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Conserved domains on  [gi|1418205693|ref|XP_025303868|]
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monoglyceride lipase isoform X2 [Canis lupus dingo]

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, ...
 48-300 5.48e-95

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: 282.16  E-value: 5.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLGH 127
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLIC 207
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 RAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:PHA02857  183 HEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKS 261

                         250
                  ....*....|...
gi 1418205693 288 VFREINMWVSQRI 300
Cdd:PHA02857  262 VMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 48-300 5.48e-95

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 282.16  E-value: 5.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLGH 127
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLIC 207
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 RAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:PHA02857  183 HEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKS 261

                         250
                  ....*....|...
gi 1418205693 288 VFREINMWVSQRI 300
Cdd:PHA02857  262 VMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 45-281 3.36e-92

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: 273.71  E-value: 3.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  45 QPLRALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFL 124
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 125 LGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSL-GPIDSSVLSRNKTEVDLYNSD 203
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418205693 204 PLICRaGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLHKEL 281
Cdd:pfam12146 161 PLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
48-298 1.39e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 148.61  E-value: 1.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDyPGLPVFLLGH 127
Cdd:COG2267    28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAkvlnlvlpnmslgpidssvlsrnktevdlynsdplic 207
Cdd:COG2267   107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA------------------------------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 raglkvcfgiqllnavTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAkSQDKTLKIYEGAYHVLHKELPEvtNS 287
Cdd:COG2267   150 ----------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EE 210

                         250
                  ....*....|.
gi 1418205693 288 VFREINMWVSQ 298
Cdd:COG2267   211 VLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 78-280 2.79e-05

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: 45.16  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  78 VFAHDHVGHGQSEGE---RMVVSDFHVFIRDVLQHV--------------------DFMQKDYPGLPVFLLGHSMGGAIA 134
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 135 ILT------AAERPSH--------FSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSLGPIDSsvLSRNKTEVDLY 200
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDII 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 201 NSDPLICRAGLKVCFGIQLLNAVTRVE---RALPKlTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVL 277
Cdd:TIGR01607 235 KFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313


                  ...
gi 1418205693 278 HKE 280
Cdd:TIGR01607 314 TIE 316
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 121-154 1.74e-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: 214008  Cd Length: 280  Bit Score: 42.60  E-value: 1.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1418205693 121 PVFLLGHSMGGAIAILTAAERPSHFSGMVLISPL 154
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 48-300 5.48e-95

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 282.16  E-value: 5.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLGH 127
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLIC 207
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 RAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:PHA02857  183 HEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKS 261

                         250
                  ....*....|...
gi 1418205693 288 VFREINMWVSQRI 300
Cdd:PHA02857  262 VMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 45-281 3.36e-92

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: 273.71  E-value: 3.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  45 QPLRALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFL 124
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 125 LGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSL-GPIDSSVLSRNKTEVDLYNSD 203
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418205693 204 PLICRaGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLHKEL 281
Cdd:pfam12146 161 PLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
48-298 1.39e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 148.61  E-value: 1.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDyPGLPVFLLGH 127
Cdd:COG2267    28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAkvlnlvlpnmslgpidssvlsrnktevdlynsdplic 207
Cdd:COG2267   107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA------------------------------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 raglkvcfgiqllnavTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAkSQDKTLKIYEGAYHVLHKELPEvtNS 287
Cdd:COG2267   150 ----------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EE 210

                         250
                  ....*....|.
gi 1418205693 288 VFREINMWVSQ 298
Cdd:COG2267   211 VLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 41-299 4.03e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 130.26  E-value: 4.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  41 PRQTQPlRALIFVSHGAGEHCGRYDE-LAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQ--KDY 117
Cdd:PLN02385   81 PENSRP-KAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVIEHYSKIKgnPEF 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLV-----LANPESATTFKVLAAKVLnlvlPNMSLGP----IDSS 188
Cdd:PLN02385  160 RGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLL----PKAKLVPqkdlAELA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 189 VLSRNKTEVDLYNsdpLIC---RAGLKVcfGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDK 265
Cdd:PLN02385  236 FRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYEKASSSDK 310

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1418205693 266 TLKIYEGAYH-VLHKELPEVTNSVFREINMWVSQR 299
Cdd:PLN02385  311 KLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 41-304 1.48e-34

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 127.97  E-value: 1.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  41 PRQTQPLRALIFVSHGAGEHCG-RYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKD--Y 117
Cdd:PLN02298   52 PSSSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeF 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVlaAKVLNLV---LPNMSLGP----IDSSVL 190
Cdd:PLN02298  132 QGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIVPtadlLEKSVK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 191 SRNKTEVDLYNsdPLICRAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIY 270
Cdd:PLN02298  210 VPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIY 287

