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Conserved domains on  [gi|189217847|ref|NP_001121362|]
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maspardin isoform b [Homo sapiens]

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, ...
 59-138 6.12e-03

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 pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 37.48  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217847   59 FFRQILALTGWGyrviAVHLFGASLGGFLAqkfAEYTHKSP-RVHSLILCNS---FSDTSIFNQTWTANSFWLMPAFMLK 134
Cdd:pfam00561  58 DLEYILEALGLE----KVNLVGHSMGGLIA---LAYAAKYPdRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVAD 130


                  ....
gi 189217847  135 KIVL 138
Cdd:pfam00561 131 FAPN 134
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-138 6.12e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 37.48  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217847   59 FFRQILALTGWGyrviAVHLFGASLGGFLAqkfAEYTHKSP-RVHSLILCNS---FSDTSIFNQTWTANSFWLMPAFMLK 134
Cdd:pfam00561  58 DLEYILEALGLE----KVNLVGHSMGGLIA---LAYAAKYPdRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVAD 130


                  ....
gi 189217847  135 KIVL 138
Cdd:pfam00561 131 FAPN 134
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-138 6.12e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 37.48  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217847   59 FFRQILALTGWGyrviAVHLFGASLGGFLAqkfAEYTHKSP-RVHSLILCNS---FSDTSIFNQTWTANSFWLMPAFMLK 134
Cdd:pfam00561  58 DLEYILEALGLE----KVNLVGHSMGGLIA---LAYAAKYPdRVKALVLLGAldpPHELDEADRFILALFPGFFDGFVAD 130


                  ....
gi 189217847  135 KIVL 138
Cdd:pfam00561 131 FAPN 134
 
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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