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Conserved domains on  [gi|1907093819|ref|XP_036013955|]
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acyloxyacyl hydrolase isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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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
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907093819 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVE 282
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSE 40
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093819   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907093819 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
 
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
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907093819 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVE 282
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSE 40
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093819   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907093819 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
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
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907093819  82 CYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:pfam03489   3 CKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
 
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
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907093819 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVE 282
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSE 40
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093819   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907093819 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
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
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907093819  82 CYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:pfam03489   3 CKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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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