NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|218777837|ref|NP_775838|]
View 

epoxide hydrolase 4 [Homo sapiens]

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

show extra options »

Show site features     Horizontal zoom: ×

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, ...
70-356 1.51e-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: 152.85  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  70 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPihRQNYKLDCLIT 149
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 150 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINfphpnvfteyilrhpaqllkssyyyffqipwfpefm 229
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 230 fsindfkvlkhlftshstgigrkgcqlttEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEND 307
Cdd:COG0596  122 -----------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLarITVPTLVIWGEKD 172
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 218777837 308 AFMEVEMAEVTKIYVKNYfRLTILSEASHWLQQDQPDIVNKLIWTFLKE 356
Cdd:COG0596  173 PIVPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
70-356 1.51e-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: 152.85  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  70 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPihRQNYKLDCLIT 149
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 150 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINfphpnvfteyilrhpaqllkssyyyffqipwfpefm 229
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 230 fsindfkvlkhlftshstgigrkgcqlttEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEND 307
Cdd:COG0596  122 -----------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLarITVPTLVIWGEKD 172
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 218777837 308 AFMEVEMAEVTKIYVKNYfRLTILSEASHWLQQDQPDIVNKLIWTFLKE 356
Cdd:COG0596  173 PIVPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
94-339 1.25e-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: 108.75  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   94 PLMLLLHGFPEFWYSWRYQLREF-KSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCVLIGHDWGG 172
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  173 MIAWLIAICYPEMVMKLIVINFPHPNVFTEYILRHPAQLLkssyyyffqiPWFPEFMFSINDFKVLKHLFTSHSTGI-GR 251
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALF----------PGFFDGFVADFAPNPLGRLVAKLLALLlLR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  252 KGCQLTTEDLEAYIYVFSQPGALSGP--INHYRNIFSCLPLKH--HMVTTPTLLLWGENDAFMEVEMAEVTKIYVKNYFR 327
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVtgALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230
                         250
                  ....*....|..
gi 218777837  328 LTIlSEASHWLQ 339
Cdd:pfam00561 231 VVI-PDAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
89-350 5.40e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 100.06  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  89 GERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCV-LIG 167
Cdd:PRK05855  21 GDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 168 HDWGGMIAWLiAICYPEmVMKLIV----INFPHPNVFTEYI---LRHP---------AQLLKSSYYYFFQIPWFPEFMFs 231
Cdd:PRK05855 101 HDWGSIQGWE-AVTRPR-AAGRIAsftsVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLW- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 232 indfkvlkhlftshSTGIGRKGCQL--TTEDLEAYIYVFSQPG--ALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWG 304
Cdd:PRK05855 178 --------------RLGLGRAWPRLlrRVEGTPVDPIPTQTTLsdGAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVP 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 218777837 305 ENDAFMEVEMAEVTKIYVKNYFRLTIlsEASHWLQQDQPDIVNKLI 350
Cdd:PRK05855 242 TGDPYVRPALYDDLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
89-193 7.16e-06

