acyloxyacyl hydrolase isoform X6 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
SGNH_hydrolase super family | cl01053 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ... |
243-282 | 1.45e-18 | ||
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. The actual alignment was detected with superfamily member cd01826: Pssm-ID: 470049 Cd Length: 305 Bit Score: 84.77 E-value: 1.45e-18
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SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
39-113 | 7.19e-12 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 60.20 E-value: 7.19e-12
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Cu-binding_MopE | pfam11617 | Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ... |
204-232 | 9.18e-05 | ||
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions. : Pssm-ID: 463309 [Multi-domain] Cd Length: 28 Bit Score: 39.02 E-value: 9.18e-05
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Name | Accession | Description | Interval | E-value | ||
acyloxyacyl_hydrolase_like | cd01826 | Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ... |
243-282 | 1.45e-18 | ||
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides. Pssm-ID: 238864 Cd Length: 305 Bit Score: 84.77 E-value: 1.45e-18
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SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
39-113 | 7.19e-12 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 60.20 E-value: 7.19e-12
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Cu-binding_MopE | pfam11617 | Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ... |
204-232 | 9.18e-05 | ||
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions. Pssm-ID: 463309 [Multi-domain] Cd Length: 28 Bit Score: 39.02 E-value: 9.18e-05
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SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
82-113 | 4.70e-04 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 37.17 E-value: 4.70e-04
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Name | Accession | Description | Interval | E-value | ||
acyloxyacyl_hydrolase_like | cd01826 | Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ... |
243-282 | 1.45e-18 | ||
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides. Pssm-ID: 238864 Cd Length: 305 Bit Score: 84.77 E-value: 1.45e-18
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SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
39-113 | 7.19e-12 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 60.20 E-value: 7.19e-12
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Cu-binding_MopE | pfam11617 | Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ... |
204-232 | 9.18e-05 | ||
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions. Pssm-ID: 463309 [Multi-domain] Cd Length: 28 Bit Score: 39.02 E-value: 9.18e-05
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SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
82-113 | 4.70e-04 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 37.17 E-value: 4.70e-04
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Blast search parameters | ||||
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