|
Name |
Accession |
Description |
Interval |
E-value |
| PhaC |
COG3243 |
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
34-350 |
2.11e-76 |
|
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 245.25 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 34 PFEIVHQSGIHSVRHYLPLTEesiavgdetlavskKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDVYLIDWG 113
Cdd:COG3243 179 PGKVVYRNDLMELIQYAPTTE--------------KVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 114 KPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQGWSMGGGIALAYTALFK---DENINKIVTFGTPIDGHANGAi 190
Cdd:COG3243 245 NPDAEDRDLGLDDYVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALLAargPDRVASLTLLATPLDFSEPGE- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 191 gqqykrLAHLLKSARINF-RKVPAKLLYTPGWANVIGFKLLDPVGSLKGYW--NLVtqlhdrefvaqHANQAAFIDsLEA 267
Cdd:COG3243 324 ------LGVFIDESQLADlEALMAAKGYLPGRLMAGAFSLLRPNDLIWSYYvnNYL-----------LGENPPPFD-LLY 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 268 -------YPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVVGSEKSEFFIG 340
Cdd:COG3243 386 wnadstrLPGRMHSQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLA 465
|
330
....*....|
gi 2534882393 341 PGGHIGIMSG 350
Cdd:COG3243 466 PGGHIGGIVN 475
|
|
| PHA_synth_III_C |
TIGR01836 |
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ... |
28-366 |
2.52e-50 |
|
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 130895 Cd Length: 350 Bit Score: 171.84 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 28 VRAGLQPFEIVHQSGIHSVRHYLPlteesiavgdetlaVSKKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDV 107
Cdd:TIGR01836 32 IEVGVTPKEVVYREDKVVLYRYTP--------------VKDNTHKTPLLIVYALVNRPYMLDLQEDRSLVRGLLERGQDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 108 YLIDWGKPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQGWSMGGGIALAYTALFKDeNINKIVTFGTPIDGHAN 187
Cdd:TIGR01836 98 YLIDWGYPDRADRYLTLDDYINGYIDKCVDYICRTSKLDQISLLGICQGGTFSLCYAALYPD-KIKNLVTMVTPVDFETP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 188 GAIGQQYKRLAHLLKsARINFRKVPAKLLYtpgwanvIGFKLLDPVG-SLKGYWNLVTQLHDREFVAQHANQAAFIDSLE 266
Cdd:TIGR01836 177 GNMLSNWARHVDIDL-AVDTMGNIPGELLN-------LTFLMLKPFSlGYQKYVNLVDILEDERKVENFLRMEKWIFDSP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 267 AYPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVVGSEKSEFFIGPGGHIG 346
Cdd:TIGR01836 249 DQAGEAFRQFVKDFYQQNGLINGEVEIGGRKVDLKNIKMPILNIYAERDHLVPPDASKALNDLVSSEDYTELSFPGGHIG 328
|
330 340
....*....|....*....|
gi 2534882393 347 IMSGKESPNTIWAKTVSWLN 366
Cdd:TIGR01836 329 IYVSGKAQKEVPPAIGKWLQ 348
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
34-366 |
9.60e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 123.67 E-value: 9.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 34 PFEIVHQSGIHSVRHYLPlteesiavgdETLAVSKKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDVYLIDWG 113
Cdd:PRK07868 39 PFQIVESVPMYRLRRYFP----------PDNRPGQPPVGPPVLMVHPMMMSADMWDVTRDDGAVGILHRAGLDPWVIDFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 114 KPTRKQAGL--TLENYIKEfLPACLNAVREHSGsKKLNLQGWSMGGGIALAYTALFKDENINKIVTFGTPIDGHANGAIG 191
Cdd:PRK07868 109 SPDKVEGGMerNLADHVVA-LSEAIDTVKDVTG-RDVHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGSPVDTLAALPMG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 192 qqykrLAHLLKSARINF--RKVPAKLlYTPGWANVIGFKLLDPVGSLKGYWNLVTQLHDREFVAQHANQAAFIDS--LEA 267
