NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1149855958|ref|XP_020138910|]
View 

monoglyceride lipase isoform X2 [Microcebus murinus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 1-250 9.14e-92

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: 271.76  E-value: 9.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:PHA02857   28 VFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPLVLAspESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKAEVELYNADPLICRAG 160
Cdd:PHA02857  108 ATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEK 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 161 LKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSqDKTLKIYEGAYHVLHKELPEVTGSVFQ 240
Cdd:PHA02857  186 IKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMK 264

                         250
                  ....*....|
gi 1149855958 241 EIKLWVSQRT 250
Cdd:PHA02857  265 EIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 1-250 9.14e-92

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 271.76  E-value: 9.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:PHA02857   28 VFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPLVLAspESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKAEVELYNADPLICRAG 160
Cdd:PHA02857  108 ATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEK 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 161 LKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSqDKTLKIYEGAYHVLHKELPEVTGSVFQ 240
Cdd:PHA02857  186 IKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMK 264

                         250
                  ....*....|
gi 1149855958 241 EIKLWVSQRT 250
Cdd:PHA02857  265 EIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 1-231 2.61e-88

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: 261.77  E-value: 2.61e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPLVLASPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKAEVELYNADPLICRa 159
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPLVHG- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149855958 160 GLKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVLHKEL 231
Cdd:pfam12146 166 GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
5-248 1.20e-41

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 142.06  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVqRDHPGLPVFLLGHSMGGAIA 84
Cdd:COG2267    35 HGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDAL-RARPGLPVVLLGHSMGGLIA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ILTAAERPGLFSGMVLISPLVLASPESATTFKVLAAkvlnlvlpnlslgpidssvlsrnkaevelynadplicraglkvs 164
Cdd:COG2267   114 LLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------------------------------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 165 fgmqllnavARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAkSQDKTLKIYEGAYHVLHKELPEVTgsVFQEIKL 244
Cdd:COG2267   150 ---------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAREE--VLAAILA 217


                  ....
gi 1149855958 245 WVSQ 248
Cdd:COG2267   218 WLER 221
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 28-230 1.03e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 45.93  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  28 VFAHDHVGHGQSGG---DRMVVSDFHVFVRDVLQHVDAVQ--------------------RDHPGLPVFLLGHSMGGAIA 84
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINdsiilenetksddesydivnTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ------------ILTAAERPGLFSGMVLISPLVLASPESaTTFKVLAAKVLNL---VLPNLSLGPIDSsvLSRNKAEVEL 149
Cdd:TIGR01607 157 lrllellgksneNNDKLNIKGCISLSGMISIKSVGSDDS-FKFKYFYLPVMNFmsrVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 150 YNADPLICRAGLKVSFGMQLLNAVARVERALPRL--TLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVL 227
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313


                  ...
gi 1149855958 228 HKE 230
Cdd:TIGR01607 314 TIE 316
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 71-104 4.42e-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: 43.75  E-value: 4.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1149855958  71 PVFLLGHSMGGAIAILTAAERPGLFSGMVLISPL 104
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 1-250 9.14e-92

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 271.76  E-value: 9.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:PHA02857   28 VFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPLVLAspESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKAEVELYNADPLICRAG 160
Cdd:PHA02857  108 ATISILAAYKNPNLFTAMILMSPLVNA--EAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEK 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 161 LKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSqDKTLKIYEGAYHVLHKELPEVTGSVFQ 240
Cdd:PHA02857  186 IKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMK 264

                         250
                  ....*....|
gi 1149855958 241 EIKLWVSQRT 250
Cdd:PHA02857  265 EIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 1-231 2.61e-88

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: 261.77  E-value: 2.61e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPLVLASPESATTFKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKAEVELYNADPLICRa 159
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPLVHG- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149855958 160 GLKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVLHKEL 231
Cdd:pfam12146 166 GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
5-248 1.20e-41

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 142.06  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVqRDHPGLPVFLLGHSMGGAIA 84
Cdd:COG2267    35 HGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDAL-RARPGLPVVLLGHSMGGLIA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ILTAAERPGLFSGMVLISPLVLASPESATTFKVLAAkvlnlvlpnlslgpidssvlsrnkaevelynadplicraglkvs 164
Cdd:COG2267   114 LLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-------------------------------------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 165 fgmqllnavARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAkSQDKTLKIYEGAYHVLHKELPEVTgsVFQEIKL 244
Cdd:COG2267   150 ---------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAREE--VLAAILA 217


                  ....
gi 1149855958 245 WVSQ 248
Cdd:COG2267   218 WLER 221
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 1-253 4.09e-33

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 122.58  E-value: 4.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCG-RYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRD--HPGLPVFLLGH 77
Cdd:PLN02298   62 IFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeFQGLPRFLYGE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  78 SMGGAIAILTAAERPGLFSGMVLISPLVLASPESATTFKVlaAKVLNLV---LPNLSLGP----IDSSVlsRNKAEVELY 150
Cdd:PLN02298  142 SMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIVPtadlLEKSV--KVPAKKIIA 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 151 NADPLICRAGLKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYH-VLHK 229
Cdd:PLN02298  218 KRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIYDGMMHsLLFG 297

                         250       260
                  ....*....|....*....|....
gi 1149855958 230 ELPEVTGSVFQEIKLWVSQRTAGA 253
Cdd:PLN02298  298 EPDENIEIVRRDILSWLNERCTGK 321
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 1-249 4.92e-33

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 122.94  E-value: 4.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRE-LAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRD--HPGLPVFLLGH 77
Cdd:PLN02385   90 VCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVIEHYSKIKGNpeFRGLPSFLFGQ 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  78 SMGGAIAILTAAERPGLFSGMVLISPLV-----LASPESATTFKVLAAKVLnlvlPNLSLGP----IDSSVLSRNKAEVE 148
Cdd:PLN02385  170 SMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLL----PKAKLVPqkdlAELAFRDLKKRKMA 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 149 LYNADPLICRAGLKVSfgMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYH-VL 227
Cdd:PLN02385  246 EYNVIAYKDKPRLRTA--VELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYHsIL 323

                         250       260
                  ....*....|....*....|..
gi 1149855958 228 HKELPEVTGSVFQEIKLWVSQR 249
Cdd:PLN02385  324 EGEPDEMIFQVLDDIISWLDSH 345
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 1-254 9.58e-31

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 117.69  E-value: 9.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   1 MFVSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMG 80
Cdd:PLN02652  139 LIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFGHSTG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIaILTAAERP---GLFSGMVLISPLVLASPESATTFKVlaAKVLNLVLPNLSLGPIDSS--VLSRNKAEVELYNADPL 155
Cdd:PLN02652  219 GAV-VLKAASYPsieDKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGANKRgiPVSRDPAALLAKYSDPL 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 156 ICRAGLKVSFGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVLHKElPEvT 235
Cdd:PLN02652  296 VYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE-PE-R 373

                         250
                  ....*....|....*....
gi 1149855958 236 GSVFQEIKLWVSQRTAGAR 254
Cdd:PLN02652  374 EEVGRDIIDWMEKRLDLVN 392
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
15-251 1.70e-25

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 100.40  E-value: 1.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  15 RELAQMLAGLDLLVFAHDHVGHGQSGGDrMVVSDFHVFVRDVLQHVDAVQRDHPglPVFLLGHSMGGAIAILTAAERPGL 94
Cdd:COG1647    32 RPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYPDV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  95 fSGMVLISPLVlaspeSATTFKVLAAKVLNLVLPNLSLGPIDssvLSRNKAEVELYNADPLICraglkvsfGMQLLNAVA 174
Cdd:COG1647   109 -AGLVLLSPAL-----KIDDPSAPLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDRTPLRA--------LAELQRLIR 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149855958 175 RVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVLH--KELPEvtgsVFQEIKLWVSQRTA 251
Cdd:COG1647   172 EVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREE----VAEEILDFLERLAA 246
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 3-226 6.39e-19

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 83.04  E-value: 6.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   3 VSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGD-RMVVS----DFHVFVrDVLQHVDAVQRDhpglPVFLLGH 77
Cdd:COG1073    42 VAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREEGSperrDARAAV-DYLRTLPGVDPE----RIGLLGI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  78 SMGGAIAILTAAERPGlFSGMVLISPlvLASPESAttFKVLAAKVLNLVLPNLSLGPIDSSvlsrnkaevelynadplic 157
Cdd:COG1073   117 SLGGGYALNAAATDPR-VKAVILDSP--FTSLEDL--AAQRAKEARGAYLPGVPYLPNVRL------------------- 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149855958 158 raglkvsfgMQLLNAVARVERALPRLTLPFLLLQGSADRLCDSKGAYLLMEgAKSQDKTLKIYEGAYHV 226
Cdd:COG1073   173 ---------ASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYE-AAAEPKELLIVPGAGHV 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 5-235 1.61e-16

