|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
40-276 |
2.43e-95 |
|
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: 281.41 E-value: 2.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 40 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMKSRHPDLPVFI 119
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 120 VGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTL-GSIESKWVSRDTTQVEAYEAD 198
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007664659 199 ELNfHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALHHDL 276
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
23-294 |
4.14e-81 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 246.72 E-value: 4.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 23 IVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 102
Cdd:PHA02857 5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 103 QHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSLTLGSIES 182
Cdd:PHA02857 85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 183 KWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApSSDKKI 262
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241
|
250 260 270
....*....|....*....|....*....|..
gi 2007664659 263 KVYEGGYHALHHDLPEVAESVLKEVTSWITER 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNR 273
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
18-293 |
5.41e-48 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 159.78 E-value: 5.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 18 ADLQHIVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 97
Cdd:COG2267 3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 98 IRDsLQHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFlakvlnhmlpsltl 177
Cdd:COG2267 83 VDD-LRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 178 gsieskwvsrdttqveayeadelnfhggirvsfgiqlmgAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApS 257
Cdd:COG2267 148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 2007664659 258 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWITE 293
Cdd:COG2267 188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
73-291 |
7.49e-11 |
|
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.
Pssm-ID: 162444 [Multi-domain] Cd Length: 332 Bit Score: 62.11 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 73 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHIDQMKS--------RHPD------------LPVFIVGHSMGGAIS 129
Cdd:TIGR01607 77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetKSDDesydivntkenrLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 130 -----ILTACERPSD---FAGVALIAPMVQM----NPDSATpFKVFLAKVLNHM-------LPSLTLGSIESKWVSrdtt 190
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 191 qvEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSI--SWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGG 268
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
|
250 260
....*....|....*....|...
gi 2007664659 269 YHALhhDLPEVAESVLKEVTSWI 291
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
100-133 |
1.03e-04 |
|
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: 42.85 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|....
gi 2007664659 100 DSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
40-276 |
2.43e-95 |
|
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: 281.41 E-value: 2.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 40 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMKSRHPDLPVFI 119
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 120 VGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTL-GSIESKWVSRDTTQVEAYEAD 198
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007664659 199 ELNfHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALHHDL 276
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
23-294 |
4.14e-81 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 246.72 E-value: 4.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 23 IVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 102
Cdd:PHA02857 5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 103 QHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSLTLGSIES 182
Cdd:PHA02857 85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 183 KWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApSSDKKI 262
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241
|
250 260 270
....*....|....*....|....*....|..
gi 2007664659 263 KVYEGGYHALHHDLPEVAESVLKEVTSWITER 294
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNR 273
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
18-293 |
5.41e-48 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 159.78 E-value: 5.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 18 ADLQHIVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 97
Cdd:COG2267 3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 98 IRDsLQHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFlakvlnhmlpsltl 177
Cdd:COG2267 83 VDD-LRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 178 gsieskwvsrdttqveayeadelnfhggirvsfgiqlmgAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApS 257
Cdd:COG2267 148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 2007664659 258 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWITE 293
Cdd:COG2267 188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
24-294 |
2.24e-47 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 162.23 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 24 VNADGLHLFCRHWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDS 101
Cdd:PLN02385 67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 102 LQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKV-LNHMLPSLTLG 178
Cdd:PLN02385 147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILIlLANLLPKAKLV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 179 SIE--SKWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAP 256
Cdd:PLN02385 227 PQKdlAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYEKAS 306
|
250 260 270
....*....|....*....|....*....|....*....
gi 2007664659 257 SSDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWITER 294
Cdd:PLN02385 307 SSDKKLKLYEDAYHSILEGEPdEMIFQVLDDIISWLDSH 345
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
28-301 |
7.06e-42 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 147.23 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 28 GLHLFCRHWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQH 104
Cdd:PLN02298 42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 105 IDQMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKV-----FLAKVLNhMLPSLTL 177
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVARFLP-TLAIVPT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 178 GSIESKWVsRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPS 257
Cdd:PLN02298 201 ADLLEKSV-KVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKS 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2007664659 258 SDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWITERLPATTPP 301
Cdd:PLN02298 280 EDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
31-295 |
2.04e-37 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 136.95 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 31 LFCRHWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMK 109
Cdd:PLN02652 123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 110 SRHPDLPVFIVGHSMGGAIsILTACERPS---DFAGVALIAPMVQMNPdsATPFKVFLAKVLNHMLPSLTLGSIESKW-- 184
Cdd:PLN02652 203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGip 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 185 VSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKV 264
Cdd:PLN02652 280 VSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359
|
250 260 270
....*....|....*....|....*....|.
gi 2007664659 265 YEGGYHALHHDlPEvAESVLKEVTSWITERL 295
Cdd:PLN02652 360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
39-285 |
4.27e-27 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 106.18 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 39 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKDFQVYIRDSLQHIDQMKSRHPdlP 116
Cdd:COG1647 12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 117 VFIVGHSMGGAISILTACERPsDFAGVALIAPMVQMNPDSAtpfkvFLAKVLNHMlpsltlgsieSKWVSRDTTQVEAYE 196
Cdd:COG1647 86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 197 ADELNFHGgIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALH--H 274
Cdd:COG1647 150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldK 228
|
250
....*....|.