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: 46.99  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   89 GERGKPLMLLLHGFP----EFWYSWRYQLREFKSEyrVVALDLRGYGETDAPIH--RQNYKLDCLITDIKDILDSLGYSK 162
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98
                          90       100       110
                  ....*....|....*....|....*....|.
gi 218777837  163 CVLIGHDWGGMIAWLIAICYPEMVMKLIVIN 193
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, ...
70-356 1.51e-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: 152.85  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  70 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPihRQNYKLDCLIT 149
Cdd:COG0596    3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 150 DIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINfphpnvfteyilrhpaqllkssyyyffqipwfpefm 229
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------ 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 230 fsindfkvlkhlftshstgigrkgcqlttEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGEND 307
Cdd:COG0596  122 -----------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLarITVPTLVIWGEKD 172
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 218777837 308 AFMEVEMAEVTKIYVKNYfRLTILSEASHWLQQDQPDIVNKLIWTFLKE 356
Cdd:COG0596  173 PIVPPALARRLAELLPNA-ELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
94-339 1.25e-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: 108.75  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   94 PLMLLLHGFPEFWYSWRYQLREF-KSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCVLIGHDWGG 172
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  173 MIAWLIAICYPEMVMKLIVINFPHPNVFTEYILRHPAQLLkssyyyffqiPWFPEFMFSINDFKVLKHLFTSHSTGI-GR 251
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALF----------PGFFDGFVADFAPNPLGRLVAKLLALLlLR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  252 KGCQLTTEDLEAYIYVFSQPGALSGP--INHYRNIFSCLPLKH--HMVTTPTLLLWGENDAFMEVEMAEVTKIYVKNYFR 327
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDYALAKSLVtgALLFIETWSTELRAKflGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230
                         250
                  ....*....|..
gi 218777837  328 LTIlSEASHWLQ 339
Cdd:pfam00561 231 VVI-PDAGHFAF 241
PRK05855 PRK05855
SDR family oxidoreductase;
89-350 5.40e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 100.06  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  89 GERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCV-LIG 167
Cdd:PRK05855  21 GDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 168 HDWGGMIAWLiAICYPEmVMKLIV----INFPHPNVFTEYI---LRHP---------AQLLKSSYYYFFQIPWFPEFMFs 231
Cdd:PRK05855 101 HDWGSIQGWE-AVTRPR-AAGRIAsftsVSGPSLDHVGFWLrsgLRRPtprrlaralGQLLRSWYIYLFHLPVLPELLW- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 232 indfkvlkhlftshSTGIGRKGCQL--TTEDLEAYIYVFSQPG--ALSGpINHYR-NIFSCL--PLKHHmVTTPTLLLWG 304
Cdd:PRK05855 178 --------------RLGLGRAWPRLlrRVEGTPVDPIPTQTTLsdGAHG-VKLYRaNMIRSLsrPRERY-TDVPVQLIVP 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 218777837 305 ENDAFMEVEMAEVTKIYVKNYFRLTIlsEASHWLQQDQPDIVNKLI 350
Cdd:PRK05855 242 TGDPYVRPALYDDLSRWVPRLWRREI--KAGHWLPMSHPQVLAAAV 285
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
73-193 1.38e-15

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 76.16  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  73 YVRIKDSG---LRFHYVAAGERGKPLMLLLHGFPefwySWRYQLREF-----KSEYRVVALDLRGYGETDAPIHRQNYKL 144
Cdd:PRK00870  23 YVDVDDGDggpLRMHYVDEGPADGPPVLLLHGEP----SWSYLYRKMipilaAAGHRVIAPDLIGFGRSDKPTRREDYTY 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 218777837 145 DCLITDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVIN 193
Cdd:PRK00870  99 ARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVAN 147
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
81-193 6.72e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.03  E-value: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  81 LRFHYVAAGERGKPLMLLLHGFPEFWYSWRYQLREF-KSEYRVVALDLRGYGETDAPiHRQNYKLDCLITDIKDILDSL- 158
Cdd:COG2267   16 LRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGP-RGHVDSFDDYVDDLRAALDALr 94
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 218777837 159 --GYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVIN 193
Cdd:COG2267   95 arPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
75-341 5.05e-13

