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Conserved domains on  [gi|2517717899|ref|XP_057246230|]
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monoglyceride lipase isoform X1 [Malurus melanocephalus]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 22-294 2.58e-98

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PHA02857:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 276  Bit Score: 290.25  E-value: 2.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  22 IINADGQYLFCRYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 102 QHIDLMKKEHPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 182 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSqDKTL 261
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2517717899 262 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 294
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 2.58e-98

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 290.25  E-value: 2.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  22 IINADGQYLFCRYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 102 QHIDLMKKEHPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 182 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSqDKTL 261
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2517717899 262 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 294
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 2.68e-91

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: 271.01  E-value: 2.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  41 PRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKEHPELPVLILG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 121 HSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSL-GSIDPNAISRNKKEMESYTSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517717899 200 VyHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSQDKTLKVYEEAYHALHKEL 275
Cdd:pfam12146 163 V-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-292 1.82e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 158.63  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  21 HIINADGQYLFCRYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 101 LQHIDLMKKEhPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAkvlnfvlpnlslgsid 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 181 pnaisrnkkemesytsdplvyhggmkvsfviqlmnaiARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVqSQDKT 260
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2517717899 261 LKVYEEAYHALHKElpEVSTSVFTEILTWIGQ 292
Cdd:COG2267   192 LVLLPGARHELLNE--PAREEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-290 2.21e-07

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 51.32  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  72 VFAHDHVGHGQSEG---DRMVVSDFHVFIRDSLQHI--------------------DLMKKEHPELPVLILGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 129 I--LTASERPSEFSGMLLISPLVVAS-----PEVATPIKVfaaKVLNFVLPNLSL-GSIDPNAISRNKKEMES------- 193
Cdd:TIGR01607 157 LrlLELLGKSNENNDKLNIKGCISLSgmisiKSVGSDDSF---KFKYFYLPVMNFmSRVFPTFRISKKIRYEKspyvndi 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 194 YTSDPLVYHGGMKVSFVIQLMNAIARIE---RALPKlTLPILVLHGSSDKLCDIRGSYLLMDTVQSQDKTLKVYEEAYHA 270
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312

                         250       260
                  ....*....|....*....|
gi 2517717899 271 LHKElpEVSTSVFTEILTWI 290
Cdd:TIGR01607 313 ITIE--PGNEEVLKKIIEWI 330
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 93-134 7.08e-04

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.15  E-value: 7.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2517717899  93 FHVFIRDSLQHIDLMKKEHPELPVLILGHSMGGAISILTASE 134
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 2.58e-98

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 290.25  E-value: 2.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  22 IINADGQYLFCRYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 102 QHIDLMKKEHPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVAspEVATPIKVFAAKVLNFVLPNLSLGSIDP 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 182 NAISRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSqDKTL 261
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2517717899 262 KVYEEAYHALHKELPEVSTSVFTEILTWIGQKV 294
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 2.68e-91

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: 271.01  E-value: 2.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  41 PRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQHIDLMKKEHPELPVLILG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 121 HSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSL-GSIDPNAISRNKKEMESYTSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517717899 200 VyHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSQDKTLKVYEEAYHALHKEL 275
Cdd:pfam12146 163 V-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-292 1.82e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 158.63  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  21 HIINADGQYLFCRYWKPAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDS 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 101 LQHIDLMKKEhPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVFAAkvlnfvlpnlslgsid 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 181 pnaisrnkkemesytsdplvyhggmkvsfviqlmnaiARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVqSQDKT 260
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2517717899 261 LKVYEEAYHALHKElpEVSTSVFTEILTWIGQ 292
Cdd:COG2267   192 LVLLPGARHELLNE--PAREEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 24-294 2.10e-41

