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Conserved domains on  [gi|1035333211|gb|ANJ02615|]
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ORF19 [Fowl aviadenovirus 11]

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, ...
 116-210 8.19e-08

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 cd00707:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 275  Bit Score: 54.17  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035333211 116 KMTPAVGVVLvdyqlyydtdglhADFRKFLAAIPDA--KKLHCIGHSAGAHACSTICRQYsqlskGHRCMRIVGL---EP 190
Cdd:cd00707    87 NNTRVVGAEL-------------AKFLDFLVDNTGLslENVHLIGHSLGAHVAGFAGKRL-----NGKLGRITGLdpaGP 148

                          90       100
                  ....*....|....*....|....
gi 1035333211 191 TFVSGG----LDKSDADYVVVLKT 210
Cdd:cd00707   149 LFSGADpedrLDPSDAQFVDVIHT 172
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 116-210 8.19e-08

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 54.17  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035333211 116 KMTPAVGVVLvdyqlyydtdglhADFRKFLAAIPDA--KKLHCIGHSAGAHACSTICRQYsqlskGHRCMRIVGL---EP 190
Cdd:cd00707    87 NNTRVVGAEL-------------AKFLDFLVDNTGLslENVHLIGHSLGAHVAGFAGKRL-----NGKLGRITGLdpaGP 148

                          90       100
                  ....*....|....*....|....
gi 1035333211 191 TFVSGG----LDKSDADYVVVLKT 210
Cdd:cd00707   149 LFSGADpedrLDPSDAQFVDVIHT 172
Lipase pfam00151
Lipase;
153-210 1.86e-03

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 41.27  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1035333211 153 KLHCIGHSAGAHACSTICRQYSQlskghRCMRIVGLEPTFVSG-------GLDKSDADYVVVLKT 210
Cdd:pfam00151 148 NVHLIGHSLGAHVAGEAGRRTNG-----KLGRITGLDPAGPYFqgtpeevRLDPGDADFVDAIHT 207
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 116-210 8.19e-08

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 54.17  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035333211 116 KMTPAVGVVLvdyqlyydtdglhADFRKFLAAIPDA--KKLHCIGHSAGAHACSTICRQYsqlskGHRCMRIVGL---EP 190
Cdd:cd00707    87 NNTRVVGAEL-------------AKFLDFLVDNTGLslENVHLIGHSLGAHVAGFAGKRL-----NGKLGRITGLdpaGP 148

                          90       100
                  ....*....|....*....|....
gi 1035333211 191 TFVSGG----LDKSDADYVVVLKT 210
Cdd:cd00707   149 LFSGADpedrLDPSDAQFVDVIHT 172
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 135-274 5.01e-05

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 44.03  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035333211 135 DGLHADFRKFLAAIPDaKKLHCIGHSAGAHACSTICRQYSQLSKGHRcMRIVGLEP------TFVSGGLDKSDADYVVVL 208
Cdd:cd00741    12 NLVLPLLKSALAQYPD-YKIHVTGHSLGGALAGLAGLDLRGRGLGRL-VRVYTFGPprvgnaAFAEDRLDPSDALFVDRI 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1035333211 209 KTQYSWITGGYTASEDLMVedkGGRSCGIHGGWSGRVCGESVwGATVCEEFSWRNTFSLSGCYHRM 274
Cdd:cd00741    90 VNDNDIVPRLPPGGEGYPH---GGAEFYINGGKSQPGCCKNV-LEAVDIDFGNIGLSGNGLCDHLR 151
Lipase pfam00151
Lipase;
153-210 1.86e-03

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 41.27  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1035333211 153 KLHCIGHSAGAHACSTICRQYSQlskghRCMRIVGLEPTFVSG-------GLDKSDADYVVVLKT 210
Cdd:pfam00151 148 NVHLIGHSLGAHVAGEAGRRTNG-----KLGRITGLDPAGPYFqgtpeevRLDPGDADFVDAIHT 207
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 94-164 5.25e-03

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 38.99  E-value: 5.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1035333211  94 VLLIPGWYLGYDDFRKVLRfhqkmtPAVGVVLVDYQLYYDTDGLH------ADFRKFLAAIPDAKKLHCIGHSAGAH 164
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLA------AGVAVLAPDLPGHGSSSPPPldladlADLAALLDELGAARPVVLVGHSLGGA 71
 
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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