|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
77-313 |
4.30e-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: 282.18 E-value: 4.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 77 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMKSRHPDLPVFI 156
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 157 VGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTL-GSIESKWVSRDTTQVEAYEAD 235
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007664657 236 ELNfHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALHHDL 313
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
60-331 |
5.68e-81 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 247.88 E-value: 5.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 60 IVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 139
Cdd:PHA02857 5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 140 QHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSLTLGSIES 219
Cdd:PHA02857 85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 220 KWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApSSDKKI 299
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241
|
250 260 270
....*....|....*....|....*....|..
gi 2007664657 300 KVYEGGYHALHHDLPEVAESVLKEVTSWITER 331
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNR 273
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
55-330 |
1.84e-47 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 159.78 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 55 ADLQHIVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 134
Cdd:COG2267 3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 135 IRDsLQHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFlakvlnhmlpsltl 214
Cdd:COG2267 83 VDD-LRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 215 gsieskwvsrdttqveayeadelnfhggirvsfgiqlmgAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApS 294
Cdd:COG2267 148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 2007664657 295 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWITE 330
Cdd:COG2267 188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
110-328 |
1.03e-10 |
|
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: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 110 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHIDQMKS--------RHPD------------LPVFIVGHSMGGAIS 166
Cdd:TIGR01607 77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetKSDDesydivntkenrLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 167 -----ILTACERPSD---FAGVALIAPMVQM----NPDSATpFKVFLAKVLNHM-------LPSLTLGSIESKWVSrdtt 227
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 228 qvEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSI--SWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGG 305
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
|
250 260
....*....|....*....|...
gi 2007664657 306 YHALhhDLPEVAESVLKEVTSWI 328
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
137-170 |
1.44e-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: 42.46 E-value: 1.44e-04
10 20 30
....*....|....*....|....*....|....
gi 2007664657 137 DSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 170
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 ... |
77-313 |
4.30e-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: 282.18 E-value: 4.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 77 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMKSRHPDLPVFI 156
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 157 VGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTL-GSIESKWVSRDTTQVEAYEAD 235
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007664657 236 ELNfHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALHHDL 313
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
60-331 |
5.68e-81 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 247.88 E-value: 5.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 60 IVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSL 139
Cdd:PHA02857 5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 140 QHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSLTLGSIES 219
Cdd:PHA02857 85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 220 KWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApSSDKKI 299
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241
|
250 260 270
....*....|....*....|....*....|..
gi 2007664657 300 KVYEGGYHALHHDLPEVAESVLKEVTSWITER 331
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWIFNR 273
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
55-330 |
1.84e-47 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 159.78 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 55 ADLQHIVNADGLHLFCRHWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVY 134
Cdd:COG2267 3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 135 IRDsLQHIDQMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFlakvlnhmlpsltl 214
Cdd:COG2267 83 VDD-LRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 215 gsieskwvsrdttqveayeadelnfhggirvsfgiqlmgAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENApS 294
Cdd:COG2267 148 ---------------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 2007664657 295 SDKKIKVYEGGYHALHHDlpEVAESVLKEVTSWITE 330
Cdd:COG2267 188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
61-331 |
3.21e-47 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 163.00 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 61 VNADGLHLFCRHWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDS 138
Cdd:PLN02385 67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 139 LQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKVFLAKV-LNHMLPSLTLG 215
Cdd:PLN02385 147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILIlLANLLPKAKLV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 216 SIE--SKWVSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAP 293
Cdd:PLN02385 227 PQKdlAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYEKAS 306
|
250 260 270
....*....|....*....|....*....|....*....
gi 2007664657 294 SSDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWITER 331
Cdd:PLN02385 307 SSDKKLKLYEDAYHSILEGEPdEMIFQVLDDIISWLDSH 345
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
65-338 |
9.55e-42 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 148.00 E-value: 9.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 65 GLHLFCRHWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQH 141
Cdd:PLN02298 42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 142 IDQMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQMNPDSATPFKV-----FLAKVLNhMLPSLTL 214
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVARFLP-TLAIVPT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 215 GSIESKWVsRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPS 294
Cdd:PLN02298 201 ADLLEKSV-KVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKS 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2007664657 295 SDKKIKVYEGGYHALHHDLP-EVAESVLKEVTSWITERLPATTPP 338
Cdd:PLN02298 280 EDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
68-332 |
3.20e-37 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 137.72 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 68 LFCRHWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQVYIRDSLQHIDQMK 146
Cdd:PLN02652 123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 147 SRHPDLPVFIVGHSMGGAIsILTACERPS---DFAGVALIAPMVQMNPdsATPFKVFLAKVLNHMLPSLTLGSIESKW-- 221
Cdd:PLN02652 203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGip 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 222 VSRDTTQVEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKV 301
Cdd:PLN02652 280 VSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359
|
250 260 270
....*....|....*....|....*....|.
gi 2007664657 302 YEGGYHALHHDlPEvAESVLKEVTSWITERL 332
Cdd:PLN02652 360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
76-322 |
7.76e-27 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 106.18 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 76 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKDFQVYIRDSLQHIDQMKSRHPdlP 153
Cdd:COG1647 12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 154 VFIVGHSMGGAISILTACERPsDFAGVALIAPMVQMNPDSAtpfkvFLAKVLNHMlpsltlgsieSKWVSRDTTQVEAYE 233
Cdd:COG1647 86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 234 ADELNFHGgIRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGGYHALH--H 311
Cdd:COG1647 150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldK 228
|
250
....*....|.
gi 2007664657 312 DLPEVAESVLK 322
Cdd:COG1647 229 DREEVAEEILD 239
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
59-333 |
5.47e-19 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 84.68 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 59 HIVNADGLHLFCRHWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmnikdFQVYIR 136
Cdd:COG1506 1 TFKSADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 137 DSLQHIDQMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVALIAPMVqmNPDSATPFKVFLAKVLNHMLPSlt 213
Cdd:COG1506 76 DVLAAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 214 lgsieskwvsrdttQVEAYEAdelnfhggirvsfgIQLMGAAARIEReipsiswPFLLLHGDADKLCDIRGSKMMYENAP 293
Cdd:COG1506 151 --------------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALK 195
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2007664657 294 SS--DKKIKVYEGGYHALhhdLPEVAESVLKEVTSWITERLP 333
Cdd:COG1506 196 KAgkPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
58-331 |
9.60e-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: 83.51 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 58 QHIVNADGLHLFCRHWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkDFQVYIRD 137
Cdd:COG0596 4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 138 SLQHIDQMKSRhpdlPVFIVGHSMGGAISILTACERPSDFAGVALIAPMVQmnpdsatpfkvFLAKVLNHMlpsltlgsi 217
Cdd:COG0596 79 LAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRRP--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 218 eskwvsrdttqveayEADELNFHGGIRVSFGIQLMGAAARIEReipsiswPFLLLHGDADKLCDIRGSKMMYENAPssDK 297
Cdd:COG0596 135 ---------------GLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190
|
250 260 270
....*....|....*....|....*....|....
gi 2007664657 298 KIKVYEGGYHALHHDLPEVaesVLKEVTSWITER 331
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
59-332 |
1.16e-18 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 83.81 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 59 HIVNADGLHLFCRHWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKDFQvyIR 136
Cdd:COG1073 14 TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 137 DSLQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVALIAPMVQMNPDSATPFKVFLAKVLNH--MLPSL 212
Cdd:COG1073 92 DARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLPGvpYLPNV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 213 TLGSIESKWVSrdttqveayeadelnfhggirvsfgiqlmgAAARIEReipsISWPFLLLHGDADKLCDIRGSKMMYENA 292
Cdd:COG1073 171 RLASLLNDEFD------------------------------PLAKIEK----ISRPLLFIHGEKDEAVPFYMSEDLYEAA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2007664657 293 PsSDKKIKVYEGGYHALHHDLPEvaESVLKEVTSWITERL 332
Cdd:COG1073 217 A-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
110-328 |
1.03e-10 |
|
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: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 110 VFAHDHVGHGQSEG---DRMNIKDFQVYIRDSLQHIDQMKS--------RHPD------------LPVFIVGHSMGGAIS 166
Cdd:TIGR01607 77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetKSDDesydivntkenrLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 167 -----ILTACERPSD---FAGVALIAPMVQM----NPDSATpFKVFLAKVLNHM-------LPSLTLGSIESKWVSrdtt 227
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 228 qvEAYEADELNFHGGIRVSFGIQLMGAAARIEREIPSI--SWPFLLLHGDADKLCDIRGSKMMYENAPSSDKKIKVYEGG 305
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
|
250 260
....*....|....*....|...
gi 2007664657 306 YHALhhDLPEVAESVLKEVTSWI 328
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
59-327 |
1.60e-10 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 60.37 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 59 HIVNADGLHLFCRHWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKDF 131
Cdd:COG0412 7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 132 QVYIRDSLQHIDQMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVAliapmvqmnpdsatpfkvflakvlnhml 209
Cdd:COG0412 87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 210 psltlgsieskwvsrdttqveayeadelNFHGGirvsfgiqlmGAAARIEREIPSISWPFLLLHGDADKLCDIRGSKMMY 289
Cdd:COG0412 138 ----------------------------SFYGG----------LPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2007664657 290 E--NAPSSDKKIKVYEGGYHALHHDL-----PEVAESVLKEVTSW 327
Cdd:COG0412 180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
82-312 |
1.47e-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: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 82 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKDFQVYirDSLQHIDQMKSRHPDLPVFIVGHSM 161
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 162 GGAISILTACERPSDFAGVALIAPMV----------------------QMNPDSATPFKVFLAKVLNHMLPSLTLGSIES 219
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDppheldeadrfilalfpgffdgFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 220 KWVSRdttqveAYEADELNFHGGIRvsFGIQLMGAAARIER--EIPSISWPFLLLHGDADKLCDIRGSKmmYENAPSSDK 297
Cdd:pfam00561 159 LLNKR------FPSGDYALAKSLVT--GALLFIETWSTELRakFLGRLDEPTLIIWGDQDPLVPPQALE--KLAQLFPNA 228
|
250
....*....|....*
gi 2007664657 298 KIKVYEGGYHALHHD 312
Cdd:pfam00561 229 RLVVIPDAGHFAFLE 243
|
|
| PRK10749 |
PRK10749 |
lysophospholipase L2; Provisional |
96-186 |
2.00e-07 |
|
lysophospholipase L2; Provisional
Pssm-ID: 182697 Cd Length: 330 Bit Score: 51.92 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 96 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKDFQVYIRDS----LQHIDQMKSRHpdlpVFIVGHSMGGAIS 166
Cdd:PRK10749 70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145
|
90 100
....*....|....*....|
gi 2007664657 167 ILTACERPSDFAGVALIAPM 186
Cdd:PRK10749 146 TLFLQRHPGVFDAIALCAPM 165
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
83-318 |
5.58e-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: 49.78 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 83 VFIAHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIKDfqvyIRDSLQHIDQMKSRHPdlpVFIVGHSMG 162
Cdd:pfam12697 1 VVLVHGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 163 GAISILTAcerPSDFAGVALIAPMVQMNPDSATPFKVFLAKVLNHMLPSLTLGSIESKWVSRDTTQVEAYEAdelNFHGG 242
Cdd:pfam12697 70 GAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA---ALARL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007664657 243 IRVSFGIQLMGAAARIEREIPsiswpfLLLHGDADKLCDIRGSKMMyenAPSSDKKIKVYEGGYHALHHDLPEVAE 318
Cdd:pfam12697 144 AALLAALALLPLAAWRDLPVP------VLVLAEEDRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
142-196 |
2.73e-06 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 48.08 E-value: 2.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 142 IDQMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVALIA--PMVQMNPDSATP 196
Cdd:COG3509 122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
76-187 |
1.33e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 76 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHG----QSEGDRMNIKDFQVYIRDSLQHID 143
Cdd:COG0400 1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFID 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2007664657 144 QMKSRH--PDLPVFIVGHSMGGAISILTACERPSDFAGVALIAPMV 187
Cdd:COG0400 79 ELEARYgiDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
137-170 |
1.44e-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: 42.46 E-value: 1.44e-04
10 20 30
....*....|....*....|....*....|....
gi 2007664657 137 DSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
157-185 |
3.38e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.24 E-value: 3.38e-04
10 20
....*....|....*....|....*....
gi 2007664657 157 VGHSMGGAISILTACERPSDFAGVALIAP 185
Cdd:PRK14875 202 VGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
135-170 |
5.10e-04 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 39.55 E-value: 5.10e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2007664657 135 IRDSLQH-IDQMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:pfam01764 45 VREQVLAeLKRLLEKYPDYSIVVTGHSLGGALASLAA 81
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
78-184 |
5.91e-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: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 78 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMnikdfQVYIRDSLQHIDQMKSRHP 150
Cdd:COG3571 7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78
|
90 100 110
....*....|....*....|....*....|....
gi 2007664657 151 DLPVFIVGHSMGGAISILTACErPSDFAGVALIA 184
Cdd:COG3571 79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
|
|
| Abhydrolase_11 |
pfam20408 |
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ... |
79-182 |
6.06e-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: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 79 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIkdFQVYIRDSLQHIdqmks 147
Cdd:pfam20408 1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71
|
90 100 110
....*....|....*....|....*....|....*
gi 2007664657 148 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVAL 182
Cdd:pfam20408 72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
136-170 |
1.08e-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: 39.02 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|....*
gi 2007664657 136 RDSLQHIDQMKSRHPDLPVFIVGHSMGGAISILTA 170
Cdd:cd00741 12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
|
|
| PLN02578 |
PLN02578 |
hydrolase |
98-329 |
1.26e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 40.21 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 98 EIAQRLKelsllVFAHDHVGHGQSegDRMNIK-DFQVYIRdslQHIDQMKSRHPDlPVFIVGHSMGGAISILTACERPSD 176
Cdd:PLN02578 108 ELAKKYK-----VYALDLLGFGWS--DKALIEyDAMVWRD---QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPEL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 177 FAGVALIAPMVQMNPDSATPFKV----------FLAKVLNHMLPSLTLG----------SIES--KWVSRDTTQVEAY-- 232
Cdd:PLN02578 177 VAGVALLNSAGQFGSESREKEEAivveetvltrFVVKPLKEWFQRVVLGflfwqakqpsRIESvlKSVYKDKSNVDDYlv 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007664657 233 ----------EADELNFhggiRVSFGIQLMGAAARIEREIPSISWPFLLLHGDADKLCdirgskmmyenAPSSDKKIKVY 302
Cdd:PLN02578 257 esitepaadpNAGEVYY----RLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWV-----------GPAKAEKIKAF 321
|
250 260 270
....*....|....*....|....*....|....
gi 2007664657 303 EGGYHALH-------HDlpEVAESVLKEVTSWIT 329
Cdd:PLN02578 322 YPDTTLVNlqaghcpHD--EVPEQVNKALLEWLS 353
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
154-198 |
2.22e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 39.18 E-value: 2.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2007664657 154 VFIVGHSMGGAISILTACERPSDFAGVALIAPmvQMNPDSATPFK 198
Cdd:COG4099 127 IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
156-185 |
5.02e-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: 5.02e-03
10 20 30
....*....|....*....|....*....|
gi 2007664657 156 IVGHSMGGAISILTACERPSDFAGVALIAP 185
Cdd:COG2819 134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
137-186 |
7.37e-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: 7.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2007664657 137 DSLQHIDQMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVALIAPM 186
Cdd:cd12809 151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
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