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Conserved domains on  [gi|30686425|ref|NP_194147|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11477252)

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
16-418 0e+00

hydrolase, alpha/beta fold family protein


:

Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 751.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   16 ISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSK 95
Cdd:PLN02894   1 MKVQLRGHEIPGHGAASSAAASAAASAETSRTRSLWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   96 IRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEA 175
Cdd:PLN02894  81 VRWFRSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  176 WFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWE 255
Cdd:PLN02894 161 WFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTKFRATWKGAVLNHLWE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  256 SNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQS 335
Cdd:PLN02894 241 SNFTPQKIIRGLGPWGPNLVRRYTTARFGAHSTGDILSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLES 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  336 ASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHdQQLLDGL 415
Cdd:PLN02894 321 ASEWKVPTTFIYGRHDWMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKYLSPDREE-RALPEGL 399

                 ...
gi 30686425  416 RLV 418
Cdd:PLN02894 400 TSA 402
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
16-418 0e+00

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 751.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   16 ISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSK 95
Cdd:PLN02894   1 MKVQLRGHEIPGHGAASSAAASAAASAETSRTRSLWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   96 IRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEA 175
Cdd:PLN02894  81 VRWFRSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  176 WFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWE 255
Cdd:PLN02894 161 WFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTKFRATWKGAVLNHLWE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  256 SNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQS 335
Cdd:PLN02894 241 SNFTPQKIIRGLGPWGPNLVRRYTTARFGAHSTGDILSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLES 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  336 ASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHdQQLLDGL 415
Cdd:PLN02894 321 ASEWKVPTTFIYGRHDWMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKYLSPDREE-RALPEGL 399

                 ...
gi 30686425  416 RLV 418
Cdd:PLN02894 400 TSA 402
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
118-403 8.25e-29

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: 112.40  E-value: 8.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 118 EGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDfTCRSTEEteawFIDSFEEWRKAQNLSNFILLG 197
Cdd:COG0596  21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA-GGYTLDD----LADDLAALLDALGLERVVLVG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 198 HSFGGYVAAKYALKHPEHVQHLILVGsagfsaeadaksEWLTKFRAtwkgavlnHLWESNFTPQKLVRglgpwgpglvnr 277
Cdd:COG0596  96 HSMGGMVALELAARHPERVAGLVLVD------------EVLAALAE--------PLRRPGLAPEALAA------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 278 yttarfgahsegtglteeeaklltdyvyhtlaakasgelclkyifSFGAFARKPLLQSASEWKVPTTFIYGMNDWM-NYQ 356
Cdd:COG0596 144 ---------------------------------------------LLRALARTDLRERLARITVPTLVIWGEKDPIvPPA 178
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 30686425 357 GAVEARKSMKvPCEIIRVPQGGHFVFIDNPIGFHSAVlyacRKFISQ 403
Cdd:COG0596 179 LARRLAELLP-NAELVVLPGAGHFPPLEQPEAFAAAL----RDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
121-386 4.89e-26

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: 105.28  E-value: 4.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   121 PTLVMVHGYGASQGFFFRNFDALA-SRFRVIAIDQLGWGGSSRPdfTCRSTEETEAwFIDSFEEWRKAQNLSNFILLGHS 199
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDD-LAEDLEYILEALGLEKVNLVGHS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   200 FGGYVAAKYALKHPEHVQHLILVGSagfsaeadakSEWLTKFRATWKGAVLNHLWESNFTPQKLVRGLGpwgpglvNRYT 279
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGA----------LDPPHELDEADRFILALFPGFFDGFVADFAPNPL-------GRLV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   280 TARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELClkYIFSFGAFARKPLLQSASEWKVPTTFIYGMNDWMN-YQGA 358
Cdd:pfam00561 141 AKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTG--ALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVpPQAL 218
                         250       260
                  ....*....|....*....|....*....
gi 30686425   359 VEARKsmKVPCEI-IRVPQGGHFVFIDNP 386
Cdd:pfam00561 219 EKLAQ--LFPNARlVVIPDAGHFAFLEGP 245
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
114-224 1.53e-19

