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Conserved domains on  [gi|408360075|sp|Q6IE26|]
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RecName: Full=Epoxide hydrolase 4; AltName: Full=Abhydrolase domain-containing protein 7; AltName: Full=Epoxide hydrolase-related protein

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

 Zoom to residue level

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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, ...
 68-354 1.79e-44

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: 152.46  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIA 147
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 148 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefm 227
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 228 fsinDFKALKHLFTSqstgigrkgrqLTTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAF 307
Cdd:COG0596  137 ----APEALAALLRA-----------LARTDLRERL---------------------------ARITVPTLVIWGEKDPI 174

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 408360075 308 MEVEMAEVTKIYVKNYfRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 354
Cdd:COG0596  175 VPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-354 1.79e-44

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: 152.46  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIA 147
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 148 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefm 227
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 228 fsinDFKALKHLFTSqstgigrkgrqLTTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAF 307
Cdd:COG0596  137 ----APEALAALLRA-----------LARTDLRERL---------------------------ARITVPTLVIWGEKDPI 174

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 408360075 308 MEVEMAEVTKIYVKNYfRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 354
Cdd:COG0596  175 VPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 92-337 9.90e-29

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: 111.83  E-value: 9.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   92 PLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGG 170
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  171 MIAWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRFPEFMFSINDFKALKHLFTSQSTGIGRK 250
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  251 GRQLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTI 328
Cdd:pfam00561 157 LPLL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233


                  ....*....
gi 408360075  329 lSEGSHWLQ 337
Cdd:pfam00561 234 -PDAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
87-348 6.46e-25

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 105.83  E-value: 6.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  87 GERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCV-LIG 165
Cdd:PRK05855  21 GDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 166 HDWGGMIAWLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRFPEFMFSI 230
Cdd:PRK05855 101 HDWGSIQGWE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 231 NDFKALKHLF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDA 306
Cdd:PRK05855 180 GLGRAWPRLLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDP 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 408360075 307 FMEVEMAEVTKIYVKNYFRLTIlsEGSHWLQQDQPDIVNGLI 348
Cdd:PRK05855 246 YVRPALYDDLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 87-191 2.19e-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: 54.69  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   87 GERGKPLMLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPAH--QESYKLDCLIADIKDILDSLGYSK 160
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 408360075  161 CVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:TIGR01250  99 FYLLGHSWGGMLAQEYALKYGQHLKGLIISS 129
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-354 1.79e-44

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: 152.46  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhqESYKLDCLIA 147
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 148 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINfphpSVFTEYilrhpAQLFRSSFYyffqiprfpefm 227
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----EVLAAL-----AEPLRRPGL------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 228 fsinDFKALKHLFTSqstgigrkgrqLTTEDLEAYVyvfsqpgalsgpinhyrnifsclplkhHMVTTPTLLLWGEEDAF 307
Cdd:COG0596  137 ----APEALAALLRA-----------LARTDLRERL---------------------------ARITVPTLVIWGEKDPI 174

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 408360075 308 MEVEMAEVTKIYVKNYfRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 354
Cdd:COG0596  175 VPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 92-337 9.90e-29

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: 111.83  E-value: 9.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   92 PLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCVLIGHDWGG 170
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  171 MIAWLIAVCYPEMIMKLIVINFPHPSVFTEYILRHPAQlfrsSFYYFFQIPRFPEFMFSINDFKALKHLFTSQSTGIGRK 250
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILA----LFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  251 GRQLtteDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKH--HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYFRLTI 328
Cdd:pfam00561 157 LPLL---NKRFPSGDYALAKSLVTGALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233


                  ....*....
gi 408360075  329 lSEGSHWLQ 337
Cdd:pfam00561 234 -PDAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
87-348 6.46e-25

