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Conserved domains on  [gi|1824615245|ref|NP_001366154|]
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epoxide hydrolase 4 isoform 2 [Mus musculus]

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 2.77e-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: 138.60  E-value: 2.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1824615245 242 WLQQDQPDIVNGLIWAFLKE 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 2.77e-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: 138.60  E-value: 2.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1824615245 242 WLQQDQPDIVNGLIWAFLKE 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 1.63e-28

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: 108.75  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRFPEFMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234


                  ....*..
gi 1824615245 238 EGSHWLQ 244
Cdd:pfam00561 235 DAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
2-255 3.14e-24

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 101.21  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCV-LIGHDWGGMIA 80
Cdd:PRK05855   29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRFPEFMFSINDFKALKH 145
Cdd:PRK05855  109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855  188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1824615245 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 3.58e-07

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: 50.07  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPAH--QESYKLDCLIADIKDILDSLGYSKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105

                          90       100
                  ....*....|....*....|....
gi 1824615245  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 2.77e-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: 138.60  E-value: 2.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAW 81
Cdd:COG0596    27 VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  82 LIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefmfsinDFKALKHLFTSqstgigrkgrqL 161
Cdd:COG0596   105 ELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL----------------APEALAALLRA-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 162 TTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGSH 241
Cdd:COG0596   149 ARTDLRERL---------------------------ARITVPTLVIWGEKDPIVPPALARRLAELLPNA-ELVVLPGAGH 200

                         250       260
                  ....*....|....*....|
gi 1824615245 242 WLQQDQPDIVNGLIWAFLKE 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 1.63e-28

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: 108.75  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMI 79
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  80 AWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRFPEFMFSINDFKALKHLFTSQSTGIGRKGR 159
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 160 QLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTIlS 237
Cdd:pfam00561 159 LL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI-P 234


                  ....*..
gi 1824615245 238 EGSHWLQ 244
Cdd:pfam00561 235 DAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
2-255 3.14e-24

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 101.21  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCV-LIGHDWGGMIA 80
Cdd:PRK05855   29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLAHDWGSIQG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  81 WLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRFPEFMFSINDFKALKH 145
Cdd:PRK05855  109 WE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRLGLGRAWPR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 146 LF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDAFMEVEMAE 221
Cdd:PRK05855  188 LLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDPYVRPALYD 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1824615245 222 VTKIYVKNYFRLTIlsEGSHWLQQDQPDIVNGLI 255
Cdd:PRK05855  254 DLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-266 4.11e-14

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 70.41  E-value: 4.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAP------AHQESYkLDCLIadikdilDSLGYSKCVLIGHD 74
Cdd:PRK03592   30 IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPdidytfADHARY-LDAWF-------DALGLDDVVLVGHD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  75 WGGMIAWLIAVCYPEMIMKLivinfphpsVFTEYILRHPA-QLFRSSFYYFFQIPRFP----EFMFSINDF--KALKHLF 147
Cdd:PRK03592  102 WGSALGFDWAARHPDRVRGI---------AFMEAIVRPMTwDDFPPAVRELFQALRSPgegeEMVLEENVFieRVLPGSI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 148 TsqstgigrkgRQLTTEDLEAYVYVFSQPGA----LSGP---------------INHYRNIFSCLPlkhhmvtTPTLLLW 208
Cdd:PRK03592  173 L----------RPLSDEEMAVYRRPFPTPESrrptLSWPrelpidgepadvvalVEEYAQWLATSD-------VPKLLIN 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1824615245 209 GEEDA-FMEVEMAEVTKIYVKNYFrLTILSEGSHWLQQDQPDIVNGLIWAFLKEETRRD 266
Cdd:PRK03592  236 AEPGAiLTTGAIRDWCRSWPNQLE-ITVFGAGLHFAQEDSPEEIGAAIAAWLRRLRLAV 293
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-98 9.71e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 68.49  E-value: 9.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAP-AHQESYklDCLIADIKDILDSL---GYSKCVLIGHDWG 76
Cdd:COG2267    32 VLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPrGHVDSF--DDYVDDLRAALDALrarPGLPVVLLGHSMG 109

                          90       100
                  ....*....|....*....|..
gi 1824615245  77 GMIAWLIAVCYPEMIMKLIVIN 98
Cdd:COG2267   110 GLIALLYAARYPDRVAGLVLLA 131
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 2-98 4.08e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 67.69  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIA 80
Cdd:PRK00870   50 LLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIG 129

                          90
                  ....*....|....*...
gi 1824615245  81 WLIAVCYPEMIMKLIVIN 98
Cdd:PRK00870  130 LRLAAEHPDRFARLVVAN 147
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 1-134 6.52e-12

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: 6.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFpefWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESykldcLIADIKDILDSLGYSK-CVLIGHDWGGMI 79
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA-----DLADLAALLDELGAARpVVLVGHSLGGAV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1824615245  80 AWLIAvcyPEMIMKLIVIN---FPHPSVFTEYILRHPAQLFRSSFYYFFQIPRFPEFM 134
Cdd:pfam12697  73 ALAAA---AAALVVGVLVAplaAPPGLLAALLALLARLGAALAAPAWLAAESLARGFL 127
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 1-255 2.90e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 62.18  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIA 80
Cdd:PRK03204   37 ILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPS-GFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  81 WLIAVCYPEMIMKLIVIN---FPHPS----VFTEYILRHPAQlfrssfyyffqiprfpefmfsindFKALKHLFTSQSTG 153
Cdd:PRK03204  116 MAVAVERADRVRGVVLGNtwfWPADTlamkAFSRVMSSPPVQ------------------------YAILRRNFFVERLI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 154 IGRKGRQLTTEDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKHHMV--------TTPTLLLWGEED-AFM-EVEMAEVT 223
Cdd:PRK03204  172 PAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLArevpatlgTKPTLLVWGMKDvAFRpKTILPRLR 251

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1824615245 224 KIYVKnyFRLTILSEGSHWLQQDQPDIVNGLI 255
Cdd:PRK03204  252 ATFPD--HVLVELPNAKHFIQEDAPDRIAAAI 281
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 1-255 1.12e-10

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 61.05  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQE--SYKLDCLIADIKDILDSLGYSKCVLIGHDWGGM 78
Cdd:PLN03084  130 VLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLESLIDELKSDKVSLVVQGYFSP 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  79 IAWLIAVCYPEMIMKLIVINFPhpsvFTEYILRHPAQLFRSSFYYFFQIprfpefmFSINDFKALKHLFTSQSTgigrkg 158
Cdd:PLN03084  210 PVVKYASAHPDKIKKLILLNPP----LTKEHAKLPSTLSEFSNFLLGEI-------FSQDPLRASDKALTSCGP------ 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 159 RQLTTEDleAYVYvfSQPGALSGP-------------------INHYRNIFSCLPLKhhmvtTPTLLLWGEEDAFMEVEM 219
Cdd:PLN03084  273 YAMKEDD--AMVY--RRPYLTSGSsgfalnaisrsmkkelkkyIEEMRSILTDKNWK-----TPITVCWGLRDRWLNYDG 343

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1824615245 220 AEVtkiYVKNY-FRLTILSEGSHWLQQDQPD----IVNGLI 255
Cdd:PLN03084  344 VED---FCKSSqHKLIELPMAGHHVQEDCGEelggIISGIL 381
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 1-95 7.49e-09

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: 54.91  E-value: 7.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEfwYSWR-----HQLreFKSEYRVVALDLRGYGESD-APAHQESYklDCLIADIKDILDSL----GYSKCVL 70
Cdd:pfam12146   7 VVLVHGLGE--HSGRyahlaDAL--AAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLPLFL 80

                          90       100
                  ....*....|....*....|....*
gi 1824615245  71 IGHDWGGMIAWLIAVCYPEMIMKLI 95
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLI 105
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-97 1.80e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.56  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESykLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAW 81
Cdd:PRK14875  135 VLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELAAAVLAFLDALGIERAHLVGHSMGGAVAL 212

                          90
                  ....*....|....*.
gi 1824615245  82 LIAVCYPEMIMKLIVI 97
Cdd:PRK14875  213 RLAARAPQRVASLTLI 228
PLN02578 PLN02578
hydrolase
 1-98 3.61e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 53.31  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDApAHQEsYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIA 80
Cdd:PLN02578   89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDK-ALIE-YDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTA 166

                          90
                  ....*....|....*...
gi 1824615245  81 WLIAVCYPEMIMKLIVIN 98
Cdd:PLN02578  167 LSTAVGYPELVAGVALLN 184
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
1-261 4.87e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.33  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEF-WYSWRHQLREFKSE-YRVVALDLRGYGESDAPAHQEsykldcLIADIKDILD---SLGY---SKCVLIG 72
Cdd:COG1506    26 VVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDylaARPYvdpDRIGIYG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  73 HDWGGMIAWLIAVCYPEMImKLIVINFPhpsvfteyilrhpaqlfrssfyyffqiprfpefmfsINDFKAlkhlFTSQST 152
Cdd:COG1506   100 HSYGGYMALLAAARHPDRF-KAAVALAG------------------------------------VSDLRS----YYGTTR 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 153 GIGRKGRQLTTEDLEAYVyvfsqpgALSgPINHYRNIfsclplkhhmvTTPTLLLWGEEDAFMEVEMAE--VTKIYVKN- 229
Cdd:COG1506   139 EYTERLMGGPWEDPEAYA-------ARS-PLAYADKL-----------KTPLLLIHGEADDRVPPEQAErlYEALKKAGk 199

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1824615245 230 YFRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 261
Cdd:COG1506   200 PVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 1-98 3.58e-07

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: 50.07  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPAH--QESYKLDCLIADIKDILDSLGYSKCVLIGHD 74
Cdd:TIGR01250  28 LLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDKFYLLGHS 105

                          90       100
                  ....*....|....*....|....
gi 1824615245  75 WGGMIAWLIAVCYPEMIMKLIVIN 98
Cdd:TIGR01250 106 WGGMLAQEYALKYGQHLKGLIISS 129
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 1-251 3.59e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 50.61  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMiA 80
Cdd:PLN02679   91 VLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP-GFSYTMETWAELILDFLEEVVQKPTVLIGNSVGSL-A 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  81 WLIAVC--YPEMIMKLIVIN----FPHPSVFTEYILRHPAQLFrSSFYYFFQIPRFPEFMFS-INDFKALKHLFTSQstg 153
Cdd:PLN02679  169 CVIAASesTRDLVRGLVLLNcaggMNNKAVVDDWRIKLLLPLL-WLIDFLLKQRGIASALFNrVKQRDNLKNILLSV--- 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 154 IGRKgrQLTTEDLeayVYVFSQPGALSGPINHYRNIFSCLPLKHHM-----VTTPTLLLWGEEDAFMEVEmAEVTKIYVK 228
Cdd:PLN02679  245 YGNK--EAVDDEL---VEIIRGPADDEGALDAFVSIVTGPPGPNPIkliprISLPILVLWGDQDPFTPLD-GPVGKYFSS 318

                         250       260
                  ....*....|....*....|....*...
gi 1824615245 229 -----NYFRLTILSEGSHWLQQDQPDIV 251
Cdd:PLN02679  319 lpsqlPNVTLYVLEGVGHCPHDDRPDLV 346
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 1-261 1.16e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 48.58  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAP----AHQES-YKLDCLIADIKDILDSLGYSKCVLIGHDW 75
Cdd:PLN02824   32 LVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPnprsAPPNSfYTFETWGEQLNDFCSDVVGDPAFVICNSV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  76 GGMIAWLIAVCYPEMIMKLIVINfphPSVFTEYILRHPA--QLFRSSFY----------YFFQIPRFPEFMFSIndfkaL 143
Cdd:PLN02824  112 GGVVGLQAAVDAPELVRGVMLIN---ISLRGLHIKKQPWlgRPFIKAFQnllretavgkAFFKSVATPETVKNI-----L 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 144 KHLFTSQStgigrkgrQLTTEDLEAYVyvfsQPGALSGPINHYRNI--FSCLPLKHHM---VTTPTLLLWGEEDAFMEVE 218
Cdd:PLN02824  184 CQCYHDDS--------AVTDELVEAIL----RPGLEPGAVDVFLDFisYSGGPLPEELlpaVKCPVLIAWGEKDPWEPVE 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1824615245 219 MAEVTKIYvKNYFRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 261
Cdd:PLN02824  252 LGRAYANF-DAVEDFIVLPGVGHCPQDEAPELVNPLIESFVAR 293
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
 24-265 2.09e-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: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  24 EYRVVALDLRGYGESDAPAHqeSYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPHPS 103
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 104 VFTeyilrhPAQlfrssfyyffqiPRFPEFMFSINDFKALKHLFTSQSTGIGRKGRQLTTEDLEAYVYVFSqpgalSGPI 183
Cdd:TIGR02240 129 VMV------PGK------------PKVLMMMASPRRYIQPSHGIHIAPDIYGGAFRRDPELAMAHASKVRS-----GGKL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 184 NHYRNIFSCLPLKH----HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGsHWLQQDQPDIVNGLIWAFL 259
Cdd:TIGR02240 186 GYYWQLFAGLGWTSihwlHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNA-ELHIIDDG-HLFLITRAEAVAPIIMKFL 263


                  ....*.
gi 1824615245 260 KEETRR 265
Cdd:TIGR02240 264 AEERQR 269
PRK10673 PRK10673
esterase;
19-98 2.61e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.42  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  19 REFKSEYRVVALDLRGYGES------DAPAHQEsykldcliaDIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIM 92
Cdd:PRK10673   37 RDLVNDHDIIQVDMRNHGLSprdpvmNYPAMAQ---------DLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRID 107


                  ....*.
gi 1824615245  93 KLIVIN 98
Cdd:PRK10673  108 KLVAID 113
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
2-118 4.41e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.47  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGF---PEFWYSWRHQLRefKSEYRVVALDLRGYGESdaPAHQESYKLDCLIADIKDILDSL--GYSKCVLIGHDWG 76
Cdd:COG1647    19 LLLHGFtgsPAEMRPLAEALA--KAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1824615245  77 GMIAWLIAVCYPEmIMKLIVIN----FPHPSVFTEYILRHPAQLFR 118
Cdd:COG1647    95 GLLALLLAARYPD-VAGLVLLSpalkIDDPSAPLLPLLKYLARSLR 139
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 1-241 1.50e-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: 45.19  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   1 MLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGEsdapaHQESYKLDclIADIKDILDSLGYSKCVLIGHDWGGMIA 80
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLGGLVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245  81 WLIAVCYPEMIMKLIVI----------NFPH---PSVFTEYilrhpAQLFRSsfyyffqiprfpEFMFSINDFKALKHLF 147
Cdd:TIGR01738  80 LHIAATHPDRVRALVTVasspcfsareDWPEgikPDVLTGF-----QQQLSD------------DYQRTIERFLALQTLG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245 148 TSQSTGIGRKGRQLttedleayvyVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEEDAFMEVEMAEVTKI 225
Cdd:TIGR01738 143 TPTARQDARALKQT----------LLARPTPNVQVLQAGLEILATVDLRQPLqnISVPFLRLYGYLDGLVPAKVVPMLDK 212

                         250
                  ....*....|....*.
gi 1824615245 226 YVKnYFRLTILSEGSH 241
Cdd:TIGR01738 213 LAP-HSELYIFAKAAH 227
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 2-101 6.13e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 41.35  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGFPEFWYSWRHQLREFKSE-YRVVALDLRGYGES-DAPAHQesykldcLIADIKDILDSLGYSKCVLIGHDWGGMI 79
Cdd:COG1075     9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSiEDSAEQ-------LAAFVDAVLAATGAEKVDLVGHSMGGLV 81

                          90       100
                  ....*....|....*....|....
gi 1824615245  80 A-WLIAVC-YPEMIMKLIVINFPH 101
Cdd:COG1075    82 ArYYLKRLgGAAKVARVVTLGTPH 105
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
25-89 3.18e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 3.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824615245  25 YRVVALDL-----RGYGESDAPAHQESYKLDCLIADIK---DILDSLGY---SKCVLIGHDWGGMIAWLIAVCYPE 89
Cdd:COG0412    57 YVVLAPDLygrggPGDDPDEARALMGALDPELLAADLRaalDWLKAQPEvdaGRVGVVGFCFGGGLALLAAARGPD 132
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 2-114 3.98e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 38.25  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615245   2 LLLHGF---PEFWYS--WRHQLREFKSEYRVVALDLRGYGESDAPAhqES-YKLDCLIADI-KDILDSLGYSKCVLIGHD 74
Cdd:PLN03087  205 LFIHGFissSAFWTEtlFPNFSDAAKSTYRLFAVDLLGFGRSPKPA--DSlYTLREHLEMIeRSVLERYKVKSFHIVAHS 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1824615245  75 WGGMIAWLIAVCYPEMIMKLIVINFPHPSV-----FTEYILRHPA 114
Cdd:PLN03087  283 LGCILALALAVKHPGAVKSLTLLAPPYYPVpkgvqATQYVMRKVA 327
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
 57-106 7.53e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 37.37  E-value: 7.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824615245  57 KDILDSLGYSKC-VLIGHDWGGMIAWLIAVCYPEMIMKLI-VINFPHPSVFT 106
Cdd:PRK06765  151 KELIKSLGIARLhAVMGPSMGGMQAQEWAVHYPHMVERMIgVIGNPQNDAWT 202
 
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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