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 88.21  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   114 FDAKEGAPTLVMVHGYGASQGFFFRNFDALASR--FRVIAIDQLGWGGSSRPDFtcrSTEE--TEAWFIDSFEEWRKAQN 189
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPGMSHEYLENLRELLKEegREVIMYDQLGCGYSDQPDD---SDEElwTIDYFVDELEEVREKLG 95
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 30686425   190 LSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGS 224
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSM 130
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
16-418 0e+00

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 751.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   16 ISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSK 95
Cdd:PLN02894   1 MKVQLRGHEIPGHGAASSAAASAAASAETSRTRSLWPSPLRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   96 IRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEA 175
Cdd:PLN02894  81 VRWFRSASNEPRFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  176 WFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWE 255
Cdd:PLN02894 161 WFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTKFRATWKGAVLNHLWE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  256 SNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQS 335
Cdd:PLN02894 241 SNFTPQKIIRGLGPWGPNLVRRYTTARFGAHSTGDILSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLES 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  336 ASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHdQQLLDGL 415
Cdd:PLN02894 321 ASEWKVPTTFIYGRHDWMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYACRKYLSPDREE-RALPEGL 399

                 ...
gi 30686425  416 RLV 418
Cdd:PLN02894 400 TSA 402
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
118-403 8.25e-29

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: 112.40  E-value: 8.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 118 EGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDfTCRSTEEteawFIDSFEEWRKAQNLSNFILLG 197
Cdd:COG0596  21 PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA-GGYTLDD----LADDLAALLDALGLERVVLVG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 198 HSFGGYVAAKYALKHPEHVQHLILVGsagfsaeadaksEWLTKFRAtwkgavlnHLWESNFTPQKLVRglgpwgpglvnr 277
Cdd:COG0596  96 HSMGGMVALELAARHPERVAGLVLVD------------EVLAALAE--------PLRRPGLAPEALAA------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 278 yttarfgahsegtglteeeaklltdyvyhtlaakasgelclkyifSFGAFARKPLLQSASEWKVPTTFIYGMNDWM-NYQ 356
Cdd:COG0596 144 ---------------------------------------------LLRALARTDLRERLARITVPTLVIWGEKDPIvPPA 178
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 30686425 357 GAVEARKSMKvPCEIIRVPQGGHFVFIDNPIGFHSAVlyacRKFISQ 403
Cdd:COG0596 179 LARRLAELLP-NAELVVLPGAGHFPPLEQPEAFAAAL----RDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
121-386 4.89e-26

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: 105.28  E-value: 4.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   121 PTLVMVHGYGASQGFFFRNFDALA-SRFRVIAIDQLGWGGSSRPdfTCRSTEETEAwFIDSFEEWRKAQNLSNFILLGHS 199
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRP--KAQDDYRTDD-LAEDLEYILEALGLEKVNLVGHS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   200 FGGYVAAKYALKHPEHVQHLILVGSagfsaeadakSEWLTKFRATWKGAVLNHLWESNFTPQKLVRGLGpwgpglvNRYT 279
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGA----------LDPPHELDEADRFILALFPGFFDGFVADFAPNPL-------GRLV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   280 TARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELClkYIFSFGAFARKPLLQSASEWKVPTTFIYGMNDWMN-YQGA 358
Cdd:pfam00561 141 AKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTG--ALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVpPQAL 218
                         250       260
                  ....*....|....*....|....*....
gi 30686425   359 VEARKsmKVPCEI-IRVPQGGHFVFIDNP 386
Cdd:pfam00561 219 EKLAQ--LFPNARlVVIPDAGHFAFLEGP 245
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
114-224 1.53e-19

