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Conserved domains on  [gi|62859767|ref|NP_001017287|]
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(Lyso)-N-acylphosphatidylethanolamine lipase [Xenopus tropicalis]

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
 14-338 8.73e-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: 212.85  E-value: 8.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   14 TGWIPS---WCPTSMSKLKAVESRILQCIKNKFSAQYVSL----PDQNKIWTLTVSPE--------LQKKT---PLVMVH 75
Cdd:PLN02894  33 RSLWPSplrWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtFDSKEdapTLVMVH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   76 GFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFP-SDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLGGFLAAS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  155 YSIKFPERVKHLILVDPWGFPTMPTDPSE--IRSPPTWVKALAAVLGRSN--PLAVVRAAGPWGPGLVQRFrpdLKRKFQ 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFG 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  231 EYF--------EDDTIMEYIYHCNAQTPSGESAFKTMMERFGWAKRPMMSRINQIpkDLPITFIYGAETWIDRSTGERVK 302
Cdd:PLN02894 270 AHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEW--KVPTTFIYGRHDWMNYEGAVEAR 347

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 62859767  303 eERSDSFVKTLAIKGASHHVYADQPGTFNAVVEEIC 338
Cdd:PLN02894 348 -KRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 14-338 8.73e-66

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 212.85  E-value: 8.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   14 TGWIPS---WCPTSMSKLKAVESRILQCIKNKFSAQYVSL----PDQNKIWTLTVSPE--------LQKKT---PLVMVH 75
Cdd:PLN02894  33 RSLWPSplrWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtFDSKEdapTLVMVH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   76 GFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFP-SDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLGGFLAAS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  155 YSIKFPERVKHLILVDPWGFPTMPTDPSE--IRSPPTWVKALAAVLGRSN--PLAVVRAAGPWGPGLVQRFrpdLKRKFQ 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFG 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  231 EYF--------EDDTIMEYIYHCNAQTPSGESAFKTMMERFGWAKRPMMSRINQIpkDLPITFIYGAETWIDRSTGERVK 302
Cdd:PLN02894 270 AHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEW--KVPTTFIYGRHDWMNYEGAVEAR 347

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 62859767  303 eERSDSFVKTLAIKGASHHVYADQPGTFNAVVEEIC 338
Cdd:PLN02894 348 -KRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-341 2.06e-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: 107.01  E-value: 2.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  68 KTPLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPegaeEQFVSSIEQWREQMGIRNMILLGHSL 147
Cdd:COG0596  23 GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTL----DDLADDLAALLDALGLERVVLVGHSM 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 148 GGFLAASYSIKFPERVKHLILVDpwgfptmptdpseirspptwvkalaavlgrsnplavvraagpwgpglvqrfrpDLKR 227
Cdd:COG0596  99 GGMVALELAARHPERVAGLVLVD-----------------------------------------------------EVLA 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 228 KFQEYFEDDtimeyiyhcnaqtPSGESAFKTMMERF-GWAKRPMMSRInqipkDLPITFIYGAE-TWIDRSTGERVKEER 305
Cdd:COG0596 126 ALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAELL 187

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62859767 306 SDSFVKTlaIKGASHHVYADQPGTFNAVVEEICDAA 341
Cdd:COG0596 188 PNAELVV--LPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-327 2.01e-25

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: 102.58  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767    69 TPLVMVHGFGGGIGLWIQNLDHLSSSR-TLHAFDLLGFGRSSRPnfPSDPEGAEEQFVSSIEQWREQMGIRNMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   148 GGFLAASYSIKFPERVKHLILVDPWGFPTMPTDPSEIR--SPPTWVKALAAVLGRsNPLAVVRAAgPWGPGLVQRFRPDL 225
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIlaLFPGFFDGFVADFAP-NPLGRLVAK-LLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   226 KRKFQEYFEDDTIMeyiyhcNAQTPSGESAFktmmERFGWAKRPMMSRINQIpkDLPITFIYGAETWIDR-STGERVKEE 304
Cdd:pfam00561 157 LPLLNKRFPSGDYA------LAKSLVTGALL----FIETWSTELRAKFLGRL--DEPTLIIWGDQDPLVPpQALEKLAQL 224

