1BU8,1TIA,1HPL,3TGL,4TGL,1LGY,1UWC,1DT3,1GPL,1ETH,1LPB,1RP1


Conserved Protein Domain Family
Lipase

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cd00741: Lipase 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 238382
Aligned: 172 rows
Threshold Bit Score: 44.4136
Created: 24-Sep-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic triadnucleophilic
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic triad
Evidence:
  • Comment:Ser - Asp - His catalytic triad
  • Comment:The Asp used in the catalytic triad of the two subfamilies differs.
  • Structure:1TIA; Penicillium triacylglycerol acylhydrolase (Lipase 3)
    View structure with Cn3D
  • Citation:PMID 7656005
  • Structure:1BU8; Rat pancreatic lipase
    View structure with Cn3D
  • Citation:PMID 9822688

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:

Feature 1                                   #                                                 
1BU8_A    121 YNTRVVGAEIAFLVQVLS.[ 9].VHLIGHSLGAHVVGEAGR.[ 7].RITGLD.[22].VDVIHTDSA.[15].HLDFF 229 Norway rat
1TIA      110 LGFWSSWKLVRDDIIKEL.[11].LVVVGHSLGAAVATLAAT.[10].KLYAYA.[18].NFRFTHTND.[15].SPEYW 219 Penicillium camemberti
EAL33696  168 NMVEDMGFLLADLVRYLH.[ 9].VYVIGHSLGAQIAGSAGK.[ 8].TIYALD.[22].VESIQTSVS.[ 8].HATFY 270 Drosophila pseudoobscura
EAL38899  141 QLVYAVAAAASNMLDYLA.[ 9].VVVVGHSLGAHVAGNVGK.[ 7].TIVGLD.[21].VEIIHTNGG.[ 9].DADFY 242 Anopheles gambiae str. ...
EAA00092  148 ARVGAVGNVVSTFINFLQ.[ 9].VSIAGHSLGAHAAGNAGF.[ 7].TIFGMD.[21].VESIHTNAG.[ 9].QASFY 249 Anopheles gambiae str. ...
EAA00017  150 NRVGAVGEVISRMINTIV.[ 9].INLIGHSLGAHVAANAGK.[ 7].TIIGLD.[21].TEAIYTNAG.[ 9].HANFY 251 Anopheles gambiae str. ...
EAA00085  158 NHINAVGLTVARFIDFLN.[ 9].VYVTGHSLGGHTAGIVGK.[ 8].TVVALD.[22].VEVIHTNGG.[ 9].LADFY 261 Anopheles gambiae str. ...
AAT27292  253 KLIETFGAELAQFIRNLN.[ 9].MYLIGHSLGAQIAGSAGK.[ 8].TIFALD.[22].VESMHTSAN.[ 8].SATFY 355 fruit fly
EAL31819  600 PMVPGVGKSVARFLSFLA.[ 9].VVVVAHSMGAHVAGFCGK.[13].YIVALD.[22].VVAIHTNGL.[ 9].HSDFY 708 Drosophila pseudoobscura
1709542   107 ENTRAVGKYIADFSKILI.[ 9].IRLIGHSLGAQIAGFAGK.[11].EIIGLD.[22].VQILHTSSN.[ 8].TVDFY 212 bald-faced hornet

Feature 1             #    
1BU8_A    230 P.[33].NHLRSY 269 Norway rat
1TIA      220 I.[37].AHIWYF 263 Penicillium camemberti
EAL33696  271 P.[14].SHKRAH 291 Drosophila pseudoobscura
EAL38899  243 P.[17].AHARAV 266 Anopheles gambiae str. PEST
EAA00092  250 P.[17].AHGRAY 273 Anopheles gambiae str. PEST
EAA00017  252 P.[17].AHNRVN 275 Anopheles gambiae str. PEST
EAA00085  262 P.[17].AHGRAF 285 Anopheles gambiae str. PEST
AAT27292  356 P.[14].SHIRSY 376 fruit fly
EAL31819  709 A.[17].AHARAV 732 Drosophila pseudoobscura
1709542   213 I.[17].SHTRAV 236 bald-faced hornet

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