|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
15-536 |
0e+00 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 576.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 15 PSRQVLTSYGPIEGRRLIHEGEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKDHVLSPKTS--P 92
Cdd:pfam00135 1 DSPVVTTSLGRVRGKRLKVDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSglE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 93 QSEDNLTLNIFTPVWTPKNETGFPVILYIHGGGFVSDSAHKYGDMSICQHLvtkDVVVVTIQYRLGFLGFWTTGDSSIPD 172
Cdd:pfam00135 81 GSEDCLYLNVYTPKELKENKNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEG---DVIVVTINYRLGPLGFLSTGDDEAPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 173 NVALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNASCSWAIHPRPLNACRNR 252
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 253 AQEIGvFDGMNTLDWVEKLRELPADKFASALNMEaVDTKTDPELLIGPKYDNLFIPR-PVMELRKE-APMKPRLLGCAKS 330
Cdd:pfam00135 238 AKLVG-CPTSDSAELVECLRSKPAEELLDAQLKL-LVYGSVPFVPFGPVVDGDFLPEhPEELLKSGnFPKVPLLIGVTKD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 331 EGLVFAFFGLNTKHPLHAVQQDVSAILSEKLFPLKARDYQEKALEKLIEIGTD----HSKEEWQRAMVDLKGDSFLNVGI 406
Cdd:pfam00135 316 EGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALREEYLDwgdrDDPETSRRALVELLTDYLFNCPV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 407 QQNVLDVleTQPSTPIYMYSFDYCNPkaygiMGFKLPFKDATHCTDISYVVGNHIVNSFDFNEEDYKMIEITTRLWTNFA 486
Cdd:pfam00135 396 IRFADLH--ASRGTPVYMYSFDYRGS-----SLRYPKWVGVDHGDELPYVFGTPFVGALLFTEEDEKLSRKMMTYWTNFA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17556436 487 KYGNPNGEGDDVahleeKWEPATiESPQTHMALTLQPKLHHVYKQGRPLF 536
Cdd:pfam00135 469 KTGNPNGPEGLP-----KWPPYT-DENGQYLSIDLEPRVKQGLKAERCAF 512
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
19-515 |
1.84e-118 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 358.95 E-value: 1.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 19 VLTSYGPIEGRRlihegEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKD---HVLSPKTSPQSE 95
Cdd:cd00312 2 VVTPNGKVRGVD-----EGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDqlgGGLWNAKLPGSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 96 DNLTLNIFTPvWTPKNETGFPVILYIHGGGFVSDSAHKYGDMSicqhLVTK--DVVVVTIQYRLGFLGFWTTGDSSIPDN 173
Cdd:cd00312 77 DCLYLNVYTP-KNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDG----LAREgdNVIVVSINYRLGVLGFLSTGDIELPGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 174 VALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNASCSWAIhprPLNAcRNRA 253
Cdd:cd00312 152 YGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAI---QENA-RGRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 254 QEIGVFDGMNTLDWVEK---LRELPADKFASALNmEAVDTKTDPELLIGPKYDNLFIPRPVMELRKE--APMKPRLLGCA 328
Cdd:cd00312 228 KRLARLLGCNDTSSAELldcLRSKSAEELLDATR-KLLLFSYSPFLPFGPVVDGDFIPDDPEELIKEgkFAKVPLIIGVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 329 KSEGLVFAFFGLNTKHPLHAVQQDVSAILSEKLFPLKARDYQEKALEKLIEiGTDHSKEEWQRaMVDLKGDSFLNVGIQQ 408
Cdd:cd00312 307 KDEGGYFAAMLLNFDAKLIIETNDRWLELLPYLLFYADDALADKVLEKYPG-DVDDSVESRKN-LSDMLTDLLFKCPARY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 409 NVLDVLETQPStPIYMYSFDYCNPKAYGIMgfkLPFKDATHCTDISYVVGNhIVNSFDFNEEDYKMIEITTRLWTNFAKY 488
Cdd:cd00312 385 FLAQHRKAGGS-PVYAYVFDHRSSLSVGRW---PPWLGTVHGDEIFFVFGN-PLLKEGLREEEEKLSRTMMKYWANFAKT 459
|
490 500
....*....|....*....|....*..
