NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|525342581|ref|NP_001266286|]
View 

acyl-protein thioesterase 1 isoform 3 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-210 4.06e-93

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: 271.17  E-value: 4.06e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHA----------------FDIIGLSPDSQEDESGI 73
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGpeipvtlnggmrmpawFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   74 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 153
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 525342581  154 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 210
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-210 4.06e-93

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: 271.17  E-value: 4.06e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHA----------------FDIIGLSPDSQEDESGI 73
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGpeipvtlnggmrmpawFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   74 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 153
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 525342581  154 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 210
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-211 4.61e-44

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 145.82  E-value: 4.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHA-----------FDIIGLspDSQEDESGIKQAAENIKALID 85
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRApvpegpggrawFDLSFL--EGREDEEGLAAAAEALAAFID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  86 Q-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPigGANRDISILQCHGDCDPLVPLM 164
Cdd:COG0400   79 ElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPE--AALAGTPVFLAHGTQDPVIPVE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 525342581 165 FGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 211
Cdd:COG0400  157 RAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 71-114 6.28e-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: 6.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342581  71 SGIKQAAENIKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 114
Cdd:cd00741    1 KGFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 11-210 4.06e-93

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: 271.17  E-value: 4.06e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   11 PAIVPAARKATAAVIFLHGLGDTGHGWAEAFA-GIRSSHIKYICPHA----------------FDIIGLSPDSQEDESGI 73
Cdd:pfam02230   4 AEVVSPRDPAQATVIFLHGLGDSGHGWADAAKtEAPLPNIKFIFPHGpeipvtlnggmrmpawFDLVGLSPNAKEDEAGI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   74 KQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIgGANRDISILQC 153
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPN-LVTKKTPIFLI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 525342581  154 HGDCDPLVPLMFGSLTVEKLKTLVNpaNVTFKTYEGMMHSSCQQEMMDVKQFIDKLL 210
Cdd:pfam02230 163 HGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
17-211 4.61e-44

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 145.82  E-value: 4.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  17 ARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHA-----------FDIIGLspDSQEDESGIKQAAENIKALID 85
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRApvpegpggrawFDLSFL--EGREDEEGLAAAAEALAAFID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  86 Q-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPigGANRDISILQCHGDCDPLVPLM 164
Cdd:COG0400   79 ElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPE--AALAGTPVFLAHGTQDPVIPVE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 525342581 165 FGSLTVEKLKTLvnPANVTFKTYEgMMHSSCQQEMMDVKQFIDKLLP 211
Cdd:COG0400  157 RAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAERLA 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-208 4.12e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.19  E-value: 4.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  15 PAARKATAAVIFLHGLGDTGHGW---AEAFA--GIRSshikyicpHAFDI--IGLSPDSQEDESGIKQAAENIKALIDQE 87
Cdd:COG2267   22 RPAGSPRGTVVLVHGLGEHSGRYaelAEALAaaGYAV--------LAFDLrgHGRSDGPRGHVDSFDDYVDDLRAALDAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  88 VKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALScwlPLRASFP-QGPIGGANRDISILQ-----------CHG 155
Cdd:COG2267   94 RAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA---PAYRADPlLGPSARWLRALRLAEalaridvpvlvLHG 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581 156 DCDPLVPlmfgsltVEKLKTLVN--PANVTFKTYEGMMH----SSCQQEMM-DVKQFIDK 208
Cdd:COG2267  169 GADRVVP-------PEAARRLAArlSPDVELVLLPGARHellnEPAREEVLaAILAWLER 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
24-194 5.85e-11

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 59.98  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  24 VIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAFDIIGLSPDSQEDES-GIKQAAENIKALIDQEVKN-GIPSNRIILGG 101
Cdd:COG4099   52 VLFLHGAGERGTDNEKQLTHGAPKFINPENQAKFPAIVLAPQCPEDDYwSDTKALDAVLALLDDLIAEyRIDPDRIYLTG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581 102 FSQGGALSLYTALTTQQKLAGVtALSCwlplrasfPQGPIGGANR--DISILQCHGDCDPLVPLMFGSLTVEKLKTLvnP 179
Cdd:COG4099  132 LSMGGYGTWDLAARYPDLFAAA-VPIC--------GGGDPANAANlkKVPVWIFHGAKDDVVPVEESRAMVEALKAA--G 200

                        170
                 ....*....|....*
gi 525342581 180 ANVTFKTYEGMMHSS 194
Cdd:COG4099  201 ADVKYTEYPGVGHNS 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
13-192 2.84e-10

