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Conserved domains on  [gi|261878516|ref|NP_001159723|]
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monoglyceride lipase isoform a [Mus musculus]

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, ...
 38-310 9.83e-106

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: 309.89  E-value: 9.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 117
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 118 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 197
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 198 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 277
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878516 278 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 310
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 38-310 9.83e-106

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 309.89  E-value: 9.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 117
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 118 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 197
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 198 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 277
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878516 278 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 310
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 57-291 3.02e-89

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: 266.39  E-value: 3.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   57 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 136
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  137 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSEVDLYNSDPL 215
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261878516  216 VCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 291
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
37-306 1.36e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.09  E-value: 1.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  37 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 114
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 115 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfvlpnmtlgr 194
Cdd:COG2267   85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 195 idssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQD 274
Cdd:COG2267  150 ---------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPD 189

                        250       260       270
                 ....*....|....*....|....*....|..
gi 261878516 275 KTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 306
Cdd:COG2267  190 VELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 88-307 6.40e-06

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: 47.08  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   88 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 144
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  145 I----LVAAERPTY----------FSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgRIDSSV-LSRNKSEVDL 209
Cdd:TIGR01607 157 LrlleLLGKSNENNdklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  210 YNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVL 287
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 261878516  288 HRElpEVTNSVLHEVNSWVS 307
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 115-150 8.68e-05

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: 43.23  E-value: 8.68e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 261878516 115 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 150
Cdd:cd00519  113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 38-310 9.83e-106

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 309.89  E-value: 9.83e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 117
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 118 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 197
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 198 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 277
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878516 278 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 310
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 57-291 3.02e-89

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: 266.39  E-value: 3.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   57 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 136
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  137 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSEVDLYNSDPL 215
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261878516  216 VCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 291
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
37-306 1.36e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.09  E-value: 1.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  37 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 114
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 115 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfvlpnmtlgr 194
Cdd:COG2267   85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 195 idssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQD 274
Cdd:COG2267  150 ---------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPD 189

                        250       260       270
                 ....*....|....*....|....*....|..
gi 261878516 275 KTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 306
Cdd:COG2267  190 VELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 39-309 6.46e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 129.87  E-value: 6.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  39 VNADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDE-LAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDV 116
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 117 LQHVDTIQ--KDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPL------VLANPESASTLKVLA-----AKLL 183
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMckiaddVVPPPLVLQILILLAnllpkAKLV 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 184 nfvlPNMTLGriDSSVLSRNKSEVDLYNSDPLVCRAGLKVcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGA 263
Cdd:PLN02385 227 ----PQKDLA--ELAFRDLKKRKMAEYNVIAYKDKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVS 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 261878516 264 YLLMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHR 309
Cdd:PLN02385 299 KFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 43-316 4.78e-33

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 124.50  E-value: 4.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  43 GQYLFCRYWKPSGT--PKALIFVSHGAGEHCG-RYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 119
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 120 VDTIQKD--YPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLV-----LANPESASTLKVLAAKLLNF--VLPNM 190
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkisdkIRPPWPIPQILTFVARFLPTlaIVPTA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 191 TLgrIDSSVLSRNKSEVDLYNsdPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESS 270
Cdd:PLN02298 202 DL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 261878516 271 RSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHRIAAAGAG 316
Cdd:PLN02298 278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 41-311 7.02e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 122.69  E-value: 7.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  41 ADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 119
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 120 VDTIQKDYPDVPIFLLGHSMGGAIsILVAAERPTY---FSGMVLISPLVLANPesASTLKVLAAKLLNFVLPNMTLGRID 196
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSIedkLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 197 SS--VLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQD 274
Cdd:PLN02652 275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 261878516 275 KTLKMYEGAYHVLHRElPEvTNSVLHEVNSWVSHRIA 311
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
55-300 2.35e-23

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 96.16  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  55 GTPKALIFVsHGAGehCGRYD--ELAHMLKGLDMLVFAHDHVGHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPdvPI 132
Cdd:COG1647   13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 133 FLLGHSMGGAISILVAAERPTyFSGMVLISPLVLANPESAstlkvLAAKLLNFVLPNMTLGRIDssvLSRNKSEVDLYNS 212
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 213 DPLVCraglkvcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--RE 290
Cdd:COG1647  158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229

                        250
                 ....*....|
gi 261878516 291 LPEVTNSVLH 300
Cdd:COG1647  230 REEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 36-301 6.95e-19

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: 83.51  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  36 PHLVNADGQYLFCRYWKPSGTPkaLIFVsHGAGEHCGRYDELAHML-KGLDmlVFAHDHVGHGQSEGERMVVSdFQVFVR 114
Cdd:COG0596    4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALaAGYR--VIAPDLRGHGRSDKPAGGYT-LDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 115 DVLQHVDTIQKDypdvPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLnfvlpnmtlgr 194
Cdd:COG0596   78 DLAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALA----------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 195 idssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVAR--VERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEssRS 272
Cdd:COG0596  143 ---------------------------------ALLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAE--LL 187

                        250       260
                 ....*....|....*....|....*....
gi 261878516 273 QDKTLKMYEGAYHVLHRELPEVTNSVLHE 301
Cdd:COG0596  188 PNAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 29-286 3.38e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 82.27  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  29 NVPYQDLpHLVNADGQYLFCRYWKPSGTPKAL--IFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVV 106
Cdd:COG1073    7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 107 SDFQvfVRDVLQHVDTIQKdYPDVP---IFLLGHSMGGAISILVAAERPtYFSGMVLISPLVLANPESASTLKVLAAKLL 183
Cdd:COG1073   86 GSPE--RRDARAAVDYLRT-LPGVDperIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 184 NFV--LPNMTLGridssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSK 261
Cdd:COG1073  162 PGVpyLPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFY 207

                        250       260
                 ....*....|....*....|....*
gi 261878516 262 GAYLLMESSrSQDKTLKMYEGAYHV 286
Cdd:COG1073  208 MSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
40-310 1.41e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.67  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  40 NADGQYLFCRYWKPSGTPKA-LIFVSHGAGEH-CGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSdfqvfVRDVL 117
Cdd:COG1506    4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 118 QHVDTIQKDyPDVP---IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLKVLAAKLLNFVLPNMtlgr 194
Cdd:COG1506   79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWED---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 195 idssvlsrnksEVDLYNSDPlvcraglkvcfgiqlLNAVARVERamprltlPFLLLQGSADRLCDSKGAYLLME--SSRS 272
Cdd:COG1506  152 -----------PEAYAARSP---------------LAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEalKKAG 198

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 261878516 273 QDKTLKMYEGAYHVLHRelpEVTNSVLHEVNSWVSHRI 310
Cdd:COG1506  199 KPVELLVYPGEGHGFSG---AGAPDYLERILDFLDRHL 233
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 88-288 2.03e-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: 60.21  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   88 VFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLA 167
Cdd:pfam00561  30 VIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  168 nPESASTLKVLAAKLLNF--------------VLPNMTLGRI---DSSVLSRNKSEVDLYNSDPLvcRAGLKVCFGIQLL 230
Cdd:pfam00561 107 -HELDEADRFILALFPGFfdgfvadfapnplgRLVAKLLALLllrLRLLKALPLLNKRFPSGDYA--LAKSLVTGALLFI 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  231 NAVARVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLmeSSRSQDKTLKMYEGAYHVLH 288
Cdd:pfam00561 184 ETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIPDAGHFAF 241
YpfH COG0400
Predicted esterase [General function prediction only];
54-179 2.73e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 50.29  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  54 SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTI 123
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261878516 124 QKDY--PDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLA 179
Cdd:COG0400   81 EARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 49-163 3.49e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.02  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  49 RYWK-PSGTPKALIFVsHG-AGEH---CGRYDELAhmlkgLDMLVFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT- 122
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAl 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261878516 123 -IQKDYpdvpifLLGHSMGGAISILVAAERPTYFSGMVLISP 163
Cdd:PRK14875 195 gIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 60-288 4.05e-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: 47.08  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   60 LIFVsHGAGEHcgrYDELAHMLKGlDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPdvpIFLLGHSM 139
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  140 GGAISILVAAerpTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgridssvLSRNKSEVDLYNSDPLVCRA 219
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAW---------LAAESLARGFLDDLPADAEW 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878516  220 GLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDskgAYLLMESSRSQDKTLKMYEGAYHVLH 288
Cdd:pfam12697 137 AAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
PLN02578 PLN02578
hydrolase
 55-307 5.47e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 47.53  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  55 GTPKALIfvsHGAGE---HCgRYD--ELAHMLKgldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypd 129
Cdd:PLN02578  86 GLPIVLI---HGFGAsafHW-RYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE--- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 130 vPIFLLGHSMGGAISILVAAERPTYFSGMVLI----------SPLVLANPESASTLKVLAAKLLNFVLPNMTLG------ 193
Cdd:PLN02578 153 -PAVLVGNSLGGFTALSTAVGYPELVAGVALLnsagqfgsesREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGflfwqa 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516 194 ----RIDSSVLS--RNKSEVDLY--------NSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCD 259
Cdd:PLN02578 232 kqpsRIESVLKSvyKDKSNVDDYlvesitepAADPNAGEVYYRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVG 311

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 261878516 260 SKGAYLLMESsrSQDKTLKMYEgAYHVLHRELPEVTNSVLHEvnsWVS 307
Cdd:PLN02578 312 PAKAEKIKAF--YPDTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 88-307 6.40e-06

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: 47.08  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516   88 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 144
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  145 I----LVAAERPTY----------FSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgRIDSSV-LSRNKSEVDL 209
Cdd:TIGR01607 157 LrlleLLGKSNENNdklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  210 YNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVL 287
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 261878516  288 HRElpEVTNSVLHEVNSWVS 307
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
PRK10749 PRK10749
lysophospholipase L2; Provisional
 73-164 8.65e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.53  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  73 RYDELAHMLKGLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILV 147
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                         90
                 ....*....|....*..
gi 261878516 148 AAERPTYFSGMVLISPL 164
Cdd:PRK10749 149 LQRHPGVFDAIALCAPM 165
COG4099 COG4099
Predicted peptidase [General function prediction only];
60-176 1.83e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.34  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  60 LIFVSHGAGEhcgRYDELAHMLK-GLDMLVfahdhvghgqSEGERmvvSDFQVFV-----------------RDVLQHVD 121
Cdd:COG4099   51 LVLFLHGAGE---RGTDNEKQLThGAPKFI----------NPENQ---AKFPAIVlapqcpeddywsdtkalDAVLALLD 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261878516 122 TIQKDYP-DvP--IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLK 176
Cdd:COG4099  115 DLIAEYRiD-PdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
37-152 6.83e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.42  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  37 HLVNADGQYLFCRYWKPSGT-PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA---HDHVGHGQSEGE---RMVVSDF 109
Cdd:COG0412    7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 261878516 110 QVFVRDVLQHVDTIQKDyPDV---PIFLLGHSMGGAISILVAAERP 152
Cdd:COG0412   87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 115-150 8.68e-05

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: 43.23  E-value: 8.68e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 261878516 115 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 150
Cdd:cd00519  113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 114-150 3.47e-04

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: 40.18  E-value: 3.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 261878516 114 RDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 150
Cdd:cd00741   12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
53-154 7.90e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.48  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  53 PSGTPKALIFVSHGAGEHCGRYDELAHML--KGldMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQH 119
Cdd:COG4188   57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLasHG--YVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQ 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261878516 120 VDTIQKDYPDVP-------IFLLGHSMGGAISILVAAERPTY 154
Cdd:COG4188  135 LLALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARLDF 176
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
134-163 1.35e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 39.58  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 261878516 134 LLGHSMGGAISILVAAERPTYFSGMVLISP 163
Cdd:COG2819  134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 131-164 2.73e-03

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: 38.75  E-value: 2.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 261878516 131 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 164
Cdd:cd12809  172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 95-150 4.22e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 4.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261878516  95 GHGQSEGERMVvSDFQVFVRDVLQHVdtiqKDYPDVPIFLLGHSMGGAISILVAAE 150
Cdd:COG3208   42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
20-152 6.87e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 37.82  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878516  20 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPSGTPKALIFVSHG-AGEHCGRY-DELAHMLKGLDMLVFAHDH 93
Cdd:COG0429   25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261878516  94 VGHGQSE---------GErmvVSDfqvfVRDVLQHvdtIQKDYPDVPIFLLGHSMGGAISILVAAERP 152
Cdd:COG0429   99 RGCGGEPnllprlyhsGD---TED----LVWVLAH---LRARYPYAPLYAVGFSLGGNLLLKYLGEQG 156
 
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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