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Conserved domains on  [gi|6754690|ref|NP_035974|]
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monoglyceride lipase isoform b [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, ...
 22-294 1.95e-105

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: 308.35  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   182 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6754690   262 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 1.95e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 308.35  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   182 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6754690   262 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 6.89e-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: 264.85  E-value: 6.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     41 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    121 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSEVDLYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754690    200 VCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 275
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-290 4.56e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.17  E-value: 4.56e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 98
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   99 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfvlpnmtlgr 178
Cdd:COG2267  85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  179 idssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQD 258
Cdd:COG2267 150 ---------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPD 189

                       250       260       270
                ....*....|....*....|....*....|..
gi 6754690  259 KTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 290
Cdd:COG2267 190 VELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-291 5.76e-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: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    129 I----LVAAERPTY----------FSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgRIDSSV-LSRNKSEVDL 193
Cdd:TIGR01607 157 LrlleLLGKSNENNdklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    194 YNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVL 271
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 6754690    272 HRElpEVTNSVLHEVNSWVS 291
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 1.08e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.85  E-value: 1.08e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6754690   99 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 1.95e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 308.35  E-value: 1.95e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   182 SVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 6754690   262 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 6.89e-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: 264.85  E-value: 6.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     41 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    121 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSEVDLYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754690    200 VCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 275
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-290 4.56e-48

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 160.17  E-value: 4.56e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 98
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   99 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfvlpnmtlgr 178
Cdd:COG2267  85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  179 idssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsSRSQD 258
Cdd:COG2267 150 ---------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPD 189

                       250       260       270
                ....*....|....*....|....*....|..
gi 6754690  259 KTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 290
Cdd:COG2267 190 VELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-293 2.58e-35

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 130.26  E-value: 2.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    23 VNADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDE-LAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDV 100
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   101 LQHVDTIQ--KDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPL------VLANPESASTLKVLA-----AKLL 167
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMckiaddVVPPPLVLQILILLAnllpkAKLV 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   168 nfvlPNMTLGriDSSVLSRNKSEVDLYNSDPLVCRAGLKVcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGA 247
Cdd:PLN02385 227 ----PQKDLA--ELAFRDLKKRKMAEYNVIAYKDKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVS 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6754690   248 YLLMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHR 293
Cdd:PLN02385 299 KFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-300 2.04e-33

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 124.89  E-value: 2.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    27 GQYLFCRYWKPSGT--PKALIFVSHGAGEHCG-RYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   104 VDTIQKD--YPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLV-----LANPESASTLKVLAAKLLNF--VLPNM 174
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkisdkIRPPWPIPQILTFVARFLPTlaIVPTA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   175 TLgrIDSSVLSRNKSEVDLYNsdPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESS 254
Cdd:PLN02298 202 DL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6754690   255 RSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHRIAAAGAG 300
Cdd:PLN02298 278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-295 4.85e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 122.69  E-value: 4.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    25 ADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   104 VDTIQKDYPDVPIFLLGHSMGGAIsILVAAERPTY---FSGMVLISPLVLANPesASTLKVLAAKLLNFVLPNMTLGRID 180
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSIedkLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   181 SS--VLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQD 258
Cdd:PLN02652 275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 6754690   259 KTLKMYEGAYHVLHRElPEvTNSVLHEVNSWVSHRIA 295
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-284 3.35e-23

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 95.39  E-value: 3.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   39 GTPKALIFVsHGAGehCGRYD--ELAHMLKGLDMLVFAHDHVGHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPdvPI 116
Cdd:COG1647  13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  117 FLLGHSMGGAISILVAAERPTyFSGMVLISPLVLANPESAstlkvLAAKLLNFVLPNMTLGRIDssvLSRNKSEVDLYNS 196
Cdd:COG1647  87 IVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  197 DPLVCraglkvcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--RE 274
Cdd:COG1647 158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229

                       250
                ....*....|
gi 6754690  275 LPEVTNSVLH 284
Cdd:COG1647 230 REEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-285 1.26e-18

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: 82.74  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   20 PHLVNADGQYLFCRYWKPSGTPkaLIFVsHGAGEHCGRYDELAHML-KGLDmlVFAHDHVGHGQSEGERMVVSdFQVFVR 98
Cdd:COG0596   4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALaAGYR--VIAPDLRGHGRSDKPAGGYT-LDDLAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   99 DVLQHVDTIQKDypdvPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLnfvlpnmtlgr 178
Cdd:COG0596  78 DLAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALA----------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  179 idssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVAR--VERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEssRS 256
Cdd:COG0596 143 ---------------------------------ALLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAE--LL 187

                       250       260
                ....*....|....*....|....*....
gi 6754690  257 QDKTLKMYEGAYHVLHRELPEVTNSVLHE 285
Cdd:COG0596 188 PNAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-270 5.30e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 81.50  E-value: 5.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   13 NVPYQDLpHLVNADGQYLFCRYWKPSGTPKAL--IFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVV 90
Cdd:COG1073   7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   91 SDFQvfVRDVLQHVDTIQKdYPDVP---IFLLGHSMGGAISILVAAERPtYFSGMVLISPLVLANPESASTLKVLAAKLL 167
Cdd:COG1073  86 GSPE--RRDARAAVDYLRT-LPGVDperIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  168 NFV--LPNMTLGridssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSK 245
Cdd:COG1073 162 PGVpyLPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFY 207

                       250       260
                ....*....|....*....|....*
gi 6754690  246 GAYLLMESSrSQDKTLKMYEGAYHV 270
Cdd:COG1073 208 MSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-294 2.45e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.90  E-value: 2.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   24 NADGQYLFCRYWKPSGTPKA-LIFVSHGAGEH-CGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSdfqvfVRDVL 101
Cdd:COG1506   4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  102 QHVDTIQKDyPDVP---IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLKVLAAKLLNFVLPNMtlgr 178
Cdd:COG1506  79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWED---- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690  179 idssvlsrnksEVDLYNSDPlvcraglkvcfgiqlLNAVARVERamprltlPFLLLQGSADRLCDSKGAYLLME--SSRS 256
Cdd:COG1506 152 -----------PEAYAARSP---------------LAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEalKKAG 198

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6754690  257 QDKTLKMYEGAYHVLHRelpEVTNSVLHEVNSWVSHRI 294
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.
 72-272 3.56e-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: 59.06  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     72 VFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLA 151
Cdd:pfam00561  30 VIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    152 nPESASTLKVLAAKLLNF--------------VLPNMTLGRI---DSSVLSRNKSEVDLYNSDPLvcRAGLKVCFGIQLL 214
Cdd:pfam00561 107 -HELDEADRFILALFPGFfdgfvadfapnplgRLVAKLLALLllrLRLLKALPLLNKRFPSGDYA--LAKSLVTGALLFI 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    215 NAVARVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLmeSSRSQDKTLKMYEGAYHVLH 272
Cdd:pfam00561 184 ETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIPDAGHFAF 241
YpfH COG0400
Predicted esterase [General function prediction only];
38-163 3.71e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 49.52  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   38 SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTI 107
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6754690  108 QKDY--PDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLA 163
Cdd:COG0400  81 EARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 4.59e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 47.63  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    33 RYWK-PSGTPKALIFVsHG-AGEH---CGRYDELAhmlkgLDMLVFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT- 106
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAl 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6754690   107 -IQKDYpdvpifLLGHSMGGAISILVAAERPTYFSGMVLISP 147
Cdd:PRK14875 195 gIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-291 5.76e-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: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    129 I----LVAAERPTY----------FSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgRIDSSV-LSRNKSEVDL 193
Cdd:TIGR01607 157 LrlleLLGKSNENNdklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    194 YNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVL 271
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 6754690    272 HRElpEVTNSVLHEVNSWVS 291
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
PLN02578 PLN02578
hydrolase
 39-291 6.09e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 47.14  E-value: 6.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    39 GTPKALIfvsHGAGEHC--GRYD--ELAHMLKgldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypdv 114
Cdd:PLN02578  86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   115 PIFLLGHSMGGAISILVAAERPTYFSGMVLI----------SPLVLANPESASTLKVLAAKLLNFVLPNMTLG------- 177
Cdd:PLN02578 153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLnsagqfgsesREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGflfwqak 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   178 ---RIDSSVLS--RNKSEVDLY--------NSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDS 244
Cdd:PLN02578 233 qpsRIESVLKSvyKDKSNVDDYlvesitepAADPNAGEVYYRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGP 312

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6754690   245 KGAYLLMESsrSQDKTLKMYEgAYHVLHRELPEVTNSVLHEvnsWVS 291
Cdd:PLN02578 313 AKAEKIKAF--YPDTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-148 8.07e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.53  E-value: 8.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    57 RYDELAHMLKGLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILV 131
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                         90
                 ....*....|....*..
gi 6754690   132 AAERPTYFSGMVLISPL 148
Cdd:PRK10749 149 LQRHPGVFDAIALCAPM 165
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-272 9.54e-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: 45.54  E-value: 9.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690     44 LIFVsHGAGEHCGRYDELAhmlkGLDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPdvpIFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALL----AAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    124 GGAISILVAAerpTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMtlgridssvLSRNKSEVDLYNSDPLVCRA 203
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAW---------LAAESLARGFLDDLPADAEW 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6754690    204 GLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDskgAYLLMESSRSQDKTLKMYEGAYHVLH 272
Cdd:pfam12697 137 AAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
COG4099 COG4099
Predicted peptidase [General function prediction only];
44-160 2.01e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 44.96  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   44 LIFVSHGAGEhcgRYDELAHMLK-GLDMLVfahdhvghgqSEGERmvvSDFQVFV-----------------RDVLQHVD 105
Cdd:COG4099  51 LVLFLHGAGE---RGTDNEKQLThGAPKFI----------NPENQ---AKFPAIVlapqcpeddywsdtkalDAVLALLD 114

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6754690  106 TIQKDYP-DvP--IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLK 160
Cdd:COG4099 115 DLIAEYRiD-PdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-136 8.99e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 8.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   21 HLVNADGQYLFCRYWKPSGT-PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412   7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6754690   94 QVFVRDVLQHVDTIQKDyPDV---PIFLLGHSMGGAISILVAAERP 136
Cdd:COG0412  87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 1.08e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.85  E-value: 1.08e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6754690   99 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 4.39e-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: 39.79  E-value: 4.39e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6754690   98 RDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00741  12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-138 9.95e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.09  E-value: 9.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690   37 PSGTPKALIFVSHGAGEHCGRYDELAHML--KGldMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQH 103
Cdd:COG4188  57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLasHG--YVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQ 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6754690  104 VDTIQKDYPDVP-------IFLLGHSMGGAISILVAAERPTY 138
Cdd:COG4188 135 LLALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARLDF 176
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
118-147 1.46e-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: 1.46e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 6754690  118 LLGHSMGGAISILVAAERPTYFSGMVLISP 147
Cdd:COG2819 134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 2.84e-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: 2.84e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 6754690  115 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 148
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 79-134 4.18e-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: 4.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6754690   79 GHGQSEGERMVvSDFQVFVRDVLQHVdtiqKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:COG3208  42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-136 7.53e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 37.43  E-value: 7.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754690    4 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPSGTPKALIFVSHG-AGEHCGRY-DELAHMLKGLDMLVFAHDH 77
Cdd:COG0429  25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6754690   78 VGHGQSE---------GErmvVSDfqvfVRDVLQHvdtIQKDYPDVPIFLLGHSMGGAISILVAAERP 136
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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