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Conserved domains on  [gi|1969806674|ref|NP_001378938|]
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(Lyso)-N-acylphosphatidylethanolamine lipase isoform b [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
 32-314 4.74e-65

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: 210.15  E-value: 4.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  32 IWTVTVSPEQNDRTpLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRET 110
Cdd:PLN02894   94 INTVTFDSKEDAPT-LVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 111 MGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 187 GPWGPGLVQRFRpdfKRKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1969806674 259 ITMIYGSDTWIDTSTGKKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 32-314 4.74e-65

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 210.15  E-value: 4.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  32 IWTVTVSPEQNDRTpLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRET 110
Cdd:PLN02894   94 INTVTFDSKEDAPT-LVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 111 MGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 187 GPWGPGLVQRFRpdfKRKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1969806674 259 ITMIYGSDTWIDTSTGKKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 42-317 2.31e-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: 108.93  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  42 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLG 120
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 121 HSLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirappawvkavasvlgrsnplavlrvagpwgpglvqrfrpD 200
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------E 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 201 FKRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGS-DTWIDTSTGKKVK 278
Cdd:COG0596   123 VLAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEkDPIVPPALARRLA 184

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1969806674 279 MQRPDSYVRdmEIKGASHHVYADQPHIFNAVVEEICDSV 317
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.
 45-270 1.34e-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: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  45 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 124 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPAWVKAVASVLGR--SNPLAVLRVAGPWGPGLVQRFRP 199
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPnpLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1969806674 200 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSDTWID 270
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLV 213
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 117-187 5.48e-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: 41.08  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 117 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PAWVKAVASVlgrSNPLAVLR 184
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                  ...
gi 1969806674 185 VAG 187
Cdd:cd12808   268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 32-314 4.74e-65

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 210.15  E-value: 4.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  32 IWTVTVSPEQNDRTpLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFP-RDPEGAEDEFVTSIETWRET 110
Cdd:PLN02894   94 INTVTFDSKEDAPT-LVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 111 MGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSE--IRAPPAWVKAVASVLGRSN--PLAVLRVA 186
Cdd:PLN02894  173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 187 GPWGPGLVQRFRpdfKRKFADFF--------EDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRkdVP 258
Cdd:PLN02894  253 GPWGPNLVRRYT---TARFGAHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEWK--VP 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1969806674 259 ITMIYGSDTWIDTSTGKKV--KMQRPDSYVRdmeIKGASHHVYADQPHIFNAVVEEIC 314
Cdd:PLN02894  328 TTFIYGRHDWMNYEGAVEArkRMKVPCEIIR---VPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 42-317 2.31e-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: 108.93  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  42 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEG-AEDefvtsIETWRETMGIPSMILLG 120
Cdd:COG0596    21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADD-----LAALLDALGLERVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 121 HSLGGFLATSYSIKYPDRVKHLILVDpwgfplrptnpseirappawvkavasvlgrsnplavlrvagpwgpglvqrfrpD 200
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVD-----------------------------------------------------E 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 201 FKRKFADFFEDDtiseyiyhcnaqnPSGETAFKAMMESF-GWARRPMLERIhlirkDVPITMIYGS-DTWIDTSTGKKVK 278
Cdd:COG0596   123 VLAALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEkDPIVPPALARRLA 184

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1969806674 279 MQRPDSYVRdmEIKGASHHVYADQPHIFNAVVEEICDSV 317
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.
 45-270 1.34e-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: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  45 TPLVMVHGFGGGVGLWILNMDSLS-ARRTLHTFDLLGFGRSSRPafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSL 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 124 GGFLATSYSIKYPDRVKHLILVDP--WGFPLRPTNPSEIRAPPAWVKAVASVLGR--SNPLAVLRVAGPWGPGLVQRFRP 199
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVADFAPnpLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1969806674 200 DFKRKFADFFEDDTISEYIYHCNAQNpsgetafkammesfGWARRPMLERIHliRKDVPITMIYGSDTWID 270
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLFIE--------------TWSTELRAKFLG--RLDEPTLIIWGDQDPLV 213
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-150 2.27e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 84.61  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  43 DRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpafPRDPEGAEDEFVTSIETWRETMGIPSMILLGHS 122
Cdd:PRK14875  130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                          90       100
                  ....*....|....*....|....*...
gi 1969806674 123 LGGFLATSYSIKYPDRVKHLILVDPWGF 150
Cdd:PRK14875  206 MGGAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
39-148 9.69e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 77.73  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  39 PEQNDRTPLVMVHGFGGGVGLWILNMDSLSARR-TLHTFDLLGFGRSSRP-AFPRDPEGAEDEFVTSIETWRETMGIPsM 116
Cdd:COG2267    23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPrGHVDSFDDYVDDLRAALDALRARPGLP-V 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1969806674 117 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPW 148
Cdd:COG2267   102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PLN02578 PLN02578
hydrolase
 40-308 3.73e-13

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 69.10  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  40 EQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIetwRETMGIPSmILL 119
Cdd:PLN02578   82 VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFV---KEVVKEPA-VLV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 120 GHSLGGFLATSYSIKYPDRVKHLILVDPWG-FplrptnPSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLV---- 194
Cdd:PLN02578  158 GNSLGGFTALSTAVGYPELVAGVALLNSAGqF------GSESREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGFLfwqa 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 195 ---QRFRPDFKRKFADFFE-DDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIhLIRKDVPITMIYG-SDTWI 269
Cdd:PLN02578  232 kqpSRIESVLKSVYKDKSNvDDYLVESITEPAADPNAGEVYYRLMSRFLFNQSRYTLDSL-LSKLSCPLLLLWGdLDPWV 310

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1969806674 270 DTSTGKKVKMQRPDSYVRDMEikgASHHVYADQPHIFNA 308
Cdd:PLN02578  311 GPAKAEKIKAFYPDTTLVNLQ---AGHCPHDEVPEQVNK 346
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 47-309 3.43e-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: 64.80  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  47 LVMVHGFGGGVGLWIlnmDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETmgipsmILLGHSLGGF 126
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 127 LATSYSikyPDRVKHLILVDPWGFPLRPtnpseIRAPPAWVKAVASVLGRSnplavlrvagpwgpglvqRFRPDFKRkfA 206
Cdd:pfam12697  72 VALAAA---AAALVVGVLVAPLAAPPGL-----LAALLALLARLGAALAAP------------------AWLAAESL--A 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 207 DFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPmlerihlirkdVPITMIYGSDTWIDTSTGKKVKMQRPDSYV 286
Cdd:pfam12697 124 RGFLDDLPADAEWAAALARLAALLAALALLPLAAWRDLP-----------VPVLVLAEEDRLVPELAQRLLAALAGARLV 192

                         250       260
                  ....*....|....*....|...
gi 1969806674 287 rdmEIKGASHHVYaDQPHIFNAV 309
Cdd:pfam12697 193 ---VLPGAGHLPL-DDPEEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 47-206 8.41e-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: 63.77  E-value: 8.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  47 LVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLLGFGRSS-RPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLG 124
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSDgKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 125 GFLATSYSIKYPDRVKHLILVDPWgfpLRPTNPSeiraPPAWVKAVASVLGRSNPLavLRVAGPWGPGLVQRfRPDFKRK 204
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAPA---LKIKPYL----APPILKLLAKLLGKLFPR--LRVPNNLLPDSLSR-DPEVVAA 156


                  ..
gi 1969806674 205 FA 206
Cdd:pfam12146 157 YA 158
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 42-312 1.55e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 60.91  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  42 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETW--------RETMGI 113
Cdd:PLN02824   27 TSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP----NPRSAPPNSFYTFETWgeqlndfcSDVVGD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 114 PSMILLgHSLGGFLATSYSIKYPDRVKHLILVDPwgfPLRPTNpseIRAPPAW----VKAVASVLgRSNPLAVLRVAGPW 189
Cdd:PLN02824  103 PAFVIC-NSVGGVVGLQAAVDAPELVRGVMLINI---SLRGLH---IKKQPWLgrpfIKAFQNLL-RETAVGKAFFKSVA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 190 GPGLVQRFrpdFKRKFADffeDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIhLIRKDVPITMIYG-SDTW 268
Cdd:PLN02824  175 TPETVKNI---LCQCYHD---DSAVTDELVEAILRPGLEPGAVDVFLDFISYSGGPLPEEL-LPAVKCPVLIAWGeKDPW 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1969806674 269 IDTSTGKkvKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEE 312
Cdd:PLN02824  248 EPVELGR--AYANFDAVEDFIVLPGVGHCPQDEAPELVNPLIES 289
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 33-146 2.62e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 60.62  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  33 WTVTVSPEQNDRTP-LVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAfprdpegaedEFVTSIETW---- 107
Cdd:PLN02679   76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP----------GFSYTMETWaeli 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1969806674 108 ----RETMGIPSmILLGHSLGGF---LATSYSikYPDRVKHLILVD 146
Cdd:PLN02679  146 ldflEEVVQKPT-VLIGNSVGSLacvIAASES--TRDLVRGLVLLN 188
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 48-171 5.49e-10

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 60.21  E-value: 5.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  48 VMVHGFGGGVGLWILNM-----DSLSARRTLHTFDLLGFGRSSRPAfprDPEGAEDEFVTSIE-TWRETMGIPSMILLGH 121
Cdd:PLN03087  205 LFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIErSVLERYKVKSFHIVAH 281

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1969806674 122 SLGGFLATSYSIKYPDRVKHLILVDPWGFPLrptnPSEIRAPPAWVKAVA 171
Cdd:PLN03087  282 SLGCILALALAVKHPGAVKSLTLLAPPYYPV----PKGVQATQYVMRKVA 327
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 41-147 1.04e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 54.84  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  41 QNDRTPLVMVHGFGGGVGLWILNMDSLSAR-RTLHTFDLlgfgrssrPAFPRDPEGAEDEFVTSIETWRETMGIPSMILL 119
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNY--------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLV 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1969806674 120 GHSLGGFLATSY--SIKYPDRVKHLILVDP 147
Cdd:COG1075    74 GHSMGGLVARYYlkRLGGAAKVARVVTLGT 103
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
30-145 1.40e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 51.94  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  30 NKIWTVTVSpEQNdrTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSrpAFprdpeGAedefvTSIETWRE 109
Cdd:PRK10349    2 NNIWWQTKG-QGN--VHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR--GF-----GA-----LSLADMAE 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1969806674 110 TM---GIPSMILLGHSLGGFLATSYSIKYPDRVKHLILV 145
Cdd:PRK10349   67 AVlqqAPDKAIWLGWSLGGLVASQIALTHPERVQALVTV 105
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
48-311 4.82e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.86  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  48 VMVHGFGGG---VGLWilnmdslsARR------TLHTFDLLGFGRSSRPAFPRDPE----GAEDEFVTSIETWRETmgip 114
Cdd:COG1647    19 LLLHGFTGSpaeMRPL--------AEAlakagyTVYAPRLPGHGTSPEDLLKTTWEdwleDVEEAYEILKAGYDKV---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 115 smILLGHSLGGFLATSYSIKYPDrVKHLILVDPwgfPLRPTNPSEIRAPpawvkavasvlgrsnplaVLRVAGPWgpglv 194
Cdd:COG1647    87 --IVIGLSMGGLLALLLAARYPD-VAGLVLLSP---ALKIDDPSAPLLP------------------LLKYLARS----- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 195 qrfrpdfKRKFADFFEDDTISEYIYHCNAQNpsgetAFKAMMESFGWARRPmLERIHlirkdVPITMIYGS-DTWIDTST 273
Cdd:COG1647   138 -------LRGIGSDIEDPEVAEYAYDRTPLR-----ALAELQRLIREVRRD-LPKIT-----APTLIIQSRkDEVVPPES 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1969806674 274 GKKVKMQRPDSYVRDMEIKGASH--HVYADQPHIFNAVVE 311
Cdd:COG1647   200 ARYIYERLGSPDKELVWLEDSGHviTLDKDREEVAEEILD 239
PRK10673 PRK10673
esterase;
38-146 1.11e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.88  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  38 SPEQ-NDRTPLVMVHG-FGGGVGLWILNMDsLSARRTLHTFDLLGFGRSsrpafPRDPEGAEDEFVTSIETWRETMGIPS 115
Cdd:PRK10673    9 TAQNpHNNSPIVLVHGlFGSLDNLGVLARD-LVNDHDIIQVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDALQIEK 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1969806674 116 MILLGHSLGGFLATSYSIKYPDRVKHLILVD 146
Cdd:PRK10673   83 ATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 40-140 4.74e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 44.21  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  40 EQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPafprDPEGAEDEFVTSIETWRETMGIPSMILL 119
Cdd:PRK03592   23 ETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLV 98

