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Conserved domains on  [gi|1907172389|ref|XP_036021996|]
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monoglyceride lipase isoform X4 [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, ...
 10-290 5.45e-88

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: 264.06  E-value: 5.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 169
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 249
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172389 250 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 290
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 10-290 5.45e-88

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 264.06  E-value: 5.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 169
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 249
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172389 250 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 290
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 10-271 5.83e-82

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: 247.13  E-value: 5.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 169
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPIL----------------------------KLLAKLLGKLFPR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 MTL-GRIDSSVLSRNKSEVDLYNSDPLVCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 248
Cdd:pfam12146 136 LRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYE 214

                         250       260
                  ....*....|....*....|...
gi 1907172389 249 SSRSQDKTLKMYEGAYHVLHREL 271
Cdd:pfam12146 215 RAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
10-286 5.25e-36

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 128.58  E-value: 5.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDyPDVPIFLLGH 89
Cdd:COG2267    28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlWVLAakllnfvlpn 169
Cdd:COG2267   107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR---------------------------WLRA---------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 mtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEs 249
Cdd:COG2267   150 --------------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA- 184

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907172389 250 SRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 286
Cdd:COG2267   185 RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 40-287 5.63e-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: 44.00  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  40 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 96
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  97 ILVaaerptyfsgmvlispLVLANPEsaSTLKDKLHItKTSLEKAAEVSVTWI----PYAF-HLWVLAAKLLNFVLPNMt 171
Cdd:TIGR01607 157 LRL----------------LELLGKS--NENNDKLNI-KGCISLSGMISIKSVgsddSFKFkYFYLPVMNFMSRVFPTF- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 172 lgRIDSSV-LSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLME 248
Cdd:TIGR01607 217 --RISKKIrYEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYN 294

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907172389 249 SSRSQDKTLKMYEGAYHVLHRElpEVTNSVLHEVNSWVS 287
Cdd:TIGR01607 295 KLSISNKELHTLEDMDHVITIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 67-102 1.27e-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: 42.46  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907172389  67 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 102
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 10-290 5.45e-88

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 264.06  E-value: 5.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:PHA02857   25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 169
Cdd:PHA02857  105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLN----------------------------LLAAKLMGIFYPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 MTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMES 249
Cdd:PHA02857  155 KIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQH 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907172389 250 SRSqDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 290
Cdd:PHA02857  235 ANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 10-271 5.83e-82

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: 247.13  E-value: 5.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlwVLAAKLLNFVLPN 169
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPIL----------------------------KLLAKLLGKLFPR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 MTL-GRIDSSVLSRNKSEVDLYNSDPLVCRaGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLME 248
Cdd:pfam12146 136 LRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYE 214

                         250       260
                  ....*....|....*....|...
gi 1907172389 249 SSRSQDKTLKMYEGAYHVLHREL 271
Cdd:pfam12146 215 RAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
10-286 5.25e-36

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 128.58  E-value: 5.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDyPDVPIFLLGH 89
Cdd:COG2267    28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKdklhitktslekaaevsvtwipyafhlWVLAakllnfvlpn 169
Cdd:COG2267   107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSAR---------------------------WLRA---------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 170 mtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEs 249
Cdd:COG2267   150 --------------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAA- 184

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907172389 250 SRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 286
Cdd:COG2267   185 RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 10-289 1.46e-27

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 109.46  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDE-LAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQ--KDYPDVPIFL 86
Cdd:PLN02385   87 KAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVIEHYSKIKgnPEFRGLPSFL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  87 LGHSMGGAISILVAAERPTYFSGMVLISPLVlanpesastlkdklhitktsleKAAEvSVTWIPYAFHLWVLAAKLL--N 164
Cdd:PLN02385  167 FGQSMGGAVALKVHLKQPNAWDGAILVAPMC----------------------KIAD-DVVPPPLVLQILILLANLLpkA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 165 FVLPNMTLGriDSSVLSRNKSEVDLYNSDPLVCRAGLKVcfGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAY 244
Cdd:PLN02385  224 KLVPQKDLA--ELAFRDLKKRKMAEYNVIAYKDKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSK 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172389 245 LLMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHR 289
Cdd:PLN02385  300 FLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 10-296 3.51e-27

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 107.94  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCG-RYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKD--YPDVPIFL 86
Cdd:PLN02298   59 RALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeFQGLPRFL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  87 LGHSMGGAISILVAAERPTYFSGMVLISPLVlanpesasTLKDKlhitktslekaaeVSVTW-IPYAFHLWVLAAKLLNF 165
Cdd:PLN02298  139 YGESMGGAICLLIHLANPEGFDGAVLVAPMC--------KISDK-------------IRPPWpIPQILTFVARFLPTLAI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 166 VlPNMTLgrIDSSVLSRNKSEVDLYNsdPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYL 245
Cdd:PLN02298  198 V-PTADL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRA 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907172389 246 LMESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHRIAAAGAG 296
Cdd:PLN02298  273 LYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 10-291 6.21e-24

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 100.35  E-value: 6.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGH 89
Cdd:PLN02652  136 RGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFGH 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  90 SMGGAIsILVAAERPTY---FSGMVLISPLVLANPEsastlkdklhitktslekaaevsvtwipyafHLWVLA-AKLLNF 165
Cdd:PLN02652  216 STGGAV-VLKAASYPSIedkLEGIVLTSPALRVKPA-------------------------------HPIVGAvAPIFSL 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 166 VLPNMTLGRIDSS--VLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGA 243
Cdd:PLN02652  264 VAPRFQFKGANKRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLAS 343

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907172389 244 YLLMESSRSQDKTLKMYEGAYHVLHRElPEvTNSVLHEVNSWVSHRIA 291
Cdd:PLN02652  344 QDLYNEAASRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
47-280 4.19e-18

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 81.53  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  47 GHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPdvPIFLLGHSMGGAISILVAAERPTyFSGMVLISPLVLANPESAST 126
Cdd:COG1647    52 GHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 127 LKDKLHITKTsleKAAEVSVTWIPYAFHLWvlaakllnfvlpnmtlgridssvlsrnksevdlYNSDPLVCraglkvcfG 206
Cdd:COG1647   128 LPLLKYLARS---LRGIGSDIEDPEVAEYA---------------------------------YDRTPLRA--------L 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172389 207 IQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--RELPEVTNSVLH 280
Cdd:COG1647   164 AELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEILD 239
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 10-266 2.11e-13

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 68.40  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQvfVRDVLQHVDTIQKdYPDVP---IFL 86
Cdd:COG1073    37 YPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RRDARAAVDYLRT-LPGVDperIGL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  87 LGHSMGGAISILVAAERPtYFSGMVLISPLVLANPESASTLKDklhitktslekAAEVSVTWIPYafhlwvlaakllnfv 166
Cdd:COG1073   114 LGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKE-----------ARGAYLPGVPY--------------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 167 LPNMTLGridssvlsrnksevdlynsdplvcraglkvcfgiQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLL 246
Cdd:COG1073   167 LPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDL 212

                         250       260
                  ....*....|....*....|
gi 1907172389 247 MESSrSQDKTLKMYEGAYHV 266
Cdd:COG1073   213 YEAA-AEPKELLIVPGAGHV 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-281 1.26e-12

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: 65.79  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389   4 EWACFGRALIFVsHGAGEHCGRYDELAHML-KGLDmlVFAHDHVGHGQSEGERMVVSdFQVFVRDVLQHVDTIQKDypdv 82
Cdd:COG0596    18 EAGPDGPPVVLL-HGLPGSSYEWRPLIPALaAGYR--VIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGLE---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  83 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlanpesaSTLKDKLHITKTSLEkaaevsvtwipyAFHLWVLAAKL 162
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL-------AALAEPLRRPGLAPE------------ALAALLRALAR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 163 LNFvlpnmtlgridssvlsrnksevdlynsdplvcraglkvcfgiqllnavarvERAMPRLTLPFLLLQGSADRLCDSKG 242
Cdd:COG0596   151 TDL---------------------------------------------------RERLARITVPTLVIWGEKDPIVPPAL 179

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907172389 243 AYLLMEssRSQDKTLKMYEGAYHVLHRELPEVTNSVLHE 281
Cdd:COG0596   180 ARRLAE--LLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 40-268 1.97e-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: 59.83  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  40 VFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVla 119
Cdd:pfam00561  30 VIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALD-- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 120 npesastlkdklhiTKTSLEKAAEVSVTWIPYAFHLWVLAAKLLNF-VLPNMTLGRI---DSSVLSRNKSEVDLYNSDPL 195
Cdd:pfam00561 105 --------------PPHELDEADRFILALFPGFFDGFVADFAPNPLgRLVAKLLALLllrLRLLKALPLLNKRFPSGDYA 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172389 196 vcRAGLKVCFGIQLLNAVARVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLmeSSRSQDKTLKMYEGAYHVLH 268
Cdd:pfam00561 171 --LAKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIPDAGHFAF 241
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-115 5.01e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.41  E-value: 5.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  12 LIFVSHGAGEH-CGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSdfqvfVRDVLQHVDTIQKDyPDVP---IFLL 87
Cdd:COG1506    25 VVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVLAAIDYLAAR-PYVDpdrIGIY 98

