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Conserved domains on  [gi|1958675256|ref|XP_008768149|]
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epoxide hydrolase 4 isoform X1 [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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1958675256 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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234


                  ....*..
gi 1958675256 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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCV-LIGHDWGGMIA 80
Cdd:PRK05855   29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRLPELMFSINDFKALKH 145
Cdd:PRK05855  109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855  188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958675256 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 1958675256   1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105

                          90       100
                  ....*....|....*....|....
gi 1958675256  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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprlpelmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234


                  ....*..
gi 1958675256 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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCV-LIGHDWGGMIA 80
Cdd:PRK05855   29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRLPELMFSINDFKALKH 145
Cdd:PRK05855  109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855  188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYK-------LDCLIadikdvlDSLGYNKCVLIGH 73
Cdd:PRK03592   30 IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP--DIDYTfadharyLDAWF-------DALGLDDVVLVGH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  74 DWGGMIAWLIAVCYPEMIMKLivinfphpsVFTEYILRHPA-QLFRSSFYYFFQIPRLP----ELMFSINDF--KALKHL 146
Cdd:PRK03592  101 DWGSALGFDWAARHPDRVRGI---------AFMEAIVRPMTwDDFPPAVRELFQALRSPgegeEMVLEENVFieRVLPGS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 147 FTsqstgigrkgRQLTTEDLEAYVYVFSQPGA----LSGP---------------INHYRNIFSCLPlkhhmvtTPTLLL 207
Cdd:PRK03592  172 IL----------RPLSDEEMAVYRRPFPTPESrrptLSWPrelpidgepadvvalVEEYAQWLATSD-------VPKLLI 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 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 1958675256   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPI-HQESYklDCLIADIKDVLDSL---GYNKCVLIGHDWG 76
Cdd:COG2267    32 VLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRgHVDSF--DDYVDDLRAALDALrarPGLPVVLLGHSMG 109

                          90       100
                  ....*....|....*....|..
gi 1958675256  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 1958675256   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PRK00870   50 LLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIG 129

                          90
                  ....*....|....*...
gi 1958675256  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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQE--SYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGM 78
Cdd:PLN03084  130 VLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLESLIDELKSDKVSLVVQGYFSP 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  79 IAWLIAVCYPEMIMKLIVINFPhpsvFTEYILRHPAQLfrSSFYYFFqiprLPELmFSINDFKALKHLFTSQSTgigrkg 158
Cdd:PLN03084  210 PVVKYASAHPDKIKKLILLNPP----LTKEHAKLPSTL--SEFSNFL----LGEI-FSQDPLRASDKALTSCGP------ 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 159 RQLTTEDleAYVYvfSQPGALSGP-------------------INHYRNIFSCLPLKhhmvtTPTLLLWGEEDAFMEVEM 219
Cdd:PLN03084  273 YAMKEDD--AMVY--RRPYLTSGSsgfalnaisrsmkkelkkyIEEMRSILTDKNWK-----TPITVCWGLRDRWLNYDG 343

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958675256 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 1958675256   1 MLLLHGFpefWYSWRHQLREFKSEYRVVALDLRGYGESDAPihqeSYKLDCLiADIKDVLDSLG-YNKCVLIGHDWGGMI 79
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADL-ADLAALLDELGaARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  80 AWLIAvcyPEMIMKLIVIN--FPHPSVFTEYILRHPAQLFRSSFYYFFQIPRLPELMFSINDFKALKHLFTSQSTGIGRK 157
Cdd:pfam12697  73 ALAAA---AAALVVGVLVAplAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 158 GRQLTTEDLEAyvyvfsqpgalsgpinhyrnifsclplkhhmVTTPTLLLWgEEDAFMEVEMAEVTKiyVKNYFRLTILS 237
Cdd:pfam12697 150 LALLPLAAWRD-------------------------------LPVPVLVLA-EEDRLVPELAQRLLA--ALAGARLVVLP 195