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 146.44  E-value: 2.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  24 NADGQYLFCRYWKP-AATPRALVFIAHGAGEHCGRY-DDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSL 101
Cdd:PLN02385   68 NSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 102 QHIDLMK--KEHPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVfaAKVLNF---VLPNLSL 176
Cdd:PLN02385  148 EHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLV--LQILILlanLLPKAKL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 177 ---GSIDPNAISRNKK-EMESYtsDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMD 252
Cdd:PLN02385  226 vpqKDLAELAFRDLKKrKMAEY--NVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYE 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2517717899 253 TVQSQDKTLKVYEEAYHA-LHKELPEVSTSVFTEILTWIGQKV 294
Cdd:PLN02385  304 KASSSDKKLKLYEDAYHSiLEGEPDEMIFQVLDDIISWLDSHS 346
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-290 1.21e-39

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 143.11  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  25 ADGQYLFCRYWKPAATP-RALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 103
Cdd:PLN02652  118 ARRNALFCRSWAPAAGEmRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 104 IDLMKKEHPELPVLILGHSMGGAIsILTASERPS---EFSGMLLISPLVVASPevATPIKVFAAKVLNFVLPNLSLGSID 180
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 181 PNAI--SRNKKEMESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSQD 258
Cdd:PLN02652  275 KRGIpvSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2517717899 259 KTLKVYEEAYHALHKElPEvSTSVFTEILTWI 290
Cdd:PLN02652  355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWM 384
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-302 2.60e-35

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 129.90  E-value: 2.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  27 GQYLFCRYWKPAAT--PRALVFIAHGAGEHCG-RYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRMVVSDFHVFIRDSLQH 103
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 104 IDLMKK--EHPELPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVASPEVATPIKVfaAKVLNFV---LPNLSlgs 178
Cdd:PLN02298  122 FNSVKQreEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLA--- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 179 IDPNA--ISRNKKEMESY---TSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDT 253
Cdd:PLN02298  197 IVPTAdlLEKSVKVPAKKiiaKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEE 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2517717899 254 VQSQDKTLKVYEEAYHA-LHKELPEVSTSVFTEILTWIGQKVPAAGEASH 302
Cdd:PLN02298  277 AKSEDKTIKIYDGMMHSlLFGEPDENIEIVRRDILSWLNERCTGKATPSE 326
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
38-295 2.74e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 103.87  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  38 AATPRALVFIaHGAGehCGRYD--DLAQKLTGLNLFVFAHDHVGHGQSEGDrMVVSDFHVFIRDSLQHIDLMKKEHPElp 115
Cdd:COG1647    12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYDK-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 116 VLILGHSMGGAISILTASERPsEFSGMLLISPlvvaspevatpikvfAAKVLNFVLPNLSLGSIDPNAISRNKKEMESYT 195
Cdd:COG1647    86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSP---------------ALKIDDPSAPLLPLLKYLARSLRGIGSDIEDPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 196 SDPLVYHGgMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSQDKTLKVYEEAYHALH--K 273
Cdd:COG1647   150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldK 228

                         250       260
                  ....*....|....*....|..
gi 2517717899 274 ELPEvstsVFTEILTWIGQKVP 295
Cdd:COG1647   229 DREE----VAEEILDFLERLAA 246
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
21-295 5.57e-18

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 81.22  E-value: 5.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  21 HIINADGQYLFCRYWKPAAT-PRALVFIAHGAGEH-CGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGDRmvvsdFHVFIR 98
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  99 DSLQHIDLMKkEHPELP---VLILGHSMGGAISILTASERPSEFSGMLLISPLVvaspevatpikvfaakvlnfvlpnlS 175
Cdd:COG1506    76 DVLAAIDYLA-ARPYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS-------------------------D 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 176 LGSIDPNAISRNKKEMESYTSDPLVYhggmkvsfviQLMNAIARIEralpKLTLPILVLHGSSDKLCDIRGSYLLMDTVQ 255
Cdd:COG1506   130 LRSYYGTTREYTERLMGGPWEDPEAY----------AARSPLAYAD----KLKTPLLLIHGEADDRVPPEQAERLYEALK 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2517717899 256 SQ--DKTLKVYEEAYHALHKelpEVSTSVFTEILTWIGQKVP 295
Cdd:COG1506   196 KAgkPVELLVYPGEGHGFSG---AGAPDYLERILDFLDRHLK 234
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 15-270 1.58e-16