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 105.83  E-value: 6.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  87 GERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESYKLDCLIADIKDILDSLGYSKCV-LIG 165
Cdd:PRK05855  21 GDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 166 HDWGGMIAWLiAVCYPEM---IMKLIVINFPHPSVFTEYI---LRHP---------AQLFRSSFYYFFQIPRFPEFMFSI 230
Cdd:PRK05855 101 HDWGSIQGWE-AVTRPRAagrIASFTSVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLWRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 231 NDFKALKHLF-TSQSTGIGRKGRQLTTEDleayvyvfsqpgALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWGEEDA 306
Cdd:PRK05855 180 GLGRAWPRLLrRVEGTPVDPIPTQTTLSD------------GAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVPTGDP 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 408360075 307 FMEVEMAEVTKIYVKNYFRLTIlsEGSHWLQQDQPDIVNGLI 348
Cdd:PRK05855 246 YVRPALYDDLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 71-191 6.79e-18

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 83.09  E-value: 6.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  71 YVRIKDSG---LRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPAHQESYKLDCLI 146
Cdd:PRK00870  23 YVDVDDGDggpLRMHYVDEGPADGPPVLLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHV 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 408360075 147 ADIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PRK00870 103 EWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVAN 147
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 71-359 1.04e-16

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 79.27  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  71 YVRIKDSglRFHYVAAGErGKPlMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAP------AHQESYkLDC 144
Cdd:PRK03592  11 RVEVLGS--RMAYIETGE-GDP-IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPdidytfADHARY-LDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 145 LIadikdilDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLivinfphpsVFTEYILRHPA-QLFRSSFYYFFQIPRF 223
Cdd:PRK03592  86 WF-------DALGLDDVVLVGHDWGSALGFDWAARHPDRVRGI---------AFMEAIVRPMTwDDFPPAVRELFQALRS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 224 P----EFMFSINDF--KALKHLFTsqstgigrkgRQLTTEDLEAYVYVFSQPGA----LSGP---------------INH 278
Cdd:PRK03592 150 PgegeEMVLEENVFieRVLPGSIL----------RPLSDEEMAVYRRPFPTPESrrptLSWPrelpidgepadvvalVEE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 279 YRNIFSCLPlkhhmvtTPTLLLWGEEDA-FMEVEMAEVTKIYVKNYFrLTILSEGSHWLQQDQPDIVNGLIWAFLKEETR 357
Cdd:PRK03592 220 YAQWLATSD-------VPKLLINAEPGAiLTTGAIRDWCRSWPNQLE-ITVFGAGLHFAQEDSPEEIGAAIAAWLRRLRL 291


                 ..
gi 408360075 358 RD 359
Cdd:PRK03592 292 AV 293
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
79-191 5.66e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.11  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  79 LRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAP-AHQESYklDCLIADIKDILDSL 156
Cdd:COG2267   16 LRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPrGHVDSF--DDYVDDLRAALDAL 93

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 408360075 157 ---GYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:COG2267   94 rarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 73-348 1.61e-13

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 71.07  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  73 RIKDSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQE--SYKLDCLIADIK 150
Cdd:PLN03084 109 QASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLE 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 151 DILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPhpsvFTEYILRHPAQLFRSSFYYFFQIprfpefmFSI 230
Cdd:PLN03084 189 SLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNPP----LTKEHAKLPSTLSEFSNFLLGEI-------FSQ 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 231 NDFKALKHLFTSQSTgigrkgRQLTTEDleAYVYvfSQPGALSGP-------------------INHYRNIFSCLPLKhh 291
Cdd:PLN03084 258 DPLRASDKALTSCGP------YAMKEDD--AMVY--RRPYLTSGSsgfalnaisrsmkkelkkyIEEMRSILTDKNWK-- 325

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 408360075 292 mvtTPTLLLWGEEDAFMEVEMAEVtkiYVKNY-FRLTILSEGSHWLQQDQPD----IVNGLI 348
Cdd:PLN03084 326 ---TPITVCWGLRDRWLNYDGVED---FCKSSqHKLIELPMAGHHVQEDCGEelggIISGIL 381
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 80-348 4.35e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 68.73  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  80 RFHYVAAGErgKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhQESYKLDCLIADIKDILDSLGYS 159
Cdd:PRK03204  25 RIHYIDEGT--GPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPS-GFGYQIDEHARVIGEFVDHLGLD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 160 KCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN---FPHPS----VFTEYILRHPAQlfrssfyyffqiprfpefmfsind 232
Cdd:PRK03204 102 RYLSMGQDWGGPISMAVAVERADRVRGVVLGNtwfWPADTlamkAFSRVMSSPPVQ------------------------ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 233 FKALKHLFTSQSTGIGRKGRQLTTEDLEAYVYVFSQPGALSGPINHYRNIFSCLPLKHHMV--------TTPTLLLWGEE 304
Cdd:PRK03204 158 YAILRRNFFVERLIPAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLArevpatlgTKPTLLVWGMK 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 408360075 305 D-AFM-EVEMAEVTKIYVKnyFRLTILSEGSHWLQQDQPDIVNGLI 348
Cdd:PRK03204 238 DvAFRpKTILPRLRATFPD--HVLVELPNAKHFIQEDAPDRIAAAI 281
PLN02578 PLN02578
hydrolase
 78-191 3.96e-11