                         250
                  ....*....|....*
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PRK03204   37 ILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERP-SGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  81 WLIAVCYPEMIMKLIVINfphpsvfteyilrhpaqlfrssfYYFFQIPRLPELMFSI------NDFKALKHLFTSQSTGI 154
Cdd:PRK03204  116 MAVAVERADRVRGVVLGN-----------------------TWFWPADTLAMKAFSRvmssppVQYAILRRNFFVERLIP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 155 GRKGRQLTTEDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKHHMV--------TTPTLLLWGEED-AFM-EVEMAEVTK 224
Cdd:PRK03204  173 AGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLArevpatlgTKPTLLVWGMKDvAFRpKTILPRLRA 252

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958675256 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 1958675256   1 MLLLHGFPEF-WYSWRHQLREFKSE-YRVVALDLRGYGESDAPIHQEsykldcLIADIKDVLD---SLGY---NKCVLIG 72
Cdd:COG1506    26 VVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDylaARPYvdpDRIGIYG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  73 HDWGGMIAWLIAVCYPEMImKLIVinfphpsvfteyilrhpaqlfrssfyyffqiprlpeLMFSINDFKAlkhlFTSQST 152
Cdd:COG1506   100 HSYGGYMALLAAARHPDRF-KAAV------------------------------------ALAGVSDLRS----YYGTTR 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 153 GIGRKGRQLTTEDLEAYVyvfsqpgALSgPINHYRNIfsclplkhhmvTTPTLLLWGEEDAFMEVEMAE--VTKIYVKN- 229
Cdd:COG1506   139 EYTERLMGGPWEDPEAYA-------ARS-PLAYADKL-----------KTPLLLIHGEADDRVPPEQAErlYEALKKAGk 199

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQesYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:PLN02578   89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTA 166

                          90
                  ....*....|....*...
gi 1958675256  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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESykLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAW 81
Cdd:PRK14875  135 VLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELAAAVLAFLDALGIERAHLVGHSMGGAVAL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  82 LIAVCYPEMIMKLIVINfPH---PSVFTEYIlrhpaQLF-RSSfyyffqiprlpelmfSINDFK-ALKHLFTSQSTgigr 156
Cdd:PRK14875  213 RLAARAPQRVASLTLIA-PAglgPEINGDYI-----DGFvAAE---------------SRRELKpVLELLFADPAL---- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 157 KGRQLtTEDLEAYVYVFSQPGALSGPINH----------YRNIFSCLPlkhhmvtTPTLLLWGEEDAFMEVEMAEVtkiy 226
Cdd:PRK14875  268 VTRQM-VEDLLKYKRLDGVDDALRALADAlfaggrqrvdLRDRLASLA-------IPVLVIWGEQDRIIPAAHAQG---- 335

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958675256 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 1958675256   1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105

                          90       100
                  ....*....|....*....|....
gi 1958675256  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 1958675256   1 MLLLHGFPEfwYSWR-----HQLreFKSEYRVVALDLRGYGESD-APIHQESYklDCLIADIKDVLDSL----GYNKCVL 70
Cdd:pfam12146   7 VVLVHGLGE--HSGRyahlaDAL--AAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLPLFL 80

                          90       100
                  ....*....|....*....|....*
gi 1958675256  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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMiA 80
Cdd:PLN02679   91 VLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP-PGFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSL-A 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  81 WLIAVC--YPEMIMKLIVIN----FPHPSVFTEYILRHPAQLFrSSFYYFFQIPRLPELMFS-INDFKALKHLFTSQstg 153
Cdd:PLN02679  169 CVIAASesTRDLVRGLVLLNcaggMNNKAVVDDWRIKLLLPLL-WLIDFLLKQRGIASALFNrVKQRDNLKNILLSV--- 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 154 IGRKgrQLTTEDLeayVYVFSQPGALSGPINHYRNIFSCLPLKHHM-----VTTPTLLLWGEEDAFMEVEmAEVTKIYVK 228
Cdd:PLN02679  245 YGNK--EAVDDEL---VEIIRGPADDEGALDAFVSIVTGPPGPNPIkliprISLPILVLWGDQDPFTPLD-GPVGKYFSS 318

                         250       260
                  ....*....|....*....|....*...
gi 1958675256 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 1958675256  24 EYRVVALDLRGYGESDAPIHqeSYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPHPS 103
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 104 VFTeyilrhPAQlfrssfyyffqiPRLPELMFSINDFKALKHLFTSQSTGIGRKGRQLTTEDLEAYVYVFSqpgalSGPI 183
Cdd:TIGR02240 129 VMV------PGK------------PKVLMMMASPRRYIQPSHGIHIAPDIYGGAFRRDPELAMAHASKVRS-----GGKL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 184 NHYRNIFSCLPLKH----HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGsHWLQQDQPDIVNGLIWAFL 259
Cdd:TIGR02240 186 GYYWQLFAGLGWTSihwlHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNA-ELHIIDDG-HLFLITRAEAVAPIIMKFL 263


                  ....*.
gi 1958675256 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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQES-----YKLDCLIADIKDVLDSLGYNKCVLIGHDW 75
Cdd:PLN02824   32 LVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfYTFETWGEQLNDFCSDVVGDPAFVICNSV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  76 GGMIAWLIAVCYPEMIMKLIVINfphPSVFTEYILRHPA--QLFRSSFY----------YFFQIPRLPELMFSIndfkaL 143
Cdd:PLN02824  112 GGVVGLQAAVDAPELVRGVMLIN---ISLRGLHIKKQPWlgRPFIKAFQnllretavgkAFFKSVATPETVKNI-----L 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 144 KHLFTSQStgigrkgrQLTTEDLEAYVyvfsQPGALSGPINHYRNI--FSCLPLKHHM---VTTPTLLLWGEEDAFMEVE 218
Cdd:PLN02824  184 CQCYHDDS--------AVTDELVEAIL----RPGLEPGAVDVFLDFisYSGGPLPEELlpaVKCPVLIAWGEKDPWEPVE 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958675256 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 1958675256  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 1958675256   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGEsdapiHQESYKLDclIADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLGGLVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256  81 WLIAVCYPEMIMKLIVI----------NFPH---PSVFTEYilrhpAQLFRSSFyyffqiprlpelMFSINDFKALKHLF 147
Cdd:TIGR01738  80 LHIAATHPDRVRALVTVasspcfsareDWPEgikPDVLTGF-----QQQLSDDY------------QRTIERFLALQTLG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675256 148 TSQSTGIGRKGRQLttedleayvyVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEEDAFMEVEMAEVTKI 225
Cdd:TIGR01738 143 TPTARQDARALKQT----------LLARPTPNVQVLQAGLEILATVDLRQPLqnISVPFLRLYGYLDGLVPAKVVPMLDK 212

                         250
                  ....*....|....*.
gi 1958675256 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 1958675256   2 LLLHGF---PEFWYSWRHQLRefKSEYRVVALDLRGYGESDAPIHQESYKlDClIADIKDVLDSL--GYNKCVLIGHDWG 76
Cdd:COG1647    19 LLLHGFtgsPAEMRPLAEALA--KAGYTVYAPRLPGHGTSPEDLLKTTWE-DW-LEDVEEAYEILkaGYDKVIVIGLSMG 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958675256  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 1958675256   2 LLLHGFPEFWYSWRHQLREFKSE-YRVVALDlrgYGESDAPIHQESYKLDcliADIKDVLDSLGYNKCVLIGHDWGGMIA 80
Cdd:COG1075     9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALN---YPSTNGSIEDSAEQLA---AFVDAVLAATGAEKVDLVGHSMGGLVA 82

                          90       100
                  ....*....|....*....|...
gi 1958675256  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 1958675256  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 1958675256   2 LLLHGF---PEFWYS--WRHQLREFKSEYRVVALDLRGYGESDAPihQES-YKLDCLIADI-KDVLDSLGYNKCVLIGHD 74
Cdd:PLN03087  205 LFIHGFissSAFWTEtlFPNFSDAAKSTYRLFAVDLLGFGRSPKP--ADSlYTLREHLEMIeRSVLERYKVKSFHIVAHS 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958675256  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 1958675256  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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