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 75.81  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGlDLLVFAHDHVGHGQSGGDRMVVSdFHVFVRDVLQHVDAVQRDhpglPVFLLGHSMGGAIA 84
Cdd:COG0596    30 HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGLE----RVVLVGHSMGGMVA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ILTAAERPGLFSGMVLISPLVlaspesattfkvlaakvlnlvlpnlslgpidssvlsrnkAEVELYNADPLICRAGLkvs 164
Cdd:COG0596   104 LELAARHPERVAGLVLVDEVL---------------------------------------AALAEPLRRPGLAPEAL--- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149855958 165 fgMQLLNAVAR--VERALPRLTLPFLLLQGSADRLCDSKGAYLLMEGAKsqDKTLKIYEGAYHVLHKELPEVT 235
Cdd:COG0596   142 --AALLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAF 210
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
5-230 2.41e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEH-CGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRmvvsdFHVFVRDVLQHVDAVqRDHPGLP---VFLLGHSMG 80
Cdd:COG1506    30 HGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVLAAIDYL-AARPYVDpdrIGIYGHSYG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  81 GAIAILTAAERPGLFSGMVLISPlvlaspesattfkvlaakVLNLVlpnlslgpidsSVLSRNKAEVELYNADPLICRAG 160
Cdd:COG1506   104 GYMALLAAARHPDRFKAAVALAG------------------VSDLR-----------SYYGTTREYTERLMGGPWEDPEA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149855958 161 LKvsfGMQLLNAVARVERalprltlPFLLLQGSADRLCDSKGAYLLMEGAKSQ--DKTLKIYEGAYHVLHKE 230
Cdd:COG1506   155 YA---ARSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 5-230 2.98e-11

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: 61.75  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGdRMVVSDFHVFvrDVLQHVDAVQRDHPGLPVFLLGHSMGGAIA 84
Cdd:pfam00561   7 HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ILTAAERPGLFSGMVLISPLVLAS-------------PESATTFKVLAAKVLNLVLPNLSLGPIDSSV--------LSRN 143
Cdd:pfam00561  84 LAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLLLRLrllkalplLNKR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 144 KAEVELYNADPLicraGLKVSFGMQLLNAVARVERaLPRLTLPFLLLQGSADRLCDSKGAYLLmeGAKSQDKTLKIYEGA 223
Cdd:pfam00561 164 FPSGDYALAKSL----VTGALLFIETWSTELRAKF-LGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIPDA 236


                  ....*..
gi 1149855958 224 YHVLHKE 230
Cdd:pfam00561 237 GHFAFLE 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 5-228 1.40e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.55  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHcgrYRELAQMLAGlDLLVFAHDHVGHGQSGGDRMVVSDfhvfVRDVLQHVDAVQRDHPglpVFLLGHSMGGAIA 84
Cdd:pfam12697   5 HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ILTAAerpGLFSGMVLISPLVLASPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKAEVELYNADplicraglkVS 164
Cdd:pfam12697  74 LAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAA---------LA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149855958 165 FGMQLLNAVARVERALPRLTLPFLLLQGSADRLCDskgAYLLMEGAKSQDKTLKIYEGAYHVLH 228
Cdd:pfam12697 142 RLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
3-94 3.17e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.58  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   3 VSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGD------RMVVSDFHVFVRDVLQHVDAVqRDHPGL---PVF 73
Cdd:COG0412    34 VLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDPELLAADLRAALDWL-KAQPEVdagRVG 112

