|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
36-507 |
0e+00 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 568.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 36 QPEVDTPLGRVRGRQVGVKDTDrMVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVERMSNSRFTLn 115
Cdd:pfam00135 2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 116 ekmkifPISEDCLTLNIYSPTEITAGD-KRPVMVWIHGGSLLVGSSTSHDGSALAAYGDVVVVTVQYRLGIFGFLSTGDK 194
Cdd:pfam00135 80 ------EGSEDCLYLNVYTPKELKENKnKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 195 HMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVISKILEDLNAWSE 274
Cdd:pfam00135 154 EAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 275 AQNFANSVACGSASPAELVQCLLQKEGKDLITKKNVNISY----------TVNDSFFPQRPQKLLANKQFPTVPYLLGVT 344
Cdd:pfam00135 234 AKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYgsvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 345 NHEFGWLLLKFWNILDKMEHLSQEDLLENSRPLLAHM--QLPPEIMPTVIDEYLDNGS--DESATRYALQELLGDITLVI 420
Cdd:pfam00135 314 KDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLlvDLPEEISAALREEYLDWGDrdDPETSRRALVELLTDYLFNC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 421 PTLIFSKYLQDAGCPVFLYEFQHTPSSFakFKPAWVKADHSSENAFVFGGPFLTDEssllafpEATEEEKQLSLTMMAQW 500
Cdd:pfam00135 394 PVIRFADLHASRGTPVYMYSFDYRGSSL--RYPKWVGVDHGDELPYVFGTPFVGAL-------LFTEEDEKLSRKMMTYW 464
|
....*..
gi 755526964 501 SQFARTG 507
Cdd:pfam00135 465 TNFAKTG 471
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
38-507 |
4.43e-152 |
|
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: 443.31 E-value: 4.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 38 EVDTPLGRVRGRQVGVkdtdrmVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVErmsNSRFTLNEK 117
Cdd:cd00312 1 LVVTPNGKVRGVDEGG------VYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQ---LGGGLWNAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 118 MkifPISEDCLTLNIYSPTEITAGDKRPVMVWIHGGSLLVGSSTSHDGSALAAYGD-VVVVTVQYRLGIFGFLSTGDKHM 196
Cdd:cd00312 72 L---PGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREGDnVIVVSINYRLGVLGFLSTGDIEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 197 PGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVIS--KILEDLNAWse 274
Cdd:cd00312 149 PGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSpwAIQENARGR-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 275 AQNFANSVACGSASPAELVQCLLQKEGKDLITKKNVNISY----------TVNDSFFPQRPQKLLANKQFPTVPYLLGVT 344
Cdd:cd00312 227 AKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFsyspflpfgpVVDGDFIPDDPEELIKEGKFAKVPLIIGVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 345 NHEFGWLLLKFWNILDKMEHLSQEDLLENSRPLLAHmqLPPEIMPTVIDEYLDNGSDESATRYALQELLGDITLVIPTLI 424
Cdd:cd00312 307 KDEGGYFAAMLLNFDAKLIIETNDRWLELLPYLLFY--ADDALADKVLEKYPGDVDDSVESRKNLSDMLTDLLFKCPARY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 425 F-SKYLQDAGCPVFLYEFQHTPSSFAKFKPAWVKADHSSENAFVFGGPFLTdessllafPEATEEEKQLSLTMMAQWSQF 503
Cdd:cd00312 385 FlAQHRKAGGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLK--------EGLREEEEKLSRTMMKYWANF 456
|
....
