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Conserved domains on  [gi|1907172387|ref|XP_036021995|]
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monoglyceride lipase isoform X3 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 13-293 1.40e-87

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: 262.90  E-value: 1.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 172
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 173 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 252
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172387 253 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 293
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 13-293 1.40e-87

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 262.90  E-value: 1.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 172
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 173 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 252
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172387 253 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 293
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 13-274 5.06e-81

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: 244.82  E-value: 5.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 172
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPIL----------------------------KLLAKLLGKLFPR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 173 MTL-GRIDSSVLSRNKSEVDLYNSDPLVCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:pfam12146 136 LRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYE 214

                         250       260
                  ....*....|....*....|...
gi 1907172387 252 SSRSQDKTLKMYEGAYHVLHREL 274
Cdd:pfam12146 215 RAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-289 1.84e-35

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 127.43  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  12 RRALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDyPDVPIFLLG 91
Cdd:COG2267    27 PRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  92 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlWVLAakllnfvlp 171
Cdd:COG2267   106 HSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR---------------------------WLRA--------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 172 nmtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:COG2267   150 ---------------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA 184

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907172387 252 sSRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 289
Cdd:COG2267   185 -RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 43-290 7.45e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 43.62  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  43 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 99
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 100 ILVaaerptyfsgmvlispLVLANPEsaSTLKDKLHItKTSLEKAAEVSVTWI----PYAF-HLWVLAAKLLNFVLPNMt 174
Cdd:TIGR01607 157 LRL----------------LELLGKS--NENNDKLNI-KGCISLSGMISIKSVgsddSFKFkYFYLPVMNFMSRVFPTF- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 175 lgRIDSSV-LSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:TIGR01607 217 --RISKKIrYEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYN 294

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907172387 252 SSRSQDKTLKMYEGAYHVLHRElpEVTNSVLHEVNSWVS 290
Cdd:TIGR01607 295 KLSISNKELHTLEDMDHVITIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 70-105 1.51e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.08  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907172387  70 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 105
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 13-293 1.40e-87

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 262.90  E-value: 1.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 172
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 173 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 252
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172387 253 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 293
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 13-274 5.06e-81

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: 244.82  E-value: 5.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 172
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPIL----------------------------KLLAKLLGKLFPR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 173 MTL-GRIDSSVLSRNKSEVDLYNSDPLVCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:pfam12146 136 LRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYE 214

                         250       260
                  ....*....|....*....|...
gi 1907172387 252 SSRSQDKTLKMYEGAYHVLHREL 274
Cdd:pfam12146 215 RAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-289 1.84e-35

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 127.43  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  12 RRALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDyPDVPIFLLG 91
Cdd:COG2267    27 PRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  92 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlWVLAakllnfvlp 171
Cdd:COG2267   106 HSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR---------------------------WLRA--------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 172 nmtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:COG2267   150 ---------------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA 184

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907172387 252 sSRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 289
Cdd:COG2267   185 -RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 13-292 2.00e-27

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 109.07  E-value: 2.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDE-LAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQ--KDYPDVPIFL 89
Cdd:PLN02385   87 KAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVIEHYSKIKgnPEFRGLPSFL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  90 LGHSMGGAISILVAAERPTYFSGMVLISPLVlanpesastlkdklhitktsleKAAEvSVTWIPYAFHLWVLAAKLL--N 167
Cdd:PLN02385  167 FGQSMGGAVALKVHLKQPNAWDGAILVAPMC----------------------KIAD-DVVPPPLVLQILILLANLLpkA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 168 FVLPNMTLGriDSSVLSRNKSEVDLYNSDPLVCRAGLKVcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAY 247
Cdd:PLN02385  224 KLVPQKDLA--ELAFRDLKKRKMAEYNVIAYKDKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSK 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172387 248 LLMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHR 292
Cdd:PLN02385  300 FLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 13-299 4.03e-27

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 107.94  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCG-RYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKD--YPDVPIFL 89
Cdd:PLN02298   59 RALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeFQGLPRFL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  90 LGHSMGGAISILVAAERPTYFSGMVLISPLVlanpesasTLKDKlhitktslekaaeVSVTW-IPYAFHLWVLAAKLLNF 168
Cdd:PLN02298  139 YGESMGGAICLLIHLANPEGFDGAVLVAPMC--------KISDK-------------IRPPWpIPQILTFVARFLPTLAI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 169 VlPNMTLgrIDSSVLSRNKSEVDLYNsdPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYL 248
Cdd:PLN02298  198 V-PTADL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRA 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907172387 249 LMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHRIAAAGAG 299
Cdd:PLN02298  273 LYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 13-294 1.29e-23

