|
Name |
Accession |
Description |
Interval |
E-value |
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
154-312 |
2.22e-25 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 101.62 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 154 DVYAFDYSGYGFSSGTQ----SEKNMYADVRAVYEHIlKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAP--L 227
Cdd:COG2267 57 AVLAFDLRGHGRSDGPRghvdSFDDYVDDLRAALDAL-RARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPayR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 228 TSALRMFCNNPDKETTCIDKICHINTRVLICHGDHDQRIPMTHGMALYENLKNPVPPLIVHGANHHSIISGEYIEVFTRI 307
Cdd:COG2267 136 ADPLLGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREEVLAAI 215
|
....*
gi 71985387 308 ASFMR 312
Cdd:COG2267 216 LAWLE 220
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
154-227 |
1.29e-10 |
|
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: 60.69 E-value: 1.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985387 154 DVYAFDYSGYGFSSGTQ----SEKNMYADVRAVYEHILKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPL 227
Cdd:pfam12146 33 AVYAYDHRGHGRSDGKRghvpSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPA 110
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
155-236 |
3.02e-04 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 41.80 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 155 VYAFDYSGYGFSSGtqsEKNMYAD----VRAVYEHIL---KTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPL 227
Cdd:PHA02857 55 VFSHDHIGHGRSNG---EKMMIDDfgvyVRDVVQHVVtikSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPL 131
|
90
....*....|
gi 71985387 228 TSALRM-FCN 236
Cdd:PHA02857 132 VNAEAVpRLN 141
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
173-238 |
8.24e-03 |
|
Lipase (class 3). 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: 238287 [Multi-domain] Cd Length: 229 Bit Score: 37.07 E-value: 8.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71985387 173 KNMYADVRAVYEHILKTRPDKKIVVIGYSIG----TTAAVDLAASNPDRLVGVVLIAP---LTSALRMFCNNP 238
Cdd:cd00519 108 KSLYNQVLPELKSALKQYPDYKIIVTGHSLGgalaSLLALDLRLRGPGSDVTVYTFGQprvGNAAFAEYLEST 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
154-312 |
2.22e-25 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 101.62 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 154 DVYAFDYSGYGFSSGTQ----SEKNMYADVRAVYEHIlKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAP--L 227
Cdd:COG2267 57 AVLAFDLRGHGRSDGPRghvdSFDDYVDDLRAALDAL-RARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPayR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 228 TSALRMFCNNPDKETTCIDKICHINTRVLICHGDHDQRIPMTHGMALYENLKNPVPPLIVHGANHHSIISGEYIEVFTRI 307
Cdd:COG2267 136 ADPLLGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREEVLAAI 215
|
....*
gi 71985387 308 ASFMR 312
Cdd:COG2267 216 LAWLE 220
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
155-312 |
1.26e-21 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 91.62 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 155 VYAFDYSGYGFSSGTQSEKnMYADVRAVYEHiLKTRPD---KKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPLTSAL 231
Cdd:COG1506 54 VLAPDYRGYGESAGDWGGD-EVDDVLAAIDY-LAARPYvdpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 232 RMF--------------CNNPD--KETTCIDKICHINTRVLICHGDHDQRIPMTHGMALYENLKNPVPP---LIVHGANh 292
Cdd:COG1506 132 SYYgttreyterlmggpWEDPEayAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPvelLVYPGEG- 210
|
170 180
....*....|....*....|
gi 71985387 293 HSIISGEYIEVFTRIASFMR 312
Cdd:COG1506 211 HGFSGAGAPDYLERILDFLD 230
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
139-313 |
4.23e-20 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 88.05 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 139 PNSMNFSTFANLFET------DVYAFDYSGYGFSSGTQSEKNMYA--DVRAVYEHiLKTRPD---KKIVVIGYSIGTTAA 207
Cdd:COG1073 45 GNGGVKEQRALYAQRlaelgfNVLAFDYRGYGESEGEPREEGSPErrDARAAVDY-LRTLPGvdpERIGLLGISLGGGYA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 208 VDLAASNPdRLVGVVLIAPLTSALRMF---------CNNPDK----ETTC----------IDKICHINTRVLICHGDHDQ 264
Cdd:COG1073 124 LNAAATDP-RVKAVILDSPFTSLEDLAaqrakeargAYLPGVpylpNVRLasllndefdpLAKIEKISRPLLFIHGEKDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71985387 265 RIPMTHGMALYENLKNPVPPLIVHGANHHSIISGEYIEVFTRIASFMRN 313
Cdd:COG1073 203 AVPFYMSEDLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDKLAEFFKK 251
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
140-312 |
1.48e-15 |
|
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: 74.65 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 140 NSMNFSTFANLFETD--VYAFDYSGYGFSSGTQSEKNMYADVRAVYEhILKTRPDKKIVVIGYSIGTTAAVDLAASNPDR 217
Cdd:COG0596 35 SSYEWRPLIPALAAGyrVIAPDLRGHGRSDKPAGGYTLDDLADDLAA-LLDALGLERVVLVGHSMGGMVALELAARHPER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 218 LVGVVLIAPLTSALRMFCNNPD-------------KETTCIDKICHINTRVLICHGDHDQRIPMTHGMALYENLKNpVPP 284
Cdd:COG0596 114 VAGLVLVDEVLAALAEPLRRPGlapealaallralARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPN-AEL 192
|
170 180
....*....|....*....|....*....
gi 71985387 285 LIVHGANHHSIIsgEYIEVFTR-IASFMR 312
Cdd:COG0596 193 VVLPGAGHFPPL--EQPEAFAAaLRDFLA 219
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
177-292 |
6.96e-12 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 64.22 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 177 ADVRAVYEHiLKTRPD---KKIVVIGYSIGTTAAVDLAASNPDrLVGVVLIAPLTSAlrmfcnnpdkeTTCIDKICHINT 253
Cdd:COG0412 91 ADLRAALDW-LKAQPEvdaGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPA-----------DDLLDLAARIKA 157
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 71985387 254 RVLICHGDHDQRIPMTHGMALYENLKNPVPPLIVH---GANH 292
Cdd:COG0412 158 PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHvypGAGH 199
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
155-313 |
9.15e-12 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 64.19 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 155 VYAFDYSGYGFSSGTQSE---KNMYADVRAVYEhILKTRPDKkIVVIGYSIGTTAAVDLAASNPDrLVGVVLIAP----- 226
Cdd:COG1647 45 VYAPRLPGHGTSPEDLLKttwEDWLEDVEEAYE-ILKAGYDK-VIVIGLSMGGLLALLLAARYPD-VAGLVLLSPalkid 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 227 -----LTSALRMF----------CNNPDKETTCIDKIC-------------------HINTRVLICHGDHDQRIPMTHGM 272
Cdd:COG1647 122 dpsapLLPLLKYLarslrgigsdIEDPEVAEYAYDRTPlralaelqrlirevrrdlpKITAPTLIIQSRKDEVVPPESAR 201
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71985387 273 ALYENLKNPVPPLIVHGANHHSIISGEYIE-VFTRIASFMRN 313
Cdd:COG1647 202 YIYERLGSPDKELVWLEDSGHVITLDKDREeVAEEILDFLER 243
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
177-313 |
2.61e-11 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 61.85 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 177 ADVRAVYEHILKTR--PDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAP-LTSALRMFCNNPDKEttcidkichiNT 253
Cdd:COG0400 71 EALAAFIDELEARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGyLPGEEALPAPEAALA----------GT 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985387 254 RVLICHGDHDQRIPMTHGMALYENLKNpvpplivHGANH--------HSIISgeyiEVFTRIASFMRN 313
Cdd:COG0400 141 PVFLAHGTQDPVIPVERAREAAEALEA-------AGADVtyreypggHEISP----EELADARAWLAE 197
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
154-227 |
1.29e-10 |
|
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: 60.69 E-value: 1.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985387 154 DVYAFDYSGYGFSSGTQ----SEKNMYADVRAVYEHILKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPL 227
Cdd:pfam12146 33 AVYAYDHRGHGRSDGKRghvpSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPA 110
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
155-292 |
2.22e-10 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 59.41 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 155 VYAFDYSGYGFSSGT----QSEKnmyADVRAVYEHiLKTRPDKKIVVIGYSIGTTAAVDLAASNPdRLVGVVLIAPltsA 230
Cdd:COG2945 58 VLRFNFRGVGRSEGEfdegRGEL---DDAAAALDW-LRAQNPLPLWLAGFSFGAYVALQLAMRLP-EVEGLILVAP---P 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985387 231 LRMFCNNPDKETTCidkichintRVLICHGDHDQRIPMTHGMALYENLKNPVPPLIVHGANH 292
Cdd:COG2945 130 VNRYDFSFLAPCPA---------PTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADH 182
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
154-230 |
2.55e-09 |
|
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: 56.74 E-value: 2.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985387 154 DVYAFDYSGYGFSSGTQSEKNMY-ADVRAVYEHILKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPLTSA 230
Cdd:pfam00561 29 RVIALDLRGFGKSSRPKAQDDYRtDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPP 106
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
173-313 |
5.27e-07 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 49.54 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 173 KNMYADVRAVYEHILK---TRPDKkIVVIGYSIG--TTAAVdlAASNPDRLVGVVLIAPLTSALRMFCN----------- 236
Cdd:pfam00326 42 QNEFDDFIAAAEYLIEqgyTDPDR-LAIWGGSYGgyLTGAA--LNQRPDLFKAAVAHVPVVDWLAYMSDtslpfteryme 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 237 --NPDKETTCIDKI--------CHINTRVLICHGDHDQRIPMTHGMALYENLK---NPVPPLIVHGANhHSIISGEY-IE 302
Cdd:pfam00326 119 wgNPWDNEEGYDYLspyspadnVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQrkgVPFLLLIFPDEG-HGIGKPRNkVE 197
|
170
....*....|.
gi 71985387 303 VFTRIASFMRN 313
Cdd:pfam00326 198 EYARELAFLLE 208
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
155-233 |
5.14e-06 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 46.70 E-value: 5.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71985387 155 VYAFDYSGYGFSSGTQSEknmYADVRAVYEHILKTRPDKKIVVIGYSIGttAAVDLAASNPDRLVGvVLIAPLTSALRM 233
Cdd:pfam12697 24 VLAPDLPGHGSSSPPPLD---LADLADLAALLDELGAARPVVLVGHSLG--GAVALAAAAAALVVG-VLVAPLAAPPGL 96
|
|
| Abhydrolase_2 |
pfam02230 |
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ... |
154-280 |
2.47e-04 |
|
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: 41.59 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 154 DVYAFDYSGYGFSSGTQSEKNMYADVraVYEHILKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPLTSALRM 233
Cdd:pfam02230 68 DLVGLSPNAKEDEAGIKNSAETIEEL--IDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTK 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71985387 234 FCNNPDKettcidkiCHINTRVLICHGDHDQRIPMTHGMALYENLKN 280
Cdd:pfam02230 146 FPSHPNL--------VTKKTPIFLIHGEEDPVVPLALGKLAKEYLKT 184
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
155-236 |
3.02e-04 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 41.80 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 155 VYAFDYSGYGFSSGtqsEKNMYAD----VRAVYEHIL---KTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAPL 227
Cdd:PHA02857 55 VFSHDHIGHGRSNG---EKMMIDDfgvyVRDVVQHVVtikSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPL 131
|
90
....*....|
gi 71985387 228 TSALRM-FCN 236
Cdd:PHA02857 132 VNAEAVpRLN 141
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
171-294 |
3.07e-04 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 41.49 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 171 SEKNMYADVRAVYEHILKTRP-DKK-IVVIGYSIGTTAAVDLAASNPDRLVGVVLIapltsalrmfCNNPDkettcIDKI 248
Cdd:COG4099 101 SDTKALDAVLALLDDLIAEYRiDPDrIYLTGLSMGGYGTWDLAARYPDLFAAAVPI----------CGGGD-----PANA 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71985387 249 CHI-NTRVLICHGDHDQRIPMTHGMALYENLKNPVPPL---IVHGANHHS 294
Cdd:COG4099 166 ANLkKVPVWIFHGAKDDVVPVEESRAMVEALKAAGADVkytEYPGVGHNS 215
|
|
| DLH |
pfam01738 |
Dienelactone hydrolase family; |
187-292 |
2.05e-03 |
|
Dienelactone hydrolase family;
Pssm-ID: 396343 [Multi-domain] Cd Length: 213 Bit Score: 38.87 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 187 LKTRP---DKKIVVIGYSIGTTAAVDLAASNPdRLVGVVLIAPLTsalrmfcnnPDKETTCIDKichINTRVLICHGDHD 263
Cdd:pfam01738 87 LKSQPevsPKKVGVVGYCMGGALAVLLAAKGP-LVDAAVGFYGVG---------PEPPLIEAPD---IKAPILFHFGEED 153
|
90 100 110
....*....|....*....|....*....|..
gi 71985387 264 QRIPMTHGMALYENLKNPVPPLIVH---GANH 292
Cdd:pfam01738 154 HFVPADSRELIEEALKAANVDHQIHsypGAGH 185
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
137-233 |
4.81e-03 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 38.34 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985387 137 LQPNSMNFSTFANLFET---DVYAFDYSGYGFSSGTQ----SEKNMYADVRAVYEHILKTRPDKKIVVIGYSIGtTAAVD 209
Cdd:PLN02652 145 LNEHSGRYLHFAKQLTScgfGVYAMDWIGHGGSDGLHgyvpSLDYVVEDTEAFLEKIRSENPGVPCFLFGHSTG-GAVVL 223
|
90 100
....*....|....*....|....*..
gi 71985387 210 LAASNP---DRLVGVVLIAPltsALRM 233
Cdd:PLN02652 224 KAASYPsieDKLEGIVLTSP---ALRV 247
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|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
155-226 |
5.24e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 38.39 E-value: 5.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985387 155 VYAFDYSGYGFSSGTQSEKNMYADVRAVyEHILKTRPDKKIVVIGYSIGTTAAVDLAASNPDRLVGVVLIAP 226
Cdd:PRK14875 160 VIALDLPGHGASSKAVGAGSLDELAAAV-LAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
173-238 |
8.24e-03 |
|
Lipase (class 3). 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: 238287 [Multi-domain] Cd Length: 229 Bit Score: 37.07 E-value: 8.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71985387 173 KNMYADVRAVYEHILKTRPDKKIVVIGYSIG----TTAAVDLAASNPDRLVGVVLIAP---LTSALRMFCNNP 238
Cdd:cd00519 108 KSLYNQVLPELKSALKQYPDYKIIVTGHSLGgalaSLLALDLRLRGPGSDVTVYTFGQprvGNAAFAEYLEST 180
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