                          90       100
                  ....*....|....*....|....*...
gi 1907172389  88 GHSMGGAISILVAAERPTYFSGMVLISP 115
Cdd:COG1506    99 GHSYGGYMALLAAARHPDRFKAAVALAG 126
YpfH COG0400
Predicted esterase [General function prediction only];
9-122 4.57e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 46.44  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389   9 GRALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTIQKD 78
Cdd:COG0400     4 AAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDELEAR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172389  79 Y--PDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPE 122
Cdd:COG0400    84 YgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
PRK10749 PRK10749
lysophospholipase L2; Provisional
 25-116 7.57e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.53  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  25 RYDELAHMLKGLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILV 99
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                          90
                  ....*....|....*..
gi 1907172389 100 AAERPTYFSGMVLISPL 116
Cdd:PRK10749  149 LQRHPGVFDAIALCAPM 165
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 40-115 7.58e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.86  E-value: 7.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172389  40 VFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT--IQKDYpdvpifLLGHSMGGAISILVAAERPTYFSGMVLISP 115
Cdd:PRK14875  160 VIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAlgIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
COG4099 COG4099
Predicted peptidase [General function prediction only];
12-129 1.02e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  12 LIFVSHGAGEhcgRYDELAHMLK-GLDMLVfahdhvghgqSEGERmvvSDFQVFV-----------------RDVLQHVD 73
Cdd:COG4099    51 LVLFLHGAGE---RGTDNEKQLThGAPKFI----------NPENQ---AKFPAIVlapqcpeddywsdtkalDAVLALLD 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172389  74 TIQKDYP-DvP--IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLKD 129
Cdd:COG4099   115 DLIAEYRiD-PdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLKK 170
PLN02578 PLN02578
hydrolase
 18-287 1.05e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 46.37  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  18 GAGEHCGRYD--ELAHMLKgldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypdvPIFLLGHSMGGAI 95
Cdd:PLN02578   96 GASAFHWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE----PAVLVGNSLGGFT 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  96 SILVAAERPTYFSGMVLISPL-VLANPES---ASTLKDKLHITKTSLEKAAEVSVTWIpYAFHLWVLAAKllnfvlpnmt 171
Cdd:PLN02578  166 ALSTAVGYPELVAGVALLNSAgQFGSESRekeEAIVVEETVLTRFVVKPLKEWFQRVV-LGFLFWQAKQP---------- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 172 lGRIDSSVLS--RNKSEVDLY--------NSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSK 241
Cdd:PLN02578  235 -SRIESVLKSvyKDKSNVDDYlvesitepAADPNAGEVYYRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPA 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907172389 242 GAYLLMESsrSQDKTLKMYEgAYHVLHRELPEVTNSVLHEvnsWVS 287
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 ...
 40-287 5.63e-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: 44.00  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  40 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 96
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  97 ILVaaerptyfsgmvlispLVLANPEsaSTLKDKLHItKTSLEKAAEVSVTWI----PYAF-HLWVLAAKLLNFVLPNMt 171
Cdd:TIGR01607 157 LRL----------------LELLGKS--NENNDKLNI-KGCISLSGMISIKSVgsddSFKFkYFYLPVMNFMSRVFPTF- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389 172 lgRIDSSV-LSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLME 248
Cdd:TIGR01607 217 --RISKKIrYEKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYN 294

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907172389 249 SSRSQDKTLKMYEGAYHVLHRElpEVTNSVLHEVNSWVS 287
Cdd:TIGR01607 295 KLSISNKELHTLEDMDHVITIE--PGNEEVLKKIIEWIS 331
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 67-102 1.27e-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: 42.46  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907172389  67 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 102
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 12-128 3.74e-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: 40.92  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  12 LIFVsHGAGEHCGRYDELAhmlkGLDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPdvpIFLLGHSM 91
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALL----AAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907172389  92 GGAISILVAAerpTYFSGMVLISPLVLANPESASTLK 128
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLA 102
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 66-102 3.85e-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: 40.18  E-value: 3.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907172389  66 RDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 102
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
86-115 1.34e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 39.58  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907172389  86 LLGHSMGGAISILVAAERPTYFSGMVLISP 115
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 83-116 2.43e-03

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


Pssm-ID: 214008  Cd Length: 280  Bit Score: 38.75  E-value: 2.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907172389  83 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 116
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 47-102 3.91e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 3.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172389  47 GHGQSEGERMVvSDFQVFVRDVLQHVdtiqKDYPDVPIFLLGHSMGGAISILVAAE 102
Cdd:COG3208    42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
10-104 5.12e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 37.64  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  10 RALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA---HDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQKDyPDV- 82
Cdd:COG0412    29 RPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDPELLAADLRAALDWLKAQ-PEVd 107

                          90       100
                  ....*....|....*....|....
gi 1907172389  83 --PIFLLGHSMGGAISILVAAERP 104
Cdd:COG0412   108 agRVGVVGFCFGGGLALLAAARGP 131
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
12-106 6.71e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 37.78  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172389  12 LIFVSHGAGEHCGRYDELAHML--KGldMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQHVDTIQKD 78
Cdd:COG4188    64 LVVLSHGLGGSREGYAYLAEHLasHG--YVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLLALNKS 141

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907172389  79 YPDVP-------IFLLGHSMGGAISILVAAERPTY 106
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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