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Conserved domains on  [gi|108948907|gb|ABG24408|]
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esterase 6, partial [Drosophila melanogaster]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 1-111 4.24e-52

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member cd00312:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 493  Bit Score: 170.21  E-value: 4.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907   1 FGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRDVGCESAeDSASLKKCLK 80
Cdd:cd00312  171 FGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCNDT-SSAELLDCLR 249

                         90       100       110
                 ....*....|....*....|....*....|.
gi 108948907  81 SKPASELVTAVRKFLIFSYVPFAPFSPVLEP 111
Cdd:cd00312  250 SKSAEELLDATRKLLLFSYSPFLPFGPVVDG 280
 
Name Accession Description Interval E-value
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-111 4.24e-52

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 170.21  E-value: 4.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907   1 FGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRDVGCESAeDSASLKKCLK 80
Cdd:cd00312  171 FGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCNDT-SSAELLDCLR 249

                         90       100       110
                 ....*....|....*....|....*....|.
gi 108948907  81 SKPASELVTAVRKFLIFSYVPFAPFSPVLEP 111
Cdd:cd00312  250 SKSAEELLDATRKLLLFSYSPFLPFGPVVDG 280
COesterase pfam00135
Carboxylesterase family;
1-111 8.10e-40

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 138.21  E-value: 8.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907    1 FGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRDVGCEsAEDSASLKKCLK 80
Cdd:pfam00135 178 FGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKELAKLVGCP-TSDSAELVECLR 256

                          90       100       110
                  ....*....|....*....|....*....|.
gi 108948907   81 SKPASELVTAVRKFLIFSYVPFAPFSPVLEP 111
Cdd:pfam00135 257 SKPAEELLDAQLKLLVYGSVPFVPFGPVVDG 287
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-109 4.30e-08

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 49.50  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907   1 FGGEPQNVLLVGHSAGGASVHLQMLREdfgqLAR----AAFSFSGNALDPWVIQKGAR-GRAF--ELGrdVGCESAEdsa 73
Cdd:COG2272  186 FGGDPDNVTIFGESAGAASVAALLASP----LAKglfhRAIAQSGAGLSVLTLAEAEAvGAAFaaALG--VAPATLA--- 256

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 108948907  74 slkkCLKSKPASELVTAVRKFLIFSYVPFaPFSPVL 109
Cdd:COG2272  257 ----ALRALPAEELLAAQAALAAEGPGGL-PFGPVV 287
 
Name Accession Description Interval E-value
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-111 4.24e-52

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 170.21  E-value: 4.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907   1 FGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRDVGCESAeDSASLKKCLK 80
Cdd:cd00312  171 FGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCNDT-SSAELLDCLR 249

                         90       100       110
                 ....*....|....*....|....*....|.
gi 108948907  81 SKPASELVTAVRKFLIFSYVPFAPFSPVLEP 111
Cdd:cd00312  250 SKSAEELLDATRKLLLFSYSPFLPFGPVVDG 280
COesterase pfam00135
Carboxylesterase family;
1-111 8.10e-40

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 138.21  E-value: 8.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907    1 FGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRDVGCEsAEDSASLKKCLK 80
Cdd:pfam00135 178 FGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKELAKLVGCP-TSDSAELVECLR 256

                          90       100       110
                  ....*....|....*....|....*....|.
gi 108948907   81 SKPASELVTAVRKFLIFSYVPFAPFSPVLEP 111
Cdd:pfam00135 257 SKPAEELLDAQLKLLVYGSVPFVPFGPVVDG 287
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-109 4.30e-08

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 49.50  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108948907   1 FGGEPQNVLLVGHSAGGASVHLQMLREdfgqLAR----AAFSFSGNALDPWVIQKGAR-GRAF--ELGrdVGCESAEdsa 73
Cdd:COG2272  186 FGGDPDNVTIFGESAGAASVAALLASP----LAKglfhRAIAQSGAGLSVLTLAEAEAvGAAFaaALG--VAPATLA--- 256

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 108948907  74 slkkCLKSKPASELVTAVRKFLIFSYVPFaPFSPVL 109
Cdd:COG2272  257 ----ALRALPAEELLAAQAALAAEGPGGL-PFGPVV 287
 
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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