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 77.26  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  15 PYKDLPH----IINADGQYLFCRYWKPA--ATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGD-R 87
Cdd:COG1073     4 PSDKVNKedvtFKSRDGIKLAGDLYLPAgaSKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  88 MVVS----DFHVFIrDSLQHidlmKKEHPELPVLILGHSMGGAISILTASERPsEFSGMLLISPLVVASPEVATPIKVFA 163
Cdd:COG1073    84 EEGSperrDARAAV-DYLRT----LPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 164 AKVLNFV--LPNLSLGSidpnaisrnkkemesytsdplvyhggmkvsfviqLMNAIARIERALPKLTLPILVLHGSSDKL 241
Cdd:COG1073   158 GAYLPGVpyLPNVRLAS----------------------------------LLNDEFDPLAKIEKISRPLLFIHGEKDEA 203

                         250       260
                  ....*....|....*....|....*....
gi 2517717899 242 CDIRGSYLLMDTVqSQDKTLKVYEEAYHA 270
Cdd:COG1073   204 VPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-292 7.05e-16

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: 75.04  E-value: 7.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  20 PHIINADGQYLFCRYWKPAATPraLVFIaHGAGEHCGRYDDLAQKLTGlNLFVFAHDHVGHGQSEGDRMVVSdFHVFIRD 99
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 100 SLQHIDLMKKEhpelPVLILGHSMGGAISILTASERPSEFSGMLLISPLVVAspevatpikvfaakvlnfVLPNLSLGSI 179
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA------------------LAEPLRRPGL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 180 DPNAISRnkkemesytsdplvyhggmkvsfviqLMNAIAR--IERALPKLTLPILVLHGSSDKLCDIRGSYLLMDTVqsQ 257
Cdd:COG0596   137 APEALAA--------------------------LLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELL--P 188

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2517717899 258 DKTLKVYEEAYHALHKELPEVstsVFTEILTWIGQ 292
Cdd:COG0596   189 NAELVVLPGAGHFPPLEQPEA---FAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 44-274 8.05e-10

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: 58.28  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  44 LVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGdRMVVSDFHVFirDSLQHIDLMKKEHPELPVLILGHSM 123
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 124 GGAISILTASERPSEFSGMLLISPLV----------------------VASPEVATPIKVFAAKVLNFVLPNLSLGSIDP 181
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDppheldeadrfilalfpgffdgFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 182 NaISRNKKEMESYTSDPLVYhggmkvsFVIQLMNAIARIERA--LPKLTLPILVLHGSSDKLCDIRGSYLLMDTVQSqdK 259
Cdd:pfam00561 159 L-LNKRFPSGDYALAKSLVT-------GALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--A 228

                         250
                  ....*....|....*
gi 2517717899 260 TLKVYEEAYHALHKE 274
Cdd:pfam00561 229 RLVVIPDAGHFAFLE 243
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-290 2.21e-07

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 51.32  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  72 VFAHDHVGHGQSEG---DRMVVSDFHVFIRDSLQHI--------------------DLMKKEHPELPVLILGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 129 I--LTASERPSEFSGMLLISPLVVAS-----PEVATPIKVfaaKVLNFVLPNLSL-GSIDPNAISRNKKEMES------- 193
Cdd:TIGR01607 157 LrlLELLGKSNENNDKLNIKGCISLSgmisiKSVGSDDSF---KFKYFYLPVMNFmSRVFPTFRISKKIRYEKspyvndi 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 194 YTSDPLVYHGGMKVSFVIQLMNAIARIE---RALPKlTLPILVLHGSSDKLCDIRGSYLLMDTVQSQDKTLKVYEEAYHA 270
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312

                         250       260
                  ....*....|....*....|
gi 2517717899 271 LHKElpEVSTSVFTEILTWI 290
Cdd:TIGR01607 313 ITIE--PGNEEVLKKIIEWI 330
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-272 6.12e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.19  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  21 HIINADGQYLFCRYWKPA-ATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSEGD------RMVVSDF 93
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAgGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  94 HVFIRDSLQHIDLMKKeHPEL---PVLILGHSMGGAISILTASERPsefsgmllisplvvaspevatpikVFAAkvlnfv 170
Cdd:COG0412    87 ELLAADLRAALDWLKA-QPEVdagRVGVVGFCFGGGLALLAAARGP------------------------DLAA------ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 171 lpnlslgsidpnAISrnkkemesytsdplvYHGGMKVsfviqlmnaiARIERALPKLTLPILVLHGSSDKLCDIRGSYLL 250
Cdd:COG0412   136 ------------AVS---------------FYGGLPA----------DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAAL 178

                         250       260
                  ....*....|....*....|....
gi 2517717899 251 MDTVQSQ--DKTLKVYEEAYHALH 272
Cdd:COG0412   179 EAALAAAgvDVELHVYPGAGHGFT 202
PLN02578 PLN02578
hydrolase
 50-290 1.82e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 48.68  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  50 GAGEHCGRYD--DLAQKLTglnlfVFAHDHVGHGQS-----EGDRMVVSDfhvfirdslQHIDLMKKEHPElPVLILGHS 122
Cdd:PLN02578   96 GASAFHWRYNipELAKKYK-----VYALDLLGFGWSdkaliEYDAMVWRD---------QVADFVKEVVKE-PAVLVGNS 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 123 MGGAISILTASERPSEFSGMLLISP-------------LVVASPEVAT-----PIK-VFAAKVLNFVLPNLSLGS-IDP- 181
Cdd:PLN02578  161 LGGFTALSTAVGYPELVAGVALLNSagqfgsesrekeeAIVVEETVLTrfvvkPLKeWFQRVVLGFLFWQAKQPSrIESv 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 182 -NAISRNKKEMESY--------TSDP---LVYHGGMKvSFVIQLMNAIarIERALPKLTLPILVLHGSSD------KLCD 243
Cdd:PLN02578  241 lKSVYKDKSNVDDYlvesitepAADPnagEVYYRLMS-RFLFNQSRYT--LDSLLSKLSCPLLLLWGDLDpwvgpaKAEK 317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2517717899 244 IRGSYllmdtvqsQDKTLkVYEEAYHALHKELPEvstSVFTEILTWI 290
Cdd:PLN02578  318 IKAFY--------PDTTL-VNLQAGHCPHDEVPE---QVNKALLEWL 352
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-272 6.39e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.31  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  44 LVFIaHGAGEHCGRYDDLAQKltglNLFVFAHDHVGHGQSEGDRMVVSDFHvfirdslQHIDLMKKEHPELPVLILGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLAA----GVAVLAPDLPGHGSSSPPPLDLADLA-------DLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 124 GGAISILTAserPSEFSGMLLISPLVVASPEVATPIKVFAAKVLNFVLPNLSLGSIDPNAISRNKKEMESYTSDPLVYHG 203
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2517717899 204 GMKVSFVIQLmnaiarieRALPKLTLPILVLHGSSDKLcdirGSYLLMDTVQSQDKTLKVYEEAYHALH 272
Cdd:pfam12697 146 LLAALALLPL--------AAWRDLPVPVLVLAEEDRLV----PELAQRLLAALAGARLVVLPGAGHLPL 202
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 5.47e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 44.16  E-value: 5.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  33 RYWK-PAATPRALVFIaHG-AGEH---CGRYDDLAQKLTglnlfVFAHDHVGHGQSeGDRMVVSDFHvFIRDSLqhIDLM 107
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALAAGRP-----VIALDLPGHGAS-SKAVGAGSLD-ELAAAV--LAFL 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2517717899 108 KKEHPElPVLILGHSMGGAISILTASERPSEFSGMLLISP 147
Cdd:PRK14875  192 DALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 93-134 7.08e-04

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.15  E-value: 7.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2517717899  93 FHVFIRDSLQHIDLMKKEHPELPVLILGHSMGGAISILTASE 134
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PRK10749 PRK10749
lysophospholipase L2; Provisional
 44-287 2.62e-03

