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Conserved domains on  [gi|261878509|ref|NP_001159721|]
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monoglyceride lipase isoform c [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, ...
 22-249 1.14e-82

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: 248.65  E-value: 1.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857 163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878509 217 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 249
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-249 1.14e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 248.65  E-value: 1.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857 163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878509 217 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 249
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-230 4.60e-65

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: 202.44  E-value: 4.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   41 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  121 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSE--------- 190
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVvaayaadpl 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261878509  191 -----------------------------------GSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 230
Cdd:pfam12146 163 vhggisartlyelldagerllrraaaitvpllllhGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-245 4.24e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 155.93  E-value: 4.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 98
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  99 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfVLPNMTLGR 178
Cdd:COG2267   85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-----LRLAEALAR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878509 179 IDSSVL--SrnkseGSADRLCDSKGAYLLMEsSRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 245
Cdd:COG2267  159 IDVPVLvlH-----GGADRVVPPEAARRLAA-RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 9.63e-05

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.46  E-value: 9.63e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 261878509  99 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00519  113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-129 2.53e-03

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 38.61  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156


                  .
gi 261878509  129 I 129
Cdd:TIGR01607 157 L 157
 
Name Accession Description Interval E-value
PHA02857 PHA02857
monoglyceride lipase; Provisional
 22-249 1.14e-82

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 248.65  E-value: 1.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  22 LVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVL 101
Cdd:PHA02857   5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 102 QHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVlaNPESASTLKVLAAKLLNFVLPNMTLGRIDS 181
Cdd:PHA02857  85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 182 SVLSRNKSE---------------------------------------------GSADRLCDSKGAYLLMESSRSqDKTL 216
Cdd:PHA02857 163 ESVSRDMDEvykyqydplvnhekikagfasqvlkatnkvrkiipkiktpililqGTNNEISDVSGAYYFMQHANC-NREI 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 261878509 217 KMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRI 249
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-230 4.60e-65

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: 202.44  E-value: 4.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   41 PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLG 120
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  121 HSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTL-GRIDSSVLSRNKSE--------- 190
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVvaayaadpl 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261878509  191 -----------------------------------GSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHREL 230
Cdd:pfam12146 163 vhggisartlyelldagerllrraaaitvpllllhGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-245 4.24e-47

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 155.93  E-value: 4.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  21 HLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHML--KGLDmlVFAHDHVGHGQSEGERMVVSDFQVFVR 98
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaaAGYA--VLAFDLRGHGRSDGPRGHVDSFDDYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  99 DVLQHVDTIQKDyPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAkllnfVLPNMTLGR 178
Cdd:COG2267   85 DLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA-----LRLAEALAR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878509 179 IDSSVL--SrnkseGSADRLCDSKGAYLLMEsSRSQDKTLKMYEGAYHVLHRELPEvtNSVLHEVNSWV 245
Cdd:COG2267  159 IDVPVLvlH-----GGADRVVPPEAARRLAA-RLSPDVELVLLPGARHELLNEPAR--EEVLAAILAWL 219
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 27-255 3.06e-25

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 101.78  E-value: 3.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  27 GQYLFCRYWKPSGT--PKALIFVSHGAGEHCG-RYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02298  42 GLSLFTRSWLPSSSspPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 104 VDTIQKD--YPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPL-------------------------VLANPESA 156
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMckisdkirppwpipqiltfvarflpTLAIVPTA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 157 STL----KVLAAKLLNFVLPN-----------MTLGRIDSSvLSRNKSE---------GSADRLCDSKGAYLLMESSRSQ 212
Cdd:PLN02298 202 DLLeksvKVPAKKIIAKRNPMryngkprlgtvVELLRVTDY-LGKKLKDvsipfivlhGSADVVTDPDVSRALYEEAKSE 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 261878509 213 DKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHRIAAAGAG 255
Cdd:PLN02298 281 DKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATP 324
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 23-248 3.20e-25

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 102.14  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  23 VNADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDE-LAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDV 100
Cdd:PLN02385  67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 101 LQHVDTIQ--KDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPL------VLANPESASTLKVLA-----AKLl 167
Cdd:PLN02385 147 IEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMckiaddVVPPPLVLQILILLAnllpkAKL- 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 168 nfvLPNMTLG------------------------RIDSSV-LSRNKSE----------------GSADRLCDSKGAYLLM 206
Cdd:PLN02385 226 ---VPQKDLAelafrdlkkrkmaeynviaykdkpRLRTAVeLLRTTQEiemqleevslpllilhGEADKVTDPSVSKFLY 302

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 261878509 207 ESSRSQDKTLKMYEGAYH-VLHRELPEVTNSVLHEVNSWVSHR 248
Cdd:PLN02385 303 EKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 25-250 8.91e-21

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 90.34  E-value: 8.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  25 ADGQYLFCRYWKP-SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQH 103
Cdd:PLN02652 118 ARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 104 VDTIQKDYPDVPIFLLGHSMGGAIsILVAAERPTY---FSGMVLISPLVLANPES------ASTLKVLAAK--------- 165
Cdd:PLN02652 198 LEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSIedkLEGIVLTSPALRVKPAHpivgavAPIFSLVAPRfqfkgankr 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 166 -----------LLNFVLPNMTLGRID----------SSVLSRN-KS--------EGSADRLCDSKGAYLLMESSRSQDKT 215
Cdd:PLN02652 277 gipvsrdpaalLAKYSDPLVYTGPIRvrtgheilriSSYLTRNfKSvtvpfmvlHGTADRVTDPLASQDLYNEAASRHKD 356

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 261878509 216 LKMYEGAYHVLHRElPEvTNSVLHEVNSWVSHRIA 250
Cdd:PLN02652 357 IKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRLD 389
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-240 1.62e-18

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: 81.20  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  20 PHLVNADGQYLFCRYWKPSGTPkaLIFVsHGAGEHCGRYDELAHML-KGLDmlVFAHDHVGHGQSEGERMVVSdFQVFVR 98
Cdd:COG0596    4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALaAGYR--VIAPDLRGHGRSDKPAGGYT-LDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  99 DVLQHVDTIQKDypdvPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPES----ASTLKVLAAKLLNFVLPNM 174
Cdd:COG0596   78 DLAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPlrrpGLAPEALAALLRALARTDL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 175 T--LGRID--SSVLSrnkseGSADRLCDSKGAYLLMEssRSQDKTLKMYEGAYHVLHRELPEVTNSVLHE 240
Cdd:COG0596  154 RerLARITvpTLVIW-----GEKDPIVPPALARRLAE--LLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 13-225 8.94e-16

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 74.57  E-value: 8.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  13 NVPYQDLpHLVNADGQYLFCRYWKPSGTPKAL--IFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVV 90
Cdd:COG1073    7 KVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  91 SDFQvfVRDVLQHVDTIQKdYPDVP---IFLLGHSMGGAISILVAAERPtYFSGMVLISPLVLANPESASTLKVLAAKLL 167
Cdd:COG1073   86 GSPE--RRDARAAVDYLRT-LPGVDperIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261878509 168 NFV--LPNMTLGR-IDSSVLSRNKSE----------GSADRLCDSKGAYLLMESSrSQDKTLKMYEGAYHV 225
Cdd:COG1073  162 PGVpyLPNVRLASlLNDEFDPLAKIEkisrpllfihGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
39-239 5.87e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.20  E-value: 5.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  39 GTPKALIFVsHGAGehCGRYD--ELAHMLKGLDMLVFAHDHVGHGQSEGErMVVSDFQVFVRDVLQHVDTIQKDYPdvPI 116
Cdd:COG1647   13 GGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 117 FLLGHSMGGAISILVAAERPTyFSGMVLISPLVLANPESASTLKVLA--------------------------------- 163
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKylarslrgigsdiedpevaeyaydrtplralae 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 164 -AKLLNFVLPNmtLGRIDSSVL---SRNksegsaDRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLH--RELPEVTNSV 237
Cdd:COG1647  166 lQRLIREVRRD--LPKITAPTLiiqSRK------DEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237


                 ..
gi 261878509 238 LH 239
Cdd:COG1647  238 LD 239
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
24-249 9.70e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 68.50  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  24 NADGQYLFCRYWKPSGTPKA-LIFVSHGAGEH-CGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSdfqvfVRDVL 101
Cdd:COG1506    4 SADGTTLPGWLYLPADGKKYpVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 102 QHVDTIQKDyPDVP---IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLKVLAAKLLNFVLPNMTLGR 178
Cdd:COG1506   79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWEDPEAY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509 179 IDSSVLSRNKS--------EGSADRLCDSKGAYLLME--SSRSQDKTLKMYEGAYHVLHRelpEVTNSVLHEVNSWVSHR 248
Cdd:COG1506  156 AARSPLAYADKlktpllliHGEADDRVPPEQAERLYEalKKAGKPVELLVYPGEGHGFSG---AGAPDYLERILDFLDRH 232


                 .
gi 261878509 249 I 249
Cdd:COG1506  233 L 233
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-148 4.09e-09

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: 55.59  E-value: 4.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261878509   72 VFAHDHVGHGQSEGeRMVVSDFQVFvrDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 148
Cdd:pfam00561  30 VIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGAL 103
YpfH COG0400
Predicted esterase [General function prediction only];
38-163 2.46e-07

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 49.91  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  38 SGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA------HDHVGHG----QSEGERMVVSDFQVFVRDVLQHVDTI 107
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261878509 108 QKDY--PDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLA 163
Cdd:COG0400   81 EARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 44-253 3.88e-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: 49.39  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   44 LIFVsHGAGEHCGRYDELAhmlkGLDMLVFAHDHVGHGQSEGERMVVSDfqvfVRDVLQHVDTIQKDYPdvpIFLLGHSM 123
Cdd:pfam12697   1 VVLV-HGAGLSAAPLAALL----AAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  124 GGAISILVAAerpTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEGSADRLCDSKGAY 203
Cdd:pfam12697  69 GGAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 261878509  204 LLMESSRSQDKTLKMYEGAYHVLH---RELPEVTNSVLHEVNSWVSHRIAAAG 253
Cdd:pfam12697 146 LLAALALLPLAAWRDLPVPVLVLAeedRLVPELAQRLLAALAGARLVVLPGAG 198
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 33-147 3.35e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 47.63  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  33 RYWK-PSGTPKALIFVsHG-AGEH---CGRYDELAhmlkgLDMLVFAHDHVGHGQSeGERMVVSDFQVFVRDVLQHVDT- 106
Cdd:PRK14875 122 RYLRlGEGDGTPVVLI-HGfGGDLnnwLFNHAALA-----AGRPVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFLDAl 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261878509 107 -IQKDYpdvpifLLGHSMGGAISILVAAERPTYFSGMVLISP 147
Cdd:PRK14875 195 gIERAH------LVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PRK10749 PRK10749
lysophospholipase L2; Provisional
 57-148 5.44e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 46.53  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  57 RYDELAHMLKGLDMLVFAHDHVGHGQS-----EGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILV 131
Cdd:PRK10749  69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLF 148

                         90
                 ....*....|....*..
gi 261878509 132 AAERPTYFSGMVLISPL 148
Cdd:PRK10749 149 LQRHPGVFDAIALCAPM 165
COG4099 COG4099
Predicted peptidase [General function prediction only];
44-160 1.79e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 44.57  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  44 LIFVSHGAGEhcgRYDELAHMLK-GLDMLVfahdhvghgqSEGERmvvSDFQVFV-----------------RDVLQHVD 105
Cdd:COG4099   51 LVLFLHGAGE---RGTDNEKQLThGAPKFI----------NPENQ---AKFPAIVlapqcpeddywsdtkalDAVLALLD 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261878509 106 TIQKDYP-DvP--IFLLGHSMGGAISILVAAERPTYFSGMVLISPlvLANPESASTLK 160
Cdd:COG4099  115 DLIAEYRiD-PdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-136 6.18e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  21 HLVNADGQYLFCRYWKPSGT-PKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFA---HDHVGHGQSEGE---RMVVSDF 93
Cdd:COG0412    7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDP 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 261878509  94 QVFVRDVLQHVDTIQKDyPDV---PIFLLGHSMGGAISILVAAERP 136
Cdd:COG0412   87 ELLAADLRAALDWLKAQ-PEVdagRVGVVGFCFGGGLALLAAARGP 131
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 99-134 9.63e-05

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


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 42.46  E-value: 9.63e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 261878509  99 DVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00519  113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
PLN02578 PLN02578
hydrolase
 39-147 3.58e-04

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 41.36  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  39 GTPKALIfvsHGAGEHC--GRYD--ELAHMLKgldmlVFAHDHVGHGQSEgERMVVSDFQVFVRDVLQHVDTIQKDypdv 114
Cdd:PLN02578  86 GLPIVLI---HGFGASAfhWRYNipELAKKYK-----VYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---- 152

                         90       100       110
                 ....*....|....*....|....*....|...
gi 261878509 115 PIFLLGHSMGGAISILVAAERPTYFSGMVLISP 147
Cdd:PLN02578 153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 98-134 4.17e-04

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


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 39.79  E-value: 4.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 261878509  98 RDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:cd00741   12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
37-138 6.26e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.48  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509  37 PSGTPKALIFVSHGAGEHCGRYDELAHML--KGldMLVFAHDHVGH-----GQSEGERMVVSDFQVF------VRDVLQH 103
Cdd:COG4188   57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLasHG--YVVAAPDHPGSnaadlSAALDGLADALDPEELwerpldLSFVLDQ 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 261878509 104 VDTIQKDYPDVP-------IFLLGHSMGGAISILVAAERPTY 138
Cdd:COG4188  135 LLALNKSDPPLAgrldldrIGVIGHSLGGYTALALAGARLDF 176
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
118-147 1.26e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 39.20  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 261878509 118 LLGHSMGGAISILVAAERPTYFSGMVLISP 147
Cdd:COG2819  134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 115-148 2.46e-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: 38.36  E-value: 2.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 261878509 115 PIFLLGHSMGGAISILVAAERPTYFSGMVLISPL 148
Cdd:cd12809  172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 79-134 2.51e-03

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 38.29  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261878509  79 GHGQSEGERMVvSDFQVFVRDVLQHVdtiqKDYPDVPIFLLGHSMGGAISILVAAE 134
Cdd:COG3208   42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 72-129 2.53e-03

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


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 38.61  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   72 VFAHDHVGHGQSEGE---RMVVSDFQVFVRDVLQHVDTIQK-------------DYPDV-------PIFLLGHSMGGAIS 128
Cdd:TIGR01607  77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYDIVntkenrlPMYIIGLSMGGNIA 156


                  .
gi 261878509  129 I 129
Cdd:TIGR01607 157 L 157
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-136 5.01e-03

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 37.43  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878509   4 ASSPRRTPQnVPYQ----DLPhlvnaDGQYLFCRYWKPSGTPKALIFVSHG-AGEHCGRY-DELAHMLKGLDMLVFAHDH 77
Cdd:COG0429   25 PSLFRRRPA-LPYRrerlELP-----DGDFVDLDWSDPPAPSKPLVVLLHGlEGSSDSHYaRGLARALYARGWDVVRLNF 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261878509  78 VGHGQSE---------GErmvVSDfqvfVRDVLQHvdtIQKDYPDVPIFLLGHSMGGAISILVAAERP 136
Cdd:COG0429   99 RGCGGEPnllprlyhsGD---TED----LVWVLAH---LRARYPYAPLYAVGFSLGGNLLLKYLGEQG 156
 
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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