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Conserved domains on  [gi|386781874|ref|NP_001247685|]
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(Lyso)-N-acylphosphatidylethanolamine lipase [Macaca mulatta]

Protein Classification

alpha/beta hydrolase domain-containing protein( domain architecture ID 1005082)

alpha/beta hydrolase (abhydrolase) domain-containing protein

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02894 super family cl30398
hydrolase, alpha/beta fold family protein
11-338 3.55e-67

hydrolase, alpha/beta fold family protein


The actual alignment was detected with superfamily member PLN02894:

Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 216.31  E-value: 3.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  11 GWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIWTVTVSPE-----------QKDRTPLVMVH 75
Cdd:PLN02894  34 SLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtfdsKEDAPTLVMVH 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  76 GFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 155 YSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPTWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfKRKFA 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---TARFG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 231 DFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSNTWIDTSTGKKV- 301
Cdd:PLN02894 270 AHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGAVEAr 347
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 386781874 302 -KMQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 348 kRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
11-338 3.55e-67

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 216.31  E-value: 3.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  11 GWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIWTVTVSPE-----------QKDRTPLVMVH 75
Cdd:PLN02894  34 SLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtfdsKEDAPTLVMVH 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  76 GFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 155 YSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPTWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfKRKFA 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---TARFG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 231 DFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSNTWIDTSTGKKV- 301
Cdd:PLN02894 270 AHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGAVEAr 347
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 386781874 302 -KMQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 348 kRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
67-341 1.16e-27

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: 107.78  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  67 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLGH 145
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVGH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 146 SLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirapptwvkavasvlgrsnplavlrvagpwgpglvqrfrpDF 225
Cdd:COG0596   97 SMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------EV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 226 KRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGSN-TWIDTSTGKKVKM 303
Cdd:COG0596  124 LAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAE 185
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 386781874 304 QRPDSYVRdmEIEGASHHVYADQPHIFNAVVEEICDSV 341
Cdd:COG0596  186 LLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-327 1.46e-23

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: 97.19  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874   69 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  148 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPTWVKAVASVLGR--SNPLAVLRVAGPWGPGLVQRFRP 223
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPnpLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  224 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSNTWIDTSTGkKVKM 303
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLVPPQA-LEKL 221
                         250       260
                  ....*....|....*....|....
gi 386781874  304 QRPDSYVRDMEIEGASHHVYADQP 327
Cdd:pfam00561 222 AQLFPNARLVVIPDAGHFAFLEGP 245
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
141-211 1.08e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 40.30  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 208
Cdd:cd12808  191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267

                 ...
gi 386781874 209 VAG 211
Cdd:cd12808  268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
11-338 3.55e-67

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 216.31  E-value: 3.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  11 GWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIWTVTVSPE-----------QKDRTPLVMVH 75
Cdd:PLN02894  34 SLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtfdsKEDAPTLVMVH 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  76 GFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 155 YSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPTWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfKRKFA 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---TARFG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 231 DFFEDDTISE--------YIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSNTWIDTSTGKKV- 301
Cdd:PLN02894 270 AHSTGDILSEeesklltdYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGAVEAr 347
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 386781874 302 -KMQRPDSYVRdmeIEGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 348 kRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
67-341 1.16e-27

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: 107.78  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  67 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLGH 145
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVGH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 146 SLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirapptwvkavasvlgrsnplavlrvagpwgpglvqrfrpDF 225
Cdd:COG0596   97 SMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------EV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 226 KRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGSN-TWIDTSTGKKVKM 303
Cdd:COG0596  124 LAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAE 185
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 386781874 304 QRPDSYVRdmEIEGASHHVYADQPHIFNAVVEEICDSV 341
Cdd:COG0596  186 LLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-327 1.46e-23

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: 97.19  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874   69 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  148 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPTWVKAVASVLGR--SNPLAVLRVAGPWGPGLVQRFRP 223
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPnpLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  224 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSNTWIDTSTGkKVKM 303
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLVPPQA-LEKL 221
                         250       260
                  ....*....|....*....|....
gi 386781874  304 QRPDSYVRDMEIEGASHHVYADQP 327
Cdd:pfam00561 222 AQLFPNARLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
67-174 2.53e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 85.00  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  67 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHS 146
Cdd:PRK14875 130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205
                         90       100
                 ....*....|....*....|....*...
gi 386781874 147 LGGFLATSYSIKYPDRVKHLILVDPWGF 174
Cdd:PRK14875 206 MGGAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
63-172 6.44e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 78.51  E-value: 6.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  63 PEQKDRTPLVMVHGFGGGVGLWILNMDSLSARR-TLHTFDLLGFGRSSRP-AFPRDPEGAEDEFVTSIETWRETMGIPsM 140
Cdd:COG2267   23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPrGHVDSFDDYVDDLRAALDALRARPGLP-V 101
                         90       100       110
                 ....*....|....*....|....*....|..
gi 386781874 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPW 172
Cdd:COG2267  102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PLN02578 PLN02578
hydrolase
64-173 1.95e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 67.17  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  64 EQKDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIetwRETMGIPSmILL 143
Cdd:PLN02578  82 VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFV---KEVVKEPA-VLV 157
                         90       100       110
                 ....*....|....*....|....*....|
gi 386781874 144 GHSLGGFLATSYSIKYPDRVKHLILVDPWG 173
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNSAG 187
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
71-230 1.02e-11

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: 63.77  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874   71 LVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLLGFGRSS-RPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLG 148
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  149 GFLATSYSIKYPDRVKHLILVDPWgfpLRPTNPSeiraPPTWVKAVASVLGRSNPLavLRVAGPWGPGLVQRfRPDFKRK 228
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAPA---LKIKPYL----APPILKLLAKLLGKLFPR--LRVPNNLLPDSLSR-DPEVVAA 156

                  ..
gi 386781874  229 FA 230
Cdd:pfam12146 157 YA 158
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
71-333 1.26e-11

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 63.26  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874   71 LVMVHGFGGGVGLWIlnmDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETmgipsmILLGHSLGGF 150
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  151 LATSYsikYPDRVKHLILVDPWGFPLRPTNPseirapptwvkavasvlgrsnplAVLRVAGPWGPGLVQRFRPDFKRkfA 230
Cdd:pfam12697  72 VALAA---AAAALVVGVLVAPLAAPPGLLAA-----------------------LLALLARLGAALAAPAWLAAESL--A 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  231 DFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPmlerihlirkdVPITMIYGSNTWIDTSTGKKVKMQRPDSYV 310
Cdd:pfam12697 124 RGFLDDLPADAEWAAALARLAALLAALALLPLAAWRDLP-----------VPVLVLAEEDRLVPELAQRLLAALAGARLV 192
                         250       260
                  ....*....|....*....|...
gi 386781874  311 rdmEIEGASHHVYaDQPHIFNAV 333
Cdd:pfam12697 193 ---VLPGAGHLPL-DDPEEVAEA 211
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
63-195 3.11e-10