gi 17556436 489 GNPNGEGddvahLEEKWEPATIESPQT 515
Cdd:cd00312 460 GNPNTEG-----NLVVWPAYTSESEKY 481
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
6-540 |
2.94e-107 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 330.31 E-value: 2.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 6 SKHTTPHYPPSRQVLTSYGPIEGRRlihegEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKDHV 85
Cdd:COG2272 2 KRLLAAAAAAAPVVRTEAGRVRGVV-----EGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 86 LS-PKTSPQSEDNLTLNiftpVWTPKNETG--FPVILYIHGGGFVSDSAHkyGDMSICQHLVTKDVVVVTIQYRLGFLGF 162
Cdd:COG2272 77 GDpGGPAPGSEDCLYLN----VWTPALAAGakLPVMVWIHGGGFVSGSGS--EPLYDGAALARRGVVVVTINYRLGALGF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 163 -----WTTGDSSIPDNVALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNAsc 237
Cdd:COG2272 151 lalpaLSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAG-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 238 sWAIHPRPlnacrnRAQEIGV-FdgMNTLDW----VEKLRELPADKFASALNmeAVDTKTDPELLIGPKYDNLFIPRPVM 312
Cdd:COG2272 229 -LSVLTLA------EAEAVGAaF--AAALGVapatLAALRALPAEELLAAQA--ALAAEGPGGLPFGPVVDGDVLPEDPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 313 EL--RKEAPMKPRLLGCAKSEGLVFAFFGlntkhplhavqqdvsailsEKLFPLKARDYQEKALEKL----IEIGTDHSK 386
Cdd:COG2272 298 EAfaAGRAADVPLLIGTNRDEGRLFAALL-------------------GDLGPLTAADYRAALRRRFgddaDEVLAAYPA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 387 EEWQRAMVDLKGDSFlnvgIQQNVLDVLETQPST--PIYMYSFDYCNPKAYGimgfklPFKDATHCTDISYVVGNHIVNS 464
Cdd:COG2272 359 ASPAEALAALATDRV----FRCPARRLAEAHAAAgaPVYLYRFDWRSPPLRG------FGLGAFHGAELPFVFGNLDAPA 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17556436 465 F-DFNEEDYKMIEITTRLWTNFAKYGNPNGEGDDvahleeKWEPATIESPQThMALTLQPKL-HHVYKQGRPLFMAKL 540
Cdd:COG2272 429 LtGLTPADRALSDQMQAYWVNFARTGDPNGPGLP------EWPAYDPEDRAV-MVFDAEPRVvNDPDAEERLDLWDGV 499
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
15-536 |
0e+00 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 576.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 15 PSRQVLTSYGPIEGRRLIHEGEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKDHVLSPKTS--P 92
Cdd:pfam00135 1 DSPVVTTSLGRVRGKRLKVDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSglE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 93 QSEDNLTLNIFTPVWTPKNETGFPVILYIHGGGFVSDSAHKYGDMSICQHLvtkDVVVVTIQYRLGFLGFWTTGDSSIPD 172
Cdd:pfam00135 81 GSEDCLYLNVYTPKELKENKNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEG---DVIVVTINYRLGPLGFLSTGDDEAPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 173 NVALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNASCSWAIHPRPLNACRNR 252
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 253 AQEIGvFDGMNTLDWVEKLRELPADKFASALNMEaVDTKTDPELLIGPKYDNLFIPR-PVMELRKE-APMKPRLLGCAKS 330
Cdd:pfam00135 238 AKLVG-CPTSDSAELVECLRSKPAEELLDAQLKL-LVYGSVPFVPFGPVVDGDFLPEhPEELLKSGnFPKVPLLIGVTKD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 331 EGLVFAFFGLNTKHPLHAVQQDVSAILSEKLFPLKARDYQEKALEKLIEIGTD----HSKEEWQRAMVDLKGDSFLNVGI 406
Cdd:pfam00135 316 EGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALREEYLDwgdrDDPETSRRALVELLTDYLFNCPV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 407 QQNVLDVleTQPSTPIYMYSFDYCNPkaygiMGFKLPFKDATHCTDISYVVGNHIVNSFDFNEEDYKMIEITTRLWTNFA 486
Cdd:pfam00135 396 IRFADLH--ASRGTPVYMYSFDYRGS-----SLRYPKWVGVDHGDELPYVFGTPFVGALLFTEEDEKLSRKMMTYWTNFA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17556436 487 KYGNPNGEGDDVahleeKWEPATiESPQTHMALTLQPKLHHVYKQGRPLF 536
Cdd:pfam00135 469 KTGNPNGPEGLP-----KWPPYT-DENGQYLSIDLEPRVKQGLKAERCAF 512
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
19-515 |
1.84e-118 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 358.95 E-value: 1.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 19 VLTSYGPIEGRRlihegEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKD---HVLSPKTSPQSE 95
Cdd:cd00312 2 VVTPNGKVRGVD-----EGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDqlgGGLWNAKLPGSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 96 DNLTLNIFTPvWTPKNETGFPVILYIHGGGFVSDSAHKYGDMSicqhLVTK--DVVVVTIQYRLGFLGFWTTGDSSIPDN 173
Cdd:cd00312 77 DCLYLNVYTP-KNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDG----LAREgdNVIVVSINYRLGVLGFLSTGDIELPGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 174 VALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNASCSWAIhprPLNAcRNRA 253
Cdd:cd00312 152 YGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAI---QENA-RGRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 254 QEIGVFDGMNTLDWVEK---LRELPADKFASALNmEAVDTKTDPELLIGPKYDNLFIPRPVMELRKE--APMKPRLLGCA 328
Cdd:cd00312 228 KRLARLLGCNDTSSAELldcLRSKSAEELLDATR-KLLLFSYSPFLPFGPVVDGDFIPDDPEELIKEgkFAKVPLIIGVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 329 KSEGLVFAFFGLNTKHPLHAVQQDVSAILSEKLFPLKARDYQEKALEKLIEiGTDHSKEEWQRaMVDLKGDSFLNVGIQQ 408
Cdd:cd00312 307 KDEGGYFAAMLLNFDAKLIIETNDRWLELLPYLLFYADDALADKVLEKYPG-DVDDSVESRKN-LSDMLTDLLFKCPARY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 409 NVLDVLETQPStPIYMYSFDYCNPKAYGIMgfkLPFKDATHCTDISYVVGNhIVNSFDFNEEDYKMIEITTRLWTNFAKY 488
Cdd:cd00312 385 FLAQHRKAGGS-PVYAYVFDHRSSLSVGRW---PPWLGTVHGDEIFFVFGN-PLLKEGLREEEEKLSRTMMKYWANFAKT 459
|
490 500
....*....|....*....|....*..
gi 17556436 489 GNPNGEGddvahLEEKWEPATIESPQT 515
Cdd:cd00312 460 GNPNTEG-----NLVVWPAYTSESEKY 481
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
6-540 |
2.94e-107 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 330.31 E-value: 2.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 6 SKHTTPHYPPSRQVLTSYGPIEGRRlihegEKQVDAFQGIPYAAPPIGNLRFALPQPHEKWTEVRETKSFGARGIQKDHV 85
Cdd:COG2272 2 KRLLAAAAAAAPVVRTEAGRVRGVV-----EGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 86 LS-PKTSPQSEDNLTLNiftpVWTPKNETG--FPVILYIHGGGFVSDSAHkyGDMSICQHLVTKDVVVVTIQYRLGFLGF 162
Cdd:COG2272 77 GDpGGPAPGSEDCLYLN----VWTPALAAGakLPVMVWIHGGGFVSGSGS--EPLYDGAALARRGVVVVTINYRLGALGF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 163 -----WTTGDSSIPDNVALHDMVFALKWVKENIGLFNGDPNNITLMGQSAGGASVDFLSISPVSRDLFQKVIPMGGNAsc 237
Cdd:COG2272 151 lalpaLSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAG-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 238 sWAIHPRPlnacrnRAQEIGV-FdgMNTLDW----VEKLRELPADKFASALNmeAVDTKTDPELLIGPKYDNLFIPRPVM 312
Cdd:COG2272 229 -LSVLTLA------EAEAVGAaF--AAALGVapatLAALRALPAEELLAAQA--ALAAEGPGGLPFGPVVDGDVLPEDPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 313 EL--RKEAPMKPRLLGCAKSEGLVFAFFGlntkhplhavqqdvsailsEKLFPLKARDYQEKALEKL----IEIGTDHSK 386
Cdd:COG2272 298 EAfaAGRAADVPLLIGTNRDEGRLFAALL-------------------GDLGPLTAADYRAALRRRFgddaDEVLAAYPA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 387 EEWQRAMVDLKGDSFlnvgIQQNVLDVLETQPST--PIYMYSFDYCNPKAYGimgfklPFKDATHCTDISYVVGNHIVNS 464
Cdd:COG2272 359 ASPAEALAALATDRV----FRCPARRLAEAHAAAgaPVYLYRFDWRSPPLRG------FGLGAFHGAELPFVFGNLDAPA 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17556436 465 F-DFNEEDYKMIEITTRLWTNFAKYGNPNGEGDDvahleeKWEPATIESPQThMALTLQPKL-HHVYKQGRPLFMAKL 540
Cdd:COG2272 429 LtGLTPADRALSDQMQAYWVNFARTGDPNGPGLP------EWPAYDPEDRAV-MVFDAEPRVvNDPDAEERLDLWDGV 499
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
106-209 |
1.37e-20 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 106 VWTPKNETG-FPVILYIHGGGFVSDSAHKYGDMsiCQHLV-TKDVVVVTIQYRLGflgfwttGDSSIPDnvALHDMVFAL 183
Cdd:COG0657 3 VYRPAGAKGpLPVVVYFHGGGWVSGSKDTHDPL--ARRLAaRAGAAVVSVDYRLA-------PEHPFPA--ALEDAYAAL 71
|
90 100
....*....|....*....|....*.
gi 17556436 184 KWVKENIGLFNGDPNNITLMGQSAGG 209
Cdd:COG0657 72 RWLRANAAELGIDPDRIAVAGDSAGG 97
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
100-209 |
1.91e-16 |
|
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.
Pssm-ID: 466583 [Multi-domain] Cd Length: 215 Bit Score: 78.38 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 100 LNIFTPvwtPKNETGFPVILYIHGGGFVSDSahKYGDMS----ICQHLVTKDVVVVTIQYRLgflgfwtTGDSSIPDnvA 175
Cdd:pfam20434 1 LDIYLP---KNAKGPYPVVIWIHGGGWNSGD--KEADMGfmtnTVKALLKAGYAVASINYRL-------STDAKFPA--Q 66
|
90 100 110
....*....|....*....|....*....|....
gi 17556436 176 LHDMVFALKWVKENIGLFNGDPNNITLMGQSAGG 209
Cdd:pfam20434 67 IQDVKAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
|
|
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
118-209 |
1.36e-15 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 400284 [Multi-domain] Cd Length: 208 Bit Score: 75.71 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 118 ILYIHGGGFVS---DSAHkygdmSICQHLVTK-DVVVVTIQYRLGflgfwttgdssiPDN---VALHDMVFALKWVKENI 190
Cdd:pfam07859 1 LVYFHGGGFVLgsaDTHD-----RLCRRLAAEaGAVVVSVDYRLA------------PEHpfpAAYDDAYAALRWLAEQA 63
|
90
....*....|....*....
gi 17556436 191 GLFNGDPNNITLMGQSAGG 209
Cdd:pfam07859 64 AELGADPSRIAVAGDSAGG 82
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
94-236 |
1.93e-10 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 61.19 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 94 SEDNLTLNIFtpVWTPKNETGFPVILYIHGGGFVSDSAHKYgdmsICQHLVTKDVVVVTIQYRlGF---LGFWTTGDssi 170
Cdd:COG1506 4 SADGTTLPGW--LYLPADGKKYPVVVYVHGGPGSRDDSFLP----LAQALASRGYAVLAPDYR-GYgesAGDWGGDE--- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17556436 171 pdnvaLHDMVFALKWVKENIGLfngDPNNITLMGQSAGGASVdfLSISPVSRDLFQKVIPMGGNAS 236
Cdd:COG1506 74 -----VDDVLAAIDYLAARPYV---DPDRIGIYGHSYGGYMA--LLAAARHPDRFKAAVALAGVSD 129
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
106-277 |
8.34e-07 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 50.35 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 106 VWTPKNETG---FPVILYIHGGGFVSDS-----AHKYGDMSICQHLVTKDVVVVTIQYRLGflGFWTTGDSsipdnvalH 177
Cdd:COG4099 37 LYLPKGYDPgkkYPLVLFLHGAGERGTDnekqlTHGAPKFINPENQAKFPAIVLAPQCPED--DYWSDTKA--------L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 178 DMVFALkwVKENIGLFNGDPNNITLMGQSAGG-ASVDFLSISPvsrDLFQKVIPMGGNASCS----------WAIHprpl 246
Cdd:COG4099 107 DAVLAL--LDDLIAEYRIDPDRIYLTGLSMGGyGTWDLAARYP---DLFAAAVPICGGGDPAnaanlkkvpvWIFH---- 177
|
170 180 190
....*....|....*....|....*....|....*
gi 17556436 247 nacrnraqeiGVFDGM----NTLDWVEKLRELPAD 277
Cdd:COG4099 178 ----------GAKDDVvpveESRAMVEALKAAGAD 202
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
93-210 |
1.44e-04 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 43.75 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 93 QSEDNLTLNifTPVWTPKNETG-FPVILYIHGGGFVSDSAHKYGdmsicQHLVTKDVVVVTIQYRlgFLGfWTTGDSSIP 171
Cdd:COG1073 16 KSRDGIKLA--GDLYLPAGASKkYPAVVVAHGNGGVKEQRALYA-----QRLAELGFNVLAFDYR--GYG-ESEGEPREE 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 17556436 172 DNVALHDMVFALKWVKEnigLFNGDPNNITLMGQSAGGA 210
Cdd:COG1073 86 GSPERRDARAAVDYLRT---LPGVDPERIGLLGISLGGG 121
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
106-277 |
6.20e-04 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 42.15 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 106 VWTP----KNETGFPVILYIHGGGFVSDSAHKYGDM-SICQHLVT----KDVVVVTIQYRLGflgfwTTGDSSIPDNVAL 176
Cdd:COG2382 99 VYLPpgydNPGKKYPVLYLLDGGGGDEQDWFDQGRLpTILDNLIAagkiPPMIVVMPDGGDG-----GDRGTEGPGNDAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 177 HDMVFA--LKWVKENIGLFNgDPNNITLMGQSAGGASVdfLSISPVSRDLFQKVIPMGGnaSCSWAIHPRPLNACRNRAQ 254
Cdd:COG2382 174 ERFLAEelIPFVEKNYRVSA-DPEHRAIAGLSMGGLAA--LYAALRHPDLFGYVGSFSG--SFWWPPGDADRGGWAELLA 248
|
170 180 190
....*....|....*....|....*....|....*..
gi 17556436 255 ------------EIGVFDGM--NTLDWVEKLRELPAD 277
Cdd:COG2382 249 agapkkplrfylDVGTEDDLleANRALAAALKAKGYD 285
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
90-212 |
1.37e-03 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 40.86 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 90 TSPQSEDNLTLNIFTPVWTPKNETG---FPVILYIHGGGfvsDSAHKYGDMSicQHLVTKDVVVVTIQY---RLGFLGFW 163
Cdd:COG4188 34 RDPSRDRPLPVDVWYPATAPADAPAggpFPLVVLSHGLG---GSREGYAYLA--EHLASHGYVVAAPDHpgsNAADLSAA 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17556436 164 TTGDSSIPDNVAL----HDMVFALKWVKE---NIGLFNG--DPNNITLMGQSAGGASV 212
Cdd:COG4188 109 LDGLADALDPEELwerpLDLSFVLDQLLAlnkSDPPLAGrlDLDRIGVIGHSLGGYTA 166
|
|
| Say1_Mug180 |
pfam10340 |
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ... |
93-266 |
2.37e-03 |
|
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.
Pssm-ID: 313549 Cd Length: 374 Bit Score: 40.59 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 93 QSEDNLTLNIFTPVWTPKNETGF-----PVILYIHGGG-----------FVSDSAHKYGDMSIcqhlVTKDVVVV----- 151
Cdd:pfam10340 95 HKYLNQDMIDSTKFWLRKVPETFdpkvdPILLYYHGGGfalklipvtlvFLNNLGKYFPDMAI----LVSDYTVTancpq 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 152 TIQYRLGFLgfwttgdssipDNVALHDmvfalkWVKENIGLfngdpNNITLMGQSAGGASVdfLSISPVSRDLFQKVIPM 231
Cdd:pfam10340 171 SYTYPLQVL-----------QCLAVYD------YLTLTKGC-----KNVTLMGDSAGGNLV--LNILLYLHKCNKVVLPK 226
|
170 180 190
....*....|....*....|....*....|....*
gi 17556436 232 GGNASCSWaihprpLNACRNRAQEIGVFDGMNTLD 266
Cdd:pfam10340 227 KAIAISPW------LNLTDRNEKEKEYMKANDKLD 255
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
100-210 |
3.65e-03 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 39.21 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 100 LNIFTPVWTPKNETGfPVILYIHGGGfvsDSAHKYGdmSICQHLVTKDVVVVTIQYRlgflGFwttGDSSIP--DNVALH 177
Cdd:COG2267 14 LRLRGRRWRPAGSPR-GTVVLVHGLG---EHSGRYA--ELAEALAAAGYAVLAFDLR----GH---GRSDGPrgHVDSFD 80
|
90 100 110
....*....|....*....|....*....|...
gi 17556436 178 DMVFALKWVKENIGLFNGDPnnITLMGQSAGGA 210
Cdd:COG2267 81 DYVDDLRAALDALRARPGLP--VVLLGHSMGGL 111
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
106-210 |
4.51e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 38.79 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556436 106 VWTPKNETGFPVILYIHGGGFVSDSAHKygdmsICQHLVTKDVVVVTIQYrLGFLGFWTTGD------SSIPDNVALHDM 179
Cdd:COG0412 20 LARPAGGGPRPGVVVLHEIFGLNPHIRD-----VARRLAAAGYVVLAPDL-YGRGGPGDDPDearalmGALDPELLAADL 93
|
90 100 110
....*....|....*....|....*....|.
gi 17556436 180 VFALKWVKENIGLfngDPNNITLMGQSAGGA 210
Cdd:COG0412 94 RAALDWLKAQPEV---DAGRVGVVGFCFGGG 121
|
|
| |
