.64 E-value: 4.55e-08
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| Ntn_hydrolase | cd01901 | The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ... |
12-155 | 6.44e-08 | ||||
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences. Pssm-ID: 238884 [Multi-domain] Cd Length: 164 Bit Score: 50.09 E-value: 6.44e-08
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| proteasome_alpha | cd01911 | proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ... |
15-171 | 3.91e-07 | ||||
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each. Pssm-ID: 238892 [Multi-domain] Cd Length: 209 Bit Score: 48.21 E-value: 3.91e-07
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| proteasome_beta_type_7 | cd03763 | proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ... |
14-155 | 3.67e-05 | ||||
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each. Pssm-ID: 239732 Cd Length: 189 Bit Score: 42.57 E-value: 3.67e-05
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| proteasome_beta | cd01912 | proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ... |
14-155 | 6.94e-05 | ||||
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each. Pssm-ID: 238893 Cd Length: 189 Bit Score: 41.66 E-value: 6.94e-05
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| Blast search parameters | ||||
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