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Conserved domains on  [gi|51242953|ref|NP_001003794|]
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monoglyceride lipase isoform 2 [Homo sapiens]

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 7.87e-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: 306.81  E-value: 7.87e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  182 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 51242953  262 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 7.87e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 306.81  E-value: 7.87e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  182 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 51242953  262 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 3.19e-92

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 273.32  E-value: 3.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    41 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   121 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51242953   200 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 275
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-292 3.22e-51

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 168.26  E-value: 3.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 101 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAkvlnlvlpnlslgpid 180
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 181 ssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKT 260
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                       250       260       270
                ....*....|....*....|....*....|..
gi 51242953 261 LKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 292
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-274 1.08e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 46.31  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    72 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   129 iLTAAERPGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDI 193
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   194 YNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHV 270
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312


                  ....
gi 51242953   271 LHKE 274
Cdd:TIGR01607 313 ITIE 316
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.94e-05

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: 45.29  E-value: 1.94e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 51242953 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 148
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-294 7.87e-105

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 306.81  E-value: 7.87e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNLSLGPIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  182 SVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqDKTL 261
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 51242953  262 KIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-275 3.19e-92

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 273.32  E-value: 3.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    41 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   121 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPL 199
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51242953   200 ICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 275
Cdd:pfam12146 163 VHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-292 3.22e-51

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 168.26  E-value: 3.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 101 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAkvlnlvlpnlslgpid 180
Cdd:COG2267  87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 181 ssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKT 260
Cdd:COG2267 150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVE 191

                       250       260       270
                ....*....|....*....|....*....|..
gi 51242953 261 LKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 292
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-293 8.40e-39

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 139.50  E-value: 8.40e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   23 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRY-EELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  101 LQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLV-----LANPESATTFKVLAAKVLnlvlPN 173
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLL----PK 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  174 LSLGP----IDSSVLSRNKTEVDIYNsdpLIC---RAGLKVcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKG 246
Cdd:PLN02385 223 AKLVPqkdlAELAFRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSV 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 51242953  247 AYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 293
Cdd:PLN02385 298 SKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-301 1.03e-37

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 136.45  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   27 GQYLFCRYWKPTGT--PKALIFVSHGAG-EHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 103
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGnDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  104 VDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVlaAKVLNLV---LPNLSLGP 178
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIVP 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  179 ----IDSSVLSRNKTEVDIYNsdPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELA 254
Cdd:PLN02298 200 tadlLEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 51242953  255 KSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 301
Cdd:PLN02298 278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-293 2.94e-36

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 133.87  E-value: 2.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   25 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 103
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  104 VDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPESATTFKVlaAKVLNLVLPNLSLGPID 180
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGAN 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  181 SS--VLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQD 258
Cdd:PLN02652 275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 51242953  259 KTLKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 293
Cdd:PLN02652 355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-282 3.74e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 103.48  E-value: 3.74e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  39 GTPKALIFVsHG--AGEHSGRYeeLARMLMGLDLLVFAHDHVGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPV 116
Cdd:COG1647  13 GGRKGVLLL-HGftGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 117 FLLGHSMGGAIAILTAAERPgHFAGMVLISPLVLANPESAttfkvLAAKVLNLVLPNLSLGPIDssvLSRNKTEVDIYNS 196
Cdd:COG1647  87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 197 DPLICraglkvcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH--KE 274
Cdd:COG1647 158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229


                ....*...
gi 51242953 275 LPEVTNSV 282
Cdd:COG1647 230 REEVAEEI 237
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-285 1.21e-21

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: 90.83  E-value: 1.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  20 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHSGRYEELARMLMGlDLLVFAHDHVGHGQSEGERMVVSdFHVFVRD 99
Cdd:COG0596   4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 100 VLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlanpesattfKVLAAkvlNLVLPNLSLGPI 179
Cdd:COG0596  79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL----------AALAE---PLRRPGLAPEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 180 DSSVLSRNKTEvdiynsdplicraglkvcfgiqllnavsrVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKsqDK 259
Cdd:COG0596 142 AALLRALARTD-----------------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NA 190

                       250       260
                ....*....|....*....|....*.
gi 51242953 260 TLKIYEGAYHVLHKELPEVTNSVFHE 285
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-270 4.45e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 87.28  E-value: 4.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  13 SIPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGE-RMV 89
Cdd:COG1073   7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  90 VS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPlvLANPESAttFKVLAAK 165
Cdd:COG1073  86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSP--FTSLEDL--AAQRAKE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 166 VLNLVLPNLSLGPIDSSVLSRNKtEVDIYNsdplicraglkvcfgiqllnavsrverALPKLTVPFLLLQGSADRLCDSK 245
Cdd:COG1073 156 ARGAYLPGVPYLPNVRLASLLND-EFDPLA---------------------------KIEKISRPLLFIHGEKDEAVPFY 207

                       250       260
                ....*....|....*....|....*
gi 51242953 246 GAYLLMELAkSQDKTLKIYEGAYHV 270
Cdd:COG1073 208 MSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-274 2.14e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 79.29  E-value: 2.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  24 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-SGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdFHVFVRDVL 101
Cdd:COG1506   4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 102 QHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesattfkvlaakVLNLVlpnlslgpi 179
Cdd:COG1506  79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG------------------VSDLR--------- 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 180 dsSVLSRNKTEVDIYNSDPLICRAGLKvcfgiqllnAVSRVERAlPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQ-- 257
Cdd:COG1506 132 --SYYGTTREYTERLMGGPWEDPEAYA---------ARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgk 199

                       250
                ....*....|....*..
gi 51242953 258 DKTLKIYEGAYHVLHKE 274
Cdd:COG1506 200 PVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 42-274 8.70e-14

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: 69.46  E-value: 8.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    42 KALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLL 119
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   120 GHSMGGAIAILTAAERPGHFAGMVLISPLVLAN-------------PESATTFKVLAAKVLNLVLPNLSLGPI---DSSV 183
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   184 LSRNKTEVDIYNSDPLIcrAGLKVCFGIQLLNAVSRVERA--LPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqdKTL 261
Cdd:pfam00561 155 KALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--ARL 230

                         250
                  ....*....|...
gi 51242953   262 KIYEGAYHVLHKE 274
Cdd:pfam00561 231 VVIPDAGHFAFLE 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-272 4.20e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.56  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    44 LIFVsHGAGEHSGRYEELARmlmgLDLLVFAHDHVGHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   124 GGAIAILTAAerpGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRA 203
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51242953   204 GLKVCFGIQLlnavsrveRALPKLTVPFLLLqGSADRLCDskgAYLLMELAKSQDKTLKIYEGAYHVLH 272
Cdd:pfam12697 146 LLAALALLPL--------AAWRDLPVPVLVL-AEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
YpfH COG0400
Predicted esterase [General function prediction only];
38-154 1.87e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 53.37  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  38 TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA------HDHVGHG----QSEGERMVVSDFHVFVRDVLQHVDSM 107
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51242953 108 QKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 154
Cdd:COG0400  81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-167 6.84e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 52.28  E-value: 6.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  21 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412   7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51242953  94 HVFVRDVLQHVD--SMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPLVLANPESATTFKVlAAKVL 167
Cdd:COG0412  87 ELLAADLRAALDwlKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLLDLAARI-KAPVL 160
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-286 2.83e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.15  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   57 RYEELARMLMGLDLLVFAHDHVGHGQS-----EGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILT 131
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  132 AAERPGHFAGMVLISPL---VLANPESATTFKVLAAKVLNLVLPNLSLG-------PIDSSVLS----RNKTEVDIYNSD 197
Cdd:PRK10749 149 LQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLThsreRYRRNLRFYADD 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  198 PLI---------CRAGLKVcfGIQLLNAVsrveralPKLTVPFLLLQGSADRLCDSkgayllmelaKSQDKTLKIYEGAY 268
Cdd:PRK10749 229 PELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEERVVDN----------RMHDRFCEARTAAG 289

                        250
                 ....*....|....*...
gi 51242953  269 HVLHKELPEVTNSVFHEI 286
Cdd:PRK10749 290 HPCEGGKPLVIKGAYHEI 307
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 3.51e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   33 RYWK-PTGTPKALIFVsHG-AGEHS---GRYEELARmlmglDLLVFAHDHVGHGQSeGERMVVSDFHVFVRDVLQHVDSM 107
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLNnwlFNHAALAA-----GRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 51242953  108 QKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 147
Cdd:PRK14875 195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-269 1.08e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 46.25  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  37 PTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH--GQSEGERMVVSDFHVF---------VRDVLQHVD 105
Cdd:COG4188  57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 106 SMQKDYPGLP-------VFLLGHSMGGAIAILTAAERPghfagmvlisplvlanpeSATTFKVLAAKVLNLVLPNLSLGP 178
Cdd:COG4188 137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953 179 IDSSVlsrnktevdiynSDPLIcRAGLkvcfgiqLLNAVSR---VERALPKLTVPFLLLQGSADRlcDSKGAY---LLME 252
Cdd:COG4188 199 LAYDL------------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFD 256

                       250
                ....*....|....*..
gi 51242953 253 LAKSQDKTLKIYEGAYH 269
Cdd:COG4188 257 LLPGADKYLLTLEGATH 273
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-274 1.08e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 46.31  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953    72 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   129 iLTAAERPGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDI 193
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   194 YNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHV 270
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHV 312


                  ....
gi 51242953   271 LHKE 274
Cdd:TIGR01607 313 ITIE 316
COG4099 COG4099
Predicted peptidase [General function prediction only];
44-160 1.21e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  44 LIFVSHGAGEhsgRYEELARMLM-GLDLLVfahdhvghGQSEGER---MVVS---------DFHVFVRDVLQHVDSMQKD 110
Cdd:COG4099  51 LVLFLHGAGE---RGTDNEKQLThGAPKFI--------NPENQAKfpaIVLApqcpeddywSDTKALDAVLALLDDLIAE 119

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 51242953 111 YPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFK 160
Cdd:COG4099 120 YRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 1.94e-05

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: 45.29  E-value: 1.94e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 51242953 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 148
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 39-157 2.11e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 45.38  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  39 GTPKALIFVSHGAG------EHSGRYEELARmlmGLDLLV----------------FAHDHVGHGQSEgermvvsdfHVF 96
Cdd:COG3509  50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD---------VAF 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51242953  97 VRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 157
Cdd:COG3509 118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 93-134 2.40e-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: 44.77  E-value: 2.40e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 51242953  93 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
99-148 3.21e-05

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 44.10  E-value: 3.21e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 51242953  99 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PL 148
Cdd:COG3571  65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPF 114
PLN02578 PLN02578
hydrolase
 39-291 4.06e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 44.45  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   39 GTPKALIfvsHGAGEHS--GRYE--ELARMLMgldllVFAHDHVGHGQS-----EGERMVVSDFHV-FVRDVLQHvdsmq 108
Cdd:PLN02578  86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSdkaliEYDAMVWRDQVAdFVKEVVKE----- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  109 kdypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL------------VLANPESA-TTFKVLAAK------VLNL 169
Cdd:PLN02578 153 ------PAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqfgsesrekeeAIVVEETVlTRFVVKPLKewfqrvVLGF 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  170 VLPNLSLGPIDSSVLS---RNKTEVDIY--------NSDP--------LICRAglkvcfgiqLLNAvSR--VERALPKLT 228
Cdd:PLN02578 227 LFWQAKQPSRIESVLKsvyKDKSNVDDYlvesitepAADPnagevyyrLMSRF---------LFNQ-SRytLDSLLSKLS 296

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51242953  229 VPFLLLQGSADRLCDSKGAYLLMELakSQDKTLkIYEGAYHVLHKELPEVTNSVFHEinmWVS 291
Cdd:PLN02578 297 CPLLLLWGDLDPWVGPAKAEKIKAF--YPDTTL-VNLQAGHCPHDEVPEQVNKALLE---WLS 353
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 1.17e-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: 41.72  E-value: 1.17e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 51242953  98 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:cd00741  12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
96-147 5.66e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 40.74  E-value: 5.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51242953  96 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 147
Cdd:COG2819 112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 37-147 1.34e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.50  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  37 PTGTPKALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdfhvfVRDVLQHVDSMQKDYPGLPV 116
Cdd:COG1075   1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS---------AEQLAAFVDAVLAATGAEKV 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 51242953 117 FLLGHSMGGAIA--ILTAAERPGHFAGMVLISP 147
Cdd:COG1075  71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
Abhydrolase_5 pfam12695
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ...
 104-193 2.12e-03

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


Pssm-ID: 315383 [Multi-domain]  Cd Length: 164  Bit Score: 38.20  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   104 VDSMQKDYPGLPVFLL-GHSMGGAIAILTAAERpGHFAGMVLisplvLANPESATTFKVLAAKVLNLVLPNLSLGPIDSS 182
Cdd:pfam12695  46 ALSIIKAHPKIQKWVVgGHSLGGVMASRFAADN-ELIKGVVF-----LASYPDKDSLSNLSFPVLSIYGTNDGVLNWKSY 119

                          90
                  ....*....|....*.
gi 51242953   183 V-----LSRNKTEVDI 193
Cdd:pfam12695 120 QknkqfLPKDTTYVSI 135
Lipase_3 pfam01764
Lipase (class 3);
111-159 3.43e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 51242953   111 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 159
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
5-151 3.43e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 38.59  E-value: 3.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953   5 SSPRRTPQsIPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHSGRY-EELARMLMGLDLLVFAHDHV 78
Cdd:COG0429  26 SLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNFR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  79 GHGQSE---------GErmvVSDfhvfVRDVLQHVdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGH---FAGMVLIS 146
Cdd:COG0429 100 GCGGEPnllprlyhsGD---TED----LVWVLAHL---RARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAVS 169


                ....*.
gi 51242953 147 -PLVLA 151
Cdd:COG0429 170 pPLDLA 175
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 37-134 3.92e-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: 3.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242953  37 PTGTPKALIFVSHGAGEHSGRYEELARmLMGLDLLVFAHDHVGHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPV 116
Cdd:COG3208   1 PRPDARLRLFCFPYAGGSASAYRPWAA-ALPPDIEVLAVQLPGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPF 74

                        90
                ....*....|....*...
gi 51242953 117 FLLGHSMGGAIAILTAAE 134
Cdd:COG3208  75 ALFGHSMGALLAFELARR 92
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
73-134 4.27e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 38.20  E-value: 4.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51242953  73 FAHDHVGHGQSEGerMVVSDFHVFVRDVLQHVDSM-QKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:COG3675  48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELLEDAlRPLSPGKRLYVTGHSLGGALATLAAAD 108
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 118-149 4.59e-03

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


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 37.83  E-value: 4.59e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51242953   118 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 149
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
PRK10673 PRK10673
esterase;
80-145 6.00e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.40  E-value: 6.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51242953   80 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 145
Cdd:PRK10673  53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-147 9.43e-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: 214007  Cd Length: 309  Bit Score: 37.22  E-value: 9.43e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 51242953 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 147
Cdd:cd12808 189 PCIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
 
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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