                         250       260
                  ....*....|....*....|...
gi 62859767   305 RSDSFVKtlAIKGASHHVYADQP 327
Cdd:pfam00561 225 FPNARLV--VIPDAGHFAFLEGP 245
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 141-211 9.02e-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: 9.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 141 ILLGHSLGGFLAASYSIKFPERVKHLILVDPWGFPTMPTDPSEIRSP------------PTWVKALAAVlgrSNPLAVVR 208
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                ...
gi 62859767 209 AAG 211
Cdd:cd12808 268 AAG 270
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 14-338 8.73e-66

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 212.85  E-value: 8.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   14 TGWIPS---WCPTSMSKLKAVESRILQCIKNKFSAQYVSL----PDQNKIWTLTVSPE--------LQKKT---PLVMVH 75
Cdd:PLN02894  33 RSLWPSplrWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIgsgpPGSKVRWFRSASNEprfintvtFDSKEdapTLVMVH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   76 GFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFP-SDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLGGFLAAS 154
Cdd:PLN02894 113 GYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTcKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  155 YSIKFPERVKHLILVDPWGFPTMPTDPSE--IRSPPTWVKALAAVLGRSN--PLAVVRAAGPWGPGLVQRFrpdLKRKFQ 230
Cdd:PLN02894 193 YALKHPEHVQHLILVGPAGFSSESDDKSEwlTKFRATWKGAVLNHLWESNftPQKIIRGLGPWGPNLVRRY---TTARFG 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  231 EYF--------EDDTIMEYIYHCNAQTPSGESAFKTMMERFGWAKRPMMSRINQIpkDLPITFIYGAETWIDRSTGERVK 302
Cdd:PLN02894 270 AHStgdilseeESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESASEW--KVPTTFIYGRHDWMNYEGAVEAR 347

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 62859767  303 eERSDSFVKTLAIKGASHHVYADQPGTFNAVVEEIC 338
Cdd:PLN02894 348 -KRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-341 2.06e-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: 107.01  E-value: 2.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  68 KTPLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPegaeEQFVSSIEQWREQMGIRNMILLGHSL 147
Cdd:COG0596  23 GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTL----DDLADDLAALLDALGLERVVLVGHSM 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 148 GGFLAASYSIKFPERVKHLILVDpwgfptmptdpseirspptwvkalaavlgrsnplavvraagpwgpglvqrfrpDLKR 227
Cdd:COG0596  99 GGMVALELAARHPERVAGLVLVD-----------------------------------------------------EVLA 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 228 KFQEYFEDDtimeyiyhcnaqtPSGESAFKTMMERF-GWAKRPMMSRInqipkDLPITFIYGAE-TWIDRSTGERVKEER 305
Cdd:COG0596 126 ALAEPLRRP-------------GLAPEALAALLRALaRTDLRERLARI-----TVPTLVIWGEKdPIVPPALARRLAELL 187

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62859767 306 SDSFVKTlaIKGASHHVYADQPGTFNAVVEEICDAA 341
Cdd:COG0596 188 PNAELVV--LPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 69-327 2.01e-25

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: 102.58  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767    69 TPLVMVHGFGGGIGLWIQNLDHLSSSR-TLHAFDLLGFGRSSRPnfPSDPEGAEEQFVSSIEQWREQMGIRNMILLGHSL 147
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRP--KAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   148 GGFLAASYSIKFPERVKHLILVDPWGFPTMPTDPSEIR--SPPTWVKALAAVLGRsNPLAVVRAAgPWGPGLVQRFRPDL 225
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFIlaLFPGFFDGFVADFAP-NPLGRLVAK-LLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   226 KRKFQEYFEDDTIMeyiyhcNAQTPSGESAFktmmERFGWAKRPMMSRINQIpkDLPITFIYGAETWIDR-STGERVKEE 304
Cdd:pfam00561 157 LPLLNKRFPSGDYA------LAKSLVTGALL----FIETWSTELRAKFLGRL--DEPTLIIWGDQDPLVPpQALEKLAQL 224

                         250       260
                  ....*....|....*....|...
gi 62859767   305 RSDSFVKtlAIKGASHHVYADQP 327
Cdd:pfam00561 225 FPNARLV--VIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 69-174 1.33e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 79.60  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   69 TPLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSrpnfPSDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLG 148
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS----KAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMG 207

                         90       100
                 ....*....|....*....|....*.
gi 62859767  149 GFLAASYSIKFPERVKHLILVDPWGF 174
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
63-196 5.82e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.81  E-value: 5.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  63 PELQKKTPLVMVHGFGGGIGLWIQNLDHLSSSR-TLHAFDLLGFGRSSRPN-FPSDPEGAEEQFVSSIEQWREQMGIRnM 140
Cdd:COG2267  23 PAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGRSDGPRgHVDSFDDYVDDLRAALDALRARPGLP-V 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62859767 141 ILLGHSLGGFLAASYSIKFPERVKHLILVDPWgfptMPTDPsEIRSPPTWVKALAA 196
Cdd:COG2267 102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPA----YRADP-LLGPSARWLRALRL 152
PLN02578 PLN02578
hydrolase
 70-332 6.75e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 65.63  E-value: 6.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   70 PLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPEGAEEQfvssIEQWREQMGIRNMILLGHSLGG 149
Cdd:PLN02578  88 PIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQ----VADFVKEVVKEPAVLVGNSLGG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  150 FLAASYSIKFPERVKHLILVDPWG-FptmptdPSEIRSPPTWVKALAAVLGRSnplaVVRAAGPWGPGLV---------- 218
Cdd:PLN02578 164 FTALSTAVGYPELVAGVALLNSAGqF------GSESREKEEAIVVEETVLTRF----VVKPLKEWFQRVVlgflfwqakq 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  219 -QRFRPDLKRKFQEYFE-DDTIMEYIYHCNAQTPSGEsAFKTMMERFgwAKRPMMSRINQIPKDL--PITFIYG-AETWI 293
Cdd:PLN02578 234 pSRIESVLKSVYKDKSNvDDYLVESITEPAADPNAGE-VYYRLMSRF--LFNQSRYTLDSLLSKLscPLLLLWGdLDPWV 310

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 62859767  294 DRSTGERVKEERSDSFVKTLAikgASHHVYADQPGTFNA 332
Cdd:PLN02578 311 GPAKAEKIKAFYPDTTLVNLQ---AGHCPHDEVPEQVNK 346
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 71-320 8.85e-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: 8.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767    71 LVMVHGFGGGIGlWIQNL-DHLS-SSRTLHAFDLLGFGRSSR-----PNFpsdpegaeEQFV----SSIEQWREQMGIRN 139
Cdd:pfam12146   7 VVLVHGLGEHSG-RYAHLaDALAaQGFAVYAYDHRGHGRSDGkrghvPSF--------DDYVddldTFVDKIREEHPGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   140 MILLGHSLGGFLAASYSIKFPERVKHLILVDPWGFPTMPtdpseirSPPTWVKALAAVLGRSNPLAVVRAAGPwgPGLVQ 219
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY-------LAPPILKLLAKLLGKLFPRLRVPNNLL--PDSLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   220 RfrpDlkRKFQEYFEDDTIMeyIYHCNAQTpsGESAFKTMMerfgWAKRpmmsRINQIpkDLPITFIYGAETWI-DRSTG 298
Cdd:pfam12146 149 R---D--PEVVAAYAADPLV--HGGISART--LYELLDAGE----RLLR----RAAAI--TVPLLLLHGGADRVvDPAGS 209

                         250       260
                  ....*....|....*....|...
gi 62859767   299 ERVkEERSDSFVKTLAI-KGASH 320
Cdd:pfam12146 210 REF-YERAGSTDKTLKLyPGLYH 231
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 57-170 7.10e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 62.55  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   57 WTLTVSPELQKKTP-LVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRP-NFPSDPEGAEEQFVSSIEQWREq 134
Cdd:PLN02679  76 YLVKGSPEVTSSGPpVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPpGFSYTMETWAELILDFLEEVVQ- 154

