|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
62-297 |
1.54e-74 |
|
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: 229.02 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 62 EIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIRDIRQHIDLIRPEYPDLPIFLY 141
Cdd:pfam12146 2 EPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 142 GHSMGGGLSVLTAHERPNYFRGILLSAPYITPSPDTATPFKVFLAQVIASVAPKLRI-GKLNSEFLSRDQKQIDEDMNDP 220
Cdd:pfam12146 82 GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981783651 221 LNdHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCNSKDKTFKIYKDCMHMLEHET 297
Cdd:pfam12146 162 LV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
41-316 |
2.55e-67 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 212.05 E-value: 2.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 41 VNHFVNADGNYLFSRYWKPEKEIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIR 120
Cdd:PHA02857 2 ANCMFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 121 DIRQHIDLIRPEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPSpdtATPF-KVFLAQVIASVAPKLRIG 199
Cdd:PHA02857 82 DVVQHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAE---AVPRlNLLAAKLMGIFYPNKIVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 200 KLNSEFLSRDQKQIDEDMNDPLNDHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCNSk 279
Cdd:PHA02857 159 KLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC- 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1981783651 280 DKTFKIYKDCMHMLEHETPEFVEEYFAEVLKWIKERI 316
Cdd:PHA02857 238 NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
43-314 |
4.22e-39 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 137.06 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 43 HFVNADGNYLFSRYWKPEKEIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIRDI 122
Cdd:COG2267 7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 123 RQHIDLIRpEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYItpspdtatpfkvflaqviasvapklrigkln 202
Cdd:COG2267 87 RAALDALR-ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAY------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 203 seflsrdqkqidedMNDPLNdhdGLRAGFAMQFLAMSDklkkiLPSLDIPIFAAHSEADAICDIGGTKLLIEvCNSKDKT 282
Cdd:COG2267 135 --------------RADPLL---GPSARWLRALRLAEA-----LARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPDVE 191
|
250 260 270
....*....|....*....|....*....|..
gi 1981783651 283 FKIYKDCMHMLEHETPEfvEEYFAEVLKWIKE 314
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
95-313 |
3.59e-06 |
|
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: 47.85 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 95 FAHDHYAHGESQG---LRCHVMDYTILIRDIRQHI--------------------DLIRPEYPDLPIFLYGHSMGGGLSV 151
Cdd:TIGR01607 78 YGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 152 ----LTAHERPNYFRG-----ILLSAPYITPSPDTATPFK---VFL--AQVIASVAPKLRIGKlnsEFLSRDQKQIDEDM 217
Cdd:TIGR01607 158 rlleLLGKSNENNDKLnikgcISLSGMISIKSVGSDDSFKfkyFYLpvMNFMSRVFPTFRISK---KIRYEKSPYVNDII 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 218 N-DPLNDHDGLRAGFAMQFLAMSDKLKKILPSL--DIPIFAAHSEADAICDIGGTKLLIEVCNSKDKTFKIYKDCMHMLE 294
Cdd:TIGR01607 235 KfDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVIT 314
|
250
....*....|....*....
gi 1981783651 295 HETPEfvEEYFAEVLKWIK 313
Cdd:TIGR01607 315 IEPGN--EEVLKKIIEWIS 331
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
115-154 |
1.13e-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: 39.77 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1981783651 115 YTILIRDIRQHIDLIRPEYPDLPIFLYGHSMGGGLSVLTA 154
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
62-297 |
1.54e-74 |
|
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: 229.02 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 62 EIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIRDIRQHIDLIRPEYPDLPIFLY 141
Cdd:pfam12146 2 EPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 142 GHSMGGGLSVLTAHERPNYFRGILLSAPYITPSPDTATPFKVFLAQVIASVAPKLRI-GKLNSEFLSRDQKQIDEDMNDP 220
Cdd:pfam12146 82 GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981783651 221 LNdHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCNSKDKTFKIYKDCMHMLEHET 297
Cdd:pfam12146 162 LV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
41-316 |
2.55e-67 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 212.05 E-value: 2.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 41 VNHFVNADGNYLFSRYWKPEKEIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIR 120
Cdd:PHA02857 2 ANCMFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 121 DIRQHIDLIRPEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPSpdtATPF-KVFLAQVIASVAPKLRIG 199
Cdd:PHA02857 82 DVVQHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAE---AVPRlNLLAAKLMGIFYPNKIVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 200 KLNSEFLSRDQKQIDEDMNDPLNDHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCNSk 279
Cdd:PHA02857 159 KLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC- 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1981783651 280 DKTFKIYKDCMHMLEHETPEFVEEYFAEVLKWIKERI 316
Cdd:PHA02857 238 NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
43-314 |
4.22e-39 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 137.06 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 43 HFVNADGNYLFSRYWKPEKEIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIRDI 122
Cdd:COG2267 7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 123 RQHIDLIRpEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYItpspdtatpfkvflaqviasvapklrigkln 202
Cdd:COG2267 87 RAALDALR-ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAY------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 203 seflsrdqkqidedMNDPLNdhdGLRAGFAMQFLAMSDklkkiLPSLDIPIFAAHSEADAICDIGGTKLLIEvCNSKDKT 282
Cdd:COG2267 135 --------------RADPLL---GPSARWLRALRLAEA-----LARIDVPVLVLHGGADRVVPPEAARRLAA-RLSPDVE 191
|
250 260 270
....*....|....*....|....*....|..
