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Conserved domains on  [gi|1918879681|ref|NP_001375242|]
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monoglyceride lipase isoform 5 [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 22-320 4.05e-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: 293.33  E-value: 4.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 182 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 261
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918879681 262 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 320
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-320 4.05e-99

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 293.33  E-value: 4.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 182 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 261
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918879681 262 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 320
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-301 1.94e-86

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: 259.84  E-value: 1.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  41 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 121 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESAttfkdysrilkhlmekasrmlkfwipRPFWVLAAKVLNLVLPNL 200
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLA--------------------------PPILKLLAKLLGKLFPRL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 201 SL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMEL 279
Cdd:pfam12146 137 RVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYER 215

                         250       260
                  ....*....|....*....|..
gi 1918879681 280 AKSQDKTLKIYEGAYHVLHKEL 301
Cdd:pfam12146 216 AGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-318 9.62e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.47  E-value: 9.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 101 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKdysrilkhlmekasrmlkfw 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR-------------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 181 iprpfWVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavsRVERALPKLTVPFLLL 260
Cdd:COG2267   146 -----WLRAL------------------------------------------------------RLAEALARIDVPVLVL 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1918879681 261 QGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 318
Cdd:COG2267   167 HGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 2.28e-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: 2.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1918879681 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 148
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-300 3.74e-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: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  72 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 129 iLTAAERPGH---------------FAGMVLISplVLANPESaTTFKDysrilkhlmekasrmlkFWIPrpfwvlAAKVL 193
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIK--SVGSDDS-FKFKY-----------------FYLP------VMNFM 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 194 NLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDS 270
Cdd:TIGR01607 210 SRVFPTFRISKKIR--YEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSY 286

                         250       260       270
                  ....*....|....*....|....*....|
gi 1918879681 271 KGAYLLMELAKSQDKTLKIYEGAYHVLHKE 300
Cdd:TIGR01607 287 EGTVSFYNKLSISNKELHTLEDMDHVITIE 316
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-320 4.05e-99

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 293.33  E-value: 4.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  22 LVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVL 101
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 102 QHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAnpesattfkdysrilkhlmEKASRMLkfwi 181
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNA-------------------EAVPRLN---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 182 prpfwVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQ 261
Cdd:PHA02857  142 -----LLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQ 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1918879681 262 GSADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 320
Cdd:PHA02857  217 GTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-301 1.94e-86

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: 259.84  E-value: 1.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  41 PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 121 HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESAttfkdysrilkhlmekasrmlkfwipRPFWVLAAKVLNLVLPNL 200
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLA--------------------------PPILKLLAKLLGKLFPRL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 201 SL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMEL 279
Cdd:pfam12146 137 RVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYER 215

                         250       260
                  ....*....|....*....|..
gi 1918879681 280 AKSQDKTLKIYEGAYHVLHKEL 301
Cdd:pfam12146 216 AGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-318 9.62e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 157.47  E-value: 9.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  21 HLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 101 LQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKdysrilkhlmekasrmlkfw 180
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR-------------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 181 iprpfWVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavsRVERALPKLTVPFLLL 260
Cdd:COG2267   146 -----WLRAL------------------------------------------------------RLAEALARIDVPVLVL 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1918879681 261 QGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 318
Cdd:COG2267   167 HGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-327 1.19e-36

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 134.13  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  27 GQYLFCRYWKPTGT--PKALIFVSHGAG-EHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 103
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGnDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 104 VDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesattfkdysrilkhlMEKASRMLkfwi 181
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAP----------------------MCKISDKI---- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 182 pRPFWVLAaKVLNLV---LPNLSLGP----IDSSVLSRNKTEVDIYNsdPLICRAGLKVCFGIQLLNAVSRVERALPKLT 254
Cdd:PLN02298  176 -RPPWPIP-QILTFVarfLPTLAIVPtadlLEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVS 251

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1918879681 255 VPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 327
Cdd:PLN02298  252 IPFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-319 1.34e-36

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 134.49  E-value: 1.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  23 VNADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRY-EELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDV 100
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFfEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 101 LQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlanpesattfkdysRIlkhlmekASRMLK 178
Cdd:PLN02385  147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMC--------------KI-------ADDVVP 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 179 FWIPRPFWVLAAKvlnlVLPNLSLGP----IDSSVLSRNKTEVDIYNsdpLIC---RAGLKVcfGIQLLNAVSRVERALP 251
Cdd:PLN02385  206 PPLVLQILILLAN----LLPKAKLVPqkdlAELAFRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLE 276

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918879681 252 KLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 319
Cdd:PLN02385  277 EVSLPLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-319 2.14e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 124.24  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  25 ADGQYLFCRYWKP-TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQH 103
Cdd:PLN02652  118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 104 VDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPesattfkdysrilkhlmekasrmlkfw 180
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKP--------------------------- 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 181 iPRPFWVLAAKVLNLVLPNLSLGPIDSS--VLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFL 258
Cdd:PLN02652  250 -AHPIVGAVAPIFSLVAPRFQFKGANKRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFM 328

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918879681 259 LLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 319
Cdd:PLN02652  329 VLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-308 4.29e-26

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 103.87  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  39 GTPKALIFVsHG--AGEHSGRYeeLARMLMGLDLLVFAHDHVGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPV 116
Cdd:COG1647    13 GGRKGVLLL-HGftGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 117 FLLGHSMGGAIAILTAAERPgHFAGMVLISPlvlanpesATTFKDYSRILKHLMEKASRMLKFWiprpfwvlaakvlnlv 196
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSP--------ALKIDDPSAPLLPLLKYLARSLRGI---------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 197 lpnlslgpidSSVLSRNKTEVDIYNSDPLICraglkvcfGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLL 276
Cdd:COG1647   142 ----------GSDIEDPEVAEYAYDRTPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYI 203

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1918879681 277 MELAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 308
Cdd:COG1647   204 YERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-311 4.10e-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: 84.28  E-value: 4.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  20 PHLVNADGQYLFCRYWKPTGTPkaLIFVsHGAGEHSGRYEELARMLMGlDLLVFAHDHVGHGQSEGERMVVSdFHVFVRD 99
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 100 VLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKDYSRILKHLMEKASRmlkf 179
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALAR---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 180 wiprpfwvlaakvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLL 259
Cdd:COG0596   151 ----------------------------------------------------------------TDLRERLARITVPTLV 166

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1918879681 260 LQGSADRLCDSKGAYLLMELAKsqDKTLKIYEGAYHVLHKELPEVTNSVFHE 311
Cdd:COG0596   167 IWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-296 3.21e-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: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  13 SIPYQDLpHLVNADGQYLFCRYWKPTGTPKAL--IFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGE-RMV 89
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  90 VS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPlvlanpesattFKDYSRI 165
Cdd:COG1073    86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSP-----------FTSLEDL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 166 LKHLMEKASRMLKFWIPrpfwvlaakvlnlVLPNLSLGpidssvlsrnktevdiynsdplicraglkvcfgiQLLNAVSR 245
Cdd:COG1073   149 AAQRAKEARGAYLPGVP-------------YLPNVRLA----------------------------------SLLNDEFD 181

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1918879681 246 VERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHV 296
Cdd:COG1073   182 PLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-300 6.93e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 6.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  24 NADGQYLFCRYWKPTGTPKA-LIFVSHGAGEH-SGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdFHVFVRDVL 101
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 102 QHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesATTFKDYSRILKHLMEKasRMLKF 179
Cdd:COG1506    79 AAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--------VSDLRSYYGTTREYTER--LMGGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 180 WIPRpfwvlaakvlnlvlpnlslgpidssvlsrnkteVDIYNSDPLicraglkvcfgiqllnavsrveRALPKLTVPFLL 259
Cdd:COG1506   149 WEDP---------------------------------EAYAARSPL----------------------AYADKLKTPLLL 173

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1918879681 260 LQGSADRLCDSKGAYLLMELAKSQ--DKTLKIYEGAYHVLHKE 300
Cdd:COG1506   174 IHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGHGFSGA 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 42-300 2.27e-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: 68.69  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  42 KALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLL 119
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 120 GHSMGGAIAILTAAERPGHFAGMVLISPLvlaNPESATTFKDYSRILKHLMEKASRMLKFwIPRPFWVLAAKVLNLVLPN 199
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGAL---DPPHELDEADRFILALFPGFFDGFVADF-APNPLGRLVAKLLALLLLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 200 LSLgpidssVLSRNKTEVDIYNSDPLIcrAGLKVCFGIQLLNAVSRVERA--LPKLTVPFLLLQGSADRLCDSKGAYLLM 277
Cdd:pfam00561 151 LRL------LKALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLA 222

                         250       260
                  ....*....|....*....|...
gi 1918879681 278 ELAKSqdKTLKIYEGAYHVLHKE 300
Cdd:pfam00561 223 QLFPN--ARLVVIPDAGHFAFLE 243
YpfH COG0400
Predicted esterase [General function prediction only];
38-154 1.84e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 53.76  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  38 TGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA------HDHVGHG----QSEGERMVVSDFHVFVRDVLQHVDSM 107
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1918879681 108 QKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 154
Cdd:COG0400    81 EARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-137 1.56e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.51  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  21 HLVNADGQYLFCRYWKPTGT-PKALIFVSHGAGEHSGRYEELARMLMGLDLLVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1918879681  94 HVFVRDVLQHVD--SMQKDYPGLPVFLLGHSMGGAIAILTAAERPG 137
Cdd:COG0412    87 ELLAADLRAALDwlKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD 132
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 2.50e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.87  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  33 RYWK-PTGTPKALIFVsHG-AGEHS---GRYEELARmlmglDLLVFAHDHVGHGQSeGERMVVSDFHVFVRDVLQHVDSM 107
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLNnwlFNHAALAA-----GRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1918879681 108 QKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 147
Cdd:PRK14875  195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-312 3.05e-07

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 51.15  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  57 RYEELARMLMGLDLLVFAHDHVGHGQS-----EGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILT 131
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 132 AAERPGHFAGMVLISPL---VLANPesattfkdySRILKHLMEKASRMLKF----------WIPRPFwvlaakVLNlvlp 198
Cdd:PRK10749  149 LQRHPGVFDAIALCAPMfgiVLPLP---------SWMARRILNWAEGHPRIrdgyaigtgrWRPLPF------AIN---- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 199 nlslgpidssVLS----RNKTEVDIYNSDPLI---------CRAGLKVcfGIQLLNAVsrveralPKLTVPFLLLQGSAD 265
Cdd:PRK10749  210 ----------VLThsreRYRRNLRFYADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEE 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1918879681 266 RLCDSkgayllmelaKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEI 312
Cdd:PRK10749  271 RVVDN----------RMHDRFCEARTAAGHPCEGGKPLVIKGAYHEI 307
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-169 1.81e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 47.85  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  44 LIFVsHGAGEHSGRYEELARmlmgLDLLVFAHDHVGHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALLA----AGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1918879681 124 GGAIAILTAAerpGHFAGMVLISPLVLANPESATTFKDYSRILKHL 169
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAAL 111
COG4099 COG4099
Predicted peptidase [General function prediction only];
97-161 8.47e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.11  E-value: 8.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1918879681  97 VRDVLQHVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFKD 161
Cdd:COG4099   106 LDAVLALLDDLIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLKK 170
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 39-157 1.91e-05

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 45.38  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  39 GTPKALIFVSHGAG------EHSGRYEELARmlmGLDLLV----------------FAHDHVGHGQSEgermvvsdfHVF 96
Cdd:COG3509    50 GAPLPLVVALHGCGgsaadfAAGTGLNALAD---REGFIVvypegtgrapgrcwnwFDGRDQRRGRDD---------VAF 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918879681  97 VRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 157
Cdd:COG3509   118 IAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 2.28e-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: 2.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1918879681 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 148
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
PLN02578 PLN02578
hydrolase
 39-317 2.48e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.60  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  39 GTPKALIfvsHGAGEHS--GRYE--ELARMLMgldllVFAHDHVGHGQSEgERMVVSDFHVFVRDVLQHVDSMQKDypgl 114
Cdd:PLN02578   86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 115 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISplvlanpeSATTFKDYSR----------------ILKHLMEKASRMLK 178
Cdd:PLN02578  153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLN--------SAGQFGSESRekeeaivveetvltrfVVKPLKEWFQRVVL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 179 FWIprpFWVLAA-----KVLNLVLpnlslgpidssvlsRNKTEVDIY--------NSDP--------LICRAglkvcfgi 237
Cdd:PLN02578  225 GFL---FWQAKQpsrieSVLKSVY--------------KDKSNVDDYlvesitepAADPnagevyyrLMSRF-------- 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 238 qLLNAvSR--VERALPKLTVPFLLLQGSADRLCDSKGAYLLMELakSQDKTLkIYEGAYHVLHKELPEVTNSVFHEinmW 315
Cdd:PLN02578  280 -LFNQ-SRytLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAF--YPDTTL-VNLQAGHCPHDEVPEQVNKALLE---W 351


                  ..
gi 1918879681 316 VS 317
Cdd:PLN02578  352 LS 353
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 93-134 2.66e-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: 2.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1918879681  93 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:cd00519   107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
99-148 3.33e-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: 3.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1918879681  99 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PL 148
Cdd:COG3571    65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPF 114
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 1.11e-04

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


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 41.72  E-value: 1.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1918879681  98 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-136 2.70e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.02  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  37 PTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH--GQSEGERMVVSDFHVF---------VRDVLQHVD 105
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLL 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1918879681 106 SMQKDYPGLP-------VFLLGHSMGGAIAILTAAERP 136
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL 174
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
96-147 7.77e-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: 7.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1918879681  96 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 147
Cdd:COG2819   112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 37-147 1.18e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  37 PTGTPKALIFVsHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERmvvsdfhvfVRDVLQHVDSMQKDYPGLPV 116
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS---------AEQLAAFVDAVLAATGAEKV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1918879681 117 FLLGHSMGGAIA--ILTAAERPGHFAGMVLISP 147
Cdd:COG1075    71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
8-178 1.53e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 39.74  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681   8 RRTPQSIPYQ----DLPhlvnaDGQYLFCRYWKPTGTPKALIFVSHG-AGEHSGRY-EELARMLMGLDLLVFAHDHVGHG 81
Cdd:COG0429    28 FRRRPALPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNFRGCG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  82 QSE---------GErmvVSDfhvfVRDVLQHVdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGH---FAGMVLIS-PL 148
Cdd:COG0429   103 GEPnllprlyhsGD---TED----LVWVLAHL---RARYPYAPLYAVGFSLGGNLLLKYLGEQGDDappLKAAVAVSpPL 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1918879681 149 VLAnpESATTFKD-----YSR-ILKHLMEKASRMLK 178
Cdd:COG0429   173 DLA--ASADRLERgfnrlYQRyFLRSLKRKLRRKLA 206
Lipase_3 pfam01764
Lipase (class 3);
111-159 3.70e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 3.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1918879681 111 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 159
Cdd:pfam01764  60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-300 3.74e-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: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  72 VFAHDHVGHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIA 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 129 iLTAAERPGH---------------FAGMVLISplVLANPESaTTFKDysrilkhlmekasrmlkFWIPrpfwvlAAKVL 193
Cdd:TIGR01607 157 -LRLLELLGKsnenndklnikgcisLSGMISIK--SVGSDDS-FKFKY-----------------FYLP------VMNFM 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681 194 NLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDS 270
Cdd:TIGR01607 210 SRVFPTFRISKKIR--YEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSY 286

                         250       260       270
                  ....*....|....*....|....*....|
gi 1918879681 271 KGAYLLMELAKSQDKTLKIYEGAYHVLHKE 300
Cdd:TIGR01607 287 EGTVSFYNKLSISNKELHTLEDMDHVITIE 316
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 37-134 4.42e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918879681  37 PTGTPKALIFVSHGAGEHSGRYEELARmLMGLDLLVFAHDHVGHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPV 116
Cdd:COG3208     1 PRPDARLRLFCFPYAGGSASAYRPWAA-ALPPDIEVLAVQLPGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPF 74

                          90
                  ....*....|....*...
gi 1918879681 117 FLLGHSMGGAIAILTAAE 134
Cdd:COG3208    75 ALFGHSMGALLAFELARR 92
Lip2 COG3675
Predicted lipase [Lipid transport and metabolism];
73-134 5.33e-03

Predicted lipase [Lipid transport and metabolism];


Pssm-ID: 442891 [Multi-domain]  Cd Length: 266  Bit Score: 37.81  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918879681  73 FAHDHVGHGQSEGerMVVSDFHVFVRDVLQHVDSM-QKDYPGLPVFLLGHSMGGAIAILTAAE 134
Cdd:COG3675    48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELLEDAlRPLSPGKRLYVTGHSLGGALATLAAAD 108
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 118-149 5.51e-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: 5.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1918879681 118 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 149
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
PRK10673 PRK10673
esterase;
80-145 7.15e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.40  E-value: 7.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1918879681  80 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 145
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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