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Conserved domains on  [gi|525342593|ref|NP_001266287|]
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acyl-protein thioesterase 1 isoform 4 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10491393)

alpha/beta hydrolase similar to acyl-protein thioesterase that hydrolyzes fatty acids from S-acylated cysteine residues in proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-212 3.68e-101

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


:

Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 291.97  E-value: 3.68e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFP-------------QCH 156
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPshpnlvtkktpifLIH 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 525342593  157 GDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 212
Cdd:pfam02230 164 GEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-212 3.68e-101

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 291.97  E-value: 3.68e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFP-------------QCH 156
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPshpnlvtkktpifLIH 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 525342593  157 GDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 212
Cdd:pfam02230 164 GEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-213 3.99e-47

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 153.91  E-value: 3.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVtlnmnVAMPSWFDIIGLspDSQEDESGIKQAAENI 96
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQ------------CHGDCDPLV 163
Cdd:COG0400   74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPApeaalagtpvflAHGTQDPVI 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 525342593 164 PLMFGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 213
Cdd:COG0400  154 PVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 87-130 5.48e-03

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: 36.32  E-value: 5.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342593  87 SGIKQAAENIKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 130
Cdd:cd00741    1 KGFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
PRK11460 PRK11460
putative hydrolase; Provisional
 25-165 7.06e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 36.55  E-value: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  25 IFLHGLGDTGHGWAE---AFAgirsshikyicphaPVRPVTLNMNVAMP---------SWFDIIGLSpdsqeDESGIKQA 92
Cdd:PRK11460  20 LLFHGVGDNPVAMGEigsWFA--------------PAFPDALVVSVGGPepsgngagrQWFSVQGIT-----EDNRQARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  93 AENIKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALS-CWLPLRASFPQ------CHGDCD 160
Cdd:PRK11460  81 AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRYASLPETAPTattihlIHGGED 159


                 ....*
gi 525342593 161 PLVPL 165
Cdd:PRK11460 160 PVIDV 164
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-212 3.68e-101

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 291.97  E-value: 3.68e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFP-------------QCH 156
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPshpnlvtkktpifLIH 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 525342593  157 GDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 212
Cdd:pfam02230 164 GEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-213 3.99e-47

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 153.91  E-value: 3.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVtlnmnVAMPSWFDIIGLspDSQEDESGIKQAAENI 96
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQ------------CHGDCDPLV 163
Cdd:COG0400   74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPApeaalagtpvflAHGTQDPVI 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 525342593 164 PLMFGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 213
Cdd:COG0400  154 PVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
COG4099 COG4099
Predicted peptidase [General function prediction only];
24-196 2.74e-10

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 58.06  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  24 VIFLHGLGDTGHGWAeafagirsSHIKYicphapvrPVTLNMNVAMPSWFDIIGLSPDSQEDES-GIKQAAENIKALIDQ 102
Cdd:COG4099   52 VLFLHGAGERGTDNE--------KQLTH--------GAPKFINPENQAKFPAIVLAPQCPEDDYwSDTKALDAVLALLDD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593 103 EVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCW-----------LPLRAsFpqcHGDCDPLVPLMFGSL 170
Cdd:COG4099  116 LIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGgdpanaanlkkVPVWI-F---HGAKDDVVPVEESRA 191

                        170       180
                 ....*....|....*....|....*.
gi 525342593 171 TVEKLKTLvnPANVTFKTYEGMMHSS 196
Cdd:COG4099  192 MVEALKAA--GADVKYTEYPGVGHNS 215
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-210 3.10e-10

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 57.70  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  15 PAARKATAAVIFLHGLGDTGHGW---AEAFA--GIrsshikyicphapvrpvtlnmNVAMPSW--FdiiGLSPDSQEDES 87
Cdd:COG2267   22 RPAGSPRGTVVLVHGLGEHSGRYaelAEALAaaGY---------------------AVLAFDLrgH---GRSDGPRGHVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  88 GIKQAAENIKALIDQEVKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALScwlPLRASFPQC------------ 155
Cdd:COG2267   78 SFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA---PAYRADPLLgpsarwlralrl 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342593 156 --------------HGDCDPLVPlmfgsltVEKLKTLVN--PANVTFKTYEGMMH----SSCQQEMM-DVKQFIDK 210
Cdd:COG2267  153 aealaridvpvlvlHGGADRVVP-------PEAARRLAArlSPDVELVLLPGARHellnEPAREEVLaAILAWLER 221
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
13-194 3.89e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 54.49  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  13 IVPAARKATA-AVIFLHG----LG--DTGHGWAEAFA---GIRSSHIKY-ICPHAPVrpvtlnmnvampswfdiiglsPD 81
Cdd:COG0657    4 YRPAGAKGPLpVVVYFHGggwvSGskDTHDPLARRLAaraGAAVVSVDYrLAPEHPF---------------------PA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  82 SQED-ESGIKQAAENIKALidqevknGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVTALSCWL-----PLRAS 151
Cdd:COG0657   63 ALEDaYAALRWLRANAAEL-------GIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLdltasPLRAD 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525342593 152 FPQ------CHGDCDPLVP--LMFgsltVEKLKTLVNPanVTFKTYEGMMH 194
Cdd:COG0657  136 LAGlpptliVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 14-165 1.17e-07