Cdd:PRK07868 187 -----IPAGLAAAAADFmaDHVFNRL-DIPGWMARTGFQMLDPVKTAKARVDFLRQLHDREALLPREQQRRFLESegWIA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 268 YPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVV-GSEKSEFFIgPGGHIG 346
Cdd:PRK07868 261 WSGPAISELLKQFIAHNRMMTGGFAINGQMVTLADITCPVLAFVGEVDDIGQPASVRGIRRAApNAEVYESLI-RAGHFG 339
|
330 340
....*....|....*....|
gi 2534882393 347 IMSGKESPNTIWAKTVSWLN 366
Cdd:PRK07868 340 LVVGSRAAQQTWPTVADWVK 359
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
74-350 |
1.89e-13 |
|
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: 69.46 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 74 PLVLIAP-LAVNMYVYdllpeRSFVRYLMAQGFDVYLIDWGKPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQG 152
Cdd:pfam00561 1 PPVLLLHgLPGSSDLW-----RKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 153 WSMGGGIALAYTALFkDENINKIVTFGTPIDGHAngaigqqykrLAHLLKSARINFrkvpakllytPGWANviGFKLLDP 232
Cdd:pfam00561 76 HSMGGLIALAYAAKY-PDRVKALVLLGALDPPHE----------LDEADRFILALF----------PGFFD--GFVADFA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 233 VGSLKGYWNLVTQLHDRefvaqhanqaaFIDSLEAYPGGALRDWFASIWLENETAHGH---FKVGKAVANFK---DITCP 306
Cdd:pfam00561 133 PNPLGRLVAKLLALLLL-----------RLRLLKALPLLNKRFPSGDYALAKSLVTGAllfIETWSTELRAKflgRLDEP 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2534882393 307 VLGIAGKSDNLANVACCKPITKVVGSEKsEFFIGPGGHIGIMSG 350
Cdd:pfam00561 202 TLIIWGDQDPLVPPQALEKLAQLFPNAR-LVVIPDAGHFAFLEG 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PhaC |
COG3243 |
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
34-350 |
2.11e-76 |
|
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 245.25 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 34 PFEIVHQSGIHSVRHYLPLTEesiavgdetlavskKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDVYLIDWG 113
Cdd:COG3243 179 PGKVVYRNDLMELIQYAPTTE--------------KVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 114 KPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQGWSMGGGIALAYTALFK---DENINKIVTFGTPIDGHANGAi 190
Cdd:COG3243 245 NPDAEDRDLGLDDYVEDGILAAVDAVREITGEDKVNLLGYCLGGTLLAIYAALLAargPDRVASLTLLATPLDFSEPGE- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 191 gqqykrLAHLLKSARINF-RKVPAKLLYTPGWANVIGFKLLDPVGSLKGYW--NLVtqlhdrefvaqHANQAAFIDsLEA 267
Cdd:COG3243 324 ------LGVFIDESQLADlEALMAAKGYLPGRLMAGAFSLLRPNDLIWSYYvnNYL-----------LGENPPPFD-LLY 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 268 -------YPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVVGSEKSEFFIG 340
Cdd:COG3243 386 wnadstrLPGRMHSQYLRDLYLENRLAKGELELGGRPVDLSDITVPVLVVAGEEDHIAPWRSVYALAQLVGGKDVTFVLA 465
|
330
....*....|
gi 2534882393 341 PGGHIGIMSG 350
Cdd:COG3243 466 PGGHIGGIVN 475
|
|
| PHA_synth_III_C |
TIGR01836 |
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ... |
28-366 |
2.52e-50 |
|
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 130895 Cd Length: 350 Bit Score: 171.84 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 28 VRAGLQPFEIVHQSGIHSVRHYLPlteesiavgdetlaVSKKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDV 107
Cdd:TIGR01836 32 IEVGVTPKEVVYREDKVVLYRYTP--------------VKDNTHKTPLLIVYALVNRPYMLDLQEDRSLVRGLLERGQDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 108 YLIDWGKPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQGWSMGGGIALAYTALFKDeNINKIVTFGTPIDGHAN 187
Cdd:TIGR01836 98 YLIDWGYPDRADRYLTLDDYINGYIDKCVDYICRTSKLDQISLLGICQGGTFSLCYAALYPD-KIKNLVTMVTPVDFETP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 188 GAIGQQYKRLAHLLKsARINFRKVPAKLLYtpgwanvIGFKLLDPVG-SLKGYWNLVTQLHDREFVAQHANQAAFIDSLE 266
Cdd:TIGR01836 177 GNMLSNWARHVDIDL-AVDTMGNIPGELLN-------LTFLMLKPFSlGYQKYVNLVDILEDERKVENFLRMEKWIFDSP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 267 AYPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVVGSEKSEFFIGPGGHIG 346
Cdd:TIGR01836 249 DQAGEAFRQFVKDFYQQNGLINGEVEIGGRKVDLKNIKMPILNIYAERDHLVPPDASKALNDLVSSEDYTELSFPGGHIG 328
|
330 340
....*....|....*....|
gi 2534882393 347 IMSGKESPNTIWAKTVSWLN 366
Cdd:TIGR01836 329 IYVSGKAQKEVPPAIGKWLQ 348
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
34-366 |
9.60e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 123.67 E-value: 9.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 34 PFEIVHQSGIHSVRHYLPlteesiavgdETLAVSKKRNKIPLVLIAPLAVNMYVYDLLPERSFVRYLMAQGFDVYLIDWG 113
Cdd:PRK07868 39 PFQIVESVPMYRLRRYFP----------PDNRPGQPPVGPPVLMVHPMMMSADMWDVTRDDGAVGILHRAGLDPWVIDFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 114 KPTRKQAGL--TLENYIKEfLPACLNAVREHSGsKKLNLQGWSMGGGIALAYTALFKDENINKIVTFGTPIDGHANGAIG 191
Cdd:PRK07868 109 SPDKVEGGMerNLADHVVA-LSEAIDTVKDVTG-RDVHLVGYSQGGMFCYQAAAYRRSKDIASIVTFGSPVDTLAALPMG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 192 qqykrLAHLLKSARINF--RKVPAKLlYTPGWANVIGFKLLDPVGSLKGYWNLVTQLHDREFVAQHANQAAFIDS--LEA 267
Cdd:PRK07868 187 -----IPAGLAAAAADFmaDHVFNRL-DIPGWMARTGFQMLDPVKTAKARVDFLRQLHDREALLPREQQRRFLESegWIA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 268 YPGGALRDWFASIWLENETAHGHFKVGKAVANFKDITCPVLGIAGKSDNLANVACCKPITKVV-GSEKSEFFIgPGGHIG 346
Cdd:PRK07868 261 WSGPAISELLKQFIAHNRMMTGGFAINGQMVTLADITCPVLAFVGEVDDIGQPASVRGIRRAApNAEVYESLI-RAGHFG 339
|
330 340
....*....|....*....|
gi 2534882393 347 IMSGKESPNTIWAKTVSWLN 366
Cdd:PRK07868 340 LVVGSRAAQQTWPTVADWVK 359
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
74-350 |
1.89e-13 |
|
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: 69.46 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 74 PLVLIAP-LAVNMYVYdllpeRSFVRYLMAQGFDVYLIDWGKPTRKQAGLTLENYIKEFLPACLNAVREHSGSKKLNLQG 152
Cdd:pfam00561 1 PPVLLLHgLPGSSDLW-----RKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 153 WSMGGGIALAYTALFkDENINKIVTFGTPIDGHAngaigqqykrLAHLLKSARINFrkvpakllytPGWANviGFKLLDP 232
Cdd:pfam00561 76 HSMGGLIALAYAAKY-PDRVKALVLLGALDPPHE----------LDEADRFILALF----------PGFFD--GFVADFA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 233 VGSLKGYWNLVTQLHDRefvaqhanqaaFIDSLEAYPGGALRDWFASIWLENETAHGH---FKVGKAVANFK---DITCP 306
Cdd:pfam00561 133 PNPLGRLVAKLLALLLL-----------RLRLLKALPLLNKRFPSGDYALAKSLVTGAllfIETWSTELRAKflgRLDEP 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2534882393 307 VLGIAGKSDNLANVACCKPITKVVGSEKsEFFIGPGGHIGIMSG 350
Cdd:pfam00561 202 TLIIWGDQDPLVPPQALEKLAQLFPNAR-LVVIPDAGHFAFLEG 244
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
71-181 |
9.34e-10 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 55.22 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 71 NKIPLVLIAPLAVNMYVYdllpeRSFVRYLMAQGFDVYLIDWGkptrkQAGLTLENYIKEfLPACLNAVREHSGSKKLNL 150
Cdd:COG1075 4 TRYPVVLVHGLGGSAASW-----APLAPRLRAAGYPVYALNYP-----STNGSIEDSAEQ-LAAFVDAVLAATGAEKVDL 72
|
90 100 110
....*....|....*....|....*....|..