gi 2007664659 275 DLPEVAESVLK 285
Cdd:COG1647 229 DREEVAEEILD 239
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
22-296 |
3.68e-19 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 84.30 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 22 HIVNADGLHLFCRHWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmnikdFQVYIR 99
Cdd:COG1506 1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 100 DSLQHIDQMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSlt 176
Cdd:COG1506 76 DVLAAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 177 lgsieskwvsrdttQVEAYEAdelnfhggirvsfgIQLMGAAARIEReipsiswPFLLLHGDADKLCDIRGSKMMYENAP 256
Cdd:COG1506 151 --------------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALK 195
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2007664659 257 SS--DKKIKVYEGGYHALhhdLPEVAESVLKEVTSWITERLP 296
Cdd:COG1506 196 KAgkPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
21-294 |
4.46e-19 |
|
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: 83.90 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 21 QHIVNADGLHLFCRHWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkDFQVYIRD 100
Cdd:COG0596 4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 101 SLQHIDQMKSRhpdlPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQmnpdsatpfkvFLAKVLNHMlpsltlgsi 180
Cdd:COG0596 79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRRP--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 181 eskwvsrdttqveayEADELNFHGGIRVSFGIQLMGAAARIEReipsiswPFLLLHGDADKLCDIRGSKMMYENAPssDK 260
Cdd:COG0596 135 ---------------GLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190
|
250 260 270
....*....|....*....|....*....|....
gi 2007664659 261 KIKVYEGGYHALHHDLPEVaesVLKEVTSWITER 294
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
22-295 |
6.76e-19 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 84.20 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 22 HIVNADGLHLFCRHWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQvyIR 99
Cdd:COG1073 14 TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 100 DSLQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVALIAPMVQMNPDSATPFKVFLAKVLNH--MLPSL 175
Cdd:COG1073 92 DARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLPGvpYLPNV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 176 TLGSIESKWVSrdttqveayeadelnfhggirvsfgiqlmgAAARIEReipsISWPFLLLHGDADKLCDIRGSKMMYENA 255
Cdd:COG1073 171 RLASLLNDEFD------------------------------PLAKIEK----ISRPLLFIHGEKDEAVPFYMSEDLYEAA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2007664659 256 PsSDKKIKVYEGGYHALHHDLPEvaESVLKEVTSWITERL 295
Cdd:COG1073 217 A-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
22-290 |
6.39e-11 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 61.14 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 22 HIVNADGLHLFCRHWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKDF 94
Cdd:COG0412 7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 95 QVYIRDSLQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVAliapmvqmnpdsatpfkvflakvlnhml 172
Cdd:COG0412 87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 173 psltlgsieskwvsrdttqveayeadelNFHGGirvsfgiqlmGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMY 252
Cdd:COG0412 138 ----------------------------SFYGG----------LPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2007664659 253 E--NAPSSDKKIKVYEGGYHALHHDL-----PEVAESVLKEVTSW 290
Cdd:COG0412 180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
73-291 |
7.49e-11 |
|
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.
Pssm-ID: 162444 [Multi-domain] Cd Length: 332 Bit Score: 62.11 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 73 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHIDQMKS--------RHPD------------LPVFIVGHSMGGAIS 129
Cdd:TIGR01607 77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetKSDDesydivntkenrLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 130 -----ILTACERPSD---FAGVALIAPMVQM----NPDSATpFKVFLAKVLNHM-------LPSLTLGSIESKWVSrdtt 190
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 191 qvEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSI--SWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGG 268
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
|
250 260
....*....|....*....|...
gi 2007664659 269 YHALhhDLPEVAESVLKEVTSWI 291
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
45-275 |
1.36e-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: 57.51 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 45 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKDFQVYirDSLQHIDQMKSRHPDLPVFIVGHSM 124
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 125 GGAISILTACERPSDFAGVALIAPMV----------------------QMNPDSATPFKVFLAKVLNHMLPSLTLGSIES 182
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDppheldeadrfilalfpgffdgFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 183 KWVSRdttqveAYEADELNFHGGIRvsFGIQLMGAAARIER--EIPSISWPFLLLHGDADKLCDIRGSKmmYENAPSSDK 260
Cdd:pfam00561 159 LLNKR------FPSGDYALAKSLVT--GALLFIETWSTELRakFLGRLDEPTLIIWGDQDPLVPPQALE--KLAQLFPNA 228
|
250
....*....|....*
gi 2007664659 261 KIKVYEGGYHALHHD 275
Cdd:pfam00561 229 RLVVIPDAGHFAFLE 243
|
|
| PRK10749 |
PRK10749 |
lysophospholipase L2; Provisional |
59-149 |
2.09e-07 |
|
lysophospholipase L2; Provisional
Pssm-ID: 182697 Cd Length: 330 Bit Score: 51.54 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 59 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKDFQVYIRDS----LQHIDQMKSRHpdlpVFIVGHSMGGAIS 129
Cdd:PRK10749 70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145
|
90 100
....*....|....*....|
gi 2007664659 130 ILTACERPSDFAGVALIAPM 149
Cdd:PRK10749 146 TLFLQRHPGVFDAIALCAPM 165
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
46-281 |
2.17e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 50.55 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 46 VFIAHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIKDfqvyIRDSLQHIDQMKSRHPdlpVFIVGHSMG 125
Cdd:pfam12697 1 VVLVHGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 126 GAISILTAcerPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTLGSIESKWVSRDTTQVEAYEAdelNFHGG 205
Cdd:pfam12697 70 GAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA---ALARL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007664659 206 IRVSFGIQLMGAAARIEREIPsiswpfLLLHGDADKLCDIRGSKMMyenAPSSDKKIKVYEGGYHALHHDLPEVAE 281
Cdd:pfam12697 144 AALLAALALLPLAAWRDLPVP------VLVLAEEDRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
105-159 |
1.76e-06 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 48.46 E-value: 1.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 105 IDQMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVALIA--PMVQMNPDSATP 159
Cdd:COG3509 122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
100-133 |
1.03e-04 |
|
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: 42.85 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|....
gi 2007664659 100 DSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
39-150 |
1.12e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 39 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHG----QSEGDRMNIKDFQVYIRDSLQHID 106
Cdd:COG0400 1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFID 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2007664659 107 QMKSRH--PDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMV 150
Cdd:COG0400 79 ELEARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
120-148 |
2.69e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.24 E-value: 2.69e-04
10 20
....*....|....*....|....*....
gi 2007664659 120 VGHSMGGAISILTACERPSDFAGVALIAP 148
Cdd:PRK14875 202 VGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
98-133 |
3.67e-04 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 39.94 E-value: 3.67e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2007664659 98 IRDSLQH-IDQMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:pfam01764 45 VREQVLAeLKRLLEKYPDYSIVVTGHSLGGALASLAA 81
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
41-147 |
4.80e-04 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 442792 [Multi-domain] Cd Length: 202 Bit Score: 40.63 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 41 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMnikdfQVYIRDSLQHIDQMKSRHP 113
Cdd:COG3571 7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78
|
90 100 110
....*....|....*....|....*....|....
gi 2007664659 114 DLPVFIVGHSMGGAISILTACErPSDFAGVALIA 147
Cdd:COG3571 79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
|
|
| Abhydrolase_11 |
pfam20408 |
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ... |
42-145 |
6.17e-04 |
|
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.
Pssm-ID: 466557 [Multi-domain] Cd Length: 193 Bit Score: 40.26 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 42 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIkdFQVYIRDSLQHIdqmks 110
Cdd:pfam20408 1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71
|
90 100 110
....*....|....*....|....*....|....*
gi 2007664659 111 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVAL 145
Cdd:pfam20408 72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
99-133 |
8.82e-04 |
|
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: 39.02 E-value: 8.82e-04
10 20 30
....*....|....*....|....*....|....*
gi 2007664659 99 RDSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 133
Cdd:cd00741 12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
|
|
| PLN02578 |
PLN02578 |
hydrolase |
61-292 |
1.00e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 40.21 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 61 EIAQRLKelsllVFAHDHVGHGQSegDRMNIK-DFQVYIRdslQHIDQMKSRHPDlPVFIVGHSMGGAISILTACERPSD 139
Cdd:PLN02578 108 ELAKKYK-----VYALDLLGFGWS--DKALIEyDAMVWRD---QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPEL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 140 FAGVALIAPMVQMNPDSATPFKV----------FLAKVLNHMLPSLTLG----------SIES--KWVSRDTTQVEAY-- 195
Cdd:PLN02578 177 VAGVALLNSAGQFGSESREKEEAivveetvltrFVVKPLKEWFQRVVLGflfwqakqpsRIESvlKSVYKDKSNVDDYlv 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664659 196 ----------EADELNFhggiRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCdirgskmmyenAPSSDKKIKVY 265
Cdd:PLN02578 257 esitepaadpNAGEVYY----RLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWV-----------GPAKAEKIKAF 321
|
250 260 270
....*....|....*....|....*....|....
gi 2007664659 266 EGGYHALH-------HDlpEVAESVLKEVTSWIT 292
Cdd:PLN02578 322 YPDTTLVNlqaghcpHD--EVPEQVNKALLEWLS 353
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
117-161 |
1.93e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 38.80 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2007664659 117 VFIVGHSMGGAISILTACERPSDFAGVALIAPmvQMNPDSATPFK 161
Cdd:COG4099 127 IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
119-148 |
4.56e-03 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 38.04 E-value: 4.56e-03
10 20 30
....*....|....*....|....*....|
gi 2007664659 119 IVGHSMGGAISILTACERPSDFAGVALIAP 148
Cdd:COG2819 134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
100-149 |
6.98e-03 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214008 Cd Length: 280 Bit Score: 37.59 E-value: 6.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2007664659 100 DSLQHIDQMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVALIAPM 149
Cdd:cd12809 151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
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