gi 755526964 504 ARTG 507
Cdd:cd00312 457 AKTG 460
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
35-507 |
1.60e-132 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 393.48 E-value: 1.60e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 35 TQPEVDTPLGRVRGRqvgvkdTDRMVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVERMSNSRFTl 114
Cdd:COG2272 11 AAPVVRTEAGRVRGV------VEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGGPA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 115 nekmkifPISEDCLTLNIYSPtEITAGDKRPVMVWIHGGSLLVGSSTS--HDGSALAAYGdVVVVTVQYRLGIFGF---- 188
Cdd:COG2272 84 -------PGSEDCLYLNVWTP-ALAAGAKLPVMVWIHGGGFVSGSGSEplYDGAALARRG-VVVVTINYRLGALGFlalp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 189 -LSTGDKHMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVISKI-L 266
Cdd:COG2272 155 aLSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLtL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 267 EDLNAWseAQNFANSVACGSASPAEL----VQCLLQKEGKdLITKKNVNISY--TVNDSFFPQRPQKLLANKQFPTVPYL 340
Cdd:COG2272 235 AEAEAV--GAAFAAALGVAPATLAALralpAEELLAAQAA-LAAEGPGGLPFgpVVDGDVLPEDPLEAFAAGRAADVPLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 341 LGVTNHEfGWLLLKFWNILDKMEHLSQEDLLEnsrpllahmQLPPEIMPTVIDEYLDNGSDESATRyalqeLLGDITLVI 420
Cdd:COG2272 312 IGTNRDE-GRLFAALLGDLGPLTAADYRAALR---------RRFGDDADEVLAAYPAASPAEALAA-----LATDRVFRC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 421 PTLIFSKYLQDAGCPVFLYEFQHTPSSFAKFKP-AWvkadHSSENAFVFGgpfLTDESSLLAFpeaTEEEKQLSLTMMAQ 499
Cdd:COG2272 377 PARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGLgAF----HGAELPFVFG---NLDAPALTGL---TPADRALSDQMQAY 446
|
....*...
gi 755526964 500 WSQFARTG 507
Cdd:COG2272 447 WVNFARTG 454
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
128-234 |
3.57e-03 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 39.70 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 128 LTLNIYSPTEitagDKRPVMVWIHGGSLLVGSSTSHDGSA--LAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GF 202
Cdd:PRK10162 69 VETRLYYPQP----DSQATLFYLHGGGFILGNLDTHDRIMrlLASYSGCTVIGIDYTLS------------PEARfpqAI 132
|
90 100 110
....*....|....*....|....*....|..
gi 755526964 203 LDVVAALRWVQGNIAPFGGDPNCVTIFGNSAG 234
Cdd:PRK10162 133 EEIVAVCCYFHQHAEDYGINMSRIGFAGDSAG 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
36-507 |
0e+00 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 568.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 36 QPEVDTPLGRVRGRQVGVKDTDrMVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVERMSNSRFTLn 115
Cdd:pfam00135 2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 116 ekmkifPISEDCLTLNIYSPTEITAGD-KRPVMVWIHGGSLLVGSSTSHDGSALAAYGDVVVVTVQYRLGIFGFLSTGDK 194
Cdd:pfam00135 80 ------EGSEDCLYLNVYTPKELKENKnKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 195 HMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVISKILEDLNAWSE 274
Cdd:pfam00135 154 EAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 275 AQNFANSVACGSASPAELVQCLLQKEGKDLITKKNVNISY----------TVNDSFFPQRPQKLLANKQFPTVPYLLGVT 344
Cdd:pfam00135 234 AKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYgsvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 345 NHEFGWLLLKFWNILDKMEHLSQEDLLENSRPLLAHM--QLPPEIMPTVIDEYLDNGS--DESATRYALQELLGDITLVI 420
Cdd:pfam00135 314 KDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLlvDLPEEISAALREEYLDWGDrdDPETSRRALVELLTDYLFNC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 421 PTLIFSKYLQDAGCPVFLYEFQHTPSSFakFKPAWVKADHSSENAFVFGGPFLTDEssllafpEATEEEKQLSLTMMAQW 500
Cdd:pfam00135 394 PVIRFADLHASRGTPVYMYSFDYRGSSL--RYPKWVGVDHGDELPYVFGTPFVGAL-------LFTEEDEKLSRKMMTYW 464
|
....*..
gi 755526964 501 SQFARTG 507
Cdd:pfam00135 465 TNFAKTG 471
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
38-507 |
4.43e-152 |
|
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: 443.31 E-value: 4.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 38 EVDTPLGRVRGRQVGVkdtdrmVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVErmsNSRFTLNEK 117
Cdd:cd00312 1 LVVTPNGKVRGVDEGG------VYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQ---LGGGLWNAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 118 MkifPISEDCLTLNIYSPTEITAGDKRPVMVWIHGGSLLVGSSTSHDGSALAAYGD-VVVVTVQYRLGIFGFLSTGDKHM 196
Cdd:cd00312 72 L---PGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREGDnVIVVSINYRLGVLGFLSTGDIEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 197 PGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVIS--KILEDLNAWse 274
Cdd:cd00312 149 PGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSpwAIQENARGR-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 275 AQNFANSVACGSASPAELVQCLLQKEGKDLITKKNVNISY----------TVNDSFFPQRPQKLLANKQFPTVPYLLGVT 344
Cdd:cd00312 227 AKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFsyspflpfgpVVDGDFIPDDPEELIKEGKFAKVPLIIGVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 345 NHEFGWLLLKFWNILDKMEHLSQEDLLENSRPLLAHmqLPPEIMPTVIDEYLDNGSDESATRYALQELLGDITLVIPTLI 424
Cdd:cd00312 307 KDEGGYFAAMLLNFDAKLIIETNDRWLELLPYLLFY--ADDALADKVLEKYPGDVDDSVESRKNLSDMLTDLLFKCPARY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 425 F-SKYLQDAGCPVFLYEFQHTPSSFAKFKPAWVKADHSSENAFVFGGPFLTdessllafPEATEEEKQLSLTMMAQWSQF 503
Cdd:cd00312 385 FlAQHRKAGGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLK--------EGLREEEEKLSRTMMKYWANF 456
|
....
gi 755526964 504 ARTG 507
Cdd:cd00312 457 AKTG 460
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
35-507 |
1.60e-132 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 393.48 E-value: 1.60e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 35 TQPEVDTPLGRVRGRqvgvkdTDRMVNVFLGIPFAQAPLGPLRFSAPLPPQPWEGVRDASINPPMCLQDVERMSNSRFTl 114
Cdd:COG2272 11 AAPVVRTEAGRVRGV------VEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGGPA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 115 nekmkifPISEDCLTLNIYSPtEITAGDKRPVMVWIHGGSLLVGSSTS--HDGSALAAYGdVVVVTVQYRLGIFGF---- 188
Cdd:COG2272 84 -------PGSEDCLYLNVWTP-ALAAGAKLPVMVWIHGGGFVSGSGSEplYDGAALARRG-VVVVTINYRLGALGFlalp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 189 -LSTGDKHMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLLSPMSAGLFHRAISQSGVVISKI-L 266
Cdd:COG2272 155 aLSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLtL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 267 EDLNAWseAQNFANSVACGSASPAEL----VQCLLQKEGKdLITKKNVNISY--TVNDSFFPQRPQKLLANKQFPTVPYL 340
Cdd:COG2272 235 AEAEAV--GAAFAAALGVAPATLAALralpAEELLAAQAA-LAAEGPGGLPFgpVVDGDVLPEDPLEAFAAGRAADVPLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 341 LGVTNHEfGWLLLKFWNILDKMEHLSQEDLLEnsrpllahmQLPPEIMPTVIDEYLDNGSDESATRyalqeLLGDITLVI 420
Cdd:COG2272 312 IGTNRDE-GRLFAALLGDLGPLTAADYRAALR---------RRFGDDADEVLAAYPAASPAEALAA-----LATDRVFRC 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 421 PTLIFSKYLQDAGCPVFLYEFQHTPSSFAKFKP-AWvkadHSSENAFVFGgpfLTDESSLLAFpeaTEEEKQLSLTMMAQ 499
Cdd:COG2272 377 PARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGLgAF----HGAELPFVFG---NLDAPALTGL---TPADRALSDQMQAY 446
|
....*...
gi 755526964 500 WSQFARTG 507
Cdd:COG2272 447 WVNFARTG 454
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
132-243 |
1.38e-21 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 132 IYSPTEitAGDKRPVMVWIHGGSLLVGSSTSHDG--SALAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GFLDVV 206
Cdd:COG0657 3 VYRPAG--AKGPLPVVVYFHGGGWVSGSKDTHDPlaRRLAARAGAAVVSVDYRLA------------PEHPfpaALEDAY 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 755526964 207 AALRWVQGNIAPFGGDPNCVTIFGNSAGGIIVSSLLL 243
Cdd:COG0657 69 AALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALAL 105
|
|
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
147-276 |
1.91e-17 |
|
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: 80.72 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 147 MVWIHGGSLLVGSSTSHDG--SALAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GFLDVVAALRWVQGNIAPFGG 221
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRlcRRLAAEAGAVVVSVDYRLA------------PEHPfpaAYDDAYAALRWLAEQAAELGA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 222 DPNCVTIFGNSAGGIIvsslllspmSAGLFHRAISQSGVVISKIL-----EDLNAWSEAQ 276
Cdd:pfam07859 69 DPSRIAVAGDSAGGNL---------AAAVALRARDEGLPKPAGQVliypgTDLRTESPSY 119
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
130-235 |
8.23e-11 |
|
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: 61.81 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 130 LNIYSPTeiTAGDKRPVMVWIHGGSLLVGSSTSHDG------SALAAYGdVVVVTVQYRLgifgflsTGDKHMPG--Nrg 201
Cdd:pfam20434 1 LDIYLPK--NAKGPYPVVIWIHGGGWNSGDKEADMGfmtntvKALLKAG-YAVASINYRL-------STDAKFPAqiQ-- 68
|
90 100 110
....*....|....*....|....*....|....
gi 755526964 202 flDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGG 235
Cdd:pfam20434 69 --DVKAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
124-260 |
4.42e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 53.87 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 124 SEDCLTLN--IYSPTEitaGDKRPVMVWIHGGSLLVGSSTSHDGSALAAYGdVVVVTVQYRlgifGF-LSTGDkhmPGNR 200
Cdd:COG1506 4 SADGTTLPgwLYLPAD---GKKYPVVVYVHGGPGSRDDSFLPLAQALASRG-YAVLAPDYR----GYgESAGD---WGGD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755526964 201 GFLDVVAALRWV--QGNIapfggDPNCVTIFGNSAGGIIVSSLLLspMSAGLFHRAISQSGV 260
Cdd:COG1506 73 EVDDVLAAIDYLaaRPYV-----DPDRIGIYGHSYGGYMALLAAA--RHPDRFKAAVALAGV 127
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
129-259 |
2.75e-03 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 39.84 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 129 TLNIYSPTEITAGDKR-PVMVWIHGGSllvGSSTS--HDGSA------LAAYGDV---VVVTVQYRLGifgflSTGDKHM 196
Cdd:COG2382 96 RVWVYLPPGYDNPGKKyPVLYLLDGGG---GDEQDwfDQGRLptildnLIAAGKIppmIVVMPDGGDG-----GDRGTEG 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526964 197 PGNRGFLDVVAA--LRWVQGNiAPFGGDPNCVTIFGNSAGGIivSSLLLSPMSAGLFHRAISQSG 259
Cdd:COG2382 168 PGNDAFERFLAEelIPFVEKN-YRVSADPEHRAIAGLSMGGL--AALYAALRHPDLFGYVGSFSG 229
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
113-261 |
2.84e-03 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 39.37 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 113 TLNEKMKIfpisedcltlNIYSPTEITAGDKRPVMVWIHGGSL--------LVGSSTSHDGSALAA-----YGDVVVVTV 179
Cdd:pfam00756 3 SLGREMKV----------QVYLPEDYPPGRKYPVLYLLDGTGWfqngpakeGLDRLAASGEIPPVIivgspRGGEVSFYS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 180 QYRLGIFGflstgdKHMPGNRGFLDVVAA--LRWVQGNiapFGGDPNCVTIFGNSAGGiiVSSLLLSPMSAGLFHRAISQ 257
Cdd:pfam00756 73 DWDRGLNA------TEGPGAYAYETFLTQelPPLLDAN---FPTAPDGRALAGQSMGG--LGALYLALKYPDLFGSVSSF 141
|
....
gi 755526964 258 SGVV 261
Cdd:pfam00756 142 SPIL 145
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
128-234 |
3.57e-03 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 39.70 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 128 LTLNIYSPTEitagDKRPVMVWIHGGSLLVGSSTSHDGSA--LAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GF 202
Cdd:PRK10162 69 VETRLYYPQP----DSQATLFYLHGGGFILGNLDTHDRIMrlLASYSGCTVIGIDYTLS------------PEARfpqAI 132
|
90 100 110
....*....|....*....|....*....|..
gi 755526964 203 LDVVAALRWVQGNIAPFGGDPNCVTIFGNSAG 234
Cdd:PRK10162 133 EEIVAVCCYFHQHAEDYGINMSRIGFAGDSAG 164
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
160-261 |
3.64e-03 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 38.75 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526964 160 STSHDGSALAAYGdVVVVTVQYR-LGIFG--FLSTGDKHMpGNRGFLDVVAALRWVqgnIAPFGGDPNCVTIFGNSAGGI 236
Cdd:pfam00326 2 SFSWNAQLLADRG-YVVAIANGRgSGGYGeaFHDAGKGDL-GQNEFDDFIAAAEYL---IEQGYTDPDRLAIWGGSYGGY 76
|
90 100
....*....|....*....|....*
gi 755526964 237 IVSSLLLspMSAGLFHRAISQSGVV 261
Cdd:pfam00326 77 LTGAALN--QRPDLFKAAVAHVPVV 99
|
|
| |
