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Conserved domains on  [gi|1958675260|ref|XP_038947587|]
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epoxide hydrolase 4 isoform X2 [Rattus norvegicus]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-216 1.21e-36

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: 128.19  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIA 147
Cdd:COG0596     3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260 148 DIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN-------------FPHPSVFTDLFNSGIAEDSWALL 214
Cdd:COG0596    78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDevlaalaeplrrpGLAPEALAALLRALARTDLRERL 157


                  ..
gi 1958675260 215 SA 216
Cdd:COG0596   158 AR 159
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 68-216 1.21e-36

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: 128.19  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIA 147
Cdd:COG0596     3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260 148 DIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN-------------FPHPSVFTDLFNSGIAEDSWALL 214
Cdd:COG0596    78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDevlaalaeplrrpGLAPEALAALLRALARTDLRERL 157


                  ..
gi 1958675260 215 SA 216
Cdd:COG0596   158 AR 159
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 92-209 8.88e-24

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: 95.26  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  92 PLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGG 170
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958675260 171 MIAWLIAVCYPEMIMKLIVINFPHPSVFTDLFNSGIAED 209
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL 119
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 71-191 9.66e-18

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 80.01  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  71 YVRIKDSG---LRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLI 146
Cdd:PRK00870   23 YVDVDDGDggpLRMHYVDEGPADGPPVLLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHV 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958675260 147 ADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PRK00870  103 EWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVAN 147
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 87-191 6.12e-10

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: 57.78  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  87 GERGKPLMLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNK 160
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958675260 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, ...
 68-216 1.21e-36

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: 128.19  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  68 THCYVRIKdsGLRFHYVAAGERGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYKLDCLIA 147
Cdd:COG0596     3 TPRFVTVD--GVRLHYREAGPDGPPV-VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKP--AGGYTLDDLAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260 148 DIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN-------------FPHPSVFTDLFNSGIAEDSWALL 214
Cdd:COG0596    78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDevlaalaeplrrpGLAPEALAALLRALARTDLRERL 157


                  ..
gi 1958675260 215 SA 216
Cdd:COG0596   158 AR 159
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 92-209 8.88e-24

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: 95.26  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  92 PLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGG 170
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958675260 171 MIAWLIAVCYPEMIMKLIVINFPHPSVFTDLFNSGIAED 209
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL 119
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 71-191 9.66e-18

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 80.01  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  71 YVRIKDSG---LRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPIHQESYKLDCLI 146
Cdd:PRK00870   23 YVDVDDGDggpLRMHYVDEGPADGPPVLLLHGEPSWSYLYRKMIPILaAAGHRVIAPDLIGFGRSDKPTRREDYTYARHV 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958675260 147 ADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PRK00870  103 EWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVAN 147
PRK05855 PRK05855
SDR family oxidoreductase;
87-174 1.87e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 77.71  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  87 GERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESYKLDCLIADIKDVLDSLGYNKCV-LIG 165
Cdd:PRK05855   21 GDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRPVhLLA 100


                  ....*....
gi 1958675260 166 HDWGGMIAW 174
Cdd:PRK05855  101 HDWGSIQGW 109
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
79-191 8.89e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.42  E-value: 8.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  79 LRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREF-KSEYRVVALDLRGYGESDAPI-HQESYklDCLIADIKDVLDSL 156
Cdd:COG2267    16 LRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRgHVDSF--DDYVDDLRAALDAL 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958675260 157 ---GYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:COG2267    94 rarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 71-184 2.39e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 67.71  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  71 YVRIKDSglRFHYVAAGErGKPlMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPihQESYK-------LD 143
Cdd:PRK03592   11 RVEVLGS--RMAYIETGE-GDP-IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP--DIDYTfadharyLD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958675260 144 CLIadikdvlDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMI 184
Cdd:PRK03592   85 AWF-------DALGLDDVVLVGHDWGSALGFDWAARHPDRV 118
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 73-202 2.48e-13

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 68.37  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  73 RIKDSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQE--SYKLDCLIADIK 150
Cdd:PLN03084  109 QASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPQPGYgfNYTLDEYVSSLE 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958675260 151 DVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVINFP----H---PS---VFTDLF 202
Cdd:PLN03084  189 SLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNPPltkeHaklPStlsEFSNFL 250
PLN02578 PLN02578
hydrolase
 78-191 3.31e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 64.86  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  78 GLRFHYVAAGErGKPLmLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQesYKLDCLIADIKDVLDSLG 157
Cdd:PLN02578   75 GHKIHYVVQGE-GLPI-VLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIE--YDAMVWRDQVADFVKEVV 150

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958675260 158 YNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PLN02578  151 KEPAVLVGNSLGGFTALSTAVGYPELVAGVALLN 184
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 80-178 9.38e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 62.95  E-value: 9.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  80 RFHYVAAGErgKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYN 159
Cdd:PRK03204   25 RIHYIDEGT--GPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERP-SGFGYQIDEHARVIGEFVDHLGLD 101

                          90
                  ....*....|....*....
gi 1958675260 160 KCVLIGHDWGGMIAWLIAV 178
Cdd:PRK03204  102 RYLSMGQDWGGPISMAVAV 120
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 67-190 1.59e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.96  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  67 GTHCYVRIkdSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQESykLDCLI 146
Cdd:PRK14875  109 PAPRKARI--GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGS--LDELA 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958675260 147 ADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVI 190
Cdd:PRK14875  185 AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
83-184 4.50e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 57.72  E-value: 4.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  83 YVAAGERGKPLMLLLHGFPEF-WYSWRHQLREFKSE-YRVVALDLRGYGESDAPIHQEsykldcLIADIKDVLD---SLG 157
Cdd:COG1506    15 YLPADGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDylaARP 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958675260 158 Y---NKCVLIGHDWGGMIAWLIAVCYPEMI 184
Cdd:COG1506    89 YvdpDRIGIYGHSYGGYMALLAAARHPDRF 118
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 87-191 6.12e-10

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: 57.78  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  87 GERGKPLMLLLHGFP----EFWYSWRHQLREFKSEyrVVALDLRGYGESDAPIH--QESYKLDCLIADIKDVLDSLGYNK 160
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPgmshEYLENLRELLKEEGRE--VIMYDQLGCGYSDQPDDsdEELWTIDYFVDELEEVREKLGLDK 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958675260 161 CVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:TIGR01250  99 FYLLGHSWGGMLAQEYALKYGQHLKGLIISS 129
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 94-177 2.01e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.56  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  94 MLLLHGFpefWYSWRHQLREFKSEYRVVALDLRGYGESDAPihqeSYKLDCLiADIKDVLDSLG-YNKCVLIGHDWGGMI 172
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPP----PLDLADL-ADLAALLDELGaARPVVLVGHSLGGAV 72


                  ....*
gi 1958675260 173 AWLIA 177
Cdd:pfam12697  73 ALAAA 77
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 91-188 1.25e-07

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 50.68  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  91 KPLMLLLHGFPEfwYSWR-----HQLreFKSEYRVVALDLRGYGESD-APIHQESYklDCLIADIKDVLDSL----GYNK 160
Cdd:pfam12146   4 RAVVVLVHGLGE--HSGRyahlaDAL--AAQGFAVYAYDHRGHGRSDgKRGHVPSF--DDYVDDLDTFVDKIreehPGLP 77

                          90       100
                  ....*....|....*....|....*...
gi 1958675260 161 CVLIGHDWGGMIAWLIAVCYPEMIMKLI 188
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLI 105
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 68-191 1.46e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 47.81  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  68 THCYVRIKDSGLRfhYVAAGERGkPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPIHQES-----YKL 142
Cdd:PLN02824    9 ETRTWRWKGYNIR--YQRAGTSG-PALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSAppnsfYTF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958675260 143 DCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PLN02824   86 ETWGEQLNDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLIN 134
PRK10673 PRK10673
esterase;
112-201 4.26e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 46.26  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260 112 REFKSEYRVVALDLRGYGESDapiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVIN 191
Cdd:PRK10673   37 RDLVNDHDIIQVDMRNHGLSP---RDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113

                          90
                  ....*....|....*...
gi 1958675260 192 FP--------HPSVFTDL 201
Cdd:PRK10673  114 IApvdyhvrrHDEIFAAI 131
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 90-177 4.33e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.68  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  90 GKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGESDAPiHQESYKLDCLIADIKDVLDSLGYNKCVLIGHDWG 169
Cdd:PLN02679   87 SGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKP-PGFSYTMETWAELILDFLEEVVQKPTVLIGNSVG 165


                  ....*...
gi 1958675260 170 GMiAWLIA 177
Cdd:PLN02679  166 SL-ACVIA 172
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
88-200 4.58e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.39  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  88 ERGKPLMLLLHGF---PEFWYSWRHQLRefKSEYRVVALDLRGYGESDAPIHQESYKlDClIADIKDVLDSL--GYNKCV 162
Cdd:COG1647    12 EGGRKGVLLLHGFtgsPAEMRPLAEALA--KAGYTVYAPRLPGHGTSPEDLLKTTWE-DW-LEDVEEAYEILkaGYDKVI 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958675260 163 LIGHDWGGMIAWLIAVCYPEmIMKLIVINfphPSVFTD 200
Cdd:COG1647    88 VIGLSMGGLLALLLAARYPD-VAGLVLLS---PALKID 121
PHA_depoly_arom TIGR02240
poly(3-hydroxyalkanoate) depolymerase; This family consists of the polyhydroxyalkanoic acid ...
 117-189 5.08e-05

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: 43.45  E-value: 5.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958675260 117 EYRVVALDLRGYGESDAPIHqeSYKLDCLIADIKDVLDSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIV 189
Cdd:TIGR02240  51 DLEVIAFDVPGVGGSSTPRH--PYRFPGLAKLAARMLDYLDYGQVNAIGVSWGGALAQQFAHDYPERCKKLIL 121
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 95-194 9.42e-05

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: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  95 LLLHGFPEFWYSWRHQLREFKSE-YRVVALDlrgYGESDAPIHQESYKLDcliADIKDVLDSLGYNKCVLIGHDWGGMIA 173
Cdd:COG1075     9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALN---YPSTNGSIEDSAEQLA---AFVDAVLAATGAEKVDLVGHSMGGLVA 82

                          90       100
                  ....*....|....*....|...
gi 1958675260 174 -WLIAVC-YPEMIMKLIVINFPH 194
Cdd:COG1075    83 rYYLKRLgGAAKVARVVTLGTPH 105
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
 140-212 7.73e-04

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 40.07  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260 140 YKLDCLIADIKDV-------LDSLGYNKC-VLIGHDWGGMIAWLIAVCYPEMIMKLI-VINFPHPSVFTdlfnSGIAEDS 210
Cdd:PRK06765  134 YGMDFPVVTILDFvrvqkelIKSLGIARLhAVMGPSMGGMQAQEWAVHYPHMVERMIgVIGNPQNDAWT----SVNVLQN 209


                  ..
gi 1958675260 211 WA 212
Cdd:PRK06765  210 WA 211
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
81-182 1.07e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  81 FHYVAAGERGKPLMLLLHGfpefWYSW----RHQLREFKSE-YRVVALDLRGYGESDAPI-----HQESYKLDCLIADIK 150
Cdd:COG0412    19 YLARPAGGGPRPGVVVLHE----IFGLnphiRDVARRLAAAgYVVLAPDLYGRGGPGDDPdearaLMGALDPELLAADLR 94

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958675260 151 DVLDSL------GYNKCVLIGHDWGGMIAWLIAVCYPE 182
Cdd:COG0412    95 AALDWLkaqpevDAGRVGVVGFCFGGGLALLAAARGPD 132
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 90-190 3.00e-03

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: 37.87  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  90 GKPLMLLLHGFPEFWYSWRHQLREFKSEYRVVALDLRGYGEsdapiHQESYKLDclIADIKDVLDSLGYNKCVLIGHDWG 169
Cdd:TIGR01738   3 GNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR-----SRGFGPLS--LADMAEAIAAQAPDPAIWLGWSLG 75

                          90       100
                  ....*....|....*....|.
gi 1958675260 170 GMIAWLIAVCYPEMIMKLIVI 190
Cdd:TIGR01738  76 GLVALHIAATHPDRVRALVTV 96
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 87-190 3.42e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 37.97  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  87 GERGKPLMLLLHGFPE---FWYswrhqlREF---KSEYRVVALDLRGYGESDAPIHQ-------ESYKLDCLIADIKdvl 153
Cdd:PLN02894  101 SKEDAPTLVMVHGYGAsqgFFF------RNFdalASRFRVIAIDQLGWGGSSRPDFTcksteetEAWFIDSFEEWRK--- 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958675260 154 dSLGYNKCVLIGHDWGGMIAWLIAVCYPEMIMKLIVI 190
Cdd:PLN02894  172 -AKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILV 207
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 90-189 4.00e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 37.51  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  90 GKPLMLLLHGFPEFWYSWRhQLREFKSEYRVVALDLRGYGESdapihqESYKLDCLiADIKDVLD----SLGYNKCVLIG 165
Cdd:PRK11126    1 GLPWLVFLHGLLGSGQDWQ-PVGEALPDYPRLYIDLPGHGGS------AAISVDGF-ADVSRLLSqtlqSYNILPYWLVG 72

                          90       100
                  ....*....|....*....|....*.
gi 1958675260 166 HDWGGMIAwLIAVCY--PEMIMKLIV 189
Cdd:PRK11126   73 YSLGGRIA-MYYACQglAGGLCGLIV 97
PRK08775 PRK08775
homoserine O-succinyltransferase;
79-194 6.99e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 37.08  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958675260  79 LRFHYVAAGERGKPLMLLLHG------------FPEF-WysWRHQLREFK----SEYRVVALDLRGY-GESDAPIHQESY 140
Cdd:PRK08775   46 LRLRYELIGPAGAPVVFVAGGisahrhvaatatFPEKgW--WEGLVGSGRaldpARFRLLAFDFIGAdGSLDVPIDTADQ 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958675260 141 kldcliAD-IKDVLDSLGYNKC-VLIGHDWGGMIAWLIAVCYPEMIMKLIVINFPH 194
Cdd:PRK08775  124 ------ADaIALLLDALGIARLhAFVGYSYGALVGLQFASRHPARVRTLVVVSGAH 173
 
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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