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 88.21  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   114 FDAKEGAPTLVMVHGYGASQGFFFRNFDALASR--FRVIAIDQLGWGGSSRPDFtcrSTEE--TEAWFIDSFEEWRKAQN 189
Cdd:TIGR01250  19 TGGEGEKIKLLLLHGGPGMSHEYLENLRELLKEegREVIMYDQLGCGYSDQPDD---SDEElwTIDYFVDELEEVREKLG 95
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 30686425   190 LSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGS 224
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSM 130
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
116-225 1.94e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 80.82  E-value: 1.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 116 AKEGAPTLVMVHGYGASQGFFFRNFDALASR-FRVIAIDQLGWGGSSRPDFTCRSTEETEAwFIDSFEEWRKAQNLSNFI 194
Cdd:COG2267  24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVD-DLRAALDALRARPGLPVV 102
                        90       100       110
                ....*....|....*....|....*....|.
gi 30686425 195 LLGHSFGGYVAAKYALKHPEHVQHLILVGSA 225
Cdd:COG2267 103 LLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
78-230 9.75e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.14  E-value: 9.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   78 TPYVQEQVSIG-----SGP-------PGSKIRWFRStsnesryintvtfdAKEGAPTLVMVHGYGASQGFFFRNFDALAS 145
Cdd:PRK14875  91 APFARRFAPEGideedAGPaprkariGGRTVRYLRL--------------GEGDGTPVVLIHGFGGDLNNWLFNHAALAA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  146 RFRVIAIDQLGWGGSSRpdftcRSTEETEAWFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSA 225
Cdd:PRK14875 157 GRPVIALDLPGHGASSK-----AVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPA 231

                 ....*
gi 30686425  226 GFSAE 230
Cdd:PRK14875 232 GLGPE 236
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
122-384 1.09e-15

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: 76.10  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   122 TLVMVHGYGASQGFFFRNFDALASR-FRVIAIDQLGWGGSsrpdftcrsteETEAWFIDSFEEW-----------RKAQN 189
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRS-----------DGKRGHVPSFDDYvddldtfvdkiREEHP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   190 LSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKseWLTKFRATWKGAVLnhlwesnftPQKLVRGlgp 269
Cdd:pfam12146  75 GLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAP--PILKLLAKLLGKLF---------PRLRVPN--- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   270 wgpglvnryttarfgahsegtglteeeaKLLTDYVYH---TLAAKASGELCLKYI------FSFGAFARkpLLQSASEWK 340
Cdd:pfam12146 141 ----------------------------NLLPDSLSRdpeVVAAYAADPLVHGGIsartlyELLDAGER--LLRRAAAIT 190
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 30686425   341 VPTTFIYGMNDWM-NYQGAVEARKSMKVP-CEIIRVPQGGHFVFID 384
Cdd:pfam12146 191 VPLLLLHGGADRVvDPAGSREFYERAGSTdKTLKLYPGLYHELLNE 236
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
100-381 7.69e-13