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 38.83  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  44 LVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSegDRMV--------------VSDFHVFIrdsLQHIDLMKK 109
Cdd:PRK10749   56 VVVICPGRIESYVKYAELAYDLFHLGYDVLIIDHRGQGRS--GRLLddphrghverfndyVDDLAAFW---QQEIQPGPY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 110 EHpelpVLILGHSMGGAISILTASERPSEFSGMLLISPLVvaspEVATPIKVFAA-KVLNFVLPN--------LSLGSID 180
Cdd:PRK10749  131 RK----RYALAHSMGGAILTLFLQRHPGVFDAIALCAPMF----GIVLPLPSWMArRILNWAEGHprirdgyaIGTGRWR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899 181 P-----NAIS----RNKKEMESYTSDPLVYHGGMKVSFVIQLMNAIARIERALPKLTLPILVLHGSSDKLCDIRgsyllm 251
Cdd:PRK10749  203 PlpfaiNVLThsreRYRRNLRFYADDPELRVGGPTYHWVRESILAGEQVLAGAGDITTPLLLLQAEEERVVDNR------ 276

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2517717899 252 dtvqSQDKTLKVYEEAYHALHKELPEVSTSVFTEIL 287
Cdd:PRK10749  277 ----MHDRFCEARTAAGHPCEGGKPLVIKGAYHEIL 308
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 96-153 3.34e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 38.21  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  96 FIRDSLqhIDLMKKEHPELPV--LILGHSMGGAISILTASERPSEFSGMLLISPLVVASP 153
Cdd:pfam00756  92 FLTQEL--PPLLDANFPTAPDgrALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSN 149
Lipase_3 pfam01764
Lipase (class 3);
108-163 3.36e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2517717899 108 KKEHPELPVLILGHSMGGAISILTASErpsefsgmllispLVVASPEVATPIKVFA 163
Cdd:pfam01764  57 LEKYPDYSIVVTGHSLGGALASLAALD-------------LVENGLRLSSRVTVVT 99
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
118-147 3.45e-03

Predicted hydrolase of the alpha/beta superfamily [General function prediction only];


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 3.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2517717899 118 ILGHSMGGAISILTASERPSEFSGMLLISP 147
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 45-134 5.76e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 37.37  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  45 VFIAHGAG--EHCgrYDDLAQKLTGLNLFVFAHDHvghGQSEGDRMVVSdfhvfiRDSL--QHIDLMKKEHPELPVLILG 120
Cdd:pfam00975   3 LFCFPPAGgsASS--FRSLARRLPPPAEVLAVQYP---GRGRGEPPLNS------IEALadEYAEALRQIQPEGPYALFG 71

                          90
                  ....*....|....
gi 2517717899 121 HSMGGAISILTASE 134
Cdd:pfam00975  72 HSMGGMLAFEVARR 85
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 93-134 6.01e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 6.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2517717899  93 FHVFIRDSLQHIDLMKKEHPELPVLILGHSMGGAISILTASE 134
Cdd:cd00741     7 ARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-137 6.16e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 37.78  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  37 PAATPRALVFIAHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGH-----GQSEGDRMVVSDFHVFI---RDSLQHIDLMK 108
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELWerpLDLSFVLDQLL 136

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2517717899 109 KEHPELPVL----------ILGHSMGGAISILTASERPS 137
Cdd:COG4188   137 ALNKSDPPLagrldldrigVIGHSLGGYTALALAGARLD 175
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 37-128 6.47e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.58  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517717899  37 PAATPRALVFIaHGAGEHCGRYDDLAQKLTGLNLFVFAHDHVGHGQSegdrmvvsdfhvfIRDS----LQHIDLMKKEHP 112
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS-------------IEDSaeqlAAFVDAVLAATG 66

                          90
                  ....*....|....*.
gi 2517717899 113 ELPVLILGHSMGGAIS 128
Cdd:COG1075    67 AEKVDLVGHSMGGLVA 82
 
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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