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 99.20  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 92
Cdd:PLN02652  136 RGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFGH 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  93 SMGGAIsILVAAERPTY---FSGMVLISPLVLANPEsastlkdklhitktslekaaevsvtwipyafHLWVLA-AKLLNF 168
Cdd:PLN02652  216 STGGAV-VLKAASYPSIedkLEGIVLTSPALRVKPA-------------------------------HPIVGAvAPIFSL 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 169 VLPNMTLGRIDSS--VLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGA 246
Cdd:PLN02652  264 VAPRFQFKGANKRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLAS 343

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907172387 247 YLLMESSRSQDKTLKMYEGAYHVLHRElPEvTNSVLHEVNSWVSHRIA 294
Cdd:PLN02652  344 QDLYNEAASRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
50-283 9.98e-18

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 80.76  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  50 GHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPdvPIFLLGHSMGGAISILVAAERPTyFSGMVLISPLVLANPESAST 129
Cdd:COG1647    52 GHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 130 LKDKLHITKTsleKAAEVSVTWIPYAFHLWvlaakllnfvlpnmtlgridssvlsrnksevdlYNSDPLVCraglkvcfG 209
Cdd:COG1647   128 LPLLKYLARS---LRGIGSDIEDPEVAEYA---------------------------------YDRTPLRA--------L 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172387 210 IQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--RELPEVTNSVLH 283
Cdd:COG1647   164 AELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEILD 239
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-269 4.43e-13

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 67.63  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQvfVRDVLQHVDTIQKdYPDVP---IFL 89
Cdd:COG1073    37 YPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RRDARAAVDYLRT-LPGVDperIGL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  90 LGHSMGGAISILVAAERPtYFSGMVLISPLVLANPESASTLKDklhitktslekAAEVSVTWIPYafhlwvlaakllnfv 169
Cdd:COG1073   114 LGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKE-----------ARGAYLPGVPY--------------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 170 LPNMTLGridssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLL 249
Cdd:COG1073   167 LPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDL 212

                         250       260
                  ....*....|....*....|
gi 1907172387 250 MESSrSQDKTLKMYEGAYHV 269
Cdd:COG1073   213 YEAA-AEPKELLIVPGAGHV 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 13-284 2.47e-11

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: 61.94  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVsHGAGEHCGRYDELAHML-KGLDmlVFAHDHVGHGQSEGERMVVSdFQVFVRDVLQHVDTIQKDypdvPIFLLG 91
Cdd:COG0596    24 PPVVLL-HGLPGSSYEWRPLIPALaAGYR--VIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGLE----RVVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  92 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKDKLHITKTSLEkaaevsvtwipyAFHLWVLAAKLlnfvlp 171
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLR------------ALARTDLRERL------ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 172 nmtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavarveramPRLTLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:COG0596   158 ----------------------------------------------------ARITVPTLVIWGEKDPIVPPALARRLAE 185

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907172387 252 ssRSQDKTLKMYEGAYHVLHRELPEVTNSVLHE 284
Cdd:COG0596   186 --LLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 43-271 2.76e-10

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 59.44  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  43 VFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVla 122
Cdd:pfam00561  30 VIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALD-- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 123 npesastlkdklhiTKTSLEKAAEVSVTWIPYAFHLWVLAAKLLNF-VLPNMTLGRI---DSSVLSRNKSEVDLYNSDPL 198
Cdd:pfam00561 105 --------------PPHELDEADRFILALFPGFFDGFVADFAPNPLgRLVAKLLALLllrLRLLKALPLLNKRFPSGDYA 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172387 199 vcRAGLKVCFGIQLLNAVARVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLmeSSRSQDKTLKMYEGAYHVLH 271
Cdd:pfam00561 171 --LAKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIPDAGHFAF 241
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-118 3.86e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.79  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  12 RRALIFVSHGAGEH-CGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSdfqvfVRDVLQHVDTIQKDyPDVP---I 87
Cdd:COG1506    22 KYPVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVLAAIDYLAAR-PYVDpdrI 95

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907172387  88 FLLGHSMGGAISILVAAERPTYFSGMVLISP 118
Cdd:COG1506    96 GIYGHSYGGYMALLAAARHPDRFKAAVALAG 126
YpfH COG0400
Predicted esterase [General function prediction only];
13-125 7.22e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  13 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTIQKDY 82
Cdd:COG0400     5 APLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDELEARY 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907172387  83 --PDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPE 125
Cdd:COG0400    85 giDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 43-118 8.11e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.86  E-value: 8.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172387  43 VFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT--IQKDYpdvpifLLGHSMGGAISILVAAERPTYFSGMVLISP 118
Cdd:PRK14875  160 VIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAlgIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK10749 PRK10749
lysophospholipase L2; Provisional
 28-119 9.69e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.53  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  28 RYDELAHMLKGLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILV 102
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90
                  ....*....|....*..
gi 1907172387 103 AAERPTYFSGMVLISPL 119
Cdd:PRK10749  149 LQRHPGVFDAIALCAPM 165
COG4099 COG4099
Predicted peptidase [General function prediction only];
15-132 1.16e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  15 LIFVSHGAGEhcgRYDELAHMLK-GLDMLVfahdhvghgqSEGERmvvSDFQVFV-----------------RDVLQHVD 76
Cdd:COG4099    51 LVLFLHGAGE---RGTDNEKQLThGAPKFI----------NPENQ---AKFPAIVlapqcpeddywsdtkalDAVLALLD 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172387  77 TIQKDYP-DvP--IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLKD 132
Cdd:COG4099   115 DLIAEYRiD-PdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLKK 170
PLN02578 PLN02578
hydrolase
 21-290 1.25e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 45.99  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  21 GAGEHCGRYD--ELAHMLKgldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypdvPIFLLGHSMGGAI 98
Cdd:PLN02578   96 GASAFHWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE----PAVLVGNSLGGFT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  99 SILVAAERPTYFSGMVLISPL-VLANPES---ASTLKDKLHITKTSLEKAAEVSVTWIpYAFHLWVLAAKllnfvlpnmt 174
Cdd:PLN02578  166 ALSTAVGYPELVAGVALLNSAgQFGSESRekeEAIVVEETVLTRFVVKPLKEWFQRVV-LGFLFWQAKQP---------- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 175 lGRIDSSVLS--RNKSEVDLY--------NSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSK 244
Cdd:PLN02578  235 -SRIESVLKSvyKDKSNVDDYlvesitepAADPNAGEVYYRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPA 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172387 245 GAYLLMESsrSQDKTLKMYEgAYHVLHRELPEVTNSVLHEvnsWVS 290
Cdd:PLN02578  314 KAEKIKAF--YPDTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 43-290 7.45e-05

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 43.62  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  43 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 99
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 100 ILVaaerptyfsgmvlispLVLANPEsaSTLKDKLHItKTSLEKAAEVSVTWI----PYAF-HLWVLAAKLLNFVLPNMt 174
Cdd:TIGR01607 157 LRL----------------LELLGKS--NENNDKLNI-KGCISLSGMISIKSVgsddSFKFkYFYLPVMNFMSRVFPTF- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387 175 lgRIDSSV-LSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLME 251
Cdd:TIGR01607 217 --RISKKIrYEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYN 294

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907172387 252 SSRSQDKTLKMYEGAYHVLHRElpEVTNSVLHEVNSWVS 290
Cdd:TIGR01607 295 KLSISNKELHTLEDMDHVITIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 70-105 1.51e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.08  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907172387  70 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 105
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 69-105 4.67e-04

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


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 39.79  E-value: 4.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172387  69 RDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 105
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 15-131 6.80e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.15  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  15 LIFVsHGAGEHCGRYDELAhmlkGLDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPdvpIFLLGHSM 94
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALL----AAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907172387  95 GGAISILVAAerpTYFSGMVLISPLVLANPESASTLK 131
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLA 102
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
89-118 1.69e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 39.20  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907172387  89 LLGHSMGGAISILVAAERPTYFSGMVLISP 118
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 2-120 2.23e-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: 38.98  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387   2 LYRRAYSLILRRALIFVSHgAGEHCGRYDELahmlkgldmlvfahdHVGHGQSEGERMvvSDFQVFVRDVLqhVDTIQKD 81
Cdd:pfam00756  45 LDRLAASGEIPPVIIVGSP-RGGEVSFYSDW---------------DRGLNATEGPGA--YAYETFLTQEL--PPLLDAN 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907172387  82 YP--DVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLV 120
Cdd:pfam00756 105 FPtaPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 86-119 2.36e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 38.75  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907172387  86 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 119
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
12-107 3.39e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  12 RRALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA---HDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQKDyPDV 85
Cdd:COG0412    28 PRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDPELLAADLRAALDWLKAQ-PEV 106

                          90       100
                  ....*....|....*....|....*
gi 1907172387  86 ---PIFLLGHSMGGAISILVAAERP 107
Cdd:COG0412   107 dagRVGVVGFCFGGGLALLAAARGP 131
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 50-105 4.94e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.52  E-value: 4.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172387  50 GHGQSEGERMVvSDFQVFVRDVLQHVdtiqKDYPDVPIFLLGHSMGGAISILVAAE 105
Cdd:COG3208    42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
15-109 8.92e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 37.39  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172387  15 LIFVSHGAGEHCGRYDELAHML--KGldMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQHVDTIQKD 81
Cdd:COG4188    64 LVVLSHGLGGSREGYAYLAEHLasHG--YVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLLALNKS 141

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907172387  82 YPDVP-------IFLLGHSMGGAISILVAAERPTY 109
Cdd:COG4188   142 DPPLAgrldldrIGVIGHSLGGYTALALAGARLDF 176
 
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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