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 69.52  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  100 RSTSNESRYintvtFDAKEGA---PTLVMVHGYgASQGFFFRN-FDALASRFRVIAIDQLGWGGSSRP------DFTcrs 169
Cdd:PLN03084 109 QASSDLFRW-----FCVESGSnnnPPVLLIHGF-PSQAYSYRKvLPVLSKNYHAIAFDWLGFGFSDKPqpgygfNYT--- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  170 TEEteawFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAgFSAEADAKSEWLTKFRATWKGAV 249
Cdd:PLN03084 180 LDE----YVSSLESLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNPP-LTKEHAKLPSTLSEFSNFLLGEI 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  250 LNH--LWESNftpqKLVRGLGPWgpglvnryttarfgahsegtGLTEEEAKLltdYVYHTLAAKASGelclkyiFSFGAF 327
Cdd:PLN03084 255 FSQdpLRASD----KALTSCGPY--------------------AMKEDDAMV---YRRPYLTSGSSG-------FALNAI 300
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30686425  328 AR---KPLLQSASE---------WKVPTTFIYGMND-WMNYQGAVEARKSMKVpcEIIRVPQGGHFV 381
Cdd:PLN03084 301 SRsmkKELKKYIEEmrsiltdknWKTPITVCWGLRDrWLNYDGVEDFCKSSQH--KLIELPMAGHHV 365
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
123-243 1.65e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 63.26  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   123 LVMVHGYGASQGFFFRnfdALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEAwFIDSFEEWRKaqnlsnFILLGHSFGG 202
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA---LLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAA-LLDELGAARP------VVLVGHSLGG 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30686425   203 YVAAKYAlkHPEHVQHLILVGSAGFSAEADAKSEWLTKFRA 243
Cdd:pfam12697  71 AVALAAA--AAALVVGVLVAPLAAPPGLLAALLALLARLGA 109
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
121-222 1.01e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 59.37  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  121 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDftCRSTEETEawfIDSFEEWrkAQNLSNFI------ 194
Cdd:PLN02824  30 PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPN--PRSAPPNS---FYTFETW--GEQLNDFCsdvvgd 102
                         90       100       110
                 ....*....|....*....|....*....|.
gi 30686425  195 ---LLGHSFGGYVAAKYALKHPEHVQHLILV 222
Cdd:PLN02824 103 pafVICNSVGGVVGLQAAVDAPELVRGVMLI 133
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
97-386 1.20e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 59.10  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   97 RWFRSTSNESRYINtvtfdakEGA-PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPD-FTCRSTEETE 174
Cdd:PRK03204  17 RWFDSSRGRIHYID-------EGTgPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSgFGYQIDEHAR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  175 AW--FIDSFeewrkaqNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRA-TWKGAVLN 251
Cdd:PRK03204  90 VIgeFVDHL-------GLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPADTLAMKAFSRVMSSpPVQYAILR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  252 HlwesNFTPQKLVRGlgpwgpGLVNRYTTARFgAHSEGTGLTEEEAKLLTDYVYHTLAAKAsgelclkyifSFGAFARKP 331
Cdd:PRK03204 163 R----NFFVERLIPA------GTEHRPSSAVM-AHYRAVQPNAAARRGVAEMPKQILAARP----------LLARLAREV 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30686425  332 LLQSASEwkvPTTFIYGMNDWMNYQGAVEARKSMKVP-CEIIRVPQGGHFVFIDNP 386
Cdd:PRK03204 222 PATLGTK---PTLLVWGMKDVAFRPKTILPRLRATFPdHVLVELPNAKHFIQEDAP 274
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
115-228 1.25e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.10  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 115 DAKEGAPTLVMVHGYGASQ-GFFFRNFDALASR-FRVIAIDQLGWGGSSRpDFTCRSTEETEAWFidsfeEWRKAQNL-- 190
Cdd:COG1506  18 ADGKKYPVVVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAG-DWGGDEVDDVLAAI-----DYLAARPYvd 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30686425 191 -SNFILLGHSFGGYVAAKYALKHPEHVQHLILVgsAGFS 228
Cdd:COG1506  92 pDRIGIYGHSYGGYMALLAAARHPDRFKAAVAL--AGVS 128
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
108-226 4.61e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 57.54  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  108 YINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPdftcrsteeteAWFIDSFEEWrkA 187
Cdd:PLN02679  76 YLVKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP-----------PGFSYTMETW--A 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30686425  188 QNLSNF---------ILLGHSFGGY---VAAkyALKHPEHVQHLILVGSAG 226
Cdd:PLN02679 143 ELILDFleevvqkptVLIGNSVGSLacvIAA--SESTRDLVRGLVLLNCAG 191
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
46-222 1.12e-08