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 60.98  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  63 PEQKDRTPLVMVHGFGGGVGLWILNM-----DSLSARRTLHTFDLLGFGRSSRPAfprDPEGAEDEFVTSIE-TWRETMG 136
Cdd:PLN03087 196 KDNKAKEDVLFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIErSVLERYK 272
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386781874 137 IPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLrptnPSEIRAPPTWVKAVA 195
Cdd:PLN03087 273 VKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAPPYYPV----PKGVQATQYVMRKVA 327
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
65-171 4.52e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 55.99  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  65 QKDRTPLVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLlgfgrssrPAFPRDPEGAEDEFVTSIETWRETMGIPSMILL 143
Cdd:COG1075    2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY--------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLV 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 386781874 144 GHSLGGFLATSY--SIKYPDRVKHLILVDP 171
Cdd:COG1075   74 GHSMGGLVARYYlkRLGGAAKVARVVTLGT 103
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
57-170 4.55e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 60.24  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  57 WTVTVSPEQKDRTP-LVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAfprdpegaedEFVTSIETW---- 131
Cdd:PLN02679  76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP----------GFSYTMETWaeli 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 386781874 132 ----RETMGIPSmILLGHSLGGF---LATSYSikYPDRVKHLILVD 170
Cdd:PLN02679 146 ldflEEVVQKPT-VLIGNSVGSLacvIAASES--TRDLVRGLVLLN 188
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
69-171 1.63e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 58.21  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  69 TPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETW--------RETMGIPSM 140
Cdd:PLN02824  30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWgeqlndfcSDVVGDPAF 105
                         90       100       110
                 ....*....|....*....|....*....|.
gi 386781874 141 ILLgHSLGGFLATSYSIKYPDRVKHLILVDP 171
Cdd:PLN02824 106 VIC-NSVGGVVGLQAAVDAPELVRGVMLINI 135
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
54-169 2.36e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 51.17  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  54 NKIWTVTVSpeqKDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIEtwre 133
Cdd:PRK10349   2 NNIWWQTKG---QGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPD---- 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 386781874 134 tmgipSMILLGHSLGGFLATSYSIKYPDRVKHLILV 169
Cdd:PRK10349  75 -----KAIWLGWSLGGLVASQIALTHPERVQALVTV 105
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
72-335 8.73e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.47  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  72 VMVHGFGGG---VGLWilnmdslsARR------TLHTFDLLGFGRSSRPAFPRDPE----GAEDEFVTSIETWRETmgip 138
Cdd:COG1647   19 LLLHGFTGSpaeMRPL--------AEAlakagyTVYAPRLPGHGTSPEDLLKTTWEdwleDVEEAYEILKAGYDKV---- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 139 smILLGHSLGGFLATSYSIKYPDrVKHLILVDPwgfPLRPTNPSEIRAPptwvkavasvlgrsnplaVLRVAGPWgpglv 218
Cdd:COG1647   87 --IVIGLSMGGLLALLLAARYPD-VAGLVLLSP---ALKIDDPSAPLLP------------------LLKYLARS----- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 219 qrfrpdfKRKFADFFEDDTISEYIYHCNAQNpsgetAFKAMMESFGWARRPmLERIHlirkdVPITMIYGSN-TWIDTST 297
Cdd:COG1647  138 -------LRGIGSDIEDPEVAEYAYDRTPLR-----ALAELQRLIREVRRD-LPKIT-----APTLIIQSRKdEVVPPES 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 386781874 298 GKKVKMQRPDSYVRDMEIEGASH--HVYADQPHIFNAVVE 335
Cdd:COG1647  200 ARYIYERLGSPDKELVWLEDSGHviTLDKDREEVAEEILD 239
PRK10673 PRK10673
esterase;
62-170 3.02e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 44.72  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  62 SPEQ-KDRTPLVMVHG-FGGGVGLWILNMDsLSARRTLHTFDLLGFGRSsrpafPRDPEGAEDEFVTSIETWRETMGIPS 139
Cdd:PRK10673   9 TAQNpHNNSPIVLVHGlFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDALQIEK 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 386781874 140 MILLGHSLGGFLATSYSIKYPDRVKHLILVD 170
Cdd:PRK10673  83 ATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
64-164 9.00e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 43.44  E-value: 9.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  64 EQKDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETWRETMGIPSMILL 143
Cdd:PRK03592  23 ETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLV 98
                         90       100
                 ....*....|....*....|.
gi 386781874 144 GHSLGGFLATSYSIKYPDRVK 164
Cdd:PRK03592  99 GHDWGSALGFDWAARHPDRVR 119
YpfH COG0400
Predicted esterase [General function prediction only];
64-188 6.59e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 40.28  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  64 EQKDRTPLVMVHGFGG----GVGLWilnmDSLSARRTLH-----TFDLLGFGRS----SRPAFPRDPEGAE---DEFVTS 127
Cdd:COG0400    1 GGPAAPLVVLLHGYGGdeedLLPLA----PELALPGAAVlapraPVPEGPGGRAwfdlSFLEGREDEEGLAaaaEALAAF 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386781874 128 IETWRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILvdpwgfpLRPTNPSEIRAPP 188
Cdd:COG0400   77 IDELEARYGIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA-------LSGYLPGEEALPA 132
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
141-211 1.08e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 40.30  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PTWVKAVASVlgrSNPLAVLR 208
Cdd:cd12808  191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267

                 ...
gi 386781874 209 VAG 211
Cdd:cd12808  268 AAG 270
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
67-171 1.39e-03

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 40.25  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  67 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETW--RETMGIPSMILLG 144
Cdd:PLN03084 126 NNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLidELKSDKVSLVVQG 205
                         90       100
                 ....*....|....*....|....*....
gi 386781874 145 HslggF--LATSYSIKYPDRVKHLILVDP 171
Cdd:PLN03084 206 Y----FspPVVKYASAHPDKIKKLILLNP 230
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
55-171 1.56e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 39.61  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  55 KIWTVTVSPEQKDRTPLVM-VHGFGGGVGL-WILNMDSLSAR--RTLhTFDLLGFGRSSRPAfprdPEGAEDEFVTSIET 130
Cdd:COG1506    9 TLPGWLYLPADGKKYPVVVyVHGGPGSRDDsFLPLAQALASRgyAVL-APDYRGYGESAGDW----GGDEVDDVLAAIDY 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 386781874 131 WRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILVDP 171
Cdd:COG1506   84 LAARPYVDPdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG 126
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
71-172 1.67e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.51  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386781874  71 LVMVHGFGGGVGLWILNMDSLsARRTLHT--FDLLGFGRSS-RPAFPRDPEgAEDeFVTSIETWRETMGIPS--MILLGH 145
Cdd:COG1073   40 VVVAHGNGGVKEQRALYAQRL-AELGFNVlaFDYRGYGESEgEPREEGSPE-RRD-ARAAVDYLRTLPGVDPerIGLLGI 116
                         90       100
                 ....*....|....*....|....*..
gi 386781874 146 SLGGFLATSYSIKYPdRVKHLILVDPW 172
Cdd:COG1073  117 SLGGGYALNAAATDP-RVKAVILDSPF 142
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
139-187 5.57e-03

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 38.19  E-value: 5.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 386781874  139 SMILLGHSLGGflATSY-SIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP 187
Cdd:pfam03403 222 KIAVIGHSFGG--ATVIqSLSEDTRFRCGIALDAWMFPVGDDVYSKARQP 269
 
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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