gi 2534882393 151 QGWSMGGGIALAYTA-LFKDENINKIVTFGTP 181
Cdd:COG1075 73 VGHSMGGLVARYYLKrLGGAAKVARVVTLGTP 104
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
53-169 |
1.44e-07 |
|
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: 51.54 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 53 TEESIAVGDETLAVSKK-RNKIPLVLIAPLAVNMYVYdllpeRSFVRYLmAQGFDVYLIDW---GKPTRKQAGLTLENYI 128
Cdd:COG0596 3 TPRFVTVDGVRLHYREAgPDGPPVVLLHGLPGSSYEW-----RPLIPAL-AAGYRVIAPDLrghGRSDKPAGGYTLDDLA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2534882393 129 KEflpacLNAVREHSGSKKLNLQGWSMGGGIALAYTALFKD 169
Cdd:COG0596 77 DD-----LAALLDALGLERVVLVGHSMGGMVALELAARHPE 112
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
94-180 |
6.85e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 46.53 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 94 RSFVRYLMAQGFDVYLIDW---GKPTRKQA-GLTLENYIKEfLPACLNAVREHSGsKKLNLQGWSMGGGIALAYtALFKD 169
Cdd:COG2267 45 AELAEALAAAGYAVLAFDLrghGRSDGPRGhVDSFDDYVDD-LRAALDALRARPG-LPVVLLGHSMGGLIALLY-AARYP 121
|
90
....*....|.
gi 2534882393 170 ENINKIVTFGT 180
Cdd:COG2267 122 DRVAGLVLLAP 132
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
96-216 |
4.06e-04 |
|
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: 41.43 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 96 FVRYLMAQGFDVYLIDWgkptR---KQAGLTleNYIKEF------LPACLNAVREHSGSKKLNLQGWSMGGGIALAYTAL 166
Cdd:pfam12146 23 LADALAAQGFAVYAYDH----RghgRSDGKR--GHVPSFddyvddLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALR 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2534882393 167 FKDeNINKIVTFGTPIDGHANGAIGqqYKRLAHLLKSARINFRKVPAKLL 216
Cdd:pfam12146 97 YPD-KVDGLILSAPALKIKPYLAPP--ILKLLAKLLGKLFPRLRVPNNLL 143
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
94-183 |
2.82e-03 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 38.84 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 94 RSFVRYLMAQGFDVYLID---WGKPTRKQAGLTLENYIkeflpACLNAVREHSG--SKKLNLQGWSMGGGIALaYTALFK 168
Cdd:COG1506 41 LPLAQALASRGYAVLAPDyrgYGESAGDWGGDEVDDVL-----AAIDYLAARPYvdPDRIGIYGHSYGGYMAL-LAAARH 114
|
90
....*....|....*
gi 2534882393 169 DENINKIVTFGTPID 183
Cdd:COG1506 115 PDRFKAAVALAGVSD 129
|
|
| Lipase_2 |
pfam01674 |
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ... |
97-184 |
3.33e-03 |
|
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.
Pssm-ID: 396304 [Multi-domain] Cd Length: 218 Bit Score: 38.48 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534882393 97 VRYLMAQGF---DVYLIDWGKPTRKQAGLTLEN--YIKEfLPACLNAVREHSGSKKLNLQGWSMGGGIAlaytalfkden 171
Cdd:pfam01674 22 SQYFKERGYtlaELYATTWGDGNESTSLQRAEKceYVKQ-IRRFIEAVLGYTGAAKVDIVAHSMGVPIA----------- 89
|
90
....*....|...
gi 2534882393 172 iNKIVTFGTPIDG 184
Cdd:pfam01674 90 -RKAILGGNCVDT 101
|
|
| |