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 56.74  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   46 RWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSKIRW----------FRSTSNESRYINTVTFD 115
Cdd:PLN03087 117 KLKMEGKCVGSCEKTSNKRKRGTKKSTLTVNSTIVEMLRGKIGGQQLHPAPRWsdcdckfctsWLSSSNESLFVHVQQPK 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  116 AKEGAPTLVMVHGYGASQGFF----FRNF-DALASRFRVIAIDQLGWGGSSRPD---FTCRS-TEETEAWFIDSFeewrk 186
Cdd:PLN03087 197 DNKAKEDVLFIHGFISSSAFWtetlFPNFsDAAKSTYRLFAVDLLGFGRSPKPAdslYTLREhLEMIERSVLERY----- 271
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 30686425  187 aqNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILV 222
Cdd:PLN03087 272 --KVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305
YpfH COG0400
Predicted esterase [General function prediction only];
116-221 1.67e-08

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 54.14  E-value: 1.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 116 AKEGAPTLVMVHGYGASQGFFFRNFDALAS-RFRVIAID---QLGWGGSSRPDFTCRSTEETEAWF------IDSF-EEW 184
Cdd:COG0400   1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALpGAAVLAPRapvPEGPGGRAWFDLSFLEGREDEEGLaaaaeaLAAFiDEL 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30686425 185 RKAQNL--SNFILLGHSFGGYVAAKYALKHPEHVQHLIL 221
Cdd:COG0400  81 EARYGIdpERIVLAGFSQGAAMALSLALRRPELLAGVVA 119
PLN02578 PLN02578
hydrolase
118-236 1.71e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 56.00  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  118 EGAPtLVMVHGYGASqGFFFR-NFDALASRFRVIAIDQLGWGGSSRPdftcrSTEETEAWFIDSFEEWRKAQNLSNFILL 196
Cdd:PLN02578  85 EGLP-IVLIHGFGAS-AFHWRyNIPELAKKYKVYALDLLGFGWSDKA-----LIEYDAMVWRDQVADFVKEVVKEPAVLV 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30686425  197 GHSFGGYVAAKYALKHPEHVQHLILVGSAG-FSAEADAKSE 236
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNSAGqFGSESREKEE 198
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
123-224 3.43e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 50.98  E-value: 3.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 123 LVMVHGYGASQGFFFRNFDALASR-FRVIAIDqLGWGGssrpdftcRSTEETEAWFIDSFEEWRKAQNLSNFILLGHSFG 201
Cdd:COG1075   8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALN-YPSTN--------GSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMG 78
                        90       100
                ....*....|....*....|....*.
gi 30686425 202 GYVaAKYALKH---PEHVQHLILVGS 224
Cdd:COG1075  79 GLV-ARYYLKRlggAAKVARVVTLGT 103
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
118-237 1.22e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 52.71  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  118 EGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSrpDFTCRSTEETEAWFIdsfeewRKAQNLSnfILLG 197
Cdd:PRK10349  11 QGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR--GFGALSLADMAEAVL------QQAPDKA--IWLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30686425  198 HSFGGYVAAKYALKHPEHVQHLILVGSAG-FSaeadAKSEW 237
Cdd:PRK10349  81 WSLGGLVASQIALTHPERVQALVTVASSPcFS----ARDEW 117
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
183-225 3.08e-07

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 50.55  E-value: 3.08e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 30686425 183 EWRKAQNLSNFILLGHSFGGYVAAKYALKHPEhVQHLILVGSA 225
Cdd:COG2945  88 DWLRAQNPLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVAPP 129
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
115-217 1.84e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 46.14  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  115 DAKEGAPtLVMVHGYGASQgFFFRN-FDALASRFRVIAIDQLGWGGSSRPDFTCRSTEET---EAWFidsfeewrKAQNL 190
Cdd:PRK03592  23 ETGEGDP-IVFLHGNPTSS-YLWRNiIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHArylDAWF--------DALGL 92
                         90       100
                 ....*....|....*....|....*..
gi 30686425  191 SNFILLGHSFGGYVAAKYALKHPEHVQ 217
Cdd:PRK03592  93 DDVVLVGHDWGSALGFDWAARHPDRVR 119
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
114-385 4.73e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 44.55  E-value: 4.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 114 FDAKEGAPTLVMVHGYGASQgFFFRNF-DALASR-FRVIAIDQLGWGGSSRpDFTCRSTEEteaWFIDSFEEWRKAQNL- 190
Cdd:COG1647   9 FFLEGGRKGVLLLHGFTGSP-AEMRPLaEALAKAgYTVYAPRLPGHGTSPE-DLLKTTWED---WLEDVEEAYEILKAGy 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 191 SNFILLGHSFGGYVAAKYALKHPEhVQHLILVGSAGFSAEADAK-SEWLTKFRATWKGavlnhlwesnftpqklvrglgp 269
Cdd:COG1647  84 DKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPlLPLLKYLARSLRG---------------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 270 wgpglvnryttarfgahsegtGLTEEEAKLLTDYVYHTLAAKAsgelcLKYIFSFGAFARKPLlqsaSEWKVPTTFIYGM 349
Cdd:COG1647 141 ---------------------IGSDIEDPEVAEYAYDRTPLRA-----LAELQRLIREVRRDL----PKITAPTLIIQSR 190
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 30686425 350 NDWM-NYQGAVEARKSMKVP-CEIIRVPQGGHFVFIDN 385
Cdd:COG1647 191 KDEVvPPESARYIYERLGSPdKELVWLEDSGHVITLDK 228
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
115-250 9.77e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 43.75  E-value: 9.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 115 DAKEGAPTLVMVHGYGASQGFFFRNFDALASR-FRVIAIDQLGWGGSS-RP-DFTCRSTEETEAWfidsfeeWRKAQNLS 191
Cdd:COG1073  32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEgEPrEEGSPERRDARAA-------VDYLRTLP 104
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30686425 192 NF-----ILLGHSFGGYVAAKYALKHPEhVQHLILVgsAGF-SAEADAKSEWLTKFRATWKGAVL 250
Cdd:COG1073 105 GVdperiGLLGISLGGGYALNAAATDPR-VKAVILD--SPFtSLEDLAAQRAKEARGAYLPGVPY 166
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
91-243 2.34e-04

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 42.92  E-value: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  91 PPG--SKIRWFRSTSNESRYINTVT----FDAKEGAPTLVMVHGYGASQGFFFRN------FDALASR-----FRVIAID 153
Cdd:COG2382  77 PHGtvETVTYPSKALGRTRRVWVYLppgyDNPGKKYPVLYLLDGGGGDEQDWFDQgrlptiLDNLIAAgkippMIVVMPD 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 154 QLGWGGSSRPDFTcrsTEETEAWFIDSF-----EEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFS 228
Cdd:COG2382 157 GGDGGDRGTEGPG---NDAFERFLAEELipfveKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWW 233
                       170
                ....*....|....*.
gi 30686425 229 AEADAKS-EWLTKFRA 243
Cdd:COG2382 234 PPGDADRgGWAELLAA 249
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
115-205 2.63e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.79  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 115 DAKEGAPTLVMVHGYGASQGFFFRNFDALASR-FRVIAIDQLG--WGGSSRPDFTCRSTEETEAWF---------IDSFE 182
Cdd:COG4188  57 PAGGPFPLVVLSHGLGGSREGYAYLAEHLASHgYVVAAPDHPGsnAADLSAALDGLADALDPEELWerpldlsfvLDQLL 136
                        90       100       110
                ....*....|....*....|....*....|
gi 30686425 183 EWRKAQ-------NLSNFILLGHSFGGYVA 205
Cdd:COG4188 137 ALNKSDpplagrlDLDRIGVIGHSLGGYTA 166
PRK05855 PRK05855
SDR family oxidoreductase;
119-163 6.50e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 41.89  E-value: 6.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 30686425  119 GAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRP 163
Cdd:PRK05855  24 DRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAP 68
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
112-212 1.14e-03

Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.