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 63.71  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  78 GLRFHYVAAGErGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDApAHQEsYKLDCLIADIKDILDSLG 157
Cdd:PLN02578  75 GHKIHYVVQGE-GLPI-VLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDK-ALIE-YDAMVWRDQVADFVKEVV 150

                         90       100       110
                 ....*....|....*....|....*....|....
gi 408360075 158 YSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PLN02578 151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVALLN 184
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 94-227 6.38e-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: 61.34  E-value: 6.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   94 MLLLHGFpefWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESykldcLIADIKDILDSLGYSK-CVLIGHDWGGMI 172
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA-----DLADLAALLDELGAARpVVLVGHSLGGAV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 408360075  173 AWLIAvcyPEMIMKLIVIN---FPHPSVFTEYILRHPAQLFRSSFYYFFQIPRFPEFM 227
Cdd:pfam12697  73 ALAAA---AAALVVGVLVAplaAPPGLLAALLALLARLGAALAAPAWLAAESLARGFL 127
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
83-354 4.07e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 59.26  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  83 YVAAGERGKPLMLLLHGFPEF-WYSWRHQLREFKSE-YRVVALDLRGYGESDAPAHQEsykldcLIADIKDILD---SLG 157
Cdd:COG1506   15 YLPADGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDylaARP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 158 Y---SKCVLIGHDWGGMIAWLIAVCYPEMImKLIVINFPhpsvfteyilrhpaqlfrssfyyffqiprfpefmfsINDFK 234
Cdd:COG1506   89 YvdpDRIGIYGHSYGGYMALLAAARHPDRF-KAAVALAG------------------------------------VSDLR 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 235 AlkhlFTSQSTGIGRKGRQLTTEDLEAYVyvfsqpgALSgPINHYRNIfsclplkhhmvTTPTLLLWGEEDAFMEVEMAE 314
Cdd:COG1506  132 S----YYGTTREYTERLMGGPWEDPEAYA-------ARS-PLAYADKL-----------KTPLLLIHGEADDRVPPEQAE 188

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 408360075 315 --VTKIYVKN-YFRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 354
Cdd:COG1506  189 rlYEALKKAGkPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-190 7.63e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.57  E-value: 7.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  67 GTHCYVRIkdSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAHQESykLDCLI 146
Cdd:PRK14875 109 PAPRKARI--GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELA 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 408360075 147 ADIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVI 190
Cdd:PRK14875 185 AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 68-354 2.51e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 57.83  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  68 THCYVRIKDSGLRfhYVAAGERGkPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAP----AHQES-YKL 142
Cdd:PLN02824   9 ETRTWRWKGYNIR--YQRAGTSG-PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPnprsAPPNSfYTF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 143 DCLIADIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINfphPSVFTEYILRHPA--QLFRSSFY----- 215
Cdd:PLN02824  86 ETWGEQLNDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLIN---ISLRGLHIKKQPWlgRPFIKAFQnllre 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 216 -----YFFQIPRFPEFMFSIndfkaLKHLFTSQStgigrkgrQLTTEDLEAYVyvfsQPGALSGPINHYRNI--FSCLPL 288
Cdd:PLN02824 163 tavgkAFFKSVATPETVKNI-----LCQCYHDDS--------AVTDELVEAIL----RPGLEPGAVDVFLDFisYSGGPL 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 408360075 289 KHHM---VTTPTLLLWGEEDAFMEVEMAEVTKIYvKNYFRLTILSEGSHWLQQDQPDIVNGLIWAFLKE 354
Cdd:PLN02824 226 PEELlpaVKCPVLIAWGEKDPWEPVELGRAYANF-DAVEDFIVLPGVGHCPQDEAPELVNPLIESFVAR 293
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 91-188 7.21e-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: 55.68  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   91 KPLMLLLHGFPEfwYSWR-----HQLreFKSEYRVVALDLRGYGESD-APAHQESYklDCLIADIKDILDSL----GYSK 160
Cdd:pfam12146   4 RAVVVLVHGLGE--HSGRyahlaDAL--AAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLP 77

                          90       100
                  ....*....|....*....|....*...
gi 408360075  161 CVLIGHDWGGMIAWLIAVCYPEMIMKLI 188
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLI 105
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 87-191 2.19e-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: 54.69  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   87 GERGKPLMLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPAH--QESYKLDCLIADIKDILDSLGYSK 160
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 408360075  161 CVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:TIGR01250  99 FYLLGHSWGGMLAQEYALKYGQHLKGLIISS 129
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 80-344 1.50e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 52.54  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  80 RFHYVAAGE----RGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPAhQESYKLDCLIADIKDILDS 155
Cdd:PLN02679  73 SINYLVKGSpevtSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPP-GFSYTMETWAELILDFLEE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 156 LGYSKCVLIGHDWGGMiAWLIAVC--YPEMIMKLIVIN----FPHPSVFTEYILRHPAQLFrSSFYYFFQIPRFPEFMFS 229
Cdd:PLN02679 152 VVQKPTVLIGNSVGSL-ACVIAASesTRDLVRGLVLLNcaggMNNKAVVDDWRIKLLLPLL-WLIDFLLKQRGIASALFN 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 230 -INDFKALKHLFTSQstgIGRKgrQLTTEDLeayVYVFSQPGALSGPINHYRNIFSCLPLKHHM-----VTTPTLLLWGE 303
Cdd:PLN02679 230 rVKQRDNLKNILLSV---YGNK--EAVDDEL---VEIIRGPADDEGALDAFVSIVTGPPGPNPIkliprISLPILVLWGD 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 408360075 304 EDAFMEVEmAEVTKIYVK-----NYFRLTILSEGSHWLQQDQPDIV 344
Cdd:PLN02679 302 QDPFTPLD-GPVGKYFSSlpsqlPNVTLYVLEGVGHCPHDDRPDLV 346
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
88-211 2.98e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 48.01  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  88 ERGKPLMLLLHGF---PEFWYSWRHQLRefKSEYRVVALDLRGYGESdaPAHQESYKLDCLIADIKDILDSL--GYSKCV 162
Cdd:COG1647   12 EGGRKGVLLLHGFtgsPAEMRPLAEALA--KAGYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAYEILkaGYDKVI 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 408360075 163 LIGHDWGGMIAWLIAVCYPEmIMKLIVIN----FPHPSVFTEYILRHPAQLFR 211
Cdd:COG1647   88 VIGLSMGGLLALLLAARYPD-VAGLVLLSpalkIDDPSAPLLPLLKYLARSLR 139
PRK10673 PRK10673
esterase;
112-191 3.73e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.80  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075 112 REFKSEYRVVALDLRGYGES------DAPAHQEsykldcliaDIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIM 185
Cdd:PRK10673  37 RDLVNDHDIIQVDMRNHGLSprdpvmNYPAMAQ---------DLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRID 107


                 ....*.
gi 408360075 186 KLIVIN 191
Cdd:PRK10673 108 KLVAID 113
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
 117-358 5.17e-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: 47.30  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  117 EYRVVALDLRGYGESDAPAHqeSYKLDCLIADIKDILDSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPHPS 196
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLILAATAAGA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  197 VFTeyilrhPAQlfrssfyyffqiPRFPEFMFSINDFKALKHLFTSQSTGIGRKGRQLTTEDLEAYVYVFSqpgalSGPI 276
Cdd:TIGR02240 129 VMV------PGK------------PKVLMMMASPRRYIQPSHGIHIAPDIYGGAFRRDPELAMAHASKVRS-----GGKL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  277 NHYRNIFSCLPLKH----HMVTTPTLLLWGEEDAFMEVEMAEVTKIYVKNYfRLTILSEGsHWLQQDQPDIVNGLIWAFL 352
Cdd:TIGR02240 186 GYYWQLFAGLGWTSihwlHKIQQPTLVLAGDDDPIIPLINMRLLAWRIPNA-ELHIIDDG-HLFLITRAEAVAPIIMKFL 263


                  ....*.
gi 408360075  353 KEETRR 358
Cdd:TIGR02240 264 AEERQR 269
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 90-334 8.44e-06

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: 46.73  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075   90 GKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGEsdapaHQESYKLDclIADIKDILDSLGYSKCVLIGHDWG 169
Cdd:TIGR01738   3 GNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  170 GMIAWLIAVCYPEMIMKLIVI----------NFPH---PSVFTEYilrhpAQLFRSsfyyffqiprfpEFMFSINDFKAL 236
Cdd:TIGR01738  76 GLVALHIAATHPDRVRALVTVasspcfsareDWPEgikPDVLTGF-----QQQLSD------------DYQRTIERFLAL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  237 KHLFTSQSTGIGRKGRQLttedleayvyVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEEDAFMEVEMAE 314
Cdd:TIGR01738 139 QTLGTPTARQDARALKQT----------LLARPTPNVQVLQAGLEILATVDLRQPLqnISVPFLRLYGYLDGLVPAKVVP 208

                         250       260
                  ....*....|....*....|
gi 408360075  315 VTKIYVKnYFRLTILSEGSH 334
Cdd:TIGR01738 209 MLDKLAP-HSELYIFAKAAH 227
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 95-194 1.61e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.58  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  95 LLLHGFPEFWYSWRHQLREFKSE-YRVVALDLRGYGES-DAPAHQesykldcLIADIKDILDSLGYSKCVLIGHDWGGMI 172
Cdd:COG1075    9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSiEDSAEQ-------LAAFVDAVLAATGAEKVDLVGHSMGGLV 81

                         90       100
                 ....*....|....*....|....
gi 408360075 173 A-WLIAVC-YPEMIMKLIVINFPH 194
Cdd:COG1075   82 ArYYLKRLgGAAKVARVVTLGTPH 105
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
81-182 2.17e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  81 FHYVAAGERGKPLMLLLHGfpefWYSW----RHQLREFKSE-YRVVALDL-----RGYGESDAPAHQESYKLDCLIADIK 150
Cdd:COG0412   19 YLARPAGGGPRPGVVVLHE----IFGLnphiRDVARRLAAAgYVVLAPDLygrggPGDDPDEARALMGALDPELLAADLR 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 408360075 151 ---DILDSLGY---SKCVLIGHDWGGMIAWLIAVCYPE 182
Cdd:COG0412   95 aalDWLKAQPEvdaGRVGVVGFCFGGGLALLAAARGPD 132
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 87-190 1.15e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 40.66  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  87 GERGKPLMLLLHGFPE---FWYswrhqlREF---KSEYRVVALDLRGYGESDAP-------AHQESYKLDCLIADIKdil 153
Cdd:PLN02894 101 SKEDAPTLVMVHGYGAsqgFFF------RNFdalASRFRVIAIDQLGWGGSSRPdftckstEETEAWFIDSFEEWRK--- 171

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 408360075 154 dSLGYSKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVI 190
Cdd:PLN02894 172 -AKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILV 207
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 95-207 9.12e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 37.87  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408360075  95 LLLHGF---PEFWYS--WRHQLREFKSEYRVVALDLRGYGESDAPAhqES-YKLDCLIADI-KDILDSLGYSKCVLIGHD 167
Cdd:PLN03087 205 LFIHGFissSAFWTEtlFPNFSDAAKSTYRLFAVDLLGFGRSPKPA--DSlYTLREHLEMIeRSVLERYKVKSFHIVAHS 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 408360075 168 WGGMIAWLIAVCYPEMIMKLIVINFPHPSV-----FTEYILRHPA 207
Cdd:PLN03087 283 LGCILALALAVKHPGAVKSLTLLAPPYYPVpkgvqATQYVMRKVA 327
 
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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