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 57.58  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  13 IVPAARKATA-AVIFLHG----LG--DTGHGWAEAFA---GIRSSHIKY-ICP-HAFdiiglsPDSQED-ESGIKQAAEN 79
Cdd:COG0657    4 YRPAGAKGPLpVVVYFHGggwvSGskDTHDPLARRLAaraGAAVVSVDYrLAPeHPF------PAALEDaYAALRWLRAN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  80 IKALidqevknGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVTALSCWLPLRASfpqgPIggaNRDIS----IL 151
Cdd:COG0657   78 AAEL-------GIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLDLTAS----PL---RADLAglppTL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 525342581 152 QCHGDCDPLVP--LMFgsltVEKLKTLVNPanVTFKTYEGMMH 192
Cdd:COG0657  144 IVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
8-193 9.59e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 53.43  E-value: 9.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   8 TPLPAIV--PAARKATAAVIFLH---GLGDTGHGWAEAFA--GIRSshikyICPHAFDiiGLSPDSQEDESG-------I 73
Cdd:COG0412   14 VTLPGYLarPAGGGPRPGVVVLHeifGLNPHIRDVARRLAaaGYVV-----LAPDLYG--RGGPGDDPDEARalmgaldP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  74 KQAAENIKALIDqEVKN--GIPSNRIILGGFSQGGALSLYTAlTTQQKLAGVTALSCWLPLrasfPQGPIGGANRDISIL 151
Cdd:COG0412   87 ELLAADLRAALD-WLKAqpEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPA----DDLLDLAARIKAPVL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 525342581 152 QCHGDCDPLVPLMfgslTVEKLKTLVNPANV--TFKTYEGMMHS 193
Cdd:COG0412  161 LLYGEKDPLVPPE----QVAALEAALAAAGVdvELHVYPGAGHG 200
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-137 2.08e-08

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 52.89  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   23 AVIFLHGLGDTGHGWAEAFAGIRSSHIKYICP----HAFDIIGLSPDSQEDESgikqAAENIKALIDqevKNGIPsnRII 98
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALdlrgFGKSSRPKAQDDYRTDD----LAEDLEYILE---ALGLE--KVN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 525342581   99 LGGFSQGGALSLYTALTTQQKLAGVTALS----------CWLPLRASFP 137
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGaldppheldeADRFILALFP 121
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 14-163 4.40e-08

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 51.93  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  14 VPAARKATAA---VIFLHGLGDTGH------GWAEA-----FA-----GIRSSHIKyiCPHAFDIIGLSPDSQEdesgik 74
Cdd:COG3509   43 VPAGYDGGAPlplVVALHGCGGSAAdfaagtGLNALadregFIvvypeGTGRAPGR--CWNWFDGRDQRRGRDD------ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  75 qaAENIKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCwLPLRASFPQGPigGANRDISILQC 153
Cdd:COG3509  115 --VAFIAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAAC--APGRPVPVLVI 189

                        170
                 ....*....|
gi 525342581 154 HGDCDPLVPL 163
Cdd:COG3509  190 HGTADPTVPY 199
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
8-211 7.86e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 51.17  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   8 TPLPA--IVPAARKATAAVIFLHGLG----DTGHGWAEAFAgirsshikyicphAFDIIGLSPD----SQEDESGIKQAA 77
Cdd:COG1506    8 TTLPGwlYLPADGKKYPVVVYVHGGPgsrdDSFLPLAQALA-------------SRGYAVLAPDyrgyGESAGDWGGDEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  78 ENIKALIDQEVKNG-IPSNRIILGGFSQGGALSLYTALTTQQK------LAGVTALSCWLPLRASFPQGPIGGANRDISI 150
Cdd:COG1506   75 DDVLAAIDYLAARPyVDPDRIGIYGHSYGGYMALLAAARHPDRfkaavaLAGVSDLRSYYGTTREYTERLMGGPWEDPEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581 151 LQ-----------------CHGDCDPLVPLMFGSLTVEKLKTlvNPANVTFKTYEGMMHSSCQQEMMD----VKQFIDKL 209
Cdd:COG1506  155 YAarsplayadklktplllIHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGHGFSGAGAPDylerILDFLDRH 232


                 ..
gi 525342581 210 LP 211
Cdd:COG1506  233 LK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-127 2.10e-07

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: 49.61  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  23 AVIFLHGLGDTGHGWAEAFAGIRSSH--IkyicphAFDII--GLSPDSQEDESgIKQAAENIKALIDQEvknGIPsnRII 98
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPALAAGYrvI------APDLRghGRSDKPAGGYT-LDDLADDLAALLDAL---GLE--RVV 92