                          90       100
                  ....*....|....*....|.
gi 1149855958  74 LLGHSMGGAIAILTAAERPGL 94
Cdd:COG0412   113 VVGFCFGGGLALLAAARGPDL 133
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 28-103 1.64e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 48.40  E-value: 1.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149855958  28 VFAHDHVGHGQSGgDRMVVSDFHVFVRDVLQHVDA--VQRDHpglpvfLLGHSMGGAIAILTAAERPGLFSGMVLISP 103
Cdd:PRK14875  160 VIALDLPGHGASS-KAVGAGSLDELAAAVLAFLDAlgIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK10749 PRK10749
lysophospholipase L2; Provisional
 13-225 3.60e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 47.30  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  13 RYRELAQMLAGLDLLVFAHDHVGHGQSGgdRMV-------VSDFHVFVRDV----LQHVDAVQRDHpglpVFLLGHSMGG 81
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSG--RLLddphrghVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  82 AIAILTAAERPGLFSGMVLISPL---VLASPESATTFKVLAAKVLNLVLPNLSLG-------PIDSSVLS----RNKAEV 147
Cdd:PRK10749  143 AILTLFLQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLThsreRYRRNL 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 148 ELYNADPLI---------CRAGLKVsfGMQLLNAVARVeralprlTLPFLLLQGSADRLCDSKGAYLLME-----GAKSQ 213
Cdd:PRK10749  223 RFYADDPELrvggptyhwVRESILA--GEQVLAGAGDI-------TTPLLLLQAEEERVVDNRMHDRFCEartaaGHPCE 293

                         250
                  ....*....|..
gi 1149855958 214 DKTLKIYEGAYH 225
Cdd:PRK10749  294 GGKPLVIKGAYH 305
YpfH COG0400
Predicted esterase [General function prediction only];
5-110 4.12e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGLDLLVFA------HDHVGHG----QSGGDRMVVSDFHVFVRDVLQHVDAVQRDHpGLP--- 71
Cdd:COG0400    12 HGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDELEARY-GIDper 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1149855958  72 VFLLGHSMGGAIAILTAAERPGLFSGMVLISPLVLASPE 110
Cdd:COG0400    91 IVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 28-230 1.03e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 45.93  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  28 VFAHDHVGHGQSGG---DRMVVSDFHVFVRDVLQHVDAVQ--------------------RDHPGLPVFLLGHSMGGAIA 84
Cdd:TIGR01607  77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINdsiilenetksddesydivnTKENRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  85 ------------ILTAAERPGLFSGMVLISPLVLASPESaTTFKVLAAKVLNL---VLPNLSLGPIDSsvLSRNKAEVEL 149
Cdd:TIGR01607 157 lrllellgksneNNDKLNIKGCISLSGMISIKSVGSDDS-FKFKYFYLPVMNFmsrVFPTFRISKKIR--YEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 150 YNADPLICRAGLKVSFGMQLLNAVARVERALPRL--TLPFLLLQGSADRLCDSKGAYLLMEGAKSQDKTLKIYEGAYHVL 227
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313


                  ...
gi 1149855958 228 HKE 230
Cdd:TIGR01607 314 TIE 316
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 71-104 4.42e-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: 43.75  E-value: 4.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1149855958  71 PVFLLGHSMGGAIAILTAAERPGLFSGMVLISPL 104
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
55-104 7.92e-05

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 42.56  E-value: 7.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1149855958  55 DVLQHVDAVQRDHPGLPVFLLGHSMGGAIAILTAAERPGLfSGMVLIS-PL 104
Cdd:COG3571    65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGGA-AGLVCLGyPF 114
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
74-103 9.49e-05

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 42.67  E-value: 9.49e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1149855958  74 LLGHSMGGAIAILTAAERPGLFSGMVLISP 103
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
COG4099 COG4099
Predicted peptidase [General function prediction only];
53-103 1.87e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 41.49  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1149855958  53 VRDVLQHVDAVQRDHPGLP--VFLLGHSMGGAIAILTAAERPGLFSGMVLISP 103
Cdd:COG4099   106 LDAVLALLDDLIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG 158
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 52-113 2.15e-04

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 41.53  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149855958  52 FVRDVlqhVDAVQRDHPGLP--VFLLGHSMGGAIAILTAAERPGLFSGMVLIS--PLVLASPESAT 113
Cdd:COG3509   117 FIAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Abhydrolase_5 pfam12695
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ...
 60-144 2.60e-04

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: 40.51  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  60 VDAVQRDHPGLPVFLL-GHSMGGAIAILTAAERpGLFSGMVLisplvLASPESATTFKVLAAKVLNLVLPNLSLGPIDSs 138
Cdd:pfam12695  46 ALSIIKAHPKIQKWVVgGHSLGGVMASRFAADN-ELIKGVVF-----LASYPDKDSLSNLSFPVLSIYGTNDGVLNWKS- 118


