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Conserved domains on  [gi|50658087|ref|NP_071343|]
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(Lyso)-N-acylphosphatidylethanolamine lipase isoform a [Homo sapiens]

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
 8-338 2.52e-66

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: 214.39  E-value: 2.52e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    8 QSQGWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIW------------TVTVSPEQNDRTpL 71
Cdd:PLN02894  31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWfrsasneprfinTVTFDSKEDAPT-L 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   72 VMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGF 150
Cdd:PLN02894 109 VMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGY 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  151 LATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfK 226
Cdd:PLN02894 189 VAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---T 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  227 RKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSDTWIDTSTG 298
Cdd:PLN02894 266 ARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGA 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 50658087  299 KKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 344 VEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 8-338 2.52e-66

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 214.39  E-value: 2.52e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    8 QSQGWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIW------------TVTVSPEQNDRTpL 71
Cdd:PLN02894  31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWfrsasneprfinTVTFDSKEDAPT-L 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   72 VMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGF 150
Cdd:PLN02894 109 VMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGY 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  151 LATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfK 226
Cdd:PLN02894 189 VAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---T 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  227 RKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSDTWIDTSTG 298
Cdd:PLN02894 266 ARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGA 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 50658087  299 KKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 344 VEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-341 3.30e-28

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: 109.32  E-value: 3.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  66 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLG 144
Cdd:COG0596  21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 145 HSLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirappawvkavasvlgrsnplavlrvagpwgpglvqrfrpD 224
Cdd:COG0596  96 HSMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------E 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 225 FKRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGS-DTWIDTSTGKKVK 302
Cdd:COG0596 123 VLAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEkDPIVPPALARRLA 184

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 50658087 303 MQRPDSYVRdmEIKGASHHVYADQPHIFNAVVEEICDSV 341
Cdd:COG0596 185 ELLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-294 2.59e-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: 96.80  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    69 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   148 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPAWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRP 223
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPNPlgRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658087   224 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSDTWID 294
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLV 213
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 141-211 8.18e-04

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: 40.69  E-value: 8.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PAWVKAVASVlgrSNPLAVLR 208
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                ...
gi 50658087 209 VAG 211
Cdd:cd12808 268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 8-338 2.52e-66

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 214.39  E-value: 2.52e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    8 QSQGWLSSWLpTWRPTSMSQLKNVEARILQCLQNKFLARYVSL----PNQNKIW------------TVTVSPEQNDRTpL 71
Cdd:PLN02894  31 RTRSLWPSPL-RWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWfrsasneprfinTVTFDSKEDAPT-L 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   72 VMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGF 150
Cdd:PLN02894 109 VMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGY 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  151 LATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRpdfK 226
Cdd:PLN02894 189 VAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRYT---T 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  227 RKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVPITMIYGSDTWIDTSTG 298
Cdd:PLN02894 266 ARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VPTTFIYGRHDWMNYEGA 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 50658087  299 KKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 338
Cdd:PLN02894 344 VEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-341 3.30e-28

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: 109.32  E-value: 3.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  66 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLG 144
Cdd:COG0596  21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 145 HSLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirappawvkavasvlgrsnplavlrvagpwgpglvqrfrpD 224
Cdd:COG0596  96 HSMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------E 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 225 FKRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGS-DTWIDTSTGKKVK 302
Cdd:COG0596 123 VLAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEkDPIVPPALARRLA 184

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 50658087 303 MQRPDSYVRdmEIKGASHHVYADQPHIFNAVVEEICDSV 341
Cdd:COG0596 185 ELLPNAELV--VLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-294 2.59e-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: 96.80  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    69 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   148 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPAWVKAVASVLGRSN--PLAVLRVAGPWGPGLVQRFRP 223
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPNPlgRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658087   224 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSDTWID 294
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLV 213
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-174 3.12e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 84.61  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   67 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHS 146
Cdd:PRK14875 130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                         90       100
                 ....*....|....*....|....*...
gi 50658087  147 LGGFLATSYSIKYPDRVKHLILVDPWGF 174
Cdd:PRK14875 206 MGGAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
63-172 1.14e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 77.73  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  63 PEQNDRTPLVMVHGFGGGVGLWILNMDSLSARR-TLHTFDLLGFGRSSRP-AFPRDPEGAEDEFVTSIETWRETMGIPsM 140
Cdd:COG2267  23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPrGHVDSFDDYVDDLRAALDALRARPGLP-V 101

                        90       100       110
                ....*....|....*....|....*....|..
gi 50658087 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPW 172
Cdd:COG2267 102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PLN02578 PLN02578
hydrolase
 64-332 8.33e-13

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 68.33  E-value: 8.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   64 EQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIetwRETMGIPSmILL 143
Cdd:PLN02578  82 VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFV---KEVVKEPA-VLV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  144 GHSLGGFLATSYSIKYPDRVKHLILVDPWG-FplrptnPSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLV---- 218
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNSAGqF------GSESREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGFLfwqa 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  219 ---QRFRPDFKRKFADFFE-DDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIhLIRKDVPITMIYG-SDTWI 293
Cdd:PLN02578 232 kqpSRIESVLKSVYKDKSNvDDYLVESITEPAADPNAGEVYYRLMSRFLFNQSRYTLDSL-LSKLSCPLLLLWGdLDPWV 310

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 50658087  294 DTSTGKKVKMQRPDSYVRDMEikgASHHVYADQPHIFNA 332
Cdd:PLN02578 311 GPAKAEKIKAFYPDTTLVNLQ---AGHCPHDEVPEQVNK 346
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 71-333 2.96e-12

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 65.19  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    71 LVMVHGFGGGVGLWIlnmDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETmgipsmILLGHSLGGF 150
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   151 LATSYSikyPDRVKHLILVDPWGFPLRPtnpseIRAPPAWVKAVASVLGRSnplavlrvagpwgpglvqRFRPDFKRkfA 230
Cdd:pfam12697  72 VALAAA---AAALVVGVLVAPLAAPPGL-----LAALLALLARLGAALAAP------------------AWLAAESL--A 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   231 DFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPmlerihlirkdVPITMIYGSDTWIDTSTGKKVKMQRPDSYV 310
Cdd:pfam12697 124 RGFLDDLPADAEWAAALARLAALLAALALLPLAAWRDLP-----------VPVLVLAEEDRLVPELAQRLLAALAGARLV 192

                         250       260
                  ....*....|....*....|...
gi 50658087   311 rdmEIKGASHHVYaDQPHIFNAV 333
Cdd:pfam12697 193 ---VLPGAGHLPL-DDPEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-230 7.25e-12

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: 64.16  E-value: 7.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087    71 LVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLLGFGRSS-RPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLG 148
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   149 GFLATSYSIKYPDRVKHLILVDPWgfpLRPTNPSeiraPPAWVKAVASVLGRSNPLavLRVAGPWGPGLVQRfRPDFKRK 228
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAPA---LKIKPYL----APPILKLLAKLLGKLFPR--LRVPNNLLPDSLSR-DPEVVAA 156


                  ..
gi 50658087   229 FA 230
Cdd:pfam12146 157 YA 158
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 66-336 2.64e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 60.52  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   66 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETW--------RETMGI 137
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWgeqlndfcSDVVGD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  138 PSMILLgHSLGGFLATSYSIKYPDRVKHLILVDPwgfPLRPTNpseIRAPPAW----VKAVASVLgRSNPLAVLRVAGPW 213
Cdd:PLN02824 103 PAFVIC-NSVGGVVGLQAAVDAPELVRGVMLINI---SLRGLH---IKKQPWLgrpfIKAFQNLL-RETAVGKAFFKSVA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  214 GPGLVQRFrpdFKRKFADffeDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIhLIRKDVPITMIYG-SDTW 292
Cdd:PLN02824 175 TPETVKNI---LCQCYHD---DSAVTDELVEAILRPGLEPGAVDVFLDFISYSGGPLPEEL-LPAVKCPVLIAWGeKDPW 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 50658087  293 IDTSTGKkvKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEE 336
Cdd:PLN02824 248 EPVELGR--AYANFDAVEDFIVLPGVGHCPQDEAPELVNPLIES 289
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 57-170 4.39e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 60.24  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   57 WTVTVSPEQNDRTP-LVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAfprdpegaedEFVTSIETW---- 131
Cdd:PLN02679  76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP----------GFSYTMETWaeli 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 50658087  132 ----RETMGIPSmILLGHSLGGF---LATSYSikYPDRVKHLILVD 170
Cdd:PLN02679 146 ldflEEVVQKPT-VLIGNSVGSLacvIAASES--TRDLVRGLVLLN 188
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 72-195 6.92e-10

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 59.82  E-value: 6.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   72 VMVHGFGGGVGLWILNM-----DSLSARRTLHTFDLLGFGRSSRPAfprDPEGAEDEFVTSIE-TWRETMGIPSMILLGH 145
Cdd:PLN03087 205 LFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIErSVLERYKVKSFHIVAH 281

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 50658087  146 SLGGFLATSYSIKYPDRVKHLILVDPWGFPLrptnPSEIRAPPAWVKAVA 195
Cdd:PLN03087 282 SLGCILALALAVKHPGAVKSLTLLAPPYYPV----PKGVQATQYVMRKVA 327
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 65-171 9.81e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 55.22  E-value: 9.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  65 QNDRTPLVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLlgfgrssrPAFPRDPEGAEDEFVTSIETWRETMGIPSMILL 143
Cdd:COG1075   2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY--------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLV 73

                        90       100       110
                ....*....|....*....|....*....|
gi 50658087 144 GHSLGGFLATSY--SIKYPDRVKHLILVDP 171
Cdd:COG1075  74 GHSMGGLVARYYlkRLGGAAKVARVVTLGT 103
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
54-169 3.08e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 50.79  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   54 NKIWTVTVSpEQNdrTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIEtwre 133
Cdd:PRK10349   2 NNIWWQTKG-QGN--VHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPD---- 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 50658087  134 tmgipSMILLGHSLGGFLATSYSIKYPDRVKHLILV 169
Cdd:PRK10349  75 -----KAIWLGWSLGGLVASQIALTHPERVQALVTV 105
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
72-335 4.90e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 47.24  E-value: 4.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  72 VMVHGFGGG---VGLWilnmdslsARR------TLHTFDLLGFGRSSRPAFPRDPE----GAEDEFVTSIETWRETmgip 138
Cdd:COG1647  19 LLLHGFTGSpaeMRPL--------AEAlakagyTVYAPRLPGHGTSPEDLLKTTWEdwleDVEEAYEILKAGYDKV---- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 139 smILLGHSLGGFLATSYSIKYPDrVKHLILVDPwgfPLRPTNPSEIRAPpawvkavasvlgrsnplaVLRVAGPWgpglv 218
Cdd:COG1647  87 --IVIGLSMGGLLALLLAARYPD-VAGLVLLSP---ALKIDDPSAPLLP------------------LLKYLARS----- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 219 qrfrpdfKRKFADFFEDDTISEYIYHCNAQNpsgetAFKAMMESFGWARRPmLERIHlirkdVPITMIYGS-DTWIDTST 297
Cdd:COG1647 138 -------LRGIGSDIEDPEVAEYAYDRTPLR-----ALAELQRLIREVRRD-LPKIT-----APTLIIQSRkDEVVPPES 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 50658087 298 GKKVKMQRPDSYVRDMEIKGASH--HVYADQPHIFNAVVE 335
Cdd:COG1647 200 ARYIYERLGSPDKELVWLEDSGHviTLDKDREEVAEEILD 239
PRK10673 PRK10673
esterase;
62-170 1.43e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.88  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   62 SPEQ-NDRTPLVMVHG-FGGGVGLWILNMDsLSARRTLHTFDLLGFGRSsrpafPRDPEGAEDEFVTSIETWRETMGIPS 139
Cdd:PRK10673   9 TAQNpHNNSPIVLVHGlFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDALQIEK 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 50658087  140 MILLGHSLGGFLATSYSIKYPDRVKHLILVD 170
Cdd:PRK10673  83 ATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 64-164 6.17e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 44.21  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   64 EQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETWRETMGIPSMILL 143
Cdd:PRK03592  23 ETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLV 98

                         90       100
                 ....*....|....*....|.
gi 50658087  144 GHSLGGFLATSYSIKYPDRVK 164
Cdd:PRK03592  99 GHDWGSALGFDWAARHPDRVR 119
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 66-171 4.50e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 41.79  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087   66 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETW--RETMGIPSMILL 143
Cdd:PLN03084 125 NNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLidELKSDKVSLVVQ 204

                         90       100       110
                 ....*....|....*....|....*....|
gi 50658087  144 GHslggF--LATSYSIKYPDRVKHLILVDP 171
Cdd:PLN03084 205 GY----FspPVVKYASAHPDKIKKLILLNP 230
YpfH COG0400
Predicted esterase [General function prediction only];
64-189 6.72e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 40.28  E-value: 6.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  64 EQNDRTPLVMVHGFGG----GVGLWilnmDSLSARRTLH-----TFDLLGFGRS----SRPAFPRDPEGAE---DEFVTS 127
Cdd:COG0400   1 GGPAAPLVVLLHGYGGdeedLLPLA----PELALPGAAVlapraPVPEGPGGRAwfdlSFLEGREDEEGLAaaaEALAAF 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50658087 128 IETWRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILvdpwgfpLRPTNPSEIRAPPA 189
Cdd:COG0400  77 IDELEARYGIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA-------LSGYLPGEEALPAP 133
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 141-211 8.18e-04

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: 40.69  E-value: 8.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087 141 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PAWVKAVASVlgrSNPLAVLR 208
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                ...
gi 50658087 209 VAG 211
Cdd:cd12808 268 AAG 270
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
55-171 1.54e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 39.61  E-value: 1.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  55 KIWTVTVSPEQNDRTPLVM-VHGFGGGVGL-WILNMDSLSAR--RTLhTFDLLGFGRSSRPAfprdPEGAEDEFVTSIET 130
Cdd:COG1506   9 TLPGWLYLPADGKKYPVVVyVHGGPGSRDDsFLPLAQALASRgyAVL-APDYRGYGESAGDW----GGDEVDDVLAAIDY 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 50658087 131 WRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILVDP 171
Cdd:COG1506  84 LAARPYVDPdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG 126
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 71-172 1.81e-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: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658087  71 LVMVHGFGGGVGLWILNMDSLsARRTLHT--FDLLGFGRSS-RPAFPRDPEgAEDeFVTSIETWRETMGIPS--MILLGH 145
Cdd:COG1073  40 VVVAHGNGGVKEQRALYAQRL-AELGFNVlaFDYRGYGESEgEPREEGSPE-RRD-ARAAVDYLRTLPGVDPerIGLLGI 116

                        90       100
                ....*....|....*....|....*..
gi 50658087 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 50658087   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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