Pssm-ID: 432755  Cd Length: 254  Bit Score: 40.38  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   112 VTFDAKEGA-PTLVMVHGYGASQGFFFRNFDALAS-RFRVIAIDQLGWGGSSRPDFtcRSTEETEAWFIDSFEEWRKAQ- 188
Cdd:pfam12740   8 VFTPTEAGTyPVLLFLHGYLLYNSFYSQLLQHIAShGFIVVAPQLYLVAGPDGDEI--KSAAKVANWLSNGLQHVLPEGv 85
                          90       100
                  ....*....|....*....|....*.
gi 30686425   189 --NLSNFILLGHSFGGYVAAKYALKH 212
Cdd:pfam12740  86 epDLSKLALSGHSRGGKTAFALALGH 111
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
195-251 1.26e-03

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


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 40.14  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   195 LLGHSFGGYVAAKYALKHPEHVQHlilVGSagFSAEADAK-SEWLTKFRATWK--GAVLN 251
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGS---VSS--FSPILNPSnSMWGPEDDPAWQegDPVLL 168
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
119-223 1.79e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 39.82  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  119 GAPTLVMVHGYGASQgfffRNFDALASR---FRVIAIDQLGWGGSsrpdftcrsteetEAWFIDSFEEWR-------KAQ 188
Cdd:PRK11126   1 GLPWLVFLHGLLGSG----QDWQPVGEAlpdYPRLYIDLPGHGGS-------------AAISVDGFADVSrllsqtlQSY 63
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 30686425  189 NLSNFILLGHSFGGYVAAKYAL-KHPEHVQHLILVG 223
Cdd:PRK11126  64 NILPYWLVGYSLGGRIAMYYACqGLAGGLCGLIVEG 99
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
119-222 2.47e-03

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 40.07  E-value: 2.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425 119 GAPTLVMVHGYGASqGFFFRNF-DALASRFRVIAIDQLGWGGSSRPDftcRSTEETEAWFIdsfEEWRKAQNLSNFILLG 197
Cdd:COG3319 600 SGPPLFCVHPAGGN-VLCYRPLaRALGPDRPVYGLQAPGLDGGEPPP---ASVEEMAARYV---EAIRAVQPEGPYHLLG 672
                        90       100
                ....*....|....*....|....*...
gi 30686425 198 HSFGGYVA---AKYALKHPEHVQHLILV 222
Cdd:COG3319 673 WSFGGLVAyemARQLEAQGEEVALLVLL 700
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
121-224 6.30e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 37.75  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425   121 PTLVMVHGYGASqGFFFRNF-DALASRFRVIAIDQLGWGGSSRPdftCRSTEETEAWFIDsfeEWRKAQNLSNFILLGHS 199
Cdd:pfam00975   1 RPLFCFPPAGGS-ASSFRSLaRRLPPPAEVLAVQYPGRGRGEPP---LNSIEALADEYAE---ALRQIQPEGPYALFGHS 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 30686425   200 FGGYVAAKYALK-----HPehVQHLILVGS 224
Cdd:pfam00975  74 MGGMLAFEVARRlerqgEA--VRSLFLSDA 101
PRK08775 PRK08775
homoserine O-succinyltransferase;
145-225 7.68e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686425  145 SRFRVIAIDQLGWGGSSRPdftcrsteeteawFIDSFEEWR-------KAQNLSNFILLGHSFGGYVAAKYALKHPEHVQ 217
Cdd:PRK08775  98 ARFRLLAFDFIGADGSLDV-------------PIDTADQADaiallldALGIARLHAFVGYSYGALVGLQFASRHPARVR 164

                 ....*...
gi 30686425  218 HLILVGSA 225
Cdd:PRK08775 165 TLVVVSGA 172
 
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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