                  ....*.
gi 1149855958 139 vLSRNK 144
Cdd:pfam12695 119 -YQKNK 123
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
3-225 2.93e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.25  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   3 VSHGAGEHCGRYRELAQMLAGLDLLVFAHDHVGHGQSGGDRMVVSDFHVF-----------VRDVLQHVDAVQRDHPGLP 71
Cdd:COG4188    67 LSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAADLSAALDGLADALdpeelwerpldLSFVLDQLLALNKSDPPLA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  72 -------VFLLGHSMGGAIAILTAAERPglfsgmvlisplvlaspeSATTFKVLAAKVLNLVLPNLSLGPIDSSVlsrnk 144
Cdd:COG4188   147 grldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPRLAYDL----- 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958 145 aevelynADPLIcRAGLkvsfgmqLLNAVAR---VERALPRLTLPFLLLQGSADRlcDSKGAY---LLMEGAKSQDKTLK 218
Cdd:COG4188   204 -------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFDLLPGADKYLL 266


                  ....*..
gi 1149855958 219 IYEGAYH 225
Cdd:COG4188   267 TLEGATH 273
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
29-90 4.47e-04

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 40.51  E-value: 4.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149855958  29 FAHDHVGHGQSGGdrMVVSDFHVFVRDVLQH-VDAVQRDHPGLPVFLLGHSMGGAIAILTAAE 90
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELlEDALRPLSPGKRLYVTGHSLGGALATLAAAD 108
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 49-90 6.41e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.15  E-value: 6.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1149855958  49 FHVFVRDVLQHVDAVQRDHPGLPVFLLGHSMGGAIAILTAAE 90
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PRK10673 PRK10673
esterase;
36-101 6.67e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 40.10  E-value: 6.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149855958  36 HGQSGgdRMVVSDFHVFVRDVLQHVDAVQRDHpglpVFLLGHSMGGAIAILTAAERPGLFSGMVLI 101
Cdd:PRK10673   53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIEK----ATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 74-109 1.09e-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: 39.37  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1149855958  74 LLGHSMGGAIAILTAAERPGLFSGMVLISPLVLASP 109
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSN 149
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 54-90 2.65e-03

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


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 37.48  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1149855958  54 RDVLQHVDAVQRDHPGLPVFLLGHSMGGAIAILTAAE 90
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
5-103 2.82e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 38.30  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958   5 HGAGEHCGRYRELAQMLAGLD-----------LLVFAHDHVGhGQSGGDRMVVSDFH-VFVRDVLQHVDA-----VQRDH 67
Cdd:COG2382   119 DGGGGDEQDWFDQGRLPTILDnliaagkippmIVVMPDGGDG-GDRGTEGPGNDAFErFLAEELIPFVEKnyrvsADPEH 197

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1149855958  68 pglpVFLLGHSMGGAIAILTAAERPGLFSGMVLISP 103
Cdd:COG2382   198 ----RAIAGLSMGGLAALYAALRHPDLFGYVGSFSG 229
PLN02578 PLN02578
hydrolase
 28-103 3.27e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 38.28  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149855958  28 VFAHDHVGHGQSGG-----DRMVVSDFHV-FVRDVLQHvdavqrdhpglPVFLLGHSMGGAIAILTAAERPGLFSGMVLI 101
Cdd:PLN02578  115 VYALDLLGFGWSDKalieyDAMVWRDQVAdFVKEVVKE-----------PAVLVGNSLGGFTALSTAVGYPELVAGVALL 183


                  ..
gi 1149855958 102 SP 103
Cdd:PLN02578  184 NS 185
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
60-89 4.01e-03

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 38.01  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1149855958  60 VDAVQRDHPGLPVFLLGHSMGGAIAILTAA 89
Cdd:COG3243   267 VDAVREITGEDKVNLLGYCLGGTLLAIYAA 296
Lipase_3 pfam01764
Lipase (class 3);
67-115 6.11e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 36.08  E-value: 6.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1149855958  67 HPGLPVFLLGHSMGGAIAILTAAerpglfsgMVLISPLVLASPESATTF 115
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH