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Conserved domains on  [gi|2034024385|dbj|GIR69827|]
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MAG: alpha/beta hydrolase [Halieaceae bacterium]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-285 2.61e-26

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: 102.77  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   1 MPEPRSVSVtaDGLRYTGLEWGPqDGEPIIALHGWLDNALSFSVVAPKLA-GYRVVALDLSGQGFSDHrsPDATYHIWDD 79
Cdd:COG0596     1 MSTPRFVTV--DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAaGYRVIAPDLRGHGRSDK--PAGGYTLDDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  80 IPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGMlphplkeenvpsqfeqaqidhrelsayrgrif 159
Cdd:COG0596    76 ADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV-------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 160 kdIEEYVAARRRLGFSEQSArliapRALVETSDGFRLTHDprlnhasaikltpamcsafYSALSAPTLALIAENGLRARA 239
Cdd:COG0596   124 --LAALAEPLRRPGLAPEAL-----AALLRALARTDLRER-------------------LARITVPTLVIWGEKDPIVPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2034024385 240 GLADAVesVSEIPDCVVESVSG-GHHTHMEEgAERVAERITRFLRSR 285
Cdd:COG0596   178 ALARRL--AELLPNAELVVLPGaGHFPPLEQ-PEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-285 2.61e-26

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: 102.77  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   1 MPEPRSVSVtaDGLRYTGLEWGPqDGEPIIALHGWLDNALSFSVVAPKLA-GYRVVALDLSGQGFSDHrsPDATYHIWDD 79
Cdd:COG0596     1 MSTPRFVTV--DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAaGYRVIAPDLRGHGRSDK--PAGGYTLDDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  80 IPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGMlphplkeenvpsqfeqaqidhrelsayrgrif 159
Cdd:COG0596    76 ADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV-------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 160 kdIEEYVAARRRLGFSEQSArliapRALVETSDGFRLTHDprlnhasaikltpamcsafYSALSAPTLALIAENGLRARA 239
Cdd:COG0596   124 --LAALAEPLRRPGLAPEAL-----AALLRALARTDLRER-------------------LARITVPTLVIWGEKDPIVPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2034024385 240 GLADAVesVSEIPDCVVESVSG-GHHTHMEEgAERVAERITRFLRSR 285
Cdd:COG0596   178 ALARRL--AELLPNAELVVLPGaGHFPPLEQ-PEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-269 6.09e-21

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: 89.10  E-value: 6.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  28 PIIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSDHRSPDATYHIWDDIPQLLSIADQLGFEKLAVAGHSRGAA 105
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArdGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 106 IAVLLASALRERCSHFVLLDGMLPHPLKEENVPSqfeQAQIDHRELSAYRGRIFKDIEE-YVAARRRLGFSEQSARLIAP 184
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRF---ILALFPGFFDGFVADFAPNPLGrLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 185 RALVETSDGFRLTHDP----RLNHASAIKLTPAMCsaFYSALSAPTLALIAENGLRARAGLADAVESVSEIPDCVVEsVS 260
Cdd:pfam00561 159 LLNKRFPSGDYALAKSlvtgALLFIETWSTELRAK--FLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-PD 235


                  ....*....
gi 2034024385 261 GGHHTHMEE 269
Cdd:pfam00561 236 AGHFAFLEG 244
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-111 3.38e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   2 PEPRSVSVTADGLRYtgLEWGPQDGEPIIALHGW---LDNALSfsVVAPKLAGYRVVALDLSGQGFSDHRSPDATYhiwD 78
Cdd:PRK14875  109 PAPRKARIGGRTVRY--LRLGEGDGTPVVLIHGFggdLNNWLF--NHAALAAGRPVIALDLPGHGASSKAVGAGSL---D 181

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2034024385  79 DIPQ-LLSIADQLGFEKLAVAGHSRGAAIAVLLA 111
Cdd:PRK14875  182 ELAAaVLAFLDALGIERAHLVGHSMGGAVALRLA 215
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 50-123 2.94e-03

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 38.26  E-value: 2.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034024385  50 AGYRVVALDLSGQGFSDHRSPDATYHIW-DDIPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVL 123
Cdd:TIGR03101  55 GGFGVLQIDLYGCGDSAGDFAAARWDVWkEDVAAAYRWLIEQGHPPVTLWGLRLGALLALDAANPLAAKCNRLVL 129
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 71-117 3.93e-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: 37.09  E-value: 3.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2034024385  71 DATYHIWDDIPQLL-SIADQLGFEKLAVAGHSRGAAIAVLLASALRER 117
Cdd:cd00741     5 KAARSLANLVLPLLkSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGR 52
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-285 2.61e-26

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: 102.77  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   1 MPEPRSVSVtaDGLRYTGLEWGPqDGEPIIALHGWLDNALSFSVVAPKLA-GYRVVALDLSGQGFSDHrsPDATYHIWDD 79
Cdd:COG0596     1 MSTPRFVTV--DGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAaGYRVIAPDLRGHGRSDK--PAGGYTLDDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  80 IPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGMlphplkeenvpsqfeqaqidhrelsayrgrif 159
Cdd:COG0596    76 ADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV-------------------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 160 kdIEEYVAARRRLGFSEQSArliapRALVETSDGFRLTHDprlnhasaikltpamcsafYSALSAPTLALIAENGLRARA 239
Cdd:COG0596   124 --LAALAEPLRRPGLAPEAL-----AALLRALARTDLRER-------------------LARITVPTLVIWGEKDPIVPP 177

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2034024385 240 GLADAVesVSEIPDCVVESVSG-GHHTHMEEgAERVAERITRFLRSR 285
Cdd:COG0596   178 ALARRL--AELLPNAELVVLPGaGHFPPLEQ-PEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-269 6.09e-21

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: 89.10  E-value: 6.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  28 PIIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSDHRSPDATYHIWDDIPQLLSIADQLGFEKLAVAGHSRGAA 105
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALArdGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 106 IAVLLASALRERCSHFVLLDGMLPHPLKEENVPSqfeQAQIDHRELSAYRGRIFKDIEE-YVAARRRLGFSEQSARLIAP 184
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRF---ILALFPGFFDGFVADFAPNPLGrLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 185 RALVETSDGFRLTHDP----RLNHASAIKLTPAMCsaFYSALSAPTLALIAENGLRARAGLADAVESVSEIPDCVVEsVS 260
Cdd:pfam00561 159 LLNKRFPSGDYALAKSlvtgALLFIETWSTELRAK--FLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-PD 235


                  ....*....
gi 2034024385 261 GGHHTHMEE 269
Cdd:pfam00561 236 AGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-124 2.95e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.81  E-value: 2.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   1 MPEPRSVSVTADGLRYTGLEWGPQDGE--PIIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSDHRSPD-ATYH 75
Cdd:COG2267     1 MTRRLVTLPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAaaGYAVLAFDLRGHGRSDGPRGHvDSFD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2034024385  76 IW-DDIPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLL 124
Cdd:COG2267    81 DYvDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLL 130
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-111 3.38e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   2 PEPRSVSVTADGLRYtgLEWGPQDGEPIIALHGW---LDNALSfsVVAPKLAGYRVVALDLSGQGFSDHRSPDATYhiwD 78
Cdd:PRK14875  109 PAPRKARIGGRTVRY--LRLGEGDGTPVVLIHGFggdLNNWLF--NHAALAAGRPVIALDLPGHGASSKAVGAGSL---D 181

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2034024385  79 DIPQ-LLSIADQLGFEKLAVAGHSRGAAIAVLLA 111
Cdd:PRK14875  182 ELAAaVLAFLDALGIERAHLVGHSMGGAVALRLA 215
PRK05855 PRK05855
SDR family oxidoreductase;
3-75 7.21e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 56.14  E-value: 7.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034024385   3 EPRSVSVTADGLRYTGLEWGPQDGEPIIALHGWLDNALSFSVVAPKLAG-YRVVALDLSGQGFSDHRSPDATYH 75
Cdd:PRK05855    2 QPRRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADrFRVVAYDVRGAGRSSAPKRTAAYT 75
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 9-139 1.25e-08

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 55.27  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   9 VTADGLRYTGLEWGPQDGEPIIALHGWLDNALSFSVVAPKLA-GYRVVALDLSGQGFSDHRSPDA--TYHIWDDIPQLLS 85
Cdd:PLN03084  110 ASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSkNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLES 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2034024385  86 IADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGmlPHPLKEENVPS 139
Cdd:PLN03084  190 LIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNP--PLTKEHAKLPS 241
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 3-129 2.10e-07

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 51.12  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   3 EPRSVSVTADG---LRYTGLEWGPQDGEPIIALHG---WldnALSFSVVAPKL--AGYRVVALDLSGQGFSDHRSPDATY 74
Cdd:PRK00870   20 APHYVDVDDGDggpLRMHYVDEGPADGPPVLLLHGepsW---SYLYRKMIPILaaAGHRVIAPDLIGFGRSDKPTRREDY 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  75 ----HI-WddipqLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGMLP 129
Cdd:PRK00870   97 tyarHVeW-----MRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTGLP 151
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 24-130 1.72e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 45.59  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  24 QDGEPIIALHGWLDNALSFSVVAPKL--AGYRVVALDLSGQGFSdhrSPDATYHIWDDIPQLLSIAdqlGFEKLAVAGHS 101
Cdd:COG1075     3 ATRYPVVLVHGLGGSAASWAPLAPRLraAGYPVYALNYPSTNGS---IEDSAEQLAAFVDAVLAAT---GAEKVDLVGHS 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2034024385 102 RGAAIAVLLASAL--RERCSHFVLLDGmlPH 130
Cdd:COG1075    77 MGGLVARYYLKRLggAAKVARVVTLGT--PH 105
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-117 2.24e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 48.07  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385   1 MPEPRSVSVTADGLRYTGLEWGpqDGEPIIALHG-------WLDnalsfsvVAPKLAGY-RVVALDLSGQGFSDhrSPDA 72
Cdd:PRK03592    4 EPPGEMRRVEVLGSRMAYIETG--EGDPIVFLHGnptssylWRN-------IIPHLAGLgRCLAPDLIGMGASD--KPDI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2034024385  73 TYHIWDDIPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRER 117
Cdd:PRK03592   73 DYTFADHARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDR 117
PLN02578 PLN02578
hydrolase
 26-181 2.40e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 48.30  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  26 GEPIIALHGWLDNALSFSVVAPKLAG-YRVVALDLSGQGFSDHRSPDATYHIWDDipQLLSIADQLGFEKLAVAGHSRGA 104
Cdd:PLN02578   86 GLPIVLIHGFGASAFHWRYNIPELAKkYKVYALDLLGFGWSDKALIEYDAMVWRD--QVADFVKEVVKEPAVLVGNSLGG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385 105 AIAVLLASALRERCSHFVLLdgmlphplkeeNVPSQF-----EQAQIDHRELSAYRGRIFKDIEEyVAARRRLGF----S 175
Cdd:PLN02578  164 FTALSTAVGYPELVAGVALL-----------NSAGQFgsesrEKEEAIVVEETVLTRFVVKPLKE-WFQRVVLGFlfwqA 231


                  ....*.
gi 2034024385 176 EQSARL 181
Cdd:PLN02578  232 KQPSRI 237
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
29-116 8.14e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.09  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  29 IIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSDHRSPDATYHIW-DDIPQLLSIAdQLGFEKLAVAGHSRGAA 105
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAkaGYTVYAPRLPGHGTSPEDLLKTTWEDWlEDVEEAYEIL-KAGYDKVIVIGLSMGGL 96

                          90
                  ....*....|.
gi 2034024385 106 IAVLLASALRE 116
Cdd:COG1647    97 LALLLAARYPD 107
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
10-112 1.07e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.78  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  10 TADGLRYTGLEWGPQDGEP---IIALHGWLDNAL-SFSVVAPKLA--GYRVVALDLSGQGFSDHrspDATYHIWDDIPQL 83
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKypvVVYVHGGPGSRDdSFLPLAQALAsrGYAVLAPDYRGYGESAG---DWGGDEVDDVLAA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2034024385  84 LSIADQLGF---EKLAVAGHSRGAAIAVLLAS 112
Cdd:COG1506    81 IDYLAARPYvdpDRIGIYGHSYGGYMALLAAA 112
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 29-131 1.91e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 44.77  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  29 IIALHGWldnALSFSVVAPKLA-GYRVVALDLSGQGFSDHRSPDatyhiWDDIPQLLSIADQLG-FEKLAVAGHSRGAAI 106
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAaGVAVLAPDLPGHGSSSPPPLD-----LADLADLAALLDELGaARPVVLVGHSLGGAV 72

                          90       100
                  ....*....|....*....|....*
gi 2034024385 107 AVLLASALRERCshfVLLDGMLPHP 131
Cdd:pfam12697  73 ALAAAAAALVVG---VLVAPLAAPP 94
YpfH COG0400
Predicted esterase [General function prediction only];
29-135 3.07e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 43.74  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  29 IIALHGWLDNALSFSVVAPKLA--GYRVVALdlsgqgfsdhRSPDATYHI---WDDIPQLLSIADQ-------------- 89
Cdd:COG0400     8 VVLLHGYGGDEEDLLPLAPELAlpGAAVLAP----------RAPVPEGPGgraWFDLSFLEGREDEeglaaaaealaafi 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2034024385  90 --------LGFEKLAVAGHSRGAAIAVLLASALRERCSHFVLLDGMLPHPLKEE 135
Cdd:COG0400    78 delearygIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALP 131
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 29-123 2.25e-04

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: 41.82  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  29 IIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSD-HRS-PDATYHIWDDIPQLLS-IADQLGFEKLAVAGHSRG 103
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAaqGFAVYAYDHRGHGRSDgKRGhVPSFDDYVDDLDTFVDkIREEHPGLPLFLLGHSMG 86

                          90       100
                  ....*....|....*....|
gi 2034024385 104 AAIAVLLASALRERCSHFVL 123
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLIL 106
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 10-115 9.11e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.90  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  10 TADGLRYTGLEWGPQDGEP----IIALHGWLDNALSFSVVAPKLA--GYRVVALDLSGQGFSDhrsPDATYHIWDDIPQL 83
Cdd:COG1073    17 SRDGIKLAGDLYLPAGASKkypaVVVAHGNGGVKEQRALYAQRLAelGFNVLAFDYRGYGESE---GEPREEGSPERRDA 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2034024385  84 LSIADQLG------FEKLAVAGHSRGAAIAVLLASALR 115
Cdd:COG1073    94 RAAVDYLRtlpgvdPERIGLLGISLGGGYALNAAATDP 131
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
10-116 2.30e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.41  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034024385  10 TADGLRYTGLEWGPQDGEP---IIALHGWldnalsFSV------VAPKLA--GYRVVALDL-SGQGFSDHRSPDATYHIW 77
Cdd:COG0412    10 TPDGVTLPGYLARPAGGGPrpgVVVLHEI------FGLnphirdVARRLAaaGYVVLAPDLyGRGGPGDDPDEARALMGA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2034024385  78 DDIPQLLSIAD----------QLGFEKLAVAGHSRGAAIAVLLASALRE 116
Cdd:COG0412    84 LDPELLAADLRaaldwlkaqpEVDAGRVGVVGFCFGGGLALLAAARGPD 132
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 50-123 2.94e-03

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 38.26  E-value: 2.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2034024385  50 AGYRVVALDLSGQGFSDHRSPDATYHIW-DDIPQLLSIADQLGFEKLAVAGHSRGAAIAVLLASALRERCSHFVL 123
Cdd:TIGR03101  55 GGFGVLQIDLYGCGDSAGDFAAARWDVWkEDVAAAYRWLIEQGHPPVTLWGLRLGALLALDAANPLAAKCNRLVL 129
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 71-117 3.93e-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: 37.09  E-value: 3.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2034024385  71 DATYHIWDDIPQLL-SIADQLGFEKLAVAGHSRGAAIAVLLASALRER 117
Cdd:cd00741     5 KAARSLANLVLPLLkSALAQYPDYKIHVTGHSLGGALAGLAGLDLRGR 52
 
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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