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 69.52  E-value: 5.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  75 RIKDSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQ--NYKLDCLITDIK 152
Cdd:PLN03084 109 QASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLE 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 153 DILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINFP----HPNVfteyilrhPAQLLKSSYYYFFQIpwfpef 228
Cdd:PLN03084 189 SLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNPPltkeHAKL--------PSTLSEFSNFLLGEI------ 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 229 mFSINDFKVLKHLFTSHSTgigrkgCQLTTEDLEAYIYVFSQPGA---------------LSGPINHYRNIFSCLPLKhh 293
Cdd:PLN03084 255 -FSQDPLRASDKALTSCGP------YAMKEDDAMVYRRPYLTSGSsgfalnaisrsmkkeLKKYIEEMRSILTDKNWK-- 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 218777837 294 mvtTPTLLLWGENDAFMEVEMAEVtkiYVKNY-FRLTILSEASHWLQQD 341
Cdd:PLN03084 326 ---TPITVCWGLRDRWLNYDGVED---FCKSSqHKLIELPMAGHHVQED 368
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
82-344 2.90e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 66.42  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  82 RFHYVAAGErgKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPiHRQNYKLDCLITDIKDILDSLGYS 161
Cdd:PRK03204  25 RIHYIDEGT--GPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERP-SGFGYQIDEHARVIGEFVDHLGLD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 162 KCVLIGHDWGGMIAWLIAICYPEMVMKLIVINfphpNVFteyilrHPAQLLKSSYyyffqipwFPEFMFSIN-DFKVLKH 240
Cdd:PRK03204 102 RYLSMGQDWGGPISMAVAVERADRVRGVVLGN----TWF------WPADTLAMKA--------FSRVMSSPPvQYAILRR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 241 LFTSHSTGIGRKGCQLTTEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHMV--------TTPTLLLWGEND-AFM- 310
Cdd:PRK03204 164 NFFVERLIPAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLArevpatlgTKPTLLVWGMKDvAFRp 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 218777837 311 EVEMAEVTKIYVKnyFRLTILSEASHWLQQDQPD 344
Cdd:PRK03204 244 KTILPRLRATFPD--HVLVELPNAKHFIQEDAPD 275
PLN02578 PLN02578
hydrolase
80-193 3.86e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 66.79  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  80 GLRFHYVAAGErGKPLmLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIhrQNYKLDCLITDIKDILDSLG 159
Cdd:PLN02578  75 GHKIHYVVQGE-GLPI-VLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKAL--IEYDAMVWRDQVADFVKEVV 150
                         90       100       110
                 ....*....|....*....|....*....|....
gi 218777837 160 YSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVIN 193
Cdd:PLN02578 151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVALLN 184
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
85-356 5.78e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.65  E-value: 5.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  85 YVAAGERGKPLMLLLHGFPEF-WYSWRYQLREFKSE-YRVVALDLRGYGETDAPIHRQNYKlDCLitDIKDILDSLGY-- 160
Cdd:COG1506   15 YLPADGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVD-DVL--AAIDYLAARPYvd 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 161 -SKCVLIGHDWGGMIAWLIAICYPEMVmKLIVINFPHPNVFTeyilrhpaqllkssyyYFFQIPWFPEFMFsindfkvlk 239
Cdd:COG1506   92 pDRIGIYGHSYGGYMALLAAARHPDRF-KAAVALAGVSDLRS----------------YYGTTREYTERLM--------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 240 hlftshstgigrkgcQLTTEDLEAYIyvfsqpgALSgPINHYRNIfsclplkhhmvTTPTLLLWGENDAFMEVEMAE--V 317
Cdd:COG1506  146 ---------------GGPWEDPEAYA-------ARS-PLAYADKL-----------KTPLLLIHGEADDRVPPEQAErlY 191
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 218777837 318 TKIYVKN-YFRLTILSEASHWLQQDQPDIVNKLIWTFLKE 356
Cdd:COG1506  192 EALKKAGkPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
73-206 9.38e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 65.02  E-value: 9.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  73 YVRIKDSglRFHYVAAGErGKPlMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAP-----IHRQNYKLDCL 147
Cdd:PRK03592  11 RVEVLGS--RMAYIETGE-GDP-IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPdidytFADHARYLDAW 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 218777837 148 ItdikdilDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLivinfphpnVFTEYILR 206
Cdd:PRK03592  87 F-------DALGLDDVVLVGHDWGSALGFDWAARHPDRVRGI---------AFMEAIVR 129
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
70-356 4.26e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 60.14  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  70 THCYVRIKDSGLRfhYVAAGERGkPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQN-----YKL 144
Cdd:PLN02824   9 ETRTWRWKGYNIR--YQRAGTSG-PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfYTF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 145 DCLITDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINfphPNVFTEYILRHPAqllkssyyyfFQIPW 224
Cdd:PLN02824  86 ETWGEQLNDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLIN---ISLRGLHIKKQPW----------LGRPF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 225 FPEFMFSINDFKVLKHLFTSHSTG--IGRKGCQ-------LTTEDLEAYIyvfsQPGALSGPINHYRNI--FSCLPLKHH 293
Cdd:PLN02824 153 IKAFQNLLRETAVGKAFFKSVATPetVKNILCQcyhddsaVTDELVEAIL----RPGLEPGAVDVFLDFisYSGGPLPEE 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218777837 294 M---VTTPTLLLWGENDAFMEVEMAEVTKIYvKNYFRLTILSEASHWLQQDQPDIVNKLIWTFLKE 356
Cdd:PLN02824 229 LlpaVKCPVLIAWGEKDPWEPVELGRAYANF-DAVEDFIVLPGVGHCPQDEAPELVNPLIESFVAR 293
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
96-179 7.42e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 58.25  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   96 MLLLHGFpefWYSWRYQLREFKSEYRVVALDLRGYGETDAPihrqNYKLDCLItDIKDILDSLGYSK-CVLIGHDWGGMI 174
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADLA-DLAALLDELGAARpVVLVGHSLGGAV 72

                  ....*
gi 218777837  175 AWLIA 179
Cdd:pfam12697  73 ALAAA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
69-192 2.32e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 58.42  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  69 GTHCYVRIkdSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQNykLDCLI 148
Cdd:PRK14875 109 PAPRKARI--GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELA 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 218777837 149 TDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVI 192
Cdd:PRK14875 185 AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
93-190 9.36e-08

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: 52.22  E-value: 9.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   93 KPLMLLLHGFPEfwYSWRYQ---LREFKSEYRVVALDLRGYGETD-APIHRQNYklDCLITDIKDILDSL----GYSKCV 164
Cdd:pfam12146   4 RAVVVLVHGLGE--HSGRYAhlaDALAAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLPLF 79
                          90       100
                  ....*....|....*....|....*.
gi 218777837  165 LIGHDWGGMIAWLIAICYPEMVMKLI 190
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLI 105
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
89-193 7.16e-06

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: 46.99  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   89 GERGKPLMLLLHGFP----EFWYSWRYQLREFKSEyrVVALDLRGYGETDAPIH--RQNYKLDCLITDIKDILDSLGYSK 162
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98
                          90       100       110
                  ....*....|....*....|....*....|.
gi 218777837  163 CVLIGHDWGGMIAWLIAICYPEMVMKLIVIN 193
Cdd:TIGR01250  99 FYLLGHSWGGMLAQEYALKYGQHLKGLIISS 129
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
97-196 1.39e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.66  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  97 LLLHGFPEFWYSWRYQLREFKSE-YRVVALDlrgYGETDAPIHRQnykLDCLITDIKDILDSLGYSKCVLIGHDWGGMIA 175
Cdd:COG1075    9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALN---YPSTNGSIEDS---AEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82
                         90       100
                 ....*....|....*....|...
gi 218777837 176 --WLIAICYPEMVMKLIVINFPH 196
Cdd:COG1075   83 ryYLKRLGGAAKVARVVTLGTPH 105
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
89-343 1.58e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 46.44  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  89 GERGKPLMLLLHGFPEfwySWRYQLREF---KSEYRVVALDLRGYGETDAPIHRqnykldCLITDIKD--ILDSL----- 158
Cdd:PLN02894 101 SKEDAPTLVMVHGYGA---SQGFFFRNFdalASRFRVIAIDQLGWGGSSRPDFT------CKSTEETEawFIDSFeewrk 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 159 --GYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVI---NFP-HPNVFTEYILRH----PAQLLKSSYYYFFQI------ 222
Cdd:PLN02894 172 akNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVgpaGFSsESDDKSEWLTKFratwKGAVLNHLWESNFTPqkiirg 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 223 --PWFPEFMfsindFKVLKHLFTSHSTGIGrkgcqLTTED---LEAYIY-VFSQPGALSGPINHYRNI--FSCLPLKH-- 292
Cdd:PLN02894 252 lgPWGPNLV-----RRYTTARFGAHSTGDI-----LSEEEsklLTDYVYhTLAAKASGELCLKYIFSFgaFARKPLLEsa 321
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218777837 293 HMVTTPTLLLWGENDaFMEVEMAEVTKIYVKNYFRLTILSEASHWLQQDQP 343
Cdd:PLN02894 322 SEWKVPTTFIYGRHD-WMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNP 371
PRK10673 PRK10673
esterase;
114-193 2.01e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.49  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 114 REFKSEYRVVALDLRGYG------ETDAPIHRQnykldclitDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVM 187
Cdd:PRK10673  37 RDLVNDHDIIQVDMRNHGlsprdpVMNYPAMAQ---------DLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRID 107

                 ....*.
gi 218777837 188 KLIVIN 193
Cdd:PRK10673 108 KLVAID 113
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
90-356 2.41e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.32  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  90 ERGKPLMLLLHGFPEFWYSWRYQLREFKSE-YRVVALDLRGYGETDAPIHRQNYKlDClITDIKDILDSL--GYSKCVLI 166
Cdd:COG1647   12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLKTTWE-DW-LEDVEEAYEILkaGYDKVIVI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 167 GHDWGGMIAWLIAICYPEmVMKLIVINfphPNVFteyiLRHPAQLLKSSYYYFfqIPWFPEFMFSINDFKVLKHlftshs 246
Cdd:COG1647   90 GLSMGGLLALLLAARYPD-VAGLVLLS---PALK----IDDPSAPLLPLLKYL--ARSLRGIGSDIEDPEVAEY------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 247 tgigrkgcqlttedleAYIYVfsqpgalsgPINHYRNIFSCL-----PLKHhmVTTPTLLLWGENDafmEVEMAEVTKIY 321
Cdd:COG1647  154 ----------------AYDRT---------PLRALAELQRLIrevrrDLPK--ITAPTLIIQSRKD---EVVPPESARYI 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 218777837 322 VKNY----FRLTILSEASHW--LQQDQPDIVNKLIwTFLKE 356
Cdd:COG1647  204 YERLgspdKELVWLEDSGHVitLDKDREEVAEEIL-DFLER 243
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
82-346 1.33e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.29  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  82 RFHYVAAGE----RGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPiHRQNYKLDCLITDIKDILDS 157
Cdd:PLN02679  73 SINYLVKGSpevtSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP-PGFSYTMETWAELILDFLEE 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 158 LGYSKCVLIGHDWGGMiAWLIAIC--YPEMVMKLIVIN----FPHPNVFTEYILRHPAQLLkSSYYYFFQIPWFPEFMFS 231
Cdd:PLN02679 152 VVQKPTVLIGNSVGSL-ACVIAASesTRDLVRGLVLLNcaggMNNKAVVDDWRIKLLLPLL-WLIDFLLKQRGIASALFN 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837 232 -INDFKVLKHLFTSHstgIGRKgcQLTTEDLeayIYVFSQPGALSGPINHYRNIFSCLPLKHHM-----VTTPTLLLWGE 305
Cdd:PLN02679 230 rVKQRDNLKNILLSV---YGNK--EAVDDEL---VEIIRGPADDEGALDAFVSIVTGPPGPNPIkliprISLPILVLWGD 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 218777837 306 NDAFMEVEmAEVTKIYVK-----NYFRLTILSEASHWLQQDQPDIV 346
Cdd:PLN02679 302 QDPFTPLD-GPVGKYFSSlpsqlPNVTLYVLEGVGHCPHDDRPDLV 346
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
119-191 2.21e-04

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: 42.29  E-value: 2.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218777837  119 EYRVVALDLRGYGETDAPihRQNYKLDCLITDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIV 191
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTP--RHPYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLIL 121
PRK08775 PRK08775
homoserine O-succinyltransferase;
81-196 5.67e-04

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 41.31  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  81 LRFHYVAAGERGKPLMLLLHG------------FPEF-WysWRYQLREFK----SEYRVVALDLRGY-GETDAPIHRQNY 142
Cdd:PRK08775  46 LRLRYELIGPAGAPVVFVAGGisahrhvaatatFPEKgW--WEGLVGSGRaldpARFRLLAFDFIGAdGSLDVPIDTADQ 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 218777837 143 KldcliTDIKDILDSLGYSKC-VLIGHDWGGMIAWLIAICYPEMVMKLIVINFPH 196
Cdd:PRK08775 124 A-----DAIALLLDALGIARLhAFVGYSYGALVGLQFASRHPARVRTLVVVSGAH 173
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
92-336 9.67e-04

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: 40.18  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837   92 GKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGEtdapiHRQNYKLDclITDIKDILDSLGYSKCVLIGHDWG 171
Cdd:TIGR01738   3 GNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  172 GMIAWLIAICYPEMVMKLIVI----------NFPH---PNVFTEYilrhpAQLLKSsyyyffqipwfpEFMFSINDFKVL 238
Cdd:TIGR01738  76 GLVALHIAATHPDRVRALVTVasspcfsareDWPEgikPDVLTGF-----QQQLSD------------DYQRTIERFLAL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  239 KHLFTSHSTGIGRKGCQLttedleayiyVFSQPGALSGPINHYRNIFSCLPLKHHM--VTTPTLLLWGENDAFMEVEMAE 316
Cdd:TIGR01738 139 QTLGTPTARQDARALKQT----------LLARPTPNVQVLQAGLEILATVDLRQPLqnISVPFLRLYGYLDGLVPAKVVP 208
                         250       260
                  ....*....|....*....|
gi 218777837  317 VTKIYVKnYFRLTILSEASH 336
Cdd:TIGR01738 209 MLDKLAP-HSELYIFAKAAH 227
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
83-179 1.85e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218777837  83 FHYVAAGERGKPLMLLLHGfpefWYSW----RYQLREFKSE-YRVVALDLRGYGETDAPIHR-----QNYKLDCLITDIK 152
Cdd:COG0412   19 YLARPAGGGPRPGVVVLHE----IFGLnphiRDVARRLAAAgYVVLAPDLYGRGGPGDDPDEaralmGALDPELLAADLR 94
                         90       100       110
                 ....*....|....*....|....*....|...
gi 218777837 153 ---DILDSLGY---SKCVLIGHDWGGMIAWLIA 179
Cdd:COG0412   95 aalDWLKAQPEvdaGRVGVVGFCFGGGLALLAA 127
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH