|
Name |
Accession |
Description |
Interval |
E-value |
| Abhydrolase_2 |
pfam02230 |
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ... |
1-168 |
1.01e-80 |
|
Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.
Pssm-ID: 396693 [Multi-domain] Cd Length: 217 Bit Score: 238.05 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 1 MPVSLNMNMAMPSWFDIIGLSPDSQEDEVGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAG 80
Cdd:pfam02230 53 IPVTLNGGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 81 VVALSCWLPLRASFPQGPiSGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMINpaNVTFRTYSGMMHSSCIEEMMDV 160
Cdd:pfam02230 133 IVAFSGFLPLPTKFPSHP-NLVTKKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDI 209
|
....*...
gi 686586446 161 KQFIDKHL 168
Cdd:pfam02230 210 KKFLSKHI 217
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
9-169 |
1.83e-39 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 132.72 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 9 MAMPSWFDIIGLspDSQEDEVGIKQAAENVKALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCW 87
Cdd:COG0400 46 PGGRAWFDLSFL--EGREDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 88 LPLRASFPqgPISGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSgMMHSSCIEEMMDVKQFIDKH 167
Cdd:COG0400 124 LPGEEALP--APEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAER 198
|
..
gi 686586446 168 LP 169
Cdd:COG0400 199 LA 200
|
|
| PRK11460 |
PRK11460 |
putative hydrolase; Provisional |
14-121 |
5.24e-04 |
|
putative hydrolase; Provisional
Pssm-ID: 183144 [Multi-domain] Cd Length: 232 Bit Score: 39.25 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 14 WFDIIGLSPDSQEDEVgikqaAENVKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VVALS-CW 87
Cdd:PRK11460 65 WFSVQGITEDNRQARV-----AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY 138
|
90 100 110
....*....|....*....|....*....|....
gi 686586446 88 lplrASFPQGPISGVnkeiAVLQCHGDCDPLVPL 121
Cdd:PRK11460 139 ----ASLPETAPTAT----TIHLIHGGEDPVIDV 164
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
30-72 |
7.23e-03 |
|
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238382 [Multi-domain] Cd Length: 153 Bit Score: 35.17 E-value: 7.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 686586446 30 GIKQAAENVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 72
Cdd:cd00741 2 GFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Abhydrolase_2 |
pfam02230 |
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ... |
1-168 |
1.01e-80 |
|
Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.
Pssm-ID: 396693 [Multi-domain] Cd Length: 217 Bit Score: 238.05 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 1 MPVSLNMNMAMPSWFDIIGLSPDSQEDEVGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAG 80
Cdd:pfam02230 53 IPVTLNGGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 81 VVALSCWLPLRASFPQGPiSGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMINpaNVTFRTYSGMMHSSCIEEMMDV 160
Cdd:pfam02230 133 IVAFSGFLPLPTKFPSHP-NLVTKKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDI 209
|
....*...
gi 686586446 161 KQFIDKHL 168
Cdd:pfam02230 210 KKFLSKHI 217
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
9-169 |
1.83e-39 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 132.72 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 9 MAMPSWFDIIGLspDSQEDEVGIKQAAENVKALIDQ-EVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCW 87
Cdd:COG0400 46 PGGRAWFDLSFL--EGREDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 88 LPLRASFPqgPISGVNKEIAVLQCHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSgMMHSSCIEEMMDVKQFIDKH 167
Cdd:COG0400 124 LPGEEALP--APEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAA--GADVTYREYP-GGHEISPEELADARAWLAER 198
|
..
gi 686586446 168 LP 169
Cdd:COG0400 199 LA 200
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
19-166 |
4.03e-10 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 56.55 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 19 GLSPDSQEDEVGIKQAAENVKALIDQEVKNgiPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALScwlPLRASFPQGP 98
Cdd:COG2267 67 GRSDGPRGHVDSFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA---PAYRADPLLG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 99 ISG-------VNKEIAVLQC-----HGDCDPLVPlmfgSLTVEKLKSMINPaNVTFRTYSGMMHSSCIEE-----MMDVK 161
Cdd:COG2267 142 PSArwlralrLAEALARIDVpvlvlHGGADRVVP----PEAARRLAARLSP-DVELVLLPGARHELLNEPareevLAAIL 216
|
....*
gi 686586446 162 QFIDK 166
Cdd:COG2267 217 AWLER 221
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
29-150 |
9.08e-09 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 29 VGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQ----KLAGVVALSCWL-----PLRASFPQGPi 99
Cdd:COG0657 62 AALEDAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLdltasPLRADLAGLP- 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 686586446 100 sgvnkeiAVLQCHGDCDPLVP--LMFgsltVEKLKSMINPanVTFRTYSGMMH 150
Cdd:COG0657 141 -------PTLIVTGEADPLVDesEAL----AAALRAAGVP--VELHVYPGGGH 180
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
34-152 |
2.48e-08 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 51.51 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 34 AAENVKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALScwlplrasfPQGPISGVN--KEIAVLQ 110
Cdd:COG4099 105 ALDAVLALLDDLIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPIC---------GGGDPANAAnlKKVPVWI 175
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 686586446 111 CHGDCDPLVPLMFGSLTVEKLKSMinPANVTFRTYSGMMHSS 152
Cdd:COG4099 176 FHGAKDDVVPVEESRAMVEALKAA--GADVKYTEYPGVGHNS 215
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
27-121 |
2.01e-07 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 49.23 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 27 DEVGIkqaaenVKALIDQEVKN-GIPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCwLPLRASFPQGPISGvnKE 105
Cdd:COG3509 113 DDVAF------IAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAACAPG--RP 183
|
90
....*....|....*.
gi 686586446 106 IAVLQCHGDCDPLVPL 121
Cdd:COG3509 184 VPVLVIHGTADPTVPY 199
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
33-169 |
1.62e-06 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 46.55 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 33 QAAENVKALIDQEVKNG-IPSNRIILGGFSQGGALSLYTALTTQQKLAGVVALSCWLPLRASFPQG-------------- 97
Cdd:COG1506 72 DEVDDVLAAIDYLAARPyVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTreyterlmggpwed 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 98 --------PISGVNK-EIAVLQCHGDCDPLVPLMFGSLTVEKLKSmiNPANVTFRTYSGMMH----SSCIEEMMDVKQFI 164
Cdd:COG1506 152 peayaarsPLAYADKlKTPLLLIHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGHgfsgAGAPDYLERILDFL 229
|
....*
gi 686586446 165 DKHLP 169
Cdd:COG1506 230 DRHLK 234
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
28-151 |
2.57e-04 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 39.95 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 28 EVGIKQAAENVKALIDqEVKN--GIPSNRIILGGFSQGGALSLYTAlTTQQKLAGVVALSCWLPLRASFPQGP-ISGvnk 104
Cdd:COG0412 83 ALDPELLAADLRAALD-WLKAqpEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPADDLLDLAArIKA--- 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 686586446 105 eiAVLQCHGDCDPLVPLMfgslTVEKLKSMINPANV--TFRTYSGMMHS 151
Cdd:COG0412 158 --PVLLLYGEKDPLVPPE----QVAALEAALAAAGVdvELHVYPGAGHG 200
|
|
| PRK11460 |
PRK11460 |
putative hydrolase; Provisional |
14-121 |
5.24e-04 |
|
putative hydrolase; Provisional
Pssm-ID: 183144 [Multi-domain] Cd Length: 232 Bit Score: 39.25 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 14 WFDIIGLSPDSQEDEVgikqaAENVKALID----QEVKNGIPSNRIILGGFSQGGALSLyTALTTQQKLAG-VVALS-CW 87
Cdd:PRK11460 65 WFSVQGITEDNRQARV-----AAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMAL-EAVKAEPGLAGrVIAFSgRY 138
|
90 100 110
....*....|....*....|....*....|....
gi 686586446 88 lplrASFPQGPISGVnkeiAVLQCHGDCDPLVPL 121
Cdd:PRK11460 139 ----ASLPETAPTAT----TIHLIHGGEDPVIDV 164
|
|
| FSH1 |
pfam03959 |
Serine hydrolase (FSH1); This is a family of serine hydrolases. |
13-120 |
1.98e-03 |
|
Serine hydrolase (FSH1); This is a family of serine hydrolases.
Pssm-ID: 461110 Cd Length: 208 Bit Score: 37.26 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686586446 13 SWFdiigLSPDSQEDEVGIKQAaenVKALIDQEVKNGiPSNRIIlgGFSQGGALSLYtALTTQQKLAG--------VVAL 84
Cdd:pfam03959 70 AWF----FGDDDTNEYLGLDES---LDYVRDYIKENG-PFDGIL--GFSQGAALAAI-LASLLEEGLPlshpplkfAILF 138
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 686586446 85 SCWLPL----RASFPQGPISgvnkeIAVLQCHGDCDPLVP 120
Cdd:pfam03959 139 SGFRPRppiyQEYYSEDPIQ-----TPSLHVIGELDTVVP 173
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
53-85 |
3.89e-03 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 36.46 E-value: 3.89e-03
10 20 30
....*....|....*....|....*....|...
gi 686586446 53 NRIILGGFSQGGALSLYTALtTQQKLAGVVALS 85
Cdd:COG1647 84 DKVIVIGLSMGGLLALLLAA-RYPDVAGLVLLS 115
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
54-95 |
5.05e-03 |
|
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: 36.33 E-value: 5.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 686586446 54 RIILGGFSQGGALSLYTALTTQQKLAGVVALS----------CWLPLRASFP 95
Cdd:pfam00561 70 KVNLVGHSMGGLIALAYAAKYPDRVKALVLLGaldppheldeADRFILALFP 121
|
|
| Cutinase |
pfam01083 |
Cutinase; |
23-82 |
6.36e-03 |
|
Cutinase;
Pssm-ID: 395860 Cd Length: 173 Bit Score: 35.40 E-value: 6.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686586446 23 DSQEDEVGIKQAAENVKALIdQEVKNGIPSNRIILGGFSQGG-----ALSLYTALtTQQKLAGVV 82
Cdd:pfam01083 50 LGQLYAGSASAGANAAAALI-NSANSKCPDTKIVLGGYSQGAqvmdnAICGLPAA-VADKVAAVV 112
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
30-72 |
7.23e-03 |
|
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238382 [Multi-domain] Cd Length: 153 Bit Score: 35.17 E-value: 7.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 686586446 30 GIKQAAENVKALIDQEVKNGI---PSNRIILGGFSQGGALSLYTAL 72
Cdd:cd00741 2 GFYKAARSLANLVLPLLKSALaqyPDYKIHVTGHSLGGALAGLAGL 47
|
|
|