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1418205693 271 EGAYH-VLHKELPEVTNSVFREINMWVSQRIGAAA 304
Cdd:PLN02298  288 DGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKA 322
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 47-307 8.40e-31

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 119.23  E-value: 8.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  47 LRALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLG 126
Cdd:PLN02652  135 MRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 127 HSMGGAIaILTAAERPS---HFSGMVLISPLVLANPESATTFKVlaAKVLNLVLPNMSLGPIDSS--VLSRNKTEVDLYN 201
Cdd:PLN02652  215 HSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGANKRgiPVSRDPAALLAKY 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 202 SDPLICRAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLHKEl 281
Cdd:PLN02652  292 SDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE- 370

                         250       260
                  ....*....|....*....|....*.
gi 1418205693 282 PEvTNSVFREINMWVSQRIGAAAGTG 307
Cdd:PLN02652  371 PE-REEVGRDIIDWMEKRLDLVNGSA 395
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
85-288 1.34e-24

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 99.63  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  85 GHGQSEGErMVVSDFHVFIRDVLQHVDFMQKDYPglPVFLLGHSMGGAIAILTAAERPsHFSGMVLISPLVLANPESAtt 164
Cdd:COG1647    52 GHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 165 fkvLAAKVLNLVLPnmSLGPIDSSVLSRNKTEVDlYNSDPLICraglkvcfGIQLLNAVTRVERALPKLTLPFLLLQGSA 244
Cdd:COG1647   126 ---PLLPLLKYLAR--SLRGIGSDIEDPEVAEYA-YDRTPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRK 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1418205693 245 DRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 288
Cdd:COG1647   192 DEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 40-276 4.22e-19

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 84.58  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  40 PPRQTQPLRALIfVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHvfIRDVLQHVDFM--QKDY 117
Cdd:COG1073    30 PAGASKKYPAVV-VAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RRDARAAVDYLrtLPGV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPsHFSGMVLISPlvLANPESAttFKVLAAKVLNLVLPNMSLGPidssvlsrNKTEV 197
Cdd:COG1073   107 DPERIGLLGISLGGGYALNAAATDP-RVKAVILDSP--FTSLEDL--AAQRAKEARGAYLPGVPYLP--------NVRLA 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418205693 198 DLYNSDplicraglkvcfgiqlLNAVTRVEralpKLTLPFLLLQGSADRLCDSKGAYLLMEsAKSQDKTLKIYEGAYHV 276
Cdd:COG1073   174 SLLNDE----------------FDPLAKIE----KISRPLLFIHGEKDEAVPFYMSEDLYE-AAAEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
41-301 3.35e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 78.91  E-value: 3.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  41 PRQTQPLRALIFVsHGAGEH-CGRYDELAQMLVGLELLVFAHDHVGHGQSEGERmvvsdFHVFIRDVLQHVDFM--QKDY 117
Cdd:COG1506    17 PADGKKYPVVVYV-HGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVLAAIDYLaaRPYV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPlvLANPESATTFKVLAAKVLNLVLPNMslgpidssvlsrnktEV 197
Cdd:COG1506    91 DPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWED---------------PE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 198 DLYNSDPLicraglkvcfgiqllnavtrveRALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQ--DKTLKIYEGAYH 275
Cdd:COG1506   154 AYAARSPL----------------------AYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGH 211

                         250       260
                  ....*....|....*....|....*.
gi 1418205693 276 VLHKelpEVTNSVFREINMWVSQRIG 301
Cdd:COG1506   212 GFSG---AGAPDYLERILDFLDRHLK 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 48-291 1.71e-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: 76.96  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVsHGAGEHCGRYDELAQMLvGLELLVFAHDHVGHGQSEGERMVVSdFHVFIRDVLQHVDFMQKDypglPVFLLGH 127
Cdd:COG0596    24 PPVVLL-HGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGLE----RVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlanpesattfKVLAAkvlNLVLPNMSLGPIDSSVLSRNKTEvdlynsdplic 207
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVL----------AALAE---PLRRPGLAPEALAALLRALARTD----------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 raglkvcfgiqllnavtrVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKsqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:COG0596   153 ------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAA 212


                  ....
gi 1418205693 288 VFRE 291
Cdd:COG0596   213 ALRD 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 49-280 6.04e-13

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: 67.14  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  49 ALIFVsHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGeRMVVSDFHVFirDVLQHVDFMQKDYPGLPVFLLGHS 128
Cdd:pfam00561   2 PVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 129 MGGAIAILTAAERPSHFSGMVLISPLVLAN-------------PESATTFKVLAAKVLNLVLPNMSLGPI---DSSVLSR 192
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 193 NKTEVDLYNSDPLIcrAGLKVCFGIQLLNAVTRVERA--LPKLTLPFLLLQGSADRLCDSKGAYLLmeSAKSQDKTLKIY 270
Cdd:pfam00561 158 PLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVI 233

                         250
                  ....*....|
gi 1418205693 271 EGAYHVLHKE 280
Cdd:pfam00561 234 PDAGHFAFLE 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 50-278 2.51e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.55  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  50 LIFVsHGAGEHcgrYDELAQmLVGLELLVFAHDHVGHGQSEGERMVVSDfhvfIRDVLQHVDFMQKDYPglpVFLLGHSM 129
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAA-LLAAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 130 GGAIAiLTAAERPSHFSgmVLISPLVLANPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLICRA 209
Cdd:pfam12697  69 GGAVA-LAAAAAALVVG--VLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418205693 210 GLKVCFGIQLlnavtrveRALPKLTLPFLLLqGSADRLCDskgAYLLMESAKSQDKTLKIYEGAYHVLH 278
Cdd:pfam12697 146 LLAALALLPL--------AAWRDLPVPVLVL-AEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
PRK10749 PRK10749
lysophospholipase L2; Provisional
 63-275 6.94e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.91  E-value: 6.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  63 RYDELAQMLVGLELLVFAHDHVGHGQS-----EGERMVVSDFHVFIRDVLQhvdFMQKDYPGLPV---FLLGHSMGGAIA 134
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAA---FWQQEIQPGPYrkrYALAHSMGGAIL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 135 ILTAAERPSHFSGMVLISPL---VLANPESATTFKVLAAKVLNLVLPNMSLG-------PIDSSVLS----RNKTEVDLY 200
Cdd:PRK10749  146 TLFLQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLThsreRYRRNLRFY 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 201 NSDPLI---------CRAGLKVcfGIQLLNAVtrveralPKLTLPFLLLQGSADRLCDSKG------AYLLMESAKSQDK 265
Cdd:PRK10749  226 ADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEERVVDNRMhdrfceARTAAGHPCEGGK 296

                         250
                  ....*....|
gi 1418205693 266 TLKIyEGAYH 275
Cdd:PRK10749  297 PLVI-KGAYH 305
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
102-153 1.61e-05

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 45.36  E-value: 1.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1418205693 102 FIRDVLQhvDFMQKDYPGLPVF--LLGHSMGGAIAILTAAERPSHFSGMVLISP 153
Cdd:COG2819   112 FLEEELK--PYIDKRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
PLN02578 PLN02578
hydrolase
 78-297 1.81e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.60  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  78 VFAHDHVGHGQSEgERMVVSDFHVFIRDVlqhVDFMqKDYPGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPL--- 154
Cdd:PLN02578  115 VYALDLLGFGWSD-KALIEYDAMVWRDQV---ADFV-KEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqf 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 155 ---------VLANPESA-TTFKVLAAK------VLNLVLPNMSLGPIDSSVLS---RNKTEVDLY--------NSDP--- 204
Cdd:PLN02578  190 gsesrekeeAIVVEETVlTRFVVKPLKewfqrvVLGFLFWQAKQPSRIESVLKsvyKDKSNVDDYlvesitepAADPnag 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 205 -----LICRAglkvcfgiqLLNAVT-RVERALPKLTLPFLLLQGSADRLCDSKGAYLLmeSAKSQDKTLkIYEGAYHVLH 278
Cdd:PLN02578  270 evyyrLMSRF---------LFNQSRyTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKI--KAFYPDTTL-VNLQAGHCPH 337

                         250
                  ....*....|....*....
gi 1418205693 279 KELPEVTNSVFREinmWVS 297
Cdd:PLN02578  338 DEVPEQVNKALLE---WLS 353
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
41-142 2.04e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.96  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  41 PRQTQPLRALIFVsHGAGEHCGRYDELAQMLVGLELLVFA---HDHVGHGQSEGE---RMVVSDFHVFIRDVLQHVDFM- 113
Cdd:COG0412    23 PAGGGPRPGVVVL-HEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDPELLAADLRAALDWLk 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1418205693 114 -QKDYPGLPVFLLGHSMGGAIAILTAAERP 142
Cdd:COG0412   102 aQPEVDAGRVGVVGFCFGGGLALLAAARGP 131
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 78-280 2.79e-05

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: 45.16  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  78 VFAHDHVGHGQSEGE---RMVVSDFHVFIRDVLQHV--------------------DFMQKDYPGLPVFLLGHSMGGAIA 134
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 135 ILT------AAERPSH--------FSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSLGPIDSsvLSRNKTEVDLY 200
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDII 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 201 NSDPLICRAGLKVCFGIQLLNAVTRVE---RALPKlTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVL 277
Cdd:TIGR01607 235 KFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313


                  ...
gi 1418205693 278 HKE 280
Cdd:TIGR01607 314 TIE 316
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 78-153 4.19e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 44.55  E-value: 4.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418205693  78 VFAHDHVGHGQSeGERMVVSDFHVFIRDVLqhvDFMqkDYPGLP-VFLLGHSMGGAIAILTAAERPSHFSGMVLISP 153
Cdd:PRK14875  160 VIALDLPGHGAS-SKAVGAGSLDELAAAVL---AFL--DALGIErAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
COG4099 COG4099
Predicted peptidase [General function prediction only];
41-166 6.07e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 43.42  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  41 PRQTQPLraLIFVsHGAGEhcgRYDEL-AQMLVGLELLVFAHDHVGHG------Q-SEGERMVVSDFHvfiRDVLQHVDF 112
Cdd:COG4099    45 PGKKYPL--VLFL-HGAGE---RGTDNeKQLTHGAPKFINPENQAKFPaivlapQcPEDDYWSDTKAL---DAVLALLDD 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 113 MQKDYPGLP--VFLLGHSMGGAIAILTAAERPSHFSGMVLISPlvLANPESATTFK 166
Cdd:COG4099   116 LIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 121-154 1.74e-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: 214008  Cd Length: 280  Bit Score: 42.60  E-value: 1.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1418205693 121 PVFLLGHSMGGAIAILTAAERPSHFSGMVLISPL 154
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-140 3.16e-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: 41.31  E-value: 3.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1418205693  99 FHVFIRDVLQHVDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
YpfH COG0400
Predicted esterase [General function prediction only];
48-160 5.97e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 40.28  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFA------HDHVGHG-----------QSEGERMVVSDFHVFIRDVLQHV 110
Cdd:COG0400     5 APLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlsflegreDEEGLAAAAEALAAFIDELEARY 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418205693 111 DFmqkdyPGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPE 160
Cdd:COG0400    85 GI-----DPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
50-275 7.37e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.86  E-value: 7.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  50 LIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGH--GQSEGERMVVSDFHVF---------IRDVLQHVDFMQKDYP 118
Cdd:COG4188    64 LVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLLALNKSDP 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 119 GLP-------VFLLGHSMGGAIAILTAAERPshfsgmvlisplvlanpeSATTFKVLAAKVLNLVLPNMSLGPIDSSVls 191
Cdd:COG4188   144 PLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPRLAYDL-- 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 192 rnktevdlynSDPLIcRAGLkvcfgiqLLNAVTR---VERALPKLTLPFLLLQGSADRlcDSKGAY---LLMESAKSQDK 265
Cdd:COG4188   204 ----------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFDLLPGADK 263

                         250
                  ....*....|
gi 1418205693 266 TLKIYEGAYH 275
Cdd:COG4188   264 YLLTLEGATH 273
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
103-140 7.44e-04

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 39.86  E-value: 7.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1418205693 103 IRDVLQHVDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3571    63 DAAWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAE 100
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 99-140 1.09e-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: 39.02  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1418205693  99 FHVFIRDVLQHVDFMQKD----YPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:cd00741     3 FYKAARSLANLVLPLLKSalaqYPDYKIHVTGHSLGGALAGLAGLD 48
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 78-163 2.84e-03

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.83  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693  78 VFAHDHVGHGQSEgermvvsdfHVFIRDVLQHvdfMQKDYPGLP--VFLLGHSMGGAIAILTAAERPSHFSGMVLIS--P 153
Cdd:COG3509   102 WFDGRDQRRGRDD---------VAFIAALVDD---LAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglP 169

                          90
                  ....*....|
gi 1418205693 154 LVLANPESAT 163
Cdd:COG3509   170 YGAASDAACA 179
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 102-155 3.02e-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: 38.60  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 102 FIRDVLqhVDFMQKDYPGLPVF--LLGHSMGGAIAILTAAERPSHFSGMVLISPLV 155
Cdd:pfam00756  92 FLTQEL--PPLLDANFPTAPDGraLAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
Lipase_3 pfam01764
Lipase (class 3);
117-165 3.03e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1418205693 117 YPGLPVFLLGHSMGGAIAILTAAerpshfsgMVLISPLVLANPESATTF 165
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
PRK10673 PRK10673
esterase;
86-151 5.85e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.79  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693  86 HGQSEgeRMVVSDFHVFIRDVLQHVDFMQKDypglPVFLLGHSMGGAIAILTAAERPSHFSGMVLI 151
Cdd:PRK10673   53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
79-140 6.59e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 37.43  E-value: 6.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418205693  79 FAHDHVGHGQSEGerMVVSDFHVFIRDVLQH-VDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELlEDALRPLSPGKRLYVTGHSLGGALATLAAAD 108
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 85-140 9.73e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 36.75  E-value: 9.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693  85 GHGQSEGERMVvSDFHVFIRDVLQHVdfmqKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3208    42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
 
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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