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 50.77  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  14 VPAARKATAA---VIFLHGLGdtghGWAEAFAgiRSSHI-------KYIC--PHAPVRPVTLNMNvampsWFDIIGLSPD 81
Cdd:COG3509   43 VPAGYDGGAPlplVVALHGCG----GSAADFA--AGTGLnaladreGFIVvyPEGTGRAPGRCWN-----WFDGRDQRRG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  82 SQEdesgikqaAENIKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQC----- 155
Cdd:COG3509  112 RDD--------VAFIAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAGLPYGAASDAACapgrp 183

                        170
                 ....*....|....*.
gi 525342593 156 ------HGDCDPLVPL 165
Cdd:COG3509  184 vpvlviHGTADPTVPY 199
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
8-195 2.09e-06

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 46.88  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   8 TPLPAIV--PAARKATAAVIFLH---GLGDTGHGWAEAFA--GirsshikYIcphapvrpvtlnmnVAMPSWFDiiGLSP 80
Cdd:COG0412   14 VTLPGYLarPAGGGPRPGVVVLHeifGLNPHIRDVARRLAaaG-------YV--------------VLAPDLYG--RGGP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  81 DSQEDESG-------IKQAAENIKALIDqEVKN--GIPSNRIILGGFSQGGALSLYTAlTTQQKLAGVTALSCWLPLRAS 151
Cdd:COG0412   71 GDDPDEARalmgaldPELLAADLRAALD-WLKAqpEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPADDL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525342593 152 FPQ----------CHGDCDPLVPLMfgslTVEKLKTLVNPANV--TFKTYEGMMHS 195
Cdd:COG0412  149 LDLaarikapvllLYGEKDPLVPPE----QVAALEAALAAAGVdvELHVYPGAGHG 200
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-143 4.43e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 43.07  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  23 AVIFLHGLGDTGHGWAEAFAGIRSSHiKYICPHAPVRpvtlnmnvampswfdiiGLSPDSQEDESgIKQAAENIKALIDQ 102
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGH-----------------GRSDKPAGGYT-LDDLADDLAALLDA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 525342593 103 EvknGIPsnRIILGGFSQGGALSLYTALTTQQKLAGVTALS 143
Cdd:COG0596   86 L---GLE--RVVLVGHSMGGMVALELAARHPERVAGLVLVD 121
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 24-138 2.92e-03

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 37.26  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   24 VIFLHGLGDTGHGWAEAFAGIRSSHIK------YIC-PHAPVRPVTLNMNVAMP----------SWFdiigLSPDSQEDE 86
Cdd:pfam03959   6 VLCLHGFGQSGEIFRAKTGALRKLLKKlgvefvYLDaPFELAEPADLPGSESEKdegeddepyrAWF----FGDDDTNEY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 525342593   87 SGIKQAaenIKALIDQEVKNGiPSNRIIlgGFSQGGALSLYtALTTQQKLAG 138
Cdd:pfam03959  82 LGLDES---LDYVRDYIKENG-PFDGIL--GFSQGAALAAI-LASLLEEGLP 126
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
24-122 3.56e-03

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 37.22  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593   24 VIFLHGLGDTGhgwaeAFAGIRS--SHIKYICPHAPVRPVTlnmnvampswfdiIGLSPDSQEDESGIKQAAENIKALID 101
Cdd:pfam02089   2 VVIWHGLGDSC-----ASPGMQSlaELIKEAHPGTYVHSID-------------IGDGPSEDRKASFFGNMNEQVEAVCE 63

                          90       100
                  ....*....|....*....|.
gi 525342593  102 QeVKNGIPSNRIILGGFSQGG 122
Cdd:pfam02089  64 Q-LKPELPANGFNAIGFSQGG 83
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 87-130 5.48e-03

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: 36.32  E-value: 5.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342593  87 SGIKQAAENIKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 130
Cdd:cd00741    1 KGFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
PRK11460 PRK11460
putative hydrolase; Provisional
 25-165 7.06e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 36.55  E-value: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  25 IFLHGLGDTGHGWAE---AFAgirsshikyicphaPVRPVTLNMNVAMP---------SWFDIIGLSpdsqeDESGIKQA 92
Cdd:PRK11460  20 LLFHGVGDNPVAMGEigsWFA--------------PAFPDALVVSVGGPepsgngagrQWFSVQGIT-----EDNRQARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342593  93 AENIKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALS-CWLPLRASFPQ------CHGDCD 160
Cdd:PRK11460  81 AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRYASLPETAPTattihlIHGGED 159


                 ....*
gi 525342593 161 PLVPL 165
Cdd:PRK11460 160 PVIDV 164
 
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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