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 62859767  135 mgiRNMILLGHSLGGF---LAASYSIkfPERVKHLILVD 170
Cdd:PLN02679 155 ---KPTVLIGNSVGSLacvIAASEST--RDLVRGLVLLN 188
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 68-171 1.02e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 57.92  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  68 KTPLVMVHGFGGGIGLWIQNLDHLSSS-RTLHAFDLLGFGRSSRPNFpsdpegaeEQFVSSIEQWREQMGIRNMILLGHS 146
Cdd:COG1075   5 RYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSA--------EQLAAFVDAVLAATGAEKVDLVGHS 76

                        90       100
                ....*....|....*....|....*...
gi 62859767 147 LGGFLAASYsIKF---PERVKHLILVDP 171
Cdd:COG1075  77 MGGLVARYY-LKRlggAAKVARVVTLGT 103
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 71-333 1.64e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 60.18  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767    71 LVMVHGFGGGIGLWiqnLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPEGAEEQFVSSIEQWREQmgirnmILLGHSLGGF 150
Cdd:pfam12697   1 VVLVHGAGLSAAPL---AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV------VLVGHSLGGA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   151 LAASYSikfPERVKHLILVDPWGFptmptdpseirsPPTWVKALAAVLGRSNPLavvRAAGPWGPGLVQRFRpdlkrkfq 230
Cdd:pfam12697  72 VALAAA---AAALVVGVLVAPLAA------------PPGLLAALLALLARLGAA---LAAPAWLAAESLARG-------- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   231 eyFEDDTIMEYIYHCNAQTPSGESAFKTMMERFGWAKRPMmsrinqipkdlPITFIYGAETWIDRSTGERVKEERSDSFV 310
Cdd:pfam12697 126 --FLDDLPADAEWAAALARLAALLAALALLPLAAWRDLPV-----------PVLVLAEEDRLVPELAQRLLAALAGARLV 192

                         250       260
                  ....*....|....*....|...
gi 62859767   311 ktlAIKGASHHVYaDQPGTFNAV 333
Cdd:pfam12697 193 ---VLPGAGHLPL-DDPEEVAEA 211
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 72-175 3.02e-10

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 60.98  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   72 VMVHGFGGGIGLWIQNL-----DHLSSSRTLHAFDLLGFGRSSRPNfpsDPEGAEEQFVSSIEQW-REQMGIRNMILLGH 145
Cdd:PLN03087 205 LFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPKPA---DSLYTLREHLEMIERSvLERYKVKSFHIVAH 281

                         90       100       110
                 ....*....|....*....|....*....|
gi 62859767  146 SLGGFLAASYSIKFPERVKHLILVDPWGFP 175
Cdd:PLN03087 282 SLGCILALALAVKHPGAVKSLTLLAPPYYP 311
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 69-171 3.59e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 60.14  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   69 TPLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNfpsdPEGAEEQFVSSIEQWREQMG--IRNMI----- 141
Cdd:PLN02824  30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPN----PRSAPPNSFYTFETWGEQLNdfCSDVVgdpaf 105

                         90       100       110
                 ....*....|....*....|....*....|
gi 62859767  142 LLGHSLGGFLAASYSIKFPERVKHLILVDP 171
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLINI 135
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
54-169 2.58e-09

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 56.95  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   54 NKIWTLTVSpelQKKTPLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPEGAEEQFVSSIEQwre 133
Cdd:PRK10349   2 NNIWWQTKG---QGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDK--- 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 62859767  134 qmgirnMILLGHSLGGFLAASYSIKFPERVKHLILV 169
Cdd:PRK10349  76 ------AIWLGWSLGGLVASQIALTHPERVQALVTV 105
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 70-164 5.22e-07

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 50.38  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   70 PLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPnfpsDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLGG 149
Cdd:PRK03592  29 PIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP----DIDYTFADHARYLDAWFDALGLDDVVLVGHDWGS 104

                         90
                 ....*....|....*
gi 62859767  150 FLAASYSIKFPERVK 164
Cdd:PRK03592 105 ALGFDWAARHPDRVR 119
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 68-210 9.13e-07

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 50.47  E-value: 9.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  68 KTPLVMVHGfGGGIGLWIQNL-DHLSSSRTLHAFDLLGFGRSSRPnFPSDPEGAEEQfvssIEQwreqmgIRNM------ 140
Cdd:COG3319 601 GPPLFCVHP-AGGNVLCYRPLaRALGPDRPVYGLQAPGLDGGEPP-PASVEEMAARY----VEA------IRAVqpegpy 668

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62859767 141 ILLGHSLGGFLA---------ASysikfpERVKHLILVDPWgfptmPTDPSEIRSPPTWVKALAAVLGRSNPLAVVRAA 210
Cdd:COG3319 669 HLLGWSFGGLVAyemarqleaQG------EEVALLVLLDSY-----APGALARLDEAELLAALLRDLARGVDLPLDAEE 736
YpfH COG0400
Predicted esterase [General function prediction only];
71-198 1.23e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 45.28  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  71 LVMVHGFGG----GIGLWiqnlDHLSSSRT----LHA-FDLLGFGRS----SRPNFPSDPEGAE---EQFVSSIEQWREQ 134
Cdd:COG0400   8 VVLLHGYGGdeedLLPLA----PELALPGAavlaPRApVPEGPGGRAwfdlSFLEGREDEEGLAaaaEALAAFIDELEAR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 135 MGI--RNMILLGHSLGGFLAASYSIKFPERVKHLI-----LVDPWGFPTMPTDPSEIR-----------SPPTWVKALAA 196
Cdd:COG0400  84 YGIdpERIVLAGFSQGAAMALSLALRRPELLAGVValsgyLPGEEALPAPEAALAGTPvflahgtqdpvIPVERAREAAE 163


                ..
gi 62859767 197 VL 198
Cdd:COG0400 164 AL 165
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 66-172 1.27e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 42.98  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  66 QKKTP-LVMVHGFGGGIGlwiqnlDHLSSSRTLH-------AFDLLGFGRSS-RPNFPSDPEGAEeqFVSSIEQWREQMG 136
Cdd:COG1073  34 SKKYPaVVVAHGNGGVKE------QRALYAQRLAelgfnvlAFDYRGYGESEgEPREEGSPERRD--ARAAVDYLRTLPG 105

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 62859767 137 IRN--MILLGHSLGGFLAASYSIKFPeRVKHLILVDPW 172
Cdd:COG1073 106 VDPerIGLLGISLGGGYALNAAATDP-RVKAVILDSPF 142
PRK10673 PRK10673
esterase;
63-170 3.51e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 41.64  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   63 PELQKKTPLVMVHGFGGgiglwiqNLDHLSS-SRTLHA------FDLLGFGRSsrpnfPSDPEGAEEQFVSSIEQWREQM 135
Cdd:PRK10673  11 QNPHNNSPIVLVHGLFG-------SLDNLGVlARDLVNdhdiiqVDMRNHGLS-----PRDPVMNYPAMAQDLLDTLDAL 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 62859767  136 GIRNMILLGHSLGGFLAASYSIKFPERVKHLILVD 170
Cdd:PRK10673  79 QIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
72-335 5.65e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 40.70  E-value: 5.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  72 VMVHGFGGG------IGLWIQNLDHlsssrTLHAFDLLGFGRSsrpnfPSDPEGaeeqfvSSIEQWRE---------QMG 136
Cdd:COG1647  19 LLLHGFTGSpaemrpLAEALAKAGY-----TVYAPRLPGHGTS-----PEDLLK------TTWEDWLEdveeayeilKAG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 137 IRNMILLGHSLGGFLAASYSIKFPErVKHLILVdpwgfptmptdpseirSPPTWVKalaavlGRSNPLAvvraagpwgpG 216
Cdd:COG1647  83 YDKVIVIGLSMGGLLALLLAARYPD-VAGLVLL----------------SPALKID------DPSAPLL----------P 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 217 LVQRFRPdLKRKFQEYFEDDTIMEYIYHcnaQTPSgeSAFKTMMERFGWAKRPmMSRINQipkdlPITFIYGAE-TWIDR 295
Cdd:COG1647 130 LLKYLAR-SLRGIGSDIEDPEVAEYAYD---RTPL--RALAELQRLIREVRRD-LPKITA-----PTLIIQSRKdEVVPP 197

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62859767 296 STGERVKEERSDSFVKTLAIKGASH--HVYADQPGTFNAVVE 335
Cdd:COG1647 198 ESARYIYERLGSPDKELVWLEDSGHviTLDKDREEVAEEILD 239
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
51-171 7.65e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 40.39  E-value: 7.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767  51 PDQNKIWTLTVSPELQKKTPLVM-VHGFGGGiglwiQNLDHLSSSRTLHA-------FDLLGFGRSSRPNFPSDpegaEE 122
Cdd:COG1506   5 ADGTTLPGWLYLPADGKKYPVVVyVHGGPGS-----RDDSFLPLAQALASrgyavlaPDYRGYGESAGDWGGDE----VD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 62859767 123 QFVSSIEQWREQMGI--RNMILLGHSLGGFLAASYSIKFPERVKHLILVDP 171
Cdd:COG1506  76 DVLAAIDYLAARPYVdpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG 126
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 141-211 9.02e-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: 9.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 141 ILLGHSLGGFLAASYSIKFPERVKHLILVDPWGFPTMPTDPSEIRSP------------PTWVKALAAVlgrSNPLAVVR 208
Cdd:cd12808 191 IVVAHSQGGGFAFEAARARPDLVRAVVALEPSGAPDPAEAAPLADVPhllvwgdyidadPRWPRYRATV---DAYAAALR 267


                ...
gi 62859767 209 AAG 211
Cdd:cd12808 268 AAG 270
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 70-171 1.14e-03

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 40.63  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767   70 PLVMVHGFGGGIGLWIQNLDHLSSSRTLHAFDLLGFGRSSRPNFPSDPEGAEEQFVSSIEQWREQMGIRNMILLGHSLGG 149
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYFS 208

                         90       100
                 ....*....|....*....|..
gi 62859767  150 FLAASYSIKFPERVKHLILVDP 171
Cdd:PLN03084 209 PPVVKYASAHPDKIKKLILLNP 230
DHR2_DOCK9 cd11698
Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 9; Dock9, also ...
 230-338 2.76e-03

Dock Homology Region 2, a GEF domain, of Class D Dedicator of Cytokinesis 9; Dock9, also called Zizimin1, is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. As a GEF, it activates the small GTPase Cdc42 by exchanging bound GDP for free GTP. It plays important roles in spine formation and dendritic growth. DOCK proteins are divided into four classes (A-D) based on sequence similarity and domain architecture; class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of Dock9, which contains the catalytic GEF activity for Cdc42. Class D DOCKs also contain a Pleckstrin homology (PH) domain at the N-terminus.


Pssm-ID: 212571  Cd Length: 415  Bit Score: 39.24  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859767 230 QEYFEDDTIMEYIYHCNAQTPSGESA---FKTMMERFGWAKRPMMS---RINqiPKDLPITFIYGAETWIDRSTGERVKE 303
Cdd:cd11698 156 QGFFEDEDGKEYIYKEPKLTPLSEISqrlLKLYSDKFGSENVKMIQdsgKVN--PKDLDSKYAYIQVTHVTPYFDEKELQ 233

                        90       100       110
                ....*....|....*....|....*....|....*
gi 62859767 304 ERSDSFVKTLAIKGASHHVYADQPGTFNAVVEEIC 338
Cdd:cd11698 234 ERKTDFERSHNIRRFMFEMPFTQSGKRQGGVEEQC 268
 
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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