                         90       100
                 ....*....|....*....|....*....
gi 525342581  99 LGGFSQGGALSLYTALTTQQKLAGVTALS 127
Cdd:COG0596   93 LVGHSMGGMVALELAARHPERVAGLVLVD 121
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
5-127 3.15e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 40.31  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   5 NMSTPLPAIVPAARKAtaaVIFLHGLGDT---GHGWAEAFA--GIRSShikyiCP----HafdiiGLSPDSQEdESGIKQ 75
Cdd:COG1647    2 KILGAEPFFLEGGRKG---VLLLHGFTGSpaeMRPLAEALAkaGYTVY-----APrlpgH-----GTSPEDLL-KTTWED 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525342581  76 AAENIKALIDQEVKNGipsNRIILGGFSQGGALSLYTALtTQQKLAGVTALS 127
Cdd:COG1647   68 WLEDVEEAYEILKAGY---DKVIVIGLSMGGLLALLLAA-RYPDVAGLVLLS 115
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 22-128 7.93e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.12  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   22 AAVIFLHGLGDtgHGW-----AEAFA--GIRSshikyicpHAFDIIG--LSPDSQEDESGIKQAAENIKALIDQeVKNGI 92
Cdd:pfam12146   5 AVVVLVHGLGE--HSGryahlADALAaqGFAV--------YAYDHRGhgRSDGKRGHVPSFDDYVDDLDTFVDK-IREEH 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 525342581   93 PSNRIILGGFSQGGALSLYTALTTQQKLAGVtALSC 128
Cdd:pfam12146  74 PGLPLFLLGHSMGGLIAALYALRYPDKVDGL-ILSA 108
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 24-127 8.15e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.50  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  24 VIFLHGLGDTGHGWAEAFAGIRSSHikyICPHAFDIIGLSPDsqedesgIKQAAENIKALIDQeVKNGIPSNRIILGGFS 103
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRAAG---YPVYALNYPSTNGS-------IEDSAEQLAAFVDA-VLAATGAEKVDLVGHS 76

                         90       100
                 ....*....|....*....|....*.
gi 525342581 104 QGGALSLY--TALTTQQKLAGVTALS 127
Cdd:COG1075   77 MGGLVARYylKRLGGAAKVARVVTLG 102
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
24-106 8.16e-04

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 39.14  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   24 VIFLHGLGDTGhgwaeAFAGIRS--SHIKYICPHAFDI---IGLSPDSQEDESGIKQAAENIKALIDQeVKNGIPSNRII 98
Cdd:pfam02089   2 VVIWHGLGDSC-----ASPGMQSlaELIKEAHPGTYVHsidIGDGPSEDRKASFFGNMNEQVEAVCEQ-LKPELPANGFN 75


                  ....*...
gi 525342581   99 LGGFSQGG 106
Cdd:pfam02089  76 AIGFSQGG 83
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 24-113 1.91e-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: 38.22  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581   24 VIFLHGLGDTGHGWAEAFAgirsshiKYICPHAFDII--GLSPDSQEDESGIKQAAENIKALIDQEvkngipsnRIILGG 101
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLA-------AGVAVLAPDLPghGSSSPPPLDLADLADLAALLDELGAAR--------PVVLVG 65

                          90
                  ....*....|..
gi 525342581  102 FSQGGALSLYTA 113
Cdd:pfam12697  66 HSLGGAVALAAA 77
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
24-162 3.17e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 37.91  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342581  24 VIFLHGLGDTGHGWAEAF-------AGIRSSHIK---YICPHAFDIIGLSPDSQEDESGIKQAAENIKALIDQE--VKNG 91
Cdd:COG2382  115 LYLLDGGGGDEQDWFDQGrlptildNLIAAGKIPpmiVVMPDGGDGGDRGTEGPGNDAFERFLAEELIPFVEKNyrVSAD 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525342581  92 iPSNRIIlGGFSQGGALSLYTALTTQQKLAGVTALS--CWLPLRASFPQGPI-----GGANRDISILQCHGDCDPLVP 162
Cdd:COG2382  195 -PEHRAI-AGLSMGGLAALYAALRHPDLFGYVGSFSgsFWWPPGDADRGGWAellaaGAPKKPLRFYLDVGTEDDLLE 270
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 71-114 6.28e-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: 6.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342581  71 SGIKQAAENIKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 114
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH