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Conserved domains on  [gi|517491153|ref|WP_018661730|]
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carboxylesterase [Heyndrickxia acidiproducens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10787854)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917|37582413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
8-247 1.46e-92

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


:

Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 272.59  E-value: 1.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   8 IPGASSFFFKGNDIGILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGTHYRDMERCTCKDWINSLEEGYRFLKQH 87
Cdd:COG1647    3 ILGAEPFFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  88 CREIFVIGQSMGGTLTLNLAEKYTDIRGIVLINAAI--NSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITYDKVPASS 165
Cdd:COG1647   83 YDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALkiDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153 166 IRELLAVMQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPLRNSYHVASLDQEKEQIAEQCSLFIQ 245
Cdd:COG1647  163 LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREEVAEEILDFLE 242


                 ..
gi 517491153 246 KV 247
Cdd:COG1647  243 RL 244
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
8-247 1.46e-92

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 272.59  E-value: 1.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   8 IPGASSFFFKGNDIGILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGTHYRDMERCTCKDWINSLEEGYRFLKQH 87
Cdd:COG1647    3 ILGAEPFFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  88 CREIFVIGQSMGGTLTLNLAEKYTDIRGIVLINAAI--NSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITYDKVPASS 165
Cdd:COG1647   83 YDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALkiDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153 166 IRELLAVMQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPLRNSYHVASLDQEKEQIAEQCSLFIQ 245
Cdd:COG1647  163 LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREEVAEEILDFLE 242


                 ..
gi 517491153 246 KV 247
Cdd:COG1647  243 RL 244
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 23-225 4.05e-21

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: 88.81  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   23 ILISHGFNGTpqSVRF--LGEYLASKGFSVHAPRLSGHG------THYRDMErctckDWINSLEEGYRFLKQ--HCREIF 92
Cdd:pfam12146   7 VVLVHGLGEH--SGRYahLADALAAQGFAVYAYDHRGHGrsdgkrGHVPSFD-----DYVDDLDTFVDKIREehPGLPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   93 VIGQSMGGTLTLNLAEKY-TDIRGIVLINAAINSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITY------------- 158
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYpDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSlsrdpevvaayaa 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517491153  159 -----DKVPASSIRELLAVMQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPLRNSYH 225
Cdd:pfam12146 160 dplvhGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
 
Name Accession Description Interval E-value
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
8-247 1.46e-92

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 272.59  E-value: 1.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   8 IPGASSFFFKGNDIGILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGTHYRDMERCTCKDWINSLEEGYRFLKQH 87
Cdd:COG1647    3 ILGAEPFFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  88 CREIFVIGQSMGGTLTLNLAEKYTDIRGIVLINAAI--NSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITYDKVPASS 165
Cdd:COG1647   83 YDKVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALkiDDPSAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRTPLRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153 166 IRELLAVMQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPLRNSYHVASLDQEKEQIAEQCSLFIQ 245
Cdd:COG1647  163 LAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREEVAEEILDFLE 242


                 ..
gi 517491153 246 KV 247
Cdd:COG1647  243 RL 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
23-246 2.85e-26

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 102.00  E-value: 2.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHG------THYRDMErctckDWINSLEEGYRFLKQHCRE-IFVIG 95
Cdd:COG2267   31 VVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGrsdgprGHVDSFD-----DYVDDLRAALDALRARPGLpVVLLG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  96 QSMGGTLTLNLAEKYTD-IRGIVLINAAInsipvlekclleqqlglidEADPDIkapgakeitydKVPASSIRELlavmq 174
Cdd:COG2267  106 HSMGGLIALLYAARYPDrVAGLVLLAPAY-------------------RADPLL-----------GPSARWLRAL----- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517491153 175 ETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIpLRNSYHVASLDQEKEQIAEQCSLFIQK 246
Cdd:COG2267  151 RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVL-LPGARHELLNEPAREEVLAAILAWLER 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 23-225 4.05e-21

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: 88.81  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   23 ILISHGFNGTpqSVRF--LGEYLASKGFSVHAPRLSGHG------THYRDMErctckDWINSLEEGYRFLKQ--HCREIF 92
Cdd:pfam12146   7 VVLVHGLGEH--SGRYahLADALAAQGFAVYAYDHRGHGrsdgkrGHVPSFD-----DYVDDLDTFVDKIREehPGLPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   93 VIGQSMGGTLTLNLAEKY-TDIRGIVLINAAINSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITY------------- 158
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYpDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSlsrdpevvaayaa 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517491153  159 -----DKVPASSIRELLAVMQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPLRNSYH 225
Cdd:pfam12146 160 dplvhGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-248 2.59e-15

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 73.03  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHG------THYRDMERCTCKDWInsleegyRFLKQHC----REIF 92
Cdd:COG1073   40 VVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGesegepREEGSPERRDARAAV-------DYLRTLPgvdpERIG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  93 VIGQSMGGTLTLNLAEKYTDIRGIVLInAAINSIPVLEKCLLEQQLGLIDEADPdikapgakeitYdkVPASSIRELLAV 172
Cdd:COG1073  113 LLGISLGGGYALNAAATDPRVKAVILD-SPFTSLEDLAAQRAKEARGAYLPGVP-----------Y--LPNVRLASLLND 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517491153 173 MQETHQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRStFKPIIPLRNSYHVASLDQEKEQIAEQCSLFIQKVM 248
Cdd:COG1073  179 EFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAE-PKELLIVPGAGHVDLYDRPEEEYFDKLAEFFKKNL 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 23-238 1.36e-14

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: 70.80  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTPQSVRFLGEYLAsKGFSVHAPRLSGHGTHYRDMERCTCKDWINSLEEgyrFLKQH-CREIFVIGQSMGGT 101
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA---LLDALgLERVVLVGHSMGGM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153 102 LTLNLAEKYTD-IRGIVLINAAINSIpvlekclleqqlglideadpdikapgAKEITYDKVPASSIRELLAVMQET--HQ 178
Cdd:COG0596  102 VALELAARHPErVAGLVLVDEVLAAL--------------------------AEPLRRPGLAPEALAALLRALARTdlRE 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517491153 179 KLSRINCPALLFQSIEDHVVPPENTNEIAAGI-RSTFKpIIPlrNSYHVASLDQeKEQIAE 238
Cdd:COG0596  156 RLARITVPTLVIWGEKDPIVPPALARRLAELLpNAELV-VLP--GAGHFPPLEQ-PEAFAA 212
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
23-216 2.22e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 67.35  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTpQSVRFLGE--YLASKGFSVHAPRLSGHGTHYRDMERctckDWINSLEEGYRFLKQHC----REIFVIGQ 96
Cdd:COG1506   26 VVYVHGGPGS-RDDSFLPLaqALASRGYAVLAPDYRGYGESAGDWGG----DEVDDVLAAIDYLAARPyvdpDRIGIYGH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  97 SMGGTLTLNLAEKYTD-IRGIVLINAAINsipvlekcLLEQQLGLIDEADPDIKAPGAKEITYDKVpaSSIRellavmqe 175
Cdd:COG1506  101 SYGGYMALLAAARHPDrFKAAVALAGVSD--------LRSYYGTTREYTERLMGGPWEDPEAYAAR--SPLA-------- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 517491153 176 thqKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKP 216
Cdd:COG1506  163 ---YADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKP 200
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 23-230 5.55e-13

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 66.37  E-value: 5.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   23 ILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGthyRDMERCTCKDWIN-SLEEGYRFLKQHC--REIFVIGQSMG 99
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFG---KSSRPKAQDDYRTdDLAEDLEYILEALglEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  100 GTLTLNLAEKYTD-IRGIVLINAAINSIP------------------VLEKC--------------LLEQQLGLIDEADP 146
Cdd:pfam00561  80 GLIALAYAAKYPDrVKALVLLGALDPPHEldeadrfilalfpgffdgFVADFapnplgrlvakllaLLLLRLRLLKALPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  147 DIKAPGAKEITYDKVPA-SSIRELLAVMQE-THQKLSRINCPALLFQSIEDHVVPPENTNEIAAGIRSTFKPIIPlrNSY 224
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVtGALLFIETWSTElRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP--DAG 237


                  ....*.
gi 517491153  225 HVASLD 230
Cdd:pfam00561 238 HFAFLE 243
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
22-175 3.31e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 55.36  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  22 GILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGTHYRDMERCtcKDWINSLEEG---------YRFLKQHCRE-- 90
Cdd:COG0412   31 GVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEA--RALMGALDPEllaadlraaLDWLKAQPEVda 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  91 --IFVIGQSMGGTLTLNLAEKYTDIRGIVlinaAINSIPVLEKClleqqlgliDEADPDIKAP-----GAKeityDK-VP 162
Cdd:COG0412  109 grVGVVGFCFGGGLALLAAARGPDLAAAV----SFYGGLPADDL---------LDLAARIKAPvlllyGEK----DPlVP 171

                        170
                 ....*....|...
gi 517491153 163 ASSIRELLAVMQE 175
Cdd:COG0412  172 PEQVAALEAALAA 184
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
 78-209 2.53e-07

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 49.97  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   78 EEGYRFLKQH----CREIFVIGQSMGGTLTLNLAEKYTDIRGIVLIN--AAINSIPVLEKcllEQQLGLIDEADPDIK-- 149
Cdd:pfam08840   7 EEAINYLLRHpkvkGPGIGLLGISKGGELALSMATFLKQITATVSINgsAVVSGDPLVYK---DNPLPPLGEGMRRIKvn 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517491153  150 APGAKEITYdkvpassIRELLAVmQETHQ---KLSRINCPALLFQSIEDHVVPPENTNEIAAG 209
Cdd:pfam08840  84 KDGLLDIRD-------MFNDPLS-KPDPKsliPVERAKGPFLFVVGQDDHNWPSVFYAKKACE 138
YcfP COG3150
Predicted esterase YcpF, UPF0227 family [General function prediction only];
27-139 2.63e-07

Predicted esterase YcpF, UPF0227 family [General function prediction only];


Pssm-ID: 442384 [Multi-domain]  Cd Length: 190  Bit Score: 49.37  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  27 HGFNGTPQSV--RFLGEYLASKGFS--VHAPRLsghgtHYRDMERctckdwINSLEEGyrfLKQHCRE-IFVIGQSMGGT 101
Cdd:COG3150    7 HGFNSSPQSAkaQLLAAYFAEHGPDieFICPQL-----PPSPAAA------IAQLEAL---IAGLPGEpLALIGSSLGGF 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517491153 102 LTLNLAEKYtDIRGiVLINAAINsiPVLekcLLEQQLG 139
Cdd:COG3150   73 YATWLAERY-GLRA-VLINPAVR--PAR---LLADYLG 103
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
23-237 2.88e-07

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 50.49  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTPQSVRFLGEYLASKGFSVHAPRlsgH-GTHYRDMER--------CTCKDWIN-------------SLEEG 80
Cdd:COG4188   65 VVLSHGLGGSREGYAYLAEHLASHGYVVAAPD---HpGSNAADLSAaldgladaLDPEELWErpldlsfvldqllALNKS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  81 YRFLK-----QHcreIFVIGQSMGGTLTLNLAEKYTDIRGivlINAAINSIPVLEKCLLEQQLGLIDEADPDIKApgAke 155
Cdd:COG4188  142 DPPLAgrldlDR---IGVIGHSLGGYTALALAGARLDFAA---LRQYCGKNPDLQCRALDLPRLAYDLRDPRIKA--V-- 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153 156 ITYDKVPASSIREllavmqethQKLSRINCPALLFQSIEDHVVP-PENTNEIAAGIRSTFKPIIPLRNSYHVASLDQEKE 234
Cdd:COG4188  212 VALAPGGSGLFGE---------EGLAAITIPVLLVAGSADDVTPaPDEQIRPFDLLPGADKYLLTLEGATHFSFLDPCTP 282


                 ...
gi 517491153 235 QIA 237
Cdd:COG4188  283 GAA 285
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 23-233 3.56e-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: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   23 ILISHGFngtPQSVRFLGEYLAsKGFSVHAPRLSGHG------THYRDMERCTckDWINSLEEGyrflkqhcREIFVIGQ 96
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLA-AGVAVLAPDLPGHGssspppLDLADLADLA--ALLDELGAA--------RPVVLVGH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153   97 SMGGTLTLNLAEkYTDIRGIVL---------INAAINSIPVLEKCLLEQQLGLIDEADPDIKAPGAKEITYDKVPASSIR 167
Cdd:pfam12697  67 SLGGAVALAAAA-AALVVGVLVaplaappglLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517491153  168 ELLAVMQETHQKLSRINCPALLFQSiEDHVVPPENTNEIAAGIRstfKPIIPLRNSYHVASLDQEK 233
Cdd:pfam12697 146 LLAALALLPLAAWRDLPVPVLVLAE-EDRLVPELAQRLLAALAG---ARLVVLPGAGHLPLDDPEE 207
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 23-119 7.83e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.97  E-value: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHGFNGTPQSVRFLGEYLASKGFSVHAPRLSGHGTHYRDMERcTCKDWINSLEEgyrflKQHCREIFVIGQSMGGTL 102
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAE-QLAAFVDAVLA-----ATGAEKVDLVGHSMGGLV 81

                         90       100
                 ....*....|....*....|
gi 517491153 103 TLNLAEKY---TDIRGIVLI 119
Cdd:COG1075   82 ARYYLKRLggaAKVARVVTL 101
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
23-119 6.23e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 36.77  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491153  23 ILISHG---FNGTPQSVRFLGEYLAS-KGFSVHAP--RLSGHGTH---YRDMERctckdwinsleeGYRFLKQHCRE--- 90
Cdd:COG0657   16 VVYFHGggwVSGSKDTHDPLARRLAArAGAAVVSVdyRLAPEHPFpaaLEDAYA------------ALRWLRANAAElgi 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517491153  91 ----IFVIGQSMGGTLTLNLAEKYTD-----IRGIVLI 119
Cdd:COG0657   84 dpdrIAVAGDSAGGHLAAALALRARDrggprPAAQVLI 121
 
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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