gi 1981783651 283 FKIYKDCMHMLEHETPEfvEEYFAEVLKWIKE 314
Cdd:COG2267 192 LVLLPGARHELLNEPAR--EEVLAAILAWLER 221
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
39-315 |
1.04e-38 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 139.14 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 39 GEVNHFVNADGNYLFSRYWKPEKE--IKALVFHVHGYAEHCGRS-KELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDY 115
Cdd:PLN02298 32 GSKSFFTSPRGLSLFTRSWLPSSSspPRALIFMVHGYGNDISWTfQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 116 TILIRDIRQHIDLIR--PEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPSPDTATPFKV-FLAQVIASV 192
Cdd:PLN02298 112 DLVVEDCLSFFNSVKqrEEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpQILTFVARF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 193 APKLRI---GKLNSEFLSRDQKQIDEDMNdPLNDHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGT 269
Cdd:PLN02298 192 LPTLAIvptADLLEKSVKVPAKKIIAKRN-PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVS 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1981783651 270 KLLIEVCNSKDKTFKIYKDCMH-MLEHETPEFVEEYFAEVLKWIKER 315
Cdd:PLN02298 271 RALYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNER 317
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
33-315 |
1.24e-34 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 129.10 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 33 FSGMPFG---EVNHFVNADGNYLFSRYWKPEK-EIKALVFHVHGYAEHCGRSKE-LAKKLMEIGVFSFAHDHYAHGESQG 107
Cdd:PLN02385 52 FKTPPSGiktEESYEVNSRGVEIFSKSWLPENsRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 108 LRCHVMDYTILIRDIRQHIDLI--RPEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPSPDTATPFKVFL 185
Cdd:PLN02385 132 LHGYIPSFDDLVDDVIEHYSKIkgNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 186 AQV-IASVAPKLRI--GKLNSEFLSRDQKQIDEDMNDPLNDHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADA 262
Cdd:PLN02385 212 ILIlLANLLPKAKLvpQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADK 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1981783651 263 ICDIGGTKLLIEVCNSKDKTFKIYKDCMH-MLEHETPEFVEEYFAEVLKWIKER 315
Cdd:PLN02385 292 VTDPSVSKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
44-316 |
8.74e-30 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 116.92 E-value: 8.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 44 FVNADGNYLFSRYWKP-EKEIKALVFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVMDYTILIRDI 122
Cdd:PLN02652 115 FYGARRNALFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 123 RQHIDLIRPEYPDLPIFLYGHSMGGGLsVLTAHERPNY---FRGILLSAPYITPSPdtATPFKVFLAQVIASVAPKLRIG 199
Cdd:PLN02652 195 EAFLEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPSIedkLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 200 KLNSEFL--SRDQKQIDEDMNDPLNDHDGLRAGFAMQFLAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCN 277
Cdd:PLN02652 272 GANKRGIpvSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAA 351
|
250 260 270
....*....|....*....|....*....|....*....
gi 1981783651 278 SKDKTFKIYKDCMHMLEHEtPEfVEEYFAEVLKWIKERI 316
Cdd:PLN02652 352 SRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
102-314 |
6.53e-16 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 75.75 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 102 HGESQG--LRCHVMDYtilIRDIRQHIDLIRPEYPdlPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPSPdtat 179
Cdd:COG1647 53 HGTSPEdlLKTTWEDW---LEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALKIDDP---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 180 pfKVFLAQVIASVAPKLRigklnseflsrdqkQIDEDMNDPLNDHDGLR----AGFAmQFLAMSDKLKKILPSLDIPIFA 255
Cdd:COG1647 124 --SAPLLPLLKYLARSLR--------------GIGSDIEDPEVAEYAYDrtplRALA-ELQRLIREVRRDLPKITAPTLI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981783651 256 AHSEADAICDIGGTKLLIEVCNSKDKTFKIYKDCMHM--LEHETpefvEEYFAEVLKWIKE 314
Cdd:COG1647 187 IQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVitLDKDR----EEVAEEILDFLER 243
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
28-314 |
3.22e-15 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 73.80 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 28 IYPKtFSGMPFGEVnHFVNADGNYLFSRYWKPEKEIKAL--VFHVHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGES 105
Cdd:COG1073 1 IFPP-SDKVNKEDV-TFKSRDGIKLAGDLYLPAGASKKYpaVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 106 QGLRCHVMDYTilIRDIRQHIDLI--RPEYPDLPIFLYGHSMGGGLSVLTAHERPNyFRGILLSAPYITpspdtatpfkv 183
Cdd:COG1073 79 EGEPREEGSPE--RRDARAAVDYLrtLPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSPFTS----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 184 fLAQVIASVApKLRIGKLNSEFLSRDQKQIDEDMNDPLNdhdglragfAMQFLAMsdklkkilpsLDIPIFAAHSEADAI 263
Cdd:COG1073 145 -LEDLAAQRA-KEARGAYLPGVPYLPNVRLASLLNDEFD---------PLAKIEK----------ISRPLLFIHGEKDEA 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1981783651 264 CDIGGTKLLIEVCnSKDKTFKIYKDCMHMLEHETPEfvEEYFAEVLKWIKE 314
Cdd:COG1073 204 VPFYMSEDLYEAA-AEPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKK 251
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
43-316 |
6.28e-11 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 61.19 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 43 HFVNADGNYLFSRYWKPEKEIKA-LVFHVHGYAehCGRSKE---LAKKLMEIGVFSFAHDHYAHGESQGLRchvmdYTIL 118
Cdd:COG1506 1 TFKSADGTTLPGWLYLPADGKKYpVVVYVHGGP--GSRDDSflpLAQALASRGYAVLAPDYRGYGESAGDW-----GGDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 119 IRDIRQHIDLI--RPEYPDLPIFLYGHSMGGGLSVLTAHERPNYFRGILLSAPYITPspdtatpfkvflaqviasvapkl 196
Cdd:COG1506 74 VDDVLAAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDL----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 197 rigklnSEFLSRDQKQIDEDMNDPLNDHDGLRagfAMQFLAMSDKLKKilpsldiPIFAAHSEADAICDIGGTKLLIEVC 276
Cdd:COG1506 131 ------RSYYGTTREYTERLMGGPWEDPEAYA---ARSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEAL 194
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1981783651 277 --NSKDKTFKIYKDCMHMLeheTPEFVEEYFAEVLKWIKERI 316
Cdd:COG1506 195 kkAGKPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHL 233
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
43-315 |
7.62e-09 |
|
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: 55.01 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 43 HFVNADGNYLFSRYWKPEKEikALVFhVHGYAEHCGRSKELAKKLMEiGVFSFAHDHYAHGESQGLRchvMDYTI--LIR 120
Cdd:COG0596 5 RFVTVDGVRLHYREAGPDGP--PVVL-LHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPA---GGYTLddLAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 121 DIRQHIDLIRPEypdlPIFLYGHSMGGGLSVLTAHERPNYFRGIllsapyitpspdtatpfkVFLAQVIASVApklrigk 200
Cdd:COG0596 78 DLAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGL------------------VLVDEVLAALA------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 201 lnseflsrdqkqidEDMNDPLNDHDGLRAGFAMqflAMSDKLKKILPSLDIPIFAAHSEADAICDIGGTKLLIEVCnsKD 280
Cdd:COG0596 129 --------------EPLRRPGLAPEALAALLRA---LARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELL--PN 189
|
250 260 270
....*....|....*....|....*....|....*
gi 1981783651 281 KTFKIYKDCMHMLEHETPefvEEYFAEVLKWIKER 315
Cdd:COG0596 190 AELVVLPGAGHFPPLEQP---EAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
64-286 |
2.05e-07 |
|
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: 50.97 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 64 KALVFHvHGYAEHCGRSKELAKKLMEIGVFSFAHDHYAHGESQGLRCHVmDYTILirDIRQHIDLIRPEYPDLPIFLYGH 143
Cdd:pfam00561 1 PPVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQD-DYRTD--DLAEDLEYILEALGLEKVNLVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 144 SMGGGLSVLTAHERPNYFRGILLSAPyITPSPDTATPFKVFLAQviasvapklrigklnseflsrDQKQIDEDMNDPLND 223
Cdd:pfam00561 77 SMGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILAL---------------------FPGFFDGFVADFAPN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 224 HDGLRAGFAMQFLAMSDKLKKILPSLD---------------------IPIFAAHSEADAICDIGGTKLLIevCNSKDKT 282
Cdd:pfam00561 135 PLGRLVAKLLALLLLRLRLLKALPLLNkrfpsgdyalakslvtgallfIETWSTELRAKFLGRLDEPTLII--WGDQDPL 212
|
....
gi 1981783651 283 FKIY 286
Cdd:pfam00561 213 VPPQ 216
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
66-303 |
5.82e-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: 49.39 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 66 LVFhVHGYAEHcgrSKELAKKLMEiGVFSFAHDHYAHGESQGlrchvMDYTIliRDIRQHIDLIRPEYPDLPIFLYGHSM 145
Cdd:pfam12697 1 VVL-VHGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSP-----PPLDL--ADLADLAALLDELGAARPVVLVGHSL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 146 GGGLSVLTAHERPnyFRGILLsAPYITPSPDTATPFKVFLAQVIASVAPKLRIGKLNSEFLSRDQKQIDEDmndpLNDHD 225
Cdd:pfam12697 69 GGAVALAAAAAAL--VVGVLV-APLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEW----AAALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981783651 226 GLRAGFAMQFLAMSDKLKKILPSLDIpifaaHSEADAICDIGGTKLLIEVcnsKDKTFKIYKDCMHMLEHETPEFVEE 303
Cdd:pfam12697 142 RLAALLAALALLPLAAWRDLPVPVLV-----LAEEDRLVPELAQRLLAAL---AGARLVVLPGAGHLPLDDPEEVAEA 211
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
95-313 |
3.59e-06 |
|
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: 47.85 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 95 FAHDHYAHGESQG---LRCHVMDYTILIRDIRQHI--------------------DLIRPEYPDLPIFLYGHSMGGGLSV 151
Cdd:TIGR01607 78 YGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 152 ----LTAHERPNYFRG-----ILLSAPYITPSPDTATPFK---VFL--AQVIASVAPKLRIGKlnsEFLSRDQKQIDEDM 217
Cdd:TIGR01607 158 rlleLLGKSNENNDKLnikgcISLSGMISIKSVGSDDSFKfkyFYLpvMNFMSRVFPTFRISK---KIRYEKSPYVNDII 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981783651 218 N-DPLNDHDGLRAGFAMQFLAMSDKLKKILPSL--DIPIFAAHSEADAICDIGGTKLLIEVCNSKDKTFKIYKDCMHMLE 294
Cdd:TIGR01607 235 KfDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVIT 314
|
250
....*....|....*....
gi 1981783651 295 HETPEfvEEYFAEVLKWIK 313
Cdd:TIGR01607 315 IEPGN--EEVLKKIIEWIS 331
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
115-154 |
1.13e-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: 39.77 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1981783651 115 YTILIRDIRQHIDLIRPEYPDLPIFLYGHSMGGGLSVLTA 154
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
115-154 |
2.74e-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: 37.87 E-value: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1981783651 115 YTILIRDIRQHIDLIRPEYPDLPIFLYGHSMGGGLSVLTA 154
Cdd:cd00741 7 ARSLANLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
118-147 |
3.12e-03 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 442792 [Multi-domain] Cd Length: 202 Bit Score: 37.94 E-value: 3.12e-03
10 20 30
....*....|....*....|....*....|
gi 1981783651 118 LIRDIRQHIDLIRPEYPDLPIFLYGHSMGG 147
Cdd:COG3571 62 LDAAWRAVIAALRARLAGLPLVIGGKSMGG 91
|
|
| |
