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Conserved domains on  [gi|686586446|ref|XP_009287617|]
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PREDICTED: acyl-protein thioesterase 1 [Aptenodytes forsteri]

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 ...
 1-168 1.01e-80

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: 238.05  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446    1 MPVSLNMNMAMPSWFDIIGLSPDSQEDEVGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAG 80
Cdd:pfam02230  53 IPVTLNGGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   81 VVALSCWLPLRASFPQGPiSGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMINpaNVTFRTYSGMMHSSCIEEMMDV 160
Cdd:pfam02230 133 IVAFSGFLPLPTKFPSHP-NLVTKKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDI 209


                  ....*...
gi 686586446  161 KQFIDKHL 168
Cdd:pfam02230 210 KKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 1-168 1.01e-80

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: 238.05  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446    1 MPVSLNMNMAMPSWFDIIGLSPDSQEDEVGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAG 80
Cdd:pfam02230  53 IPVTLNGGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   81 VVALSCWLPLRASFPQGPiSGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMINpaNVTFRTYSGMMHSSCIEEMMDV 160
Cdd:pfam02230 133 IVAFSGFLPLPTKFPSHP-NLVTKKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDI 209


                  ....*...
gi 686586446  161 KQFIDKHL 168
Cdd:pfam02230 210 KKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
9-169 1.83e-39

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 132.72  E-value: 1.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   9 MAMPSWFDIIGLspDSQEDEVGIKQAAENVKALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCW 87
Cdd:COG0400   46 PGGRAWFDLSFL--EGREDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  88 LPLRASFPqgPISGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSgMMHSSCIEEMMDVKQFIDKH 167
Cdd:COG0400  124 LPGEEALP--APEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAER 198


                 ..
gi 686586446 168 LP 169
Cdd:COG0400  199 LA 200
PRK11460 PRK11460
putative hydrolase; Provisional
 14-121 5.24e-04

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 39.25  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  14 WFDIIGLSPDSQEDEVgikqaAENVKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VVALS-CW 87
Cdd:PRK11460  65 WFSVQGITEDNRQARV-----AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY 138

                         90       100       110
                 ....*....|....*....|....*....|....
gi 686586446  88 lplrASFPQGPISGVnkeiAVLQCHGDCDPLVPL 121
Cdd:PRK11460 139 ----ASLPETAPTAT----TIHLIHGGEDPVIDV 164
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 30-72 7.23e-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: 35.17  E-value: 7.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 686586446  30 GIKQAAENVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 72
Cdd:cd00741    2 GFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 1-168 1.01e-80

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: 238.05  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446    1 MPVSLNMNMAMPSWFDIIGLSPDSQEDEVGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAG 80
Cdd:pfam02230  53 IPVTLNGGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   81 VVALSCWLPLRASFPQGPiSGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMINpaNVTFRTYSGMMHSSCIEEMMDV 160
Cdd:pfam02230 133 IVAFSGFLPLPTKFPSHP-NLVTKKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDI 209


                  ....*...
gi 686586446  161 KQFIDKHL 168
Cdd:pfam02230 210 KKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
9-169 1.83e-39

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 132.72  E-value: 1.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   9 MAMPSWFDIIGLspDSQEDEVGIKQAAENVKALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCW 87
Cdd:COG0400   46 PGGRAWFDLSFL--EGREDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  88 LPLRASFPqgPISGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSgMMHSSCIEEMMDVKQFIDKH 167
Cdd:COG0400  124 LPGEEALP--APEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAER 198


                 ..
gi 686586446 168 LP 169
Cdd:COG0400  199 LA 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
19-166 4.03e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 56.55  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  19 GLSPDSQEDEVGIKQAAENVKALIDQEVKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALScwlPLRASFPQGP 98
Cdd:COG2267   67 GRSDGPRGHVDSFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA---PAYRADPLLG 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  99 ISG-------VNKEIAVLQC-----HGDCDPLVPlmfgSLTVEKLKSMINPaNVTFRTYSGMMHSSCIEE-----MMDVK 161
Cdd:COG2267  142 PSArwlralrLAEALARIDVpvlvlHGGADRVVP----PEAARRLAARLSP-DVELVLLPGARHELLNEPareevLAAIL 216


                 ....*
gi 686586446 162 QFIDK 166
Cdd:COG2267  217 AWLER 221
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
29-150 9.08e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 52.57  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  29 VGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVVALSCWL-----PLRASFPQGPi 99
Cdd:COG0657   62 AALEDAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLdltasPLRADLAGLP- 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 686586446 100 sgvnkeiAVLQCHGDCDPLVP--LMFgsltVEKLKSMINPanVTFRTYSGMMH 150
Cdd:COG0657  141 -------PTLIVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
COG4099 COG4099
Predicted peptidase [General function prediction only];
34-152 2.48e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 51.51  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  34 AAENVKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALScwlplrasfPQGPISGVN--KEIAVLQ 110
Cdd:COG4099  105 ALDAVLALLDDLIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPIC---------GGGDPANAAnlKKVPVWI 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 686586446 111 CHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSGMMHSS 152
Cdd:COG4099  176 FHGAKDDVVPVEESRAMVEALKAA--GADVKYTEYPGVGHNS 215
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 27-121 2.01e-07

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 49.23  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  27 DEVGIkqaaenVKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCwLPLRASFPQGPISGvnKE 105
Cdd:COG3509  113 DDVAF------IAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAACAPG--RP 183

                         90
                 ....*....|....*.
gi 686586446 106 IAVLQCHGDCDPLVPL 121
Cdd:COG3509  184 VPVLVIHGTADPTVPY 199
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
33-169 1.62e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 46.55  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  33 QAAENVKALIDQEVKNG-IPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCWLPLRASFPQG-------------- 97
Cdd:COG1506   72 DEVDDVLAAIDYLAARPyVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTreyterlmggpwed 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  98 --------PISGVNK-EIAVLQCHGDCDPLVPLMFGSLTVEKLKSmiNPANVTFRTYSGMMH----SSCIEEMMDVKQFI 164
Cdd:COG1506  152 peayaarsPLAYADKlKTPLLLIHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGHgfsgAGAPDYLERILDFL 229


                 ....*
gi 686586446 165 DKHLP 169
Cdd:COG1506  230 DRHLK 234
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
28-151 2.57e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  28 EVGIKQAAENVKALIDqEVKN--GIPSNRIILGGFSQGGALSLYTAlTTQQKLAGVVALSCWLPLRASFPQGP-ISGvnk 104
Cdd:COG0412   83 ALDPELLAADLRAALD-WLKAqpEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPADDLLDLAArIKA--- 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 686586446 105 eiAVLQCHGDCDPLVPLMfgslTVEKLKSMINPANV--TFRTYSGMMHS 151
Cdd:COG0412  158 --PVLLLYGEKDPLVPPE----QVAALEAALAAAGVdvELHVYPGAGHG 200
PRK11460 PRK11460
putative hydrolase; Provisional
 14-121 5.24e-04

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 39.25  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446  14 WFDIIGLSPDSQEDEVgikqaAENVKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VVALS-CW 87
Cdd:PRK11460  65 WFSVQGITEDNRQARV-----AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY 138

                         90       100       110
                 ....*....|....*....|....*....|....
gi 686586446  88 lplrASFPQGPISGVnkeiAVLQCHGDCDPLVPL 121
Cdd:PRK11460 139 ----ASLPETAPTAT----TIHLIHGGEDPVIDV 164
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 13-120 1.98e-03

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


Pssm-ID: 461110  Cd Length: 208  Bit Score: 37.26  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446   13 SWFdiigLSPDSQEDEVGIKQAaenVKALIDQEVKNGiPSNRIIlgGFSQGGALSLYtALTTQQKLAG--------VVAL 84
Cdd:pfam03959  70 AWF----FGDDDTNEYLGLDES---LDYVRDYIKENG-PFDGIL--GFSQGAALAAI-LASLLEEGLPlshpplkfAILF 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 686586446   85 SCWLPL----RASFPQGPISgvnkeIAVLQCHGDCDPLVP 120
Cdd:pfam03959 139 SGFRPRppiyQEYYSEDPIQ-----TPSLHVIGELDTVVP 173
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
53-85 3.89e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 36.46  E-value: 3.89e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 686586446  53 NRIILGGFSQGGALSLYTALtTQQKLAGVVALS 85
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAA-RYPDVAGLVLLS 115
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 54-95 5.05e-03

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: 36.33  E-value: 5.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 686586446   54 RIILGGFSQGGALSLYTALTTQQKLAGVVALS----------CWLPLRASFP 95
Cdd:pfam00561  70 KVNLVGHSMGGLIALAYAAKYPDRVKALVLLGaldppheldeADRFILALFP 121
Cutinase pfam01083
Cutinase;
23-82 6.36e-03

Cutinase;


Pssm-ID: 395860  Cd Length: 173  Bit Score: 35.40  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686586446   23 DSQEDEVGIKQAAENVKALIdQEVKNGIPSNRIILGGFSQGG-----ALSLYTALtTQQKLAGVV 82
Cdd:pfam01083  50 LGQLYAGSASAGANAAAALI-NSANSKCPDTKIVLGGYSQGAqvmdnAICGLPAA-VADKVAAVV 112
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 30-72 7.23e-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: 35.17  E-value: 7.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 686586446  30 GIKQAAENVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 72
Cdd:cd00741    2 GFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 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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