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Conserved domains on  [gi|446341196|ref|WP_000419051|]
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MULTISPECIES: S-formylglutathione hydrolase [Enterobacteriaceae]

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, ...
 2-274 1.89e-139

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 TIGR02821:

Pssm-ID: 473884  Cd Length: 275  Bit Score: 393.76  E-value: 1.89e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196    2 ELIEKHASFGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196   82 SPRGSHVAD-ADRYDLGQGAGFYLNATQAPWNEHYKMYDYIRNELPDLVMQHFPAT-TRKSISGHSMGGLGALVLALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDgERQGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  160 DEYVSVSAFSPIVSPSQVPWGQQAFAAYLGENKDAWLNYDPVSLISQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQE 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 446341196  240 MNIKTLIRYHEGYDHSYYFVSSFIGEHIAYHANKL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-274 1.89e-139

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 393.76  E-value: 1.89e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196    2 ELIEKHASFGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196   82 SPRGSHVAD-ADRYDLGQGAGFYLNATQAPWNEHYKMYDYIRNELPDLVMQHFPAT-TRKSISGHSMGGLGALVLALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDgERQGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  160 DEYVSVSAFSPIVSPSQVPWGQQAFAAYLGENKDAWLNYDPVSLISQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQE 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 446341196  240 MNIKTLIRYHEGYDHSYYFVSSFIGEHIAYHANKL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 10-276 5.32e-130

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 369.88  E-value: 5.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  10 FGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGSHV- 88
Cdd:PLN02442  14 FGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPRGLNVe 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  89 ADADRYDLGQGAGFYLNATQAPWnEHYKMYDYIRNELPDLVMQHFPA--TTRKSISGHSMGGLGALVLALRNPDEYVSVS 166
Cdd:PLN02442  94 GEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQldTSRASIFGHSMGGHGALTIYLKNPDKYKSVS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 167 AFSPIVSPSQVPWGQQAFAAYLGENKDAWLNYDPVSLISQGQRV-AEIMVDQGLSDDFYAEQLRTPNLEKICQEMNIKTL 245
Cdd:PLN02442 173 AFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVsATILIDQGEADKFLKEQLLPENFEEACKEAGAPVT 252

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446341196 246 IRYHEGYDHSYYFVSSFIGEHIAYHANKLNM 276
Cdd:PLN02442 253 LRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
11-275 2.24e-105

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 306.37  E-value: 2.24e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  11 GGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDtsprgshvad 90
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  91 adrydlGQGAGFYLNATQAPwNEHYKMYDYIRNELPDLVMQHFPA---TTRKSISGHSMGGLGALVLALRNPDEYVSVSA 167
Cdd:COG0627   71 ------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVsadRERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 168 FSPIVSPSQVPWGQQAFAAYLG-ENKDAWLNYDPVSLISQGQRVAEIMVDQGLSDDFYAEQlrTPNLEKICQEMNIKTLI 246
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKLRAGLPLYIDCGTADPFFLEA--NRQLHAALRAAGIPHTY 221

                        250       260
                 ....*....|....*....|....*....
gi 446341196 247 RYHEGYdHSYYFVSSFIGEHIAYHANKLN 275
Cdd:COG0627  222 RERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-269 1.08e-81

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


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 245.83  E-value: 1.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196   21 SQSLKCEMNVGVYLP-PKAANEKLPVLYWLSGlTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGSHVADADRYDLGqg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  100 agfyLNATQAPWNEHYKmyDYIRNELPDLVMQHFP-ATTRKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSPSQVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPtAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  179 WGQqafaaylgENKDAWLNYDPVSLI---SQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQEMNIKTLI--RYHEGYD 253
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLAvalSANNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAEQLayRGVGGYD 223

                         250       260
                  ....*....|....*....|...
gi 446341196  254 HSY-------YFVSSFIGEHIAY 269
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 115-193 4.14e-03

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: 37.84  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 115 YKMYDYIRNELPDLVMQHFPATTRKSIS--GHSMGG----LGALVLALRNPDEYVSVSAF-SPIVspsqvpwGQQAFAAY 187
Cdd:cd00519  104 YSAYKSLYNQVLPELKSALKQYPDYKIIvtGHSLGGalasLLALDLRLRGPGSDVTVYTFgQPRV-------GNAAFAEY 176


                 ....*.
gi 446341196 188 LGENKD 193
Cdd:cd00519  177 LESTKG 182
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-274 1.89e-139

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 393.76  E-value: 1.89e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196    2 ELIEKHASFGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196   82 SPRGSHVAD-ADRYDLGQGAGFYLNATQAPWNEHYKMYDYIRNELPDLVMQHFPAT-TRKSISGHSMGGLGALVLALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDgERQGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  160 DEYVSVSAFSPIVSPSQVPWGQQAFAAYLGENKDAWLNYDPVSLISQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQE 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 446341196  240 MNIKTLIRYHEGYDHSYYFVSSFIGEHIAYHANKL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 10-276 5.32e-130

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 369.88  E-value: 5.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  10 FGGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGSHV- 88
Cdd:PLN02442  14 FGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPRGLNVe 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  89 ADADRYDLGQGAGFYLNATQAPWnEHYKMYDYIRNELPDLVMQHFPA--TTRKSISGHSMGGLGALVLALRNPDEYVSVS 166
Cdd:PLN02442  94 GEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQldTSRASIFGHSMGGHGALTIYLKNPDKYKSVS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 167 AFSPIVSPSQVPWGQQAFAAYLGENKDAWLNYDPVSLISQGQRV-AEIMVDQGLSDDFYAEQLRTPNLEKICQEMNIKTL 245
Cdd:PLN02442 173 AFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVsATILIDQGEADKFLKEQLLPENFEEACKEAGAPVT 252

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446341196 246 IRYHEGYDHSYYFVSSFIGEHIAYHANKLNM 276
Cdd:PLN02442 253 LRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
11-275 2.24e-105

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 306.37  E-value: 2.24e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  11 GGWQNVYRHYSQSLKCEMNVGVYLPPKAANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDtsprgshvad 90
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  91 adrydlGQGAGFYLNATQAPwNEHYKMYDYIRNELPDLVMQHFPA---TTRKSISGHSMGGLGALVLALRNPDEYVSVSA 167
Cdd:COG0627   71 ------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVsadRERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 168 FSPIVSPSQVPWGQQAFAAYLG-ENKDAWLNYDPVSLISQGQRVAEIMVDQGLSDDFYAEQlrTPNLEKICQEMNIKTLI 246
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKLRAGLPLYIDCGTADPFFLEA--NRQLHAALRAAGIPHTY 221

                        250       260
                 ....*....|....*....|....*....
gi 446341196 247 RYHEGYdHSYYFVSSFIGEHIAYHANKLN 275
Cdd:COG0627  222 RERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-269 1.08e-81

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


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 245.83  E-value: 1.08e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196   21 SQSLKCEMNVGVYLP-PKAANEKLPVLYWLSGlTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGSHVADADRYDLGqg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  100 agfyLNATQAPWNEHYKmyDYIRNELPDLVMQHFP-ATTRKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSPSQVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPtAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  179 WGQqafaaylgENKDAWLNYDPVSLI---SQGQRVAEIMVDQGLSDDFYAEQLRTPNLEKICQEMNIKTLI--RYHEGYD 253
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLAvalSANNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAEQLayRGVGGYD 223

                         250       260
                  ....*....|....*....|...
gi 446341196  254 HSY-------YFVSSFIGEHIAY 269
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
20-266 4.00e-22

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 93.38  E-value: 4.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  20 YSQSLKCEMNVGVYLPP--KAANEKLPVLYWLSGLTCNEQNFITKSG----MQRYAAEHNI---IVVAPDtsprgSHVAD 90
Cdd:COG2382   87 PSKALGRTRRVWVYLPPgyDNPGKKYPVLYLLDGGGGDEQDWFDQGRlptiLDNLIAAGKIppmIVVMPD-----GGDGG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  91 ADRYDLGQGAGFYlnatqapwnehykmyDYIRNELPDLVMQHFPATTRKS---ISGHSMGGLGALVLALRNPDEYVSVSA 167
Cdd:COG2382  162 DRGTEGPGNDAFE---------------RFLAEELIPFVEKNYRVSADPEhraIAGLSMGGLAALYAALRHPDLFGYVGS 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 168 FSPivspsqvpwgqqafaaYLGENKDAWLNYDPVSLISQGQRVAE--IMVDQGLSDDFYAEQLRtpnLEKICQEMniktl 245
Cdd:COG2382  227 FSG----------------SFWWPPGDADRGGWAELLAAGAPKKPlrFYLDVGTEDDLLEANRA---LAAALKAK----- 282

                        250       260
                 ....*....|....*....|.
gi 446341196 246 iryheGYDHSYYFVSsfiGEH 266
Cdd:COG2382  283 -----GYDVEYREFP---GGH 295
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
20-170 3.45e-08

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 53.07  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  20 YSQSLKCEMNVGVYLPP--KAANEKLPVLYWLSGltcnEQNFITKSGMQRYAAEHN-----IIVVAPDT----------- 81
Cdd:COG2819   13 ESPILGEDRRIRVYLPPgyDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGIGNgddgerrlrdy 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  82 SPRGSHVADADRYDLGQGAGFYlnatqapwnehykmyDYIRNELPDLVMQHFPATT-RKSISGHSMGGLGALVLALRNPD 160
Cdd:COG2819   89 TPPPAPGYPGPGGPGGGADAFL---------------RFLEEELKPYIDKRYRTDPeRTGLIGHSLGGLFSLYALLKYPD 153

                        170
                 ....*....|
gi 446341196 161 EYVSVSAFSP 170
Cdd:COG2819  154 LFGRYIAISP 163
COG4099 COG4099
Predicted peptidase [General function prediction only];
32-218 1.21e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 45.34  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  32 VYLPPK-AANEKLPVLYWL--SGLTCNEQNFITKSGMQRYA-----AEHNIIVVAPdtsprgshvadadrydlgqgagfy 103
Cdd:COG4099   37 LYLPKGyDPGKKYPLVLFLhgAGERGTDNEKQLTHGAPKFInpenqAKFPAIVLAP------------------------ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 104 lnatQAPWNEHYKMYDYIR--NELPDLVMQHFPA-TTRKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSPSQVPW- 179
Cdd:COG4099   93 ----QCPEDDYWSDTKALDavLALLDDLIAEYRIdPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDPANAANl 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446341196 180 GQQAFAAYLGENkdawlnyDPVSLISQGQRVAEIMVDQG 218
Cdd:COG4099  169 KKVPVWIFHGAK-------DDVVPVEESRAMVEALKAAG 200
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 32-169 2.12e-05

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 44.99  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  32 VYLPPKA-ANEKLPVLYWLSGLTCNEQNFITKSGMQRYAAEHNIIVVAPDTSPRGS----HVADADRYDLGQG-AGFyLN 105
Cdd:COG3509   41 LYVPAGYdGGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPgrcwNWFDGRDQRRGRDdVAF-IA 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446341196 106 AtqapwnehykMYDYirnelpdlVMQHFPA-TTRKSISGHSMGGLGALVLALRNPDEYVSVSAFS 169
Cdd:COG3509  120 A----------LVDD--------LAARYGIdPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
32-206 3.43e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.85  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  32 VYLPPKaaNEKLPVLYWLSGLTCNEQNFItkSGMQRYAAEHNIIVVAPDtsPRGShvadadrydlGQGAGfylNATQAPW 111
Cdd:COG1506   14 LYLPAD--GKKYPVVVYVHGGPGSRDDSF--LPLAQALASRGYAVLAPD--YRGY----------GESAG---DWGGDEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 112 NEHYKMYDYirnelpdLVMQHFPATTRKSISGHSMGGLGALVLALRNPDEYVSVSAFSPIVSP----SQVPWGQQAFAAY 187
Cdd:COG1506   75 DDVLAAIDY-------LAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLrsyyGTTREYTERLMGG 147

                        170
                 ....*....|....*....
gi 446341196 188 LGENKDAWLNYDPVSLISQ 206
Cdd:COG1506  148 PWEDPEAYAARSPLAYADK 166
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 143-189 4.07e-03

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: 37.58  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446341196  143 GHSMGGLGALVLALRNPDEYVSVSAFSP--IVSPSQVPWGQQAFAAYLG 189
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDKVDGLILSAPalKIKPYLAPPILKLLAKLLG 130
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 115-193 4.14e-03

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: 37.84  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196 115 YKMYDYIRNELPDLVMQHFPATTRKSIS--GHSMGG----LGALVLALRNPDEYVSVSAF-SPIVspsqvpwGQQAFAAY 187
Cdd:cd00519  104 YSAYKSLYNQVLPELKSALKQYPDYKIIvtGHSLGGalasLLALDLRLRGPGSDVTVYTFgQPRV-------GNAAFAEY 176


                 ....*.
gi 446341196 188 LGENKD 193
Cdd:cd00519  177 LESTKG 182
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 113-194 9.32e-03

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: 36.71  E-value: 9.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446341196  113 EHYKMYDYIRNELPDlvmqhfpatTRKSISGHSMGGLGALVLALRNPDE---YVSVSAFSPIVSPSQ--------VPWGQ 181
Cdd:pfam00561  54 DLAEDLEYILEALGL---------EKVNLVGHSMGGLIALAYAAKYPDRvkaLVLLGALDPPHELDEadrfilalFPGFF 124

                          90
                  ....*....|...
gi 446341196  182 QAFAAYLGENKDA 194
Cdd:pfam00561 125 DGFVADFAPNPLG 137
 
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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