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Conserved domains on  [gi|157819471|ref|NP_001099464|]
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epoxide hydrolase 4 [Rattus norvegicus]

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, ...
2-261 8.11e-40

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: 137.44  E-value: 8.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596   27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596  105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596  149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200
                        250       260
                 ....*....|....*....|
gi 157819471 242 WLQQDQPDIVNGLIWAFLRE 261
Cdd:COG0596  201 FPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-261 8.11e-40

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: 137.44  E-value: 8.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596   27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596  105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596  149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200
                        250       260
                 ....*....|....*....|
gi 157819471 242 WLQQDQPDIVNGLIWAFLRE 261
Cdd:COG0596  201 FPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
1-244 1.00e-27

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: 106.82  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234

                  ....*..
gi 157819471  238 EGSHWLQ 244
Cdd:pfam00561 235 DAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
2-255 1.95e-26

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 107.76  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCV-LIGHDWGGMIA 80
Cdd:PRK05855  29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRLPELMFSINDFKALKH 145
Cdd:PRK05855 109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855 188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157819471 222 VTKIYVKNYFRLTIlsEGSHWLQQDQPDIVNGLI 255
Cdd:PRK05855 254 DLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
1-98 6.58e-08

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: 52.38  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105
                          90       100
                  ....*....|....*....|....
gi 157819471   75 WGGMIAWLIAVCYPEMIMKLIVIN 98
Cdd:TIGR01250 106 WGGMLAQEYALKYGQHLKGLIISS 129
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-261 8.11e-40

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: 137.44  E-value: 8.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596   27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596  105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596  149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200
                        250       260
                 ....*....|....*....|
gi 157819471 242 WLQQDQPDIVNGLIWAFLRE 261
Cdd:COG0596  201 FPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
1-244 1.00e-27

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: 106.82  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234

                  ....*..
gi 157819471  238 EGSHWLQ 244
Cdd:pfam00561 235 DAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
2-255 1.95e-26

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 107.76  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCV-LIGHDWGGMIA 80
Cdd:PRK05855  29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRLPELMFSINDFKALKH 145
Cdd:PRK05855 109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855 188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157819471 222 VTKIYVKNYFRLTIlsEGSHWLQQDQPDIVNGLI 255
Cdd:PRK05855 254 DLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
1-266 3.69e-14

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 70.79  E-value: 3.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYK-------LDCLIadikdvlDSLGYNKCVLIGH 73
Cdd:PRK03592  30 IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP--DIDYTfadharyLDAWF-------DALGLDDVVLVGH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  74 DWGGMIAWLIAVCYPEMIMKLivinfphpsVFTEYILRHPA-QLFRSSFYYFFQIPRLP----ELMFSINDF--KALKHL 146
Cdd:PRK03592 101 DWGSALGFDWAARHPDRVRGI---------AFMEAIVRPMTwDDFPPAVRELFQALRSPgegeEMVLEENVFieRVLPGS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 147 FTsqstgigrkgRQLTTEDLEAYVYVFSQPGA----LSGP---------------INHYRNIFSCLPlkhhmvtTPTLLL 207
Cdd:PRK03592 172 IL----------RPLSDEEMAVYRRPFPTPESrrptLSWPrelpidgepadvvalVEEYAQWLATSD-------VPKLLI 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 208 WGEEDA-FMEVEMAEVTKIYVKNYFrLTILSEGSHWLQQDQPDIVNGLIWAFLREETRRD 266
Cdd:PRK03592 235 NAEPGAiLTTGAIRDWCRSWPNQLE-ITVFGAGLHFAQEDSPEEIGAAIAAWLRRLRLAV 293
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-98 1.82e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 67.72  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPI-HQESYklDCLIADIKDVLDSL---GYNKCVLIGHDWG 76
Cdd:COG2267   32 VLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRgHVDSF--DDYVDDLRAALDALrarPGLPVVLLGHSMG 109
                         90       100
                 ....*....|....*....|..
gi 157819471  77 GMIAWLIAVCYPEMIMKLIVIN 98
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLLA 131
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
2-98 3.01e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 65.37  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PRK00870  50 LLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIG 129
                         90
                 ....*....|....*...
gi 157819471  81 WLIAVCYPEMIMKLIVIN 98
Cdd:PRK00870 130 LRLAAEHPDRFARLVVAN 147
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
1-255 1.11e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 64.13  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQE--SYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGM 78
Cdd:PLN03084 130 VLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLESLIDELKSDKVSLVVQGYFSP 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  79 IAWLIAVCYPEMIMKLIVINFPhpsvFTEYILRHPAQLfrSSFYYFFqiprLPELmFSINDFKALKHLFTSQSTgigrkg 158
Cdd:PLN03084 210 PVVKYASAHPDKIKKLILLNPP----LTKEHAKLPSTL--SEFSNFL----LGEI-FSQDPLRASDKALTSCGP------ 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 159 RQLTTEDleAYVYvfSQPGALSGP-------------------INHYRNIFSCLPLKhhmvtTPTLLLWGEEDAFMEVEM 219
Cdd:PLN03084 273 YAMKEDD--AMVY--RRPYLTSGSsgfalnaisrsmkkelkkyIEEMRSILTDKNWK-----TPITVCWGLRDRWLNYDG 343
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157819471 220 AEVtkiYVKNY-FRLTILSEGSHWLQQDQPD----IVNGLI 255
Cdd:PLN03084 344 VED---FCKSSqHKLIELPMAGHHVQEDCGEelggIISGIL 381
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
1-252 2.14e-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: 61.72  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFpefWYSWRHQLREFKSEYRVVALDLRGYGESDAPihqeSYKLDCLiADIKDVLDSLG-YNKCVLIGHDWGGMI 79
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADL-ADLAALLDELGaARPVVLVGHSLGGAV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   80 AWLIAvcyPEMIMKLIVIN--FPHPSVFTEYILRHPAQLFRSSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRK 157
Cdd:pfam12697  73 ALAAA---AAALVVGVLVAplAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  158 GRQLTTEDLEAyvyvfsqpgalsgpinhyrnifsclplkhhmVTTPTLLLWgEEDAFMEVEMAEVTKiyVKNYFRLTILS 237
Cdd:pfam12697 150 LALLPLAAWRD-------------------------------LPVPVLVLA-EEDRLVPELAQRLLA--ALAGARLVVLP 195
                         250
                  ....*....|....*
gi 157819471  238 EGSHWLqQDQPDIVN 252
Cdd:pfam12697 196 GAGHLP-LDDPEEVA 209
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
1-255 3.75e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 61.80  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PRK03204  37 ILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERP-SGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPIS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  81 WLIAVCYPEMIMKLIVINfphpsvfteyilrhpaqlfrssfYYFFQIPRLPELMFSI------NDFKALKHLFTSQSTGI 154
Cdd:PRK03204 116 MAVAVERADRVRGVVLGN-----------------------TWFWPADTLAMKAFSRvmssppVQYAILRRNFFVERLIP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 155 GRKGRQLTTEDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKHHMV--------TTPTLLLWGEED-AFM-EVEMAEVTK 224
Cdd:PRK03204 173 AGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLArevpatlgTKPTLLVWGMKDvAFRpKTILPRLRA 252
                        250       260       270
                 ....*....|....*....|....*....|.
gi 157819471 225 IYVKnyFRLTILSEGSHWLQQDQPDIVNGLI 255
Cdd:PRK03204 253 TFPD--HVLVELPNAKHFIQEDAPDRIAAAI 281
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
1-261 8.74e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 54.64  E-value: 8.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEF-WYSWRHQLREFKSE-YRVVALDLRGYGESDAPIHQEsykldcLIADIKDVLD---SLGY---NKCVLIG 72
Cdd:COG1506   26 VVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDylaARPYvdpDRIGIYG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  73 HDWGGMIAWLIAVCYPEMImKLIVinfphpsvfteyilrhpaqlfrssfyyffqiprlpeLMFSINDFKAlkhlFTSQST 152
Cdd:COG1506  100 HSYGGYMALLAAARHPDRF-KAAV------------------------------------ALAGVSDLRS----YYGTTR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 153 GIGRKGRQLTTEDLEAYVyvfsqpgALSgPINHYRNIfsclplkhhmvTTPTLLLWGEEDAFMEVEMAE--VTKIYVKN- 229
Cdd:COG1506  139 EYTERLMGGPWEDPEAYA-------ARS-PLAYADKL-----------KTPLLLIHGEADDRVPPEQAErlYEALKKAGk 199
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157819471 230 YFRLTILSEGSHWLQQDQPDIVNGLIWAFLRE 261
Cdd:COG1506  200 PVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PLN02578 PLN02578
hydrolase
1-98 1.03e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 55.23  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQesYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PLN02578  89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTA 166
                         90
                 ....*....|....*...
gi 157819471  81 WLIAVCYPEMIMKLIVIN 98
Cdd:PLN02578 167 LSTAVGYPELVAGVALLN 184
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
2-260 1.26e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.95  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESykLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:PRK14875 135 VLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELAAAVLAFLDALGIERAHLVGHSMGGAVAL 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  82 LIAVCYPEMIMKLIVINfPH---PSVFTEYIlrhpaQLF-RSSfyyffqiprlpelmfSINDFK-ALKHLFTSQSTgigr 156
Cdd:PRK14875 213 RLAARAPQRVASLTLIA-PAglgPEINGDYI-----DGFvAAE---------------SRRELKpVLELLFADPAL---- 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 157 KGRQLtTEDLEAYVYVFSQPGALSGPINH----------YRNIFSCLPlkhhmvtTPTLLLWGEEDAFMEVEMAEVtkiy 226
Cdd:PRK14875 268 VTRQM-VEDLLKYKRLDGVDDALRALADAlfaggrqrvdLRDRLASLA-------IPVLVIWGEQDRIIPAAHAQG---- 335
                        250       260       270
                 ....*....|....*....|....*....|....
gi 157819471 227 VKNYFRLTILSEGSHWLQQDQPDIVNGLIWAFLR 260
Cdd:PRK14875 336 LPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
1-98 6.58e-08