                          90       100
                  ....*....|....*....|.
gi 1969806674 120 GHSLGGFLATSYSIKYPDRVK 140
Cdd:PRK03592   99 GHDWGSALGFDWAARHPDRVR 119
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 42-147 3.56e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 41.79  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  42 NDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETW--RETMGIPSMILL 119
Cdd:PLN03084  125 NNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLidELKSDKVSLVVQ 204

                          90       100       110
                  ....*....|....*....|....*....|
gi 1969806674 120 GHslggF--LATSYSIKYPDRVKHLILVDP 147
Cdd:PLN03084  205 GY----FspPVVKYASAHPDKIKKLILLNP 230
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 117-187 5.48e-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: 41.08  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674 117 ILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP------------PAWVKAVASVlgrSNPLAVLR 184
Cdd:cd12808   191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                  ...
gi 1969806674 185 VAG 187
Cdd:cd12808   268 AAG 270
YpfH COG0400
Predicted esterase [General function prediction only];
40-165 6.26e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 40.28  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  40 EQNDRTPLVMVHGFGG----GVGLWilnmDSLSARRTLH-----TFDLLGFGRS----SRPAFPRDPEGAE---DEFVTS 103
Cdd:COG0400     1 GGPAAPLVVLLHGYGGdeedLLPLA----PELALPGAAVlapraPVPEGPGGRAwfdlSFLEGREDEEGLAaaaEALAAF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1969806674 104 IETWRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILvdpwgfpLRPTNPSEIRAPPA 165
Cdd:COG0400    77 IDELEARYGIDPerIVLAGFSQGAAMALSLALRRPELLAGVVA-------LSGYLPGEEALPAP 133
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
31-147 1.50e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 39.23  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  31 KIWTVTVSPEQNDRTPLVM-VHGFGGGVGL-WILNMDSLSAR--RTLhTFDLLGFGRSSRPAfprdPEGAEDEFVTSIET 106
Cdd:COG1506     9 TLPGWLYLPADGKKYPVVVyVHGGPGSRDDsFLPLAQALASRgyAVL-APDYRGYGESAGDW----GGDEVDDVLAAIDY 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1969806674 107 WRETMGIPS--MILLGHSLGGFLATSYSIKYPDRVKHLILVDP 147
Cdd:COG1506    84 LAARPYVDPdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG 126
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 47-148 2.24e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.13  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806674  47 LVMVHGFGGGVGLWILNMDSLsARRTLHT--FDLLGFGRSS-RPAFPRDPEgAEDeFVTSIETWRETMGIPS--MILLGH 121
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRL-AELGFNVlaFDYRGYGESEgEPREEGSPE-RRD-ARAAVDYLRTLPGVDPerIGLLGI 116

                          90       100
                  ....*....|....*....|....*..
gi 1969806674 122 SLGGFLATSYSIKYPdRVKHLILVDPW 148
Cdd:COG1073   117 SLGGGYALNAAATDP-RVKAVILDSPF 142
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 115-163 4.94e-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: 4.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1969806674 115 SMILLGHSLGGflATSY-SIKYPDRVKHLILVDPWGFPLRPTNPSEIRAP 163
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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