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Conserved domains on  [gi|1918876719|ref|NP_001375241|]
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monoglyceride lipase isoform 4 [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, ...
 32-330 3.80e-99

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: 294.10  E-value: 3.80e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 192 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 271
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918876719 272 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 330
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-330 3.80e-99

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 294.10  E-value: 3.80e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 192 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 271
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918876719 272 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 330
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-311 8.70e-87

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: 260.99  E-value: 8.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESAttfkdysrilkhlmekasrmlkfwipRPFWVLAAKVLNLVLPNL 210
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLA--------------------------PPILKLLAKLLGKLFPRL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 211 SL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMEL 289
Cdd:pfam12146 137 RVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYER 215

                         250       260
                  ....*....|....*....|..
gi 1918876719 290 AKSQDKTLKIYEGAYHVLHKEL 311
Cdd:pfam12146 216 AGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-328 4.66e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 158.63  E-value: 4.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKdysrilkhlmekasrmlkfw 190
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR-------------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 191 iprpfWVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavsRVERALPKLTVPFLLL 270
Cdd:COG2267   146 -----WLRAL------------------------------------------------------RLAEALARIDVPVLVL 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1918876719 271 QGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 328
Cdd:COG2267   167 HGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.32e-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: 2.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1918876719 103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-310 3.97e-03

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: 38.61  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 139 iLTAAERPGH---------------FAGMVLISplVLANPESaTTFKDysrilkhlmekasrmlkFWIPrpfwvlAAKVL 203
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIK--SVGSDDS-FKFKY-----------------FYLP------VMNFM 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 204 NLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDS 280
Cdd:TIGR01607 210 SRVFPTFRISKKIR--YEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSY 286

                         250       260       270
                  ....*....|....*....|....*....|
gi 1918876719 281 KGAYLLMELAKSQDKTLKIYEGAYHVLHKE 310
Cdd:TIGR01607 287 EGTVSFYNKLSISNKELHTLEDMDHVITIE 316
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 32-330 3.80e-99

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 294.10  E-value: 3.80e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  32 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 111
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 112 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 191
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 192 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 271
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918876719 272 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 330
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 51-311 8.70e-87

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: 260.99  E-value: 8.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  51 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 130
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 131 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESAttfkdysrilkhlmekasrmlkfwipRPFWVLAAKVLNLVLPNL 210
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLA--------------------------PPILKLLAKLLGKLFPRL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 211 SL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMEL 289
Cdd:pfam12146 137 RVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYER 215

                         250       260
                  ....*....|....*....|..
gi 1918876719 290 AKSQDKTLKIYEGAYHVLHKEL 311
Cdd:pfam12146 216 AGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-328 4.66e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 158.63  E-value: 4.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  31 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 111 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKdysrilkhlmekasrmlkfw 190
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR-------------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 191 iprpfWVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavsRVERALPKLTVPFLLL 270
Cdd:COG2267   146 -----WLRAL------------------------------------------------------RLAEALARIDVPVLVL 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1918876719 271 QGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 328
Cdd:COG2267   167 HGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 33-329 2.14e-36

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 134.11  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  33 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRY-EELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 110
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 111 LQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlanpesattfkdysRIlkhlmekASRMLK 188
Cdd:PLN02385  147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMC--------------KI-------ADDVVP 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 189 FWIPRPFWVLAAKvlnlVLPNLSLGP----IDSSVLSRNKTEVDIYNsdpLIC---RAGLKVcfGIQLLNAVSRVERALP 261
Cdd:PLN02385  206 PPLVLQILILLAN----LLPKAKLVPqkdlAELAFRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLE 276

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918876719 262 KLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 329
Cdd:PLN02385  277 EVSLPLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 37-337 2.18e-36

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 133.75  E-value: 2.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  37 GQYLFCRYWKPTGT--PKALIFVSHGAG-EHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGnDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 114 VDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesattfkdysrilkhlMEKASRMLkfwi 191
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAP----------------------MCKISDKI---- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 192 pRPFWVLAaKVLNLV---LPNLSLGP----IDSSVLSRNKTEVDIYNsdPLICRAGLKVCFGIQLLNAVSRVERALPKLT 264
Cdd:PLN02298  176 -RPPWPIP-QILTFVarfLPTLAIVPtadlLEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVS 251

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1918876719 265 VPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 337
Cdd:PLN02298  252 IPFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 35-329 2.54e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 124.24  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  35 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 113
Cdd:PLN02652  118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 114 VDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPesattfkdysrilkhlmekasrmlkfw 190
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKP--------------------------- 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 191 iPRPFWVLAAKVLNLVLPNLSLGPIDSS--VLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFL 268
Cdd:PLN02652  250 -AHPIVGAVAPIFSLVAPRFQFKGANKRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFM 328

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918876719 269 LLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 329
Cdd:PLN02652  329 VLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
49-318 3.34e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 104.25  E-value: 3.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  49 GTPKALIFVsHG--AGEHSGRYeeLARMLMGLDLLVFAHDHVGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPV 126
Cdd:COG1647    13 GGRKGVLLL-HGftGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 127 FLLGHSMGGAIAILTAAERPgHFAGMVLISPlvlanpesATTFKDYSRILKHLMEKASRMLKFWiprpfwvlaakvlnlv 206
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSP--------ALKIDDPSAPLLPLLKYLARSLRGI---------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 207 lpnlslgpidSSVLSRNKTEVDIYNSDPLICraglkvcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLL 286
Cdd:COG1647   142 ----------GSDIEDPEVAEYAYDRTPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYI 203

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1918876719 287 MELAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 318
Cdd:COG1647   204 YERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 30-321 2.97e-19

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


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 85.05  E-value: 2.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  30 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHSGRYEELARMLMGlDLLVFAHDHVGHGQSEGERMVVSdFHVFVRD 109
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 110 VLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKDYSRILKHLMEKASRmlkf 189
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALAR---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 190 wiprpfwvlaakvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLL 269
Cdd:COG0596   151 ----------------------------------------------------------------TDLRERLARITVPTLV 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1918876719 270 LQGSADRLCDSKGAYLLMELAKsqDKTLKIYEGAYHVLHKELPEVTNSVFHE 321
Cdd:COG0596   167 IWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-306 2.95e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 82.66  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  23 SIPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGE-RMV 99
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 100 VS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPlvlanpesattFKDYSRI 175
Cdd:COG1073    86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSP-----------FTSLEDL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 176 LKHLMEkasRMLKFWIPRPFWvlaakvlnlvLPNLSLGpidssvlsrnktevdiynsdplicraglkvcfgiQLLNAVSR 255
Cdd:COG1073   149 AAQRAK---EARGAYLPGVPY----------LPNVRLA----------------------------------SLLNDEFD 181

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1918876719 256 VERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHV 306
Cdd:COG1073   182 PLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-310 5.07e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.13  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  34 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-SGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdFHVFVRDVL 111
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 112 QHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesATTFKDYSRILKHLMEKasRMLKF 189
Cdd:COG1506    79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--------VSDLRSYYGTTREYTER--LMGGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 190 WIPRpfwvlaakvlnlvlpnlslgpidssvlsrnkteVDIYNSDPLicraglkvcfgiqllnavsrveRALPKLTVPFLL 269
Cdd:COG1506   149 WEDP---------------------------------EAYAARSPL----------------------AYADKLKTPLLL 173

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1918876719 270 LQGSADRLCDSKGAYLLMELAKSQ--DKTLKIYEGAYHVLHKE 310
Cdd:COG1506   174 IHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 52-310 1.62e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 69.07  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  52 KALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLL 129
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 130 GHSMGGAIAILTAAERPGHFAGMVLISPLvlaNPESATTFKDYSRILKHLMEKASRMLKFwIPRPFWVLAAKVLNLVLPN 209
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGAL---DPPHELDEADRFILALFPGFFDGFVADF-APNPLGRLVAKLLALLLLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 210 LSLgpidssVLSRNKTEVDIYNSDPLIcrAGLKVCFGIQLLNAVSRVERA--LPKLTVPFLLLQGSADRLCDSKGAYLLM 287
Cdd:pfam00561 151 LRL------LKALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLA 222

                         250       260
                  ....*....|....*....|...
gi 1918876719 288 ELAKSqdKTLKIYEGAYHVLHKE 310
Cdd:pfam00561 223 QLFPN--ARLVVIPDAGHFAFLE 243
YpfH COG0400
Predicted esterase [General function prediction only];
48-164 1.62e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 53.76  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  48 TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA------HDHVGHG----QSEGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1918876719 118 QKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 164
Cdd:COG0400    81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
31-147 1.35e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.51  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  31 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA---HDHVGHGQSEGE---RMVVSDF 103
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1918876719 104 HVFVRDVLQHVD--SMQKDYPGLPVFLLGHSMGGAIAILTAAERPG 147
Cdd:COG0412    87 ELLAADLRAALDwlKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD 132
PRK10749 PRK10749
lysophospholipase L2; Provisional
 67-322 2.52e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.54  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  67 RYEELARMLMGLDLLVFAHDHVGHGQS-----EGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILT 141
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 142 AAERPGHFAGMVLISPL---VLANPesattfkdySRILKHLMEKASRMLKF----------WIPRPFwvlaakVLNlvlp 208
Cdd:PRK10749  149 LQRHPGVFDAIALCAPMfgiVLPLP---------SWMARRILNWAEGHPRIrdgyaigtgrWRPLPF------AIN---- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 209 nlslgpidssVLS----RNKTEVDIYNSDPLI---------CRAGLKVcfGIQLLNAVsrveralPKLTVPFLLLQGSAD 275
Cdd:PRK10749  210 ----------VLThsreRYRRNLRFYADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEE 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1918876719 276 RLCDSkgayllmelaKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEI 322
Cdd:PRK10749  271 RVVDN----------RMHDRFCEARTAAGHPCEGGKPLVIKGAYHEI 307
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-157 2.62e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.87  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  43 RYWK-PTGTPKALIFVsHG-AGEHS---GRYEELARmlmglDLLVFAHDHVGHGQSeGERMVVSDFHVFVRDVLQHVDSM 117
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLNnwlFNHAALAA-----GRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1918876719 118 QKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:PRK14875  195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 54-179 1.33e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.62  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  54 LIFVsHGAGEHSGRYEELARmlmgLDLLVFAHDHVGHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSM 133
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1918876719 134 GGAIAILTAAerpGHFAGMVLISPLVLANPESATTFKDYSRILKHL 179
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAAL 111
COG4099 COG4099
Predicted peptidase [General function prediction only];
107-171 8.19e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.50  E-value: 8.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1918876719 107 VRDVLQHVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFKD 171
Cdd:COG4099   106 LDAVLALLDDLIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLKK 170
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 49-167 1.86e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 45.77  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  49 GTPKALIFVSHGAG------EHSGRYEELARmlmGLDLLV----------------FAHDHVGHGQSEgermvvsdfHVF 106
Cdd:COG3509    50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD---------VAF 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918876719 107 VRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 167
Cdd:COG3509   118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
PLN02578 PLN02578
hydrolase
 49-327 2.08e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.60  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  49 GTPKALIfvsHGAGEHS--GRYE--ELARMLMgldllVFAHDHVGHGQSEgERMVVSDFHVFVRDVLQHVDSMQKDypgl 124
Cdd:PLN02578   86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 125 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISplvlanpeSATTFKDYSR----------------ILKHLMEKASRMLK 188
Cdd:PLN02578  153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLN--------SAGQFGSESRekeeaivveetvltrfVVKPLKEWFQRVVL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 189 FWIprpFWVLAA-----KVLNLVLpnlslgpidssvlsRNKTEVDIY--------NSDP--------LICRAglkvcfgi 247
Cdd:PLN02578  225 GFL---FWQAKQpsrieSVLKSVY--------------KDKSNVDDYlvesitepAADPnagevyyrLMSRF-------- 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 248 qLLNAvSR--VERALPKLTVPFLLLQGSADRLCDSKGAYLLMELakSQDKTLkIYEGAYHVLHKELPEVTNSVFHEinmW 325
Cdd:PLN02578  280 -LFNQ-SRytLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAF--YPDTTL-VNLQAGHCPHDEVPEQVNKALLE---W 351


                  ..
gi 1918876719 326 VS 327
Cdd:PLN02578  352 LS 353
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 103-144 2.32e-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: 2.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1918876719 103 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 125-158 2.38e-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: 2.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1918876719 125 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 158
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
109-158 3.46e-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: 3.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1918876719 109 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PL 158
Cdd:COG3571    65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPF 114
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 108-144 9.77e-05

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: 42.10  E-value: 9.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1918876719 108 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
47-146 2.77e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.02  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  47 PTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH--GQSEGERMVVSDFHVF---------VRDVLQHVD 115
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1918876719 116 SMQKDYPGLP-------VFLLGHSMGGAIAILTAAERP 146
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL 174
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
106-157 7.51e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 40.35  E-value: 7.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1918876719 106 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 157
Cdd:COG2819   112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 47-157 9.43e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 38.27  E-value: 9.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  47 PTGTPKALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdfhvfVRDVLQHVDSMQKDYPGLPV 126
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS---------AEQLAAFVDAVLAATGAEKV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1918876719 127 FLLGHSMGGAIA--ILTAAERPGHFAGMVLISP 157
Cdd:COG1075    71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
15-188 1.24e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 40.13  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  15 SSPRRTPQsIPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHSGRY-EELARMLMGLDLLVFAHDHV 88
Cdd:COG0429    26 SLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNFR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  89 GHGQSE---------GErmvVSDfhvfVRDVLQHVdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGH---FAGMVLIS 156
Cdd:COG0429   100 GCGGEPnllprlyhsGD---TED----LVWVLAHL---RARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAVS 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1918876719 157 -PLVLAnpESATTFKD-----YSR-ILKHLMEKASRMLK 188
Cdd:COG0429   170 pPLDLA--ASADRLERgfnrlYQRyFLRSLKRKLRRKLA 206
Lipase_3 pfam01764
Lipase (class 3);
121-169 3.36e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1918876719 121 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 169
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 82-310 3.97e-03

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: 38.61  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  82 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 138
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 139 iLTAAERPGH---------------FAGMVLISplVLANPESaTTFKDysrilkhlmekasrmlkFWIPrpfwvlAAKVL 203
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIK--SVGSDDS-FKFKY-----------------FYLP------VMNFM 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719 204 NLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDS 280
Cdd:TIGR01607 210 SRVFPTFRISKKIR--YEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSY 286

                         250       260       270
                  ....*....|....*....|....*....|
gi 1918876719 281 KGAYLLMELAKSQDKTLKIYEGAYHVLHKE 310
Cdd:TIGR01607 287 EGTVSFYNKLSISNKELHTLEDMDHVITIE 316
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 47-144 4.19e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 38.29  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918876719  47 PTGTPKALIFVSHGAGEHSGRYEELARmLMGLDLLVFAHDHVGHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPV 126
Cdd:COG3208     1 PRPDARLRLFCFPYAGGSASAYRPWAA-ALPPDIEVLAVQLPGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPF 74

                          90
                  ....*....|....*...
gi 1918876719 127 FLLGHSMGGAIAILTAAE 144
Cdd:COG3208    75 ALFGHSMGALLAFELARR 92
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
83-144 4.71e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 38.20  E-value: 4.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918876719  83 FAHDHVGHGQSEGerMVVSDFHVFVRDVLQHVDSM-QKDYPGLPVFLLGHSMGGAIAILTAAE 144
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELLEDAlRPLSPGKRLYVTGHSLGGALATLAAAD 108
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 128-159 5.98e-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: 5.98e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1918876719 128 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 159
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
PRK10673 PRK10673
esterase;
90-155 7.35e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.40  E-value: 7.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1918876719  90 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 155
Cdd:PRK10673   53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
 
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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