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Conserved domains on  [gi|1958774783|ref|XP_038965234|]
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acyl-protein thioesterase 1 isoform X3 [Rattus norvegicus]

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 ...
 8-213 6.07e-100

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: 289.28  E-value: 6.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783   8 APMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIKSSHIKYICPHAPVMPVTLNMSMMMPSWFDIIGLSPDSQEDE 86
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  87 SGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSaNRDISV 166
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLV-TKKTPI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774783 167 LQCHGDCDPLVPLMFGSLTVERLKGLVNpaNVTFKVYEGMMHSSCQQ 213
Cdd:pfam02230 160 FLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGR 204
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 8-213 6.07e-100

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: 289.28  E-value: 6.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783   8 APMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIKSSHIKYICPHAPVMPVTLNMSMMMPSWFDIIGLSPDSQEDE 86
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  87 SGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSaNRDISV 166
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLV-TKKTPI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774783 167 LQCHGDCDPLVPLMFGSLTVERLKGLVNpaNVTFKVYEGMMHSSCQQ 213
Cdd:pfam02230 160 FLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGR 204
YpfH COG0400
Predicted esterase [General function prediction only];
17-228 9.90e-47

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 153.52  E-value: 9.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIKSSHIKYICPHAPVMPVtlnmsMMMPSWFDIIGLspDSQEDESGIKQAAETV 96
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFsqGPINSANRDISVLQCHGDCDP 175
Cdd:COG0400    74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEAL--PAPEAALAGTPVFLAHGTQDP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958774783 176 LVPLMFGSLTVERLKGLvnPANVTFKVYEgMMHSSCQQqqhVVPKAKKRLSSR 228
Cdd:COG0400   152 VIPVERAREAAEALEAA--GADVTYREYP-GGHEISPE---ELADARAWLAER 198
PRK11460 PRK11460
putative hydrolase; Provisional
 25-208 1.45e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 38.48  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  25 IFLHGLGDTGHGWAEAfagikSSHIKYICPHAPVMPVTLNMSMMMP---SWFDIIGLSpdsqeDESGIKQAAETVKALID 101
Cdd:PRK11460   20 LLFHGVGDNPVAMGEI-----GSWFAPAFPDALVVSVGGPEPSGNGagrQWFSVQGIT-----EDNRQARVAAIMPTFIE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783 102 ----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALScwlplrASFSQGPiNSANRDISVLQCHGDCDPL 176
Cdd:PRK11460   90 tvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFS------GRYASLP-ETAPTATTIHLIHGGEDPV 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958774783 177 VPLMFGSLTVERLKGLvnPANVTFKVYEGMMH 208
Cdd:PRK11460  162 IDVAHAVAAQEALISL--GGDVTLDIVEDLGH 191
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 87-130 9.88e-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: 35.55  E-value: 9.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774783  87 SGIKQAAETVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 130
Cdd:cd00741     1 KGFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 8-213 6.07e-100

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: 289.28  E-value: 6.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783   8 APMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIKSSHIKYICPHAPVMPVTLNMSMMMPSWFDIIGLSPDSQEDE 86
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  87 SGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSaNRDISV 166
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLV-TKKTPI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774783 167 LQCHGDCDPLVPLMFGSLTVERLKGLVNpaNVTFKVYEGMMHSSCQQ 213
Cdd:pfam02230 160 FLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGR 204
YpfH COG0400
Predicted esterase [General function prediction only];
17-228 9.90e-47

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 153.52  E-value: 9.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIKSSHIKYICPHAPVMPVtlnmsMMMPSWFDIIGLspDSQEDESGIKQAAETV 96
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFsqGPINSANRDISVLQCHGDCDP 175
Cdd:COG0400    74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEAL--PAPEAALAGTPVFLAHGTQDP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958774783 176 LVPLMFGSLTVERLKGLvnPANVTFKVYEgMMHSSCQQqqhVVPKAKKRLSSR 228
Cdd:COG0400   152 VIPVERAREAAEALEAA--GADVTYREYP-GGHEISPE---ELADARAWLAER 198
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-208 1.56e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.56  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  15 PAARKATAAVIFLHGLGDTGHGW---AEAFA--GIksshikyicphAPVMpvtlnmsmmmpswFDI--IGLSPDSQEDES 87
Cdd:COG2267    22 RPAGSPRGTVVLVHGLGEHSGRYaelAEALAaaGY-----------AVLA-------------FDLrgHGRSDGPRGHVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  88 GIKQAAETVKALIDQEVKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALS--------CWLPLRASFSQGPINS 159
Cdd:COG2267    78 SFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLApayradplLGPSARWLRALRLAEA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958774783 160 ANR-DISVLQCHGDCDPLVPlmfgSLTVERLKGLVNPaNVTFKVYEGMMH 208
Cdd:COG2267   156 LARiDVPVLVLHGGADRVVP----PEAARRLAARLSP-DVELVLLPGARH 200
COG4099 COG4099
Predicted peptidase [General function prediction only];
24-210 9.97e-11

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 59.60  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  24 VIFLHGLGDTGhgwaeafagikSSHIKYICPHAPVMPVTLNmsmmmPSWFDIIGLSPDSQEDES-GIKQAAETVKALIDQ 102
Cdd:COG4099    52 VLFLHGAGERG-----------TDNEKQLTHGAPKFINPEN-----QAKFPAIVLAPQCPEDDYwSDTKALDAVLALLDD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783 103 EVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVtALSCwlplrasfSQGPINSANR--DISVLQCHGDCDPLVPL 179
Cdd:COG4099   116 LIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAA-VPIC--------GGGDPANAANlkKVPVWIFHGAKDDVVPV 186

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958774783 180 MFGSLTVERLKGLvnPANVTFKVYEGMMHSS 210
Cdd:COG4099   187 EESRAMVEALKAA--GADVKYTEYPGVGHNS 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
15-208 1.79e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 55.65  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  15 PAARKATA-AVIFLHG----LG--DTGHGWAEAFA---GIKSSHIKY-ICPHAPVmpvtlnmsmmmpswfdiiglsPDSQ 83
Cdd:COG0657     6 PAGAKGPLpVVVYFHGggwvSGskDTHDPLARRLAaraGAAVVSVDYrLAPEHPF---------------------PAAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  84 EDesgikqAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVTALSCWL-----PLRASFSQ 154
Cdd:COG0657    65 ED------AYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLdltasPLRADLAG 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774783 155 GPinsanrdiSVLQCHGDCDPLVP--LMFgsltVERLKGLVNPanVTFKVYEGMMH 208
Cdd:COG0657   139 LP--------PTLIVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 96-188 3.77e-07

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 49.62  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  96 VKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCwLPLRASFSQGPinSANRDISVLQCHGDCD 174
Cdd:COG3509   118 IAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAAC--APGRPVPVLVIHGTAD 194

                          90
                  ....*....|....
gi 1958774783 175 PLVPLMFGSLTVER 188
Cdd:COG3509   195 PTVPYAGAEETLAQ 208
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-208 3.48e-06

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: 46.15  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  23 AVIFLHGLGDTGHGWAEAFAGIkSSHIKYICPHAPVMpvtlnmsmmmpswfdiiGLSPDSQEDESgIKQAAETVKALIDQ 102
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGH-----------------GRSDKPAGGYT-LDDLADDLAALLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783 103 EvknGIPsnRIILGGFSQGGALSLYTALTTQQKLAGVTALS-----------CWLPLRASFSQGPINSANRDIS------ 165
Cdd:COG0596    86 L---GLE--RVVLVGHSMGGMVALELAARHPERVAGLVLVDevlaalaeplrRPGLAPEALAALLRALARTDLRerlari 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958774783 166 ---VLQCHGDCDPLVPLMFGSLTVERLKglvnpaNVTFKVYEGMMH 208
Cdd:COG0596   161 tvpTLVIWGEKDPIVPPALARRLAELLP------NAELVVLPGAGH 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
96-208 1.12e-04

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.93  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  96 VKALIDQevkNGIPSNRIILGGFSQGGALSLYTALTTQQK------LAGVTALSCWLPLRASFSQG-------------- 155
Cdd:COG1506    81 IDYLAAR---PYVDPDRIGIYGHSYGGYMALLAAARHPDRfkaavaLAGVSDLRSYYGTTREYTERlmggpwedpeayaa 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774783 156 --PINSANR-DISVLQCHGDCDPLVPLMFGSLTVERLKGlvNPANVTFKVYEGMMH 208
Cdd:COG1506   158 rsPLAYADKlKTPLLLIHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGH 211
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 24-223 1.39e-04

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


Pssm-ID: 461110  Cd Length: 208  Bit Score: 41.50  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  24 VIFLHGLGDTGHGWAEAFAGIKSSHIK------YIC-PHAPVMPVTLNMSMMMP----------SWFdiigLSPDSQEDE 86
Cdd:pfam03959   6 VLCLHGFGQSGEIFRAKTGALRKLLKKlgvefvYLDaPFELAEPADLPGSESEKdegeddepyrAWF----FGDDDTNEY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  87 SGIKqaaETVKALIDQEVKNGiPSNRIIlgGFSQGGALSLYtALTTQQKLAGVT--------ALSCWLPL----RASFSQ 154
Cdd:pfam03959  82 LGLD---ESLDYVRDYIKENG-PFDGIL--GFSQGAALAAI-LASLLEEGLPLShpplkfaiLFSGFRPRppiyQEYYSE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774783 155 GPINsanrdISVLQCHGDCDPLVPLmfgsltvERLKGLVNpanvTFK----VYEgmmHSscqqQQHVVPKAKK 223
Cdd:pfam03959 155 DPIQ-----TPSLHVIGELDTVVPE-------ERSEKLAE----ACKnsptVLE---HP----GGHFVPNSKD 204
PRK11460 PRK11460
putative hydrolase; Provisional
 25-208 1.45e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 38.48  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783  25 IFLHGLGDTGHGWAEAfagikSSHIKYICPHAPVMPVTLNMSMMMP---SWFDIIGLSpdsqeDESGIKQAAETVKALID 101
Cdd:PRK11460   20 LLFHGVGDNPVAMGEI-----GSWFAPAFPDALVVSVGGPEPSGNGagrQWFSVQGIT-----EDNRQARVAAIMPTFIE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774783 102 ----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALScwlplrASFSQGPiNSANRDISVLQCHGDCDPL 176
Cdd:PRK11460   90 tvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFS------GRYASLP-ETAPTATTIHLIHGGEDPV 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958774783 177 VPLMFGSLTVERLKGLvnPANVTFKVYEGMMH 208
Cdd:PRK11460  162 IDVAHAVAAQEALISL--GGDVTLDIVEDLGH 191
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 87-130 9.88e-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: 35.55  E-value: 9.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774783  87 SGIKQAAETVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 130
Cdd:cd00741     1 KGFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
 
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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