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: 52.38  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105
                          90       100
                  ....*....|....*....|....
gi 157819471   75 WGGMIAWLIAVCYPEMIMKLIVIN 98
Cdd:TIGR01250 106 WGGMLAQEYALKYGQHLKGLIISS 129
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
1-95 1.80e-07

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: 50.68  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFPEfwYSWR-----HQLreFKSEYRVVALDLRGYGESD-APIHQESYklDCLIADIKDVLDSL----GYNKCVL 70
Cdd:pfam12146   7 VVLVHGLGE--HSGRyahlaDAL--AAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLPLFL 80
                          90       100
                  ....*....|....*....|....*
gi 157819471   71 IGHDWGGMIAWLIAVCYPEMIMKLI 95
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLI 105
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
1-251 1.30e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 48.68  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMiA 80
Cdd:PLN02679  91 VLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP-PGFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSL-A 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  81 WLIAVC--YPEMIMKLIVIN----FPHPSVFTEYILRHPAQLFrSSFYYFFQIPRLPELMFS-INDFKALKHLFTSQstg 153
Cdd:PLN02679 169 CVIAASesTRDLVRGLVLLNcaggMNNKAVVDDWRIKLLLPLL-WLIDFLLKQRGIASALFNrVKQRDNLKNILLSV--- 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 154 IGRKgrQLTTEDLeayVYVFSQPGALSGPINHYRNIFSCLPLKHHM-----VTTPTLLLWGEEDAFMEVEmAEVTKIYVK 228
Cdd:PLN02679 245 YGNK--EAVDDEL---VEIIRGPADDEGALDAFVSIVTGPPGPNPIkliprISLPILVLWGDQDPFTPLD-GPVGKYFSS 318
                        250       260
                 ....*....|....*....|....*...
gi 157819471 229 -----NYFRLTILSEGSHWLQQDQPDIV 251
Cdd:PLN02679 319 lpsqlPNVTLYVLEGVGHCPHDDRPDLV 346
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
24-265 2.44e-06

poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans, Pseudomonas putida BM01, and related species. This enzyme is part of polyester storage and mobilization system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on carbon sources such as benzoic acid or phenylacetic acid. [Energy metabolism, Other]


Pssm-ID: 131294  Cd Length: 276  Bit Score: 47.68  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   24 EYRVVALDLRGYGESDAPIHqeSYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPHPS 103
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  104 VFTeyilrhPAQlfrssfyyffqiPRLPELMFSINDFKALKHLFTSQSTGIGRKGRQLTTEDLEAYVYVFSqpgalSGPI 183
Cdd:TIGR02240 129 VMV------PGK------------PKVLMMMASPRRYIQPSHGIHIAPDIYGGAFRRDPELAMAHASKVRS-----GGKL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  184 NHYRNIFSCLPLKH----HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGsHWLQQDQPDIVNGLIWAFL 259
Cdd:TIGR02240 186 GYYWQLFAGLGWTSihwlHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNA-ELHIIDDG-HLFLITRAEAVAPIIMKFL 263

                  ....*.
gi 157819471  260 REETRR 265
Cdd:TIGR02240 264 AEERQR 269
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
1-258 3.21e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 47.43  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQES-----YKLDCLIADIKDVLDSLGYNKCVLIGHDW 75
Cdd:PLN02824  32 LVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfYTFETWGEQLNDFCSDVVGDPAFVICNSV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  76 GGMIAWLIAVCYPEMIMKLIVINfphPSVFTEYILRHPA--QLFRSSFY----------YFFQIPRLPELMFSIndfkaL 143
Cdd:PLN02824 112 GGVVGLQAAVDAPELVRGVMLIN---ISLRGLHIKKQPWlgRPFIKAFQnllretavgkAFFKSVATPETVKNI-----L 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471 144 KHLFTSQStgigrkgrQLTTEDLEAYVyvfsQPGALSGPINHYRNI--FSCLPLKHHM---VTTPTLLLWGEEDAFMEVE 218
Cdd:PLN02824 184 CQCYHDDS--------AVTDELVEAIL----RPGLEPGAVDVFLDFisYSGGPLPEELlpaVKCPVLIAWGEKDPWEPVE 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157819471 219 MAEVTKIYvKNYFRLTILSEGSHWLQQDQPDIVNGLIWAF 258
Cdd:PLN02824 252 LGRAYANF-DAVEDFIVLPGVGHCPQDEAPELVNPLIESF 290
PRK10673 PRK10673
esterase;
19-98 6.76e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 46.26  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  19 REFKSEYRVVALDLRGYGESDapiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 98
Cdd:PRK10673  37 RDLVNDHDIIQVDMRNHGLSP---RDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
1-241 1.73e-05

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 44.81  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471    1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGEsdapiHQESYKLDclIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLGGLVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   81 WLIAVCYPEMIMKLIVI----------NFPH---PSVFTEYilrhpAQLFRSSFyyffqiprlpelMFSINDFKALKHLF 147
Cdd:TIGR01738  80 LHIAATHPDRVRALVTVasspcfsareDWPEgikPDVLTGF-----QQQLSDDY------------QRTIERFLALQTLG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471  148 TSQSTGIGRKGRQLttedleayvyVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEEDAFMEVEMAEVTKI 225
Cdd:TIGR01738 143 TPTARQDARALKQT----------LLARPTPNVQVLQAGLEILATVDLRQPLqnISVPFLRLYGYLDGLVPAKVVPMLDK 212
                         250
                  ....*....|....*.
gi 157819471  226 YVKnYFRLTILSEGSH 241
Cdd:TIGR01738 213 LAP-HSELYIFAKAAH 227
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
2-118 2.73e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 44.16  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGF---PEFWYSWRHQLRefKSEYRVVALDLRGYGESDAPIHQESYKlDClIADIKDVLDSL--GYNKCVLIGHDWG 76
Cdd:COG1647   19 LLLHGFtgsPAEMRPLAEALA--KAGYTVYAPRLPGHGTSPEDLLKTTWE-DW-LEDVEEAYEILkaGYDKVIVIGLSMG 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157819471  77 GMIAWLIAVCYPEmIMKLIVIN----FPHPSVFTEYILRHPAQLFR 118
Cdd:COG1647   95 GLLALLLAARYPD-VAGLVLLSpalkIDDPSAPLLPLLKYLARSLR 139
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
2-101 2.75e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 42.12  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGFPEFWYSWRHQLREFKSE-YRVVALDlrgYGESDAPIHQESYKLDcliADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:COG1075    9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALN---YPSTNGSIEDSAEQLA---AFVDAVLAATGAEKVDLVGHSMGGLVA 82
                         90       100
                 ....*....|....*....|...
gi 157819471  81 -WLIAVC-YPEMIMKLIVINFPH 101
Cdd:COG1075   83 rYYLKRLgGAAKVARVVTLGTPH 105
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
47-106 3.05e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 38.53  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819471  47 YKLDCLIADIKDV-------LDSLGYNKC-VLIGHDWGGMIAWLIAVCYPEMIMKLI-VINFPHPSVFT 106
Cdd:PRK06765 134 YGMDFPVVTILDFvrvqkelIKSLGIARLhAVMGPSMGGMQAQEWAVHYPHMVERMIgVIGNPQNDAWT 202
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
2-114 5.29e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 37.87  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819471   2 LLLHGF---PEFWYS--WRHQLREFKSEYRVVALDLRGYGESDAPihQES-YKLDCLIADI-KDVLDSLGYNKCVLIGHD 74
Cdd:PLN03087 205 LFIHGFissSAFWTEtlFPNFSDAAKSTYRLFAVDLLGFGRSPKP--ADSlYTLREHLEMIeRSVLERYKVKSFHIVAHS 282
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157819471  75 WGGMIAWLIAVCYPEMIMKLIVINFPHPSV-----FTEYILRHPA 114
Cdd:PLN03087 283 LGCILALALAVKHPGAVKSLTLLAPPYYPVpkgvqATQYVMRKVA 327
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
25-89 8.89e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 36.48  E-value: 8.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819471  25 YRVVALDLRGYGESDAPI-----HQESYKLDCLIADIKDVLDSL------GYNKCVLIGHDWGGMIAWLIAVCYPE 89
Cdd:COG0412   57 YVVLAPDLYGRGGPGDDPdearaLMGALDPELLAADLRAALDWLkaqpevDAGRVGVVGFCFGGGLALLAAARGPD 132
 
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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