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Conserved domains on  [gi|5453722|ref|NP_006321|]
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acyl-protein thioesterase 1 isoform 1 [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 ...
 11-226 7.88e-107

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: 306.61  E-value: 7.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 169
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5453722    170 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 226
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-226 7.88e-107

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: 306.61  E-value: 7.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 169
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5453722    170 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 226
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-227 1.66e-50

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 163.15  E-value: 1.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVtlnmnVAMPSWFDIIGLspDSQEDESGIKQAAENI 96
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPigGANRDISILQCHGDCDP 175
Cdd:COG0400  74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPE--AALAGTPVFLAHGTQDP 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5453722  176 LVPLMFGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 227
Cdd:COG0400 152 VIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
PRK11460 PRK11460
putative hydrolase; Provisional
 25-179 3.35e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 37.71  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    25 IFLHGLGDTGHGWAE---AFAgirsshikyicphaPVRPVTLNMNVAMP---------SWFDIIGLSpdsqeDESGIKQA 92
Cdd:PRK11460  20 LLFHGVGDNPVAMGEigsWFA--------------PAFPDALVVSVGGPepsgngagrQWFSVQGIT-----EDNRQARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    93 AENIKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALS-CWlplrASFPQGPIGganrDISI 166
Cdd:PRK11460  81 AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY----ASLPETAPT----ATTI 151

                        170
                 ....*....|...
gi 5453722   167 LQCHGDCDPLVPL 179
Cdd:PRK11460 152 HLIHGGEDPVIDV 164
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 87-130 6.74e-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: 35.94  E-value: 6.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 5453722   87 SGIKQAAENIKALIDQEVKNGI---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 ...
 11-226 7.88e-107

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: 306.61  E-value: 7.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGI 89
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     90 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 169
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5453722    170 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 226
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-227 1.66e-50

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 163.15  E-value: 1.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVtlnmnVAMPSWFDIIGLspDSQEDESGIKQAAENI 96
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAAEAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   97 KALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPigGANRDISILQCHGDCDP 175
Cdd:COG0400  74 AAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPE--AALAGTPVFLAHGTQDP 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5453722  176 LVPLMFGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 227
Cdd:COG0400 152 VIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-224 1.77e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.56  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   15 PAARKATAAVIFLHGLGDTGHGW---AEAFA--GIrsshikyicphapvrpvtlnmNVAMPSW--FdiiGLSPDSQEDES 87
Cdd:COG2267  22 RPAGSPRGTVVLVHGLGEHSGRYaelAEALAaaGY---------------------AVLAFDLrgH---GRSDGPRGHVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   88 GIKQAAENIKALIDQEVKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALScwlPLRASFP-QGPIGGANRDISI 166
Cdd:COG2267  78 SFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA---PAYRADPlLGPSARWLRALRL 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453722  167 LQ-----------CHGDCDPLVPlmfgsltVEKLKTLVN--PANVTFKTYEGMMH----SSCQQEMM-DVKQFIDK 224
Cdd:COG2267 153 AEalaridvpvlvLHGGADRVVP-------PEAARRLAArlSPDVELVLLPGARHellnEPAREEVLaAILAWLER 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
24-210 7.37e-10

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 56.90  E-value: 7.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   24 VIFLHGLGDTGHGWAeafagirsSHIKYicphapvrPVTLNMNVAMPSWFDIIGLSPDSQEDES-GIKQAAENIKALIDQ 102
Cdd:COG4099  52 VLFLHGAGERGTDNE--------KQLTH--------GAPKFINPENQAKFPAIVLAPQCPEDDYwSDTKALDAVLALLDD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722  103 EVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVtALSCwlplrasfPQGPIGGANR--DISILQCHGDCDPLVPL 179
Cdd:COG4099 116 LIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAA-VPIC--------GGGDPANAANlkKVPVWIFHGAKDDVVPV 186

                       170       180       190
                ....*....|....*....|....*....|.
gi 5453722  180 MFGSLTVEKLKTLvnPANVTFKTYEGMMHSS 210
Cdd:COG4099 187 EESRAMVEALKAA--GADVKYTEYPGVGHNS 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
13-208 9.87e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 53.34  E-value: 9.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   13 IVPAARKATA-AVIFLHG----LG--DTGHGWAEAFA---GIRSSHIKY-ICPHAPVrpvtlnmnvampswfdiiglsPD 81
Cdd:COG0657   4 YRPAGAKGPLpVVVYFHGggwvSGskDTHDPLARRLAaraGAAVVSVDYrLAPEHPF---------------------PA 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   82 SQED-ESGIKQAAENIKALidqevknGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVTALSCWLPLRASfpqgP 156
Cdd:COG0657  63 ALEDaYAALRWLRANAAEL-------GIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLDLTAS----P 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5453722  157 IggaNRDIS----ILQCHGDCDPLVP--LMFgsltVEKLKTLVNPanVTFKTYEGMMH 208
Cdd:COG0657 132 L---RADLAglppTLIVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 14-179 3.89e-08

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 52.70  E-value: 3.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   14 VPAARKATAA---VIFLHGLGdtghGWAEAFAgiRSSHI-------KYIC--PHAPVRPVTLNMNvampsWFDIIGLSPD 81
Cdd:COG3509  43 VPAGYDGGAPlplVVALHGCG----GSAADFA--AGTGLnaladreGFIVvyPEGTGRAPGRCWN-----WFDGRDQRRG 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   82 SQEdesgikqaAENIKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCwLPLRASFPQGPigGA 160
Cdd:COG3509 112 RDD--------VAFIAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAAC--AP 180

                       170
                ....*....|....*....
gi 5453722  161 NRDISILQCHGDCDPLVPL 179
Cdd:COG3509 181 GRPVPVLVIHGTADPTVPY 199
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
8-209 1.04e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.04  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    8 TPLPAIV--PAARKATAAVIFLH---GLGDTGHGWAEAFA--GirsshikYIcphapvrpvtlnmnVAMPSWFDiiGLSP 80
Cdd:COG0412  14 VTLPGYLarPAGGGPRPGVVVLHeifGLNPHIRDVARRLAaaG-------YV--------------VLAPDLYG--RGGP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   81 DSQEDESG-------IKQAAENIKALIDqEVKN--GIPSNRIILGGFSQGGALSLYTAlTTQQKLAGVTALSCWLPLras 151
Cdd:COG0412  71 GDDPDEARalmgaldPELLAADLRAALD-WLKAqpEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPA--- 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722  152 fPQGPIGGANRDISILQCHGDCDPLVPLMfgslTVEKLKTLVNPANV--TFKTYEGMMHS 209
Cdd:COG0412 146 -DDLLDLAARIKAPVLLLYGEKDPLVPPE----QVAALEAALAAAGVdvELHVYPGAGHG 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
8-227 6.01e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.78  E-value: 6.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    8 TPLPA--IVPAARKATAAVIFLHGLG----DTGHGWAEAFAgirsshikyicphapvrpvTLNMNVAMPswfDIIGlspD 81
Cdd:COG1506   8 TTLPGwlYLPADGKKYPVVVYVHGGPgsrdDSFLPLAQALA-------------------SRGYAVLAP---DYRG---Y 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   82 SQEDESGIKQAAENIKALIDQEVKNG-IPSNRIILGGFSQGGALSLYTALTTQQK------LAGVTALSCWLPLRASFPQ 154
Cdd:COG1506  63 GESAGDWGGDEVDDVLAAIDYLAARPyVDPDRIGIYGHSYGGYMALLAAARHPDRfkaavaLAGVSDLRSYYGTTREYTE 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722  155 GPIGGANRDISILQ-----------------CHGDCDPLVPLMFGSLTVEKLKTlvNPANVTFKTYEGMMHSSCQQEMMD 217
Cdd:COG1506 143 RLMGGPWEDPEAYAarsplayadklktplllIHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGHGFSGAGAPD 220

                       250
                ....*....|....
gi 5453722  218 ----VKQFIDKLLP 227
Cdd:COG1506 221 ylerILDFLDRHLK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-143 5.41e-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: 42.68  E-value: 5.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722   23 AVIFLHGLGDTGHGWAEAFAGIRSSHiKYICPHAPVRpvtlnmnvampswfdiiGLSPDSQEDESgIKQAAENIKALIDQ 102
Cdd:COG0596  25 PVVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGH-----------------GRSDKPAGGYT-LDDLADDLAALLDA 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 5453722  103 EvknGIPsnRIILGGFSQGGALSLYTALTTQQKLAGVTALS 143
Cdd:COG0596  86 L---GLE--RVVLVGHSMGGMVALELAARHPERVAGLVLVD 121
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 24-178 1.02e-03

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


Pssm-ID: 461110  Cd Length: 208  Bit Score: 38.80  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     24 VIFLHGLGDTGHGWAEAFAGIRSSHIK------YIC-PHAPVRPVTLNMNVAMP----------SWFdiigLSPDSQEDE 86
Cdd:pfam03959   6 VLCLHGFGQSGEIFRAKTGALRKLLKKlgvefvYLDaPFELAEPADLPGSESEKdegeddepyrAWF----FGDDDTNEY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     87 SGIKQAaenIKALIDQEVKNGiPSNRIIlgGFSQGGALSLYtALTTQQKLAGVT--------ALSCWLPL----RASFPQ 154
Cdd:pfam03959  82 LGLDES---LDYVRDYIKENG-PFDGIL--GFSQGAALAAI-LASLLEEGLPLShpplkfaiLFSGFRPRppiyQEYYSE 154

                         170       180
                  ....*....|....*....|....
gi 5453722    155 GPIGganrdISILQCHGDCDPLVP 178
Cdd:pfam03959 155 DPIQ-----TPSLHVIGELDTVVP 173
PRK11460 PRK11460
putative hydrolase; Provisional
 25-179 3.35e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 37.71  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    25 IFLHGLGDTGHGWAE---AFAgirsshikyicphaPVRPVTLNMNVAMP---------SWFDIIGLSpdsqeDESGIKQA 92
Cdd:PRK11460  20 LLFHGVGDNPVAMGEigsWFA--------------PAFPDALVVSVGGPepsgngagrQWFSVQGIT-----EDNRQARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722    93 AENIKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VTALS-CWlplrASFPQGPIGganrDISI 166
Cdd:PRK11460  81 AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY----ASLPETAPT----ATTI 151

                        170
                 ....*....|...
gi 5453722   167 LQCHGDCDPLVPL 179
Cdd:PRK11460 152 HLIHGGEDPVIDV 164
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
24-122 4.04e-03

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 37.22  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453722     24 VIFLHGLGDTGhgwaeAFAGIRS--SHIKYICPHAPVRPVTlnmnvampswfdiIGLSPDSQEDESGIKQAAENIKALID 101
Cdd:pfam02089   2 VVIWHGLGDSC-----ASPGMQSlaELIKEAHPGTYVHSID-------------IGDGPSEDRKASFFGNMNEQVEAVCE 63

                          90       100
                  ....*....|....*....|.
gi 5453722    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 6.74e-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: 35.94  E-value: 6.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 5453722   87 SGIKQAAENIKALIDQEVKNGI---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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