NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2168696672|ref|NP_001385526|]
View 

monoglyceride lipase isoform 1 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 38-312 7.01e-107

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: 312.98  E-value: 7.01e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 117
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 118 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 197
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 198 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 277
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2168696672 278 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 312
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 38-312 7.01e-107

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 312.98  E-value: 7.01e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 117
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 118 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 197
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 198 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 277
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2168696672 278 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 312
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 57-291 1.17e-91

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: 272.55  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  57 PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLG 136
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 137 HSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISL-GRIDSSVLSRNKSEVDLYNSDPL 215
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696672 216 iCHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKEL 291
Cdd:pfam12146 163 -VHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
37-306 9.16e-49

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.48  E-value: 9.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  37 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 116
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 117 LQHVNTVQKDyPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAkllnfvlpnislgrid 196
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 197 ssvlsrnksevdlynsdplichagvkvcfgiqllnavSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKT 276
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSP-DVE 191

                         250       260       270
                  ....*....|....*....|....*....|
gi 2168696672 277 LKMYEGAYHVLHKELPEvtNSVLHEINTWV 306
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 88-307 1.67e-06

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: 49.01  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  88 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDLLQHVNTVQK-------------DYPEV-------PVFLLGHSMGGAIS 144
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 145 ILA------AAERPTH--------FSGMILISPLILANPESASTLKVLAAKLLNFVLPNIslgRIDSSV-LSRNKSEVDL 209
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 210 YNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVL 287
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 2168696672 288 HKElpEVTNSVLHEINTWVS 307
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 131-164 1.50e-04

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: 42.60  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2168696672 131 PVFLLGHSMGGAISILAAAERPTHFSGMILISPL 164
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 38-312 7.01e-107

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 312.98  E-value: 7.01e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  38 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLL 117
Cdd:PHA02857    5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 118 QHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlaNPESASTLKVLAAKLLNFVLPNISLGRIDS 197
Cdd:PHA02857   85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 198 SVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKTL 277
Cdd:PHA02857  163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREI 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2168696672 278 KMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAV 312
Cdd:PHA02857  242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRVKV 276
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 57-291 1.17e-91

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: 272.55  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  57 PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLG 136
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 137 HSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISL-GRIDSSVLSRNKSEVDLYNSDPL 215
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696672 216 iCHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKEL 291
Cdd:pfam12146 163 -VHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
37-306 9.16e-49

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 162.48  E-value: 9.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  37 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 116
Cdd:COG2267     7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 117 LQHVNTVQKDyPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAkllnfvlpnislgrid 196
Cdd:COG2267    87 RAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA---------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 197 ssvlsrnksevdlynsdplichagvkvcfgiqllnavSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqDKT 276
Cdd:COG2267   150 -------------------------------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSP-DVE 191

                         250       260       270
                  ....*....|....*....|....*....|
gi 2168696672 277 LKMYEGAYHVLHKELPEvtNSVLHEINTWV 306
Cdd:COG2267   192 LVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 39-309 3.26e-34

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 127.95  E-value: 3.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  39 VNADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDE-LAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDL 116
Cdd:PLN02385   67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 117 LQHVNTVqKDYPEV---PVFLLGHSMGGAISILAAAERPTHFSGMILISPLI-----LANPESASTLKVLAAKLL--NFV 186
Cdd:PLN02385  147 IEHYSKI-KGNPEFrglPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLLpkAKL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 187 LPNISLGriDSSVLSRNKSEVDLYNsdpLICHAG-VKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYL 265
Cdd:PLN02385  226 VPQKDLA--ELAFRDLKKRKMAEYN---VIAYKDkPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKF 300

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2168696672 266 LMESSPSQDKTLKMYEGAYH-VLHKELPEVTNSVLHEINTWVSHR 309
Cdd:PLN02385  301 LYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 43-311 3.92e-33

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 124.50  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  43 GQYLFCRYWKPSGT--PKALIFVSHGAGEHCG-RYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQH 119
Cdd:PLN02298   42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 120 VNTVQKD--YPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLI-----LANPESASTLKVLAAKLLNF--VLPNI 190
Cdd:PLN02298  122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkisdkIRPPWPIPQILTFVARFLPTlaIVPTA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 191 SLgrIDSSVLSRNKSEVDLYNsdPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESS 270
Cdd:PLN02298  202 DL--LEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEA 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2168696672 271 PSQDKTLKMYEGAYH-VLHKELPEVTNSVLHEINTWVSHRIA 311
Cdd:PLN02298  278 KSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCT 319
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 41-311 2.26e-32

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 123.85  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  41 ADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQH 119
Cdd:PLN02652  118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 120 VNTVQKDYPEVPVFLLGHSMGGAIsILAAAERPT---HFSGMILISPLILANPesASTLKVLAAKLLNFVLPNISLGRID 196
Cdd:PLN02652  198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGAN 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 197 SS--VLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQD 274
Cdd:PLN02652  275 KRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRH 354

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2168696672 275 KTLKMYEGAYHVLHKElPEvTNSVLHEINTWVSHRIA 311
Cdd:PLN02652  355 KDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
55-300 1.95e-24

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 99.25  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  55 GTPKALIFVsHGAGehCGRYD--ELAQMLKRLDMLVFAHDHVGHGQSEGErMVVSDFQVFVRDLLQHVNTVQKDYPEVpv 132
Cdd:COG1647    13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYDKV-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 133 FLLGHSMGGAISILAAAERPtHFSGMILISPLILANPESAstlkvLAAKLLNFVLPNISLGRIDssvLSRNKSEVDLYNS 212
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 213 DPLIChagvkvcfGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLH--KE 290
Cdd:COG1647   158 TPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKD 229

                         250
                  ....*....|
gi 2168696672 291 LPEVTNSVLH 300
Cdd:COG1647   230 REEVAEEILD 239
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 36-301 2.05e-20

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: 87.75  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  36 PHLVNADGQYLFCRYWKPSGTPkaLIFVsHGAGEHCGRYDELAQMLKRlDMLVFAHDHVGHGQSEGERMVVSdFQVFVRD 115
Cdd:COG0596     4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYT-LDDLADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 116 LLQHVNTVQKDypevPVFLLGHSMGGAISILAAAERPTHFSGMILISPLIlanpesastlKVLAAKLLNFVLPNISLGRi 195
Cdd:COG0596    79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL----------AALAEPLRRPGLAPEALAA- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 196 dssvlsrnksevdlynsdplichagvkvcfgiqLLNAVSR--VERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPsq 273
Cdd:COG0596   144 ---------------------------------LLRALARtdLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP-- 188

                         250       260
                  ....*....|....*....|....*...
gi 2168696672 274 DKTLKMYEGAYHVLHKELPEVTNSVLHE 301
Cdd:COG0596   189 NAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 29-286 1.48e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 83.43  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  29 NVPYQDLpHLVNADGQYLFCRYWKPSGTPKAL--IFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGE-RMV 105
Cdd:COG1073     7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpREE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 106 VS----DFQVFVRDLLQhvntvQKDYPEVPVFLLGHSMGGAISILAAAERPtHFSGMILISPLILANPESASTLKVLAAK 181
Cdd:COG1073    86 GSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 182 LLNFV--LPNISLGridssvlsrnksevdlynsdplichagvkvcfgiQLLNAVSRVERAMPRLTLPFLLLQGSADRLCD 259
Cdd:COG1073   160 YLPGVpyLPNVRLA----------------------------------SLLNDEFDPLAKIEKISRPLLFIHGEKDEAVP 205

                         250       260
                  ....*....|....*....|....*..
gi 2168696672 260 SKGAYLLMESSPsQDKTLKMYEGAYHV 286
Cdd:COG1073   206 FYMSEDLYEAAA-EPKELLIVPGAGHV 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
40-310 1.37e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 74.67  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  40 NADGQYLFCRYWKPSGTPKA-LIFVSHGAGEH-CGRYDELAQMLKRLDMLVFAHDHVGHGQSEGE--RMVVSDFQVFVRD 115
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDwgGDEVDDVLAAIDY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 116 LLQhvntvQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLilanpesastlkvlaakllnfvlpnISLGRI 195
Cdd:COG1506    84 LAA-----RPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGV-------------------------SDLRSY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 196 DSSVLSRNKSEVDLYNSDPlichagvkvcfgiQLLNAVSRVERAmPRLTLPFLLLQGSADRLCDSKGAYLLME--SSPSQ 273
Cdd:COG1506   134 YGTTREYTERLMGGPWEDP-------------EAYAARSPLAYA-DKLKTPLLLIHGEADDRVPPEQAERLYEalKKAGK 199

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2168696672 274 DKTLKMYEGAYHVLHKelpEVTNSVLHEINTWVSHRI 310
Cdd:COG1506   200 PVELLVYPGEGHGFSG---AGAPDYLERILDFLDRHL 233
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 58-290 8.30e-12

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: 64.06  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  58 KALIFVsHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGeRMVVSDFQVFvrDLLQHVNTVQKDYPEVPVFLLGH 137
Cdd:pfam00561   1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 138 SMGGAISILAAAERPTHFSGMILISPlILANPESASTLKVLAAKLLNFV------LPNISLGRI-----------DSSVL 200
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFdgfvadFAPNPLGRLvakllallllrLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 201 SRNKSEVDLYNSDPLIchAGVKVCFGIQLLNAVSRVERA--MPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSqdKTLK 278
Cdd:pfam00561 156 ALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--ARLV 231

                         250
                  ....*....|..
gi 2168696672 279 MYEGAYHVLHKE 290
Cdd:pfam00561 232 VIPDAGHFAFLE 243
YpfH COG0400
Predicted esterase [General function prediction only];
54-179 1.98e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 50.68  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  54 SGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDLLQHVNTV 123
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696672 124 QKDY--PEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLA 179
Cdd:COG0400    81 EARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 60-288 7.27e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 49.01  E-value: 7.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  60 LIFVsHGAGEHcgrYDELAQMLKRlDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDLLQHVNTVQKDYPevpVFLLGHSM 139
Cdd:pfam12697   1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 140 GGAISILAAAERPTHfsgMILISPLILANPESASTLKVLAAKLLNFVLPNISLGRIDSSVLSRNKSEVDLYNsdplicha 219
Cdd:pfam12697  69 GGAVALAAAAAALVV---GVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWA-------- 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696672 220 gVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMEsspSQDKTLKMYEGAYHVLH 288
Cdd:pfam12697 138 -AALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAA---LAGARLVVLPGAGHLPL 202
PLN02578 PLN02578
hydrolase
 55-307 7.91e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 49.84  E-value: 7.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  55 GTPKALIfvsHGAGE---HCgRYD--ELAQMLKrldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDLLQHVNTVQKDype 129
Cdd:PLN02578   86 GLPIVLI---HGFGAsafHW-RYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE--- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 130 vPVFLLGHSMGGAISILAAAERPTHFSGMILI----------SPLILANPESASTLKVLAAKLLNFVLPNISLG------ 193
Cdd:PLN02578  153 -PAVLVGNSLGGFTALSTAVGYPELVAGVALLnsagqfgsesREKEEAIVVEETVLTRFVVKPLKEWFQRVVLGflfwqa 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 194 ----RIDSSVLS--RNKSEVDLY--------NSDPlicHAGvKVCFGIQ---LLNAvSR--VERAMPRLTLPFLLLQGSA 254
Cdd:PLN02578  232 kqpsRIESVLKSvyKDKSNVDDYlvesitepAADP---NAG-EVYYRLMsrfLFNQ-SRytLDSLLSKLSCPLLLLWGDL 306

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2168696672 255 DRLCDSKGAYLLMESSPsqDKTLKMYEgAYHVLHKELPEVTNSVLHEintWVS 307
Cdd:PLN02578  307 DPWVGPAKAEKIKAFYP--DTTLVNLQ-AGHCPHDEVPEQVNKALLE---WLS 353
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 88-307 1.67e-06

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: 49.01  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  88 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDLLQHVNTVQK-------------DYPEV-------PVFLLGHSMGGAIS 144
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 145 ILA------AAERPTH--------FSGMILISPLILANPESASTLKVLAAKLLNFVLPNIslgRIDSSV-LSRNKSEVDL 209
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTF---RISKKIrYEKSPYVNDI 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 210 YNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRL--TLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVL 287
Cdd:TIGR01607 234 IKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313

                         250       260
                  ....*....|....*....|
gi 2168696672 288 HKElpEVTNSVLHEINTWVS 307
Cdd:TIGR01607 314 TIE--PGNEEVLKKIIEWIS 331
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
37-152 9.57e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 46.11  E-value: 9.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  37 HLVNADGQYLFCRYWKPSGT-PKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFA---HDHVGHGQSEGE---RMVVSDF 109
Cdd:COG0412     7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2168696672 110 QVFVRDLLQHVNTVQKDyPEV---PVFLLGHSMGGAISILAAAERP 152
Cdd:COG0412    87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
PRK10749 PRK10749
lysophospholipase L2; Provisional
 73-164 1.57e-05

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 45.76  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  73 RYDELAQMLKRLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDL----LQHVNTvqkdYPEVPVFLLGHSMGGAI 143
Cdd:PRK10749   69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQP----GPYRKRYALAHSMGGAI 144

                          90       100
                  ....*....|....*....|.
gi 2168696672 144 SILAAAERPTHFSGMILISPL 164
Cdd:PRK10749  145 LTLFLQRHPGVFDAIALCAPM 165
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 49-163 8.14e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 43.78  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  49 RYWK-PSGTPKALIFVsHG-AGEH---CGRYDELAqmlkrLDMLVFAHDHVGHGQSeGERMVVSDFQVFVRDLLQHVNTV 123
Cdd:PRK14875  122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAL 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2168696672 124 QKDypevPVFLLGHSMGGAISILAAAERPTHFSGMILISP 163
Cdd:PRK14875  195 GIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 131-164 1.50e-04

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: 42.60  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2168696672 131 PVFLLGHSMGGAISILAAAERPTHFSGMILISPL 164
Cdd:cd12809   172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
134-163 1.55e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 42.67  E-value: 1.55e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2168696672 134 LLGHSMGGAISILAAAERPTHFSGMILISP 163
Cdd:COG2819   134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 115-150 3.94e-04

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 40.92  E-value: 3.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2168696672 115 DLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAE 150
Cdd:cd00519   113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
COG4099 COG4099
Predicted peptidase [General function prediction only];
60-176 5.95e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 40.72  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  60 LIFVSHGAGEhcgRYDELAQML-------------KRLDMLVFAhdhvghGQ-SEGERMVVSDFQVFVRDLLQHVntvQK 125
Cdd:COG4099    51 LVLFLHGAGE---RGTDNEKQLthgapkfinpenqAKFPAIVLA------PQcPEDDYWSDTKALDAVLALLDDL---IA 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2168696672 126 DYPEVP--VFLLGHSMGGAISILAAAERPTHFSGMILISPliLANPESASTLK 176
Cdd:COG4099   119 EYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 114-150 1.01e-03

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


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 39.02  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2168696672 114 RDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAE 150
Cdd:cd00741    12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 53-163 1.15e-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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  53 PSGTPKALIFVsHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSegermvvsdFQVFVRDLLQHVNTVQKDYPEVPV 132
Cdd:COG1075     1 YAATRYPVVLV-HGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS---------IEDSAEQLAAFVDAVLAATGAEKV 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2168696672 133 FLLGHSMGGAIS--ILAAAERPTHFSGMILISP 163
Cdd:COG1075    71 DLVGHSMGGLVAryYLKRLGGAAKVARVVTLGT 103
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 93-172 1.17e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 39.75  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  93 HVGHGQSEGERMvvSDFQVFVRD-LLQhvnTVQKDYPEVPVF--LLGHSMGGAISILAAAERPTHFSGMILISPliLANP 169
Cdd:pfam00756  75 DRGLNATEGPGA--YAYETFLTQeLPP---LLDANFPTAPDGraLAGQSMGGLGALYLALKYPDLFGSVSSFSP--ILNP 147


                  ...
gi 2168696672 170 ESA 172
Cdd:pfam00756 148 SNS 150
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
53-285 3.04e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 38.93  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  53 PSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDLLQHVN 121
Cdd:COG4188    57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQLL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 122 TVQKDYPEVP-------VFLLGHSMGGAISILAAAERPthfsgmilisplilanpeSASTLKVLAAKLLNFVLPNISLGR 194
Cdd:COG4188   137 ALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672 195 IDSSVlsrnksevdlynSDPLIcHAGVkvcfgiqLLNAVSR---VERAMPRLTLPFLLLQGSADRlcDSKGAY---LLME 268
Cdd:COG4188   199 LAYDL------------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFD 256

                         250
                  ....*....|....*..
gi 2168696672 269 SSPSQDKTLKMYEGAYH 285
Cdd:COG4188   257 LLPGADKYLLTLEGATH 273
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
20-154 5.45e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 38.20  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696672  20 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPSGTPKALIFVSHG-AGEHCGRY-DELAQMLKRLDMLVFAHDH 93
Cdd:COG0429    25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696672  94 VGHGqseGE--RMVVS----DFQvfvrDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTH 154
Cdd:COG0429    99 RGCG---GEpnLLPRLyhsgDTE----DLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDD 158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH