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Conserved domains on  [gi|568956102|ref|XP_006530720|]
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carboxylesterase 3B isoform X6 [Mus musculus]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10444481)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate, and lipase, which hydrolyzes triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids

CATH:  3.40.50.1820
EC:  3.1.1.-
PubMed:  8453375|3163407|8280778|9704093|11099800
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
36-362 7.30e-149

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 430.96  E-value: 7.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102   36 QPEVDTPLGRVRGRQVGVKDTDrMVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDVEKMinsrfglN 115
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLT-------S 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  116 EKIKIFPISEDCLTLNIYSPTEITAGD-KRPVMVWIHGGSLLVGSSTSQDGSALAAYGDVVVVTVQYRLGIFGFLSTGDK 194
Cdd:pfam00135  74 PGSSGLEGSEDCLYLNVYTPKELKENKnKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  195 HMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTIMMEDMKPWPE 274
Cdd:pfam00135 154 EAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  275 AQNFANSVACGSASPAELVQCLLQKEGKDLIKQKNVNISY----------IVNDSFFPQRPEKLLADQQFPTVPYLLGVT 344
Cdd:pfam00135 234 AKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYgsvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGVT 313

                         330
                  ....*....|....*...
gi 568956102  345 NHEFGWLLLKAPPSSAIS 362
Cdd:pfam00135 314 KDEGLLFAAYILDNVDIL 331
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
36-362 7.30e-149

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 430.96  E-value: 7.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102   36 QPEVDTPLGRVRGRQVGVKDTDrMVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDVEKMinsrfglN 115
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLT-------S 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  116 EKIKIFPISEDCLTLNIYSPTEITAGD-KRPVMVWIHGGSLLVGSSTSQDGSALAAYGDVVVVTVQYRLGIFGFLSTGDK 194
Cdd:pfam00135  74 PGSSGLEGSEDCLYLNVYTPKELKENKnKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  195 HMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTIMMEDMKPWPE 274
Cdd:pfam00135 154 EAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  275 AQNFANSVACGSASPAELVQCLLQKEGKDLIKQKNVNISY----------IVNDSFFPQRPEKLLADQQFPTVPYLLGVT 344
Cdd:pfam00135 234 AKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYgsvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGVT 313

                         330
                  ....*....|....*...
gi 568956102  345 NHEFGWLLLKAPPSSAIS 362
Cdd:pfam00135 314 KDEGLLFAAYILDNVDIL 331
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 38-357 5.30e-121

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: 5.30e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  38 EVDTPLGRVRGRQVGVkdtdrmVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDVEkmiNSRFGLNEK 117
Cdd:cd00312    1 LVVTPNGKVRGVDEGG------VYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQ---LGGGLWNAK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 118 IkifPISEDCLTLNIYSPTEITAGDKRPVMVWIHGGSLLVGSSTSQDGSALAAYGD-VVVVTVQYRLGIFGFLSTGDKHM 196
Cdd:cd00312   72 L---PGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREGDnVIVVSINYRLGVLGFLSTGDIEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 197 PGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTimmedmkPWPEAQ 276
Cdd:cd00312  149 PGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALS-------PWAIQE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 277 N-------FANSVACGSASPAELVQCLLQKEGKDLIK-QKNVNISYIVND---------SFFPQRPEKLLADQQFPTVPY 339
Cdd:cd00312  222 NargrakrLARLLGCNDTSSAELLDCLRSKSAEELLDaTRKLLLFSYSPFlpfgpvvdgDFIPDDPEELIKEGKFAKVPL 301

                        330
                 ....*....|....*...
gi 568956102 340 LLGVTNHEFGWLLLKAPP 357
Cdd:cd00312  302 IIGVTKDEGGYFAAMLLN 319
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
37-362 4.49e-113

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 338.79  E-value: 4.49e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  37 PEVDTPLGRVRGRqvgvkdTDRMVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDvekMINSRFGLNE 116
Cdd:COG2272   13 PVVRTEAGRVRGV------VEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQP---PRPGDPGGPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 117 kikifPISEDCLTLNIYSPtEITAGDKRPVMVWIHGGSLLVGSSTS--QDGSALAAYGdVVVVTVQYRLGIFGF-----L 189
Cdd:COG2272   84 -----PGSEDCLYLNVWTP-ALAAGAKLPVMVWIHGGGFVSGSGSEplYDGAALARRG-VVVVTINYRLGALGFlalpaL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 190 STGDKHMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTIMmedm 269
Cdd:COG2272  157 SGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL---- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 270 kPWPEAQ----NFANSVACGSASPAelvqCLLQKEGKDLIK-QKNVNISY--------IVNDSFFPQRPEKLLADQQFPT 336
Cdd:COG2272  233 -TLAEAEavgaAFAAALGVAPATLA----ALRALPAEELLAaQAALAAEGpgglpfgpVVDGDVLPEDPLEAFAAGRAAD 307

                        330       340
                 ....*....|....*....|....*.
gi 568956102 337 VPYLLGVTNHEFGWLLLKAPPSSAIS 362
Cdd:COG2272  308 VPLLIGTNRDEGRLFAALLGDLGPLT 333
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
36-362 7.30e-149

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 430.96  E-value: 7.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102   36 QPEVDTPLGRVRGRQVGVKDTDrMVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDVEKMinsrfglN 115
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLT-------S 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  116 EKIKIFPISEDCLTLNIYSPTEITAGD-KRPVMVWIHGGSLLVGSSTSQDGSALAAYGDVVVVTVQYRLGIFGFLSTGDK 194
Cdd:pfam00135  74 PGSSGLEGSEDCLYLNVYTPKELKENKnKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  195 HMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTIMMEDMKPWPE 274
Cdd:pfam00135 154 EAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  275 AQNFANSVACGSASPAELVQCLLQKEGKDLIKQKNVNISY----------IVNDSFFPQRPEKLLADQQFPTVPYLLGVT 344
Cdd:pfam00135 234 AKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYgsvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGVT 313

                         330
                  ....*....|....*...
gi 568956102  345 NHEFGWLLLKAPPSSAIS 362
Cdd:pfam00135 314 KDEGLLFAAYILDNVDIL 331
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 38-357 5.30e-121

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: 5.30e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  38 EVDTPLGRVRGRQVGVkdtdrmVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDVEkmiNSRFGLNEK 117
Cdd:cd00312    1 LVVTPNGKVRGVDEGG------VYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQ---LGGGLWNAK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 118 IkifPISEDCLTLNIYSPTEITAGDKRPVMVWIHGGSLLVGSSTSQDGSALAAYGD-VVVVTVQYRLGIFGFLSTGDKHM 196
Cdd:cd00312   72 L---PGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAREGDnVIVVSINYRLGVLGFLSTGDIEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 197 PGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTimmedmkPWPEAQ 276
Cdd:cd00312  149 PGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALS-------PWAIQE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 277 N-------FANSVACGSASPAELVQCLLQKEGKDLIK-QKNVNISYIVND---------SFFPQRPEKLLADQQFPTVPY 339
Cdd:cd00312  222 NargrakrLARLLGCNDTSSAELLDCLRSKSAEELLDaTRKLLLFSYSPFlpfgpvvdgDFIPDDPEELIKEGKFAKVPL 301

                        330
                 ....*....|....*...
gi 568956102 340 LLGVTNHEFGWLLLKAPP 357
Cdd:cd00312  302 IIGVTKDEGGYFAAMLLN 319
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
37-362 4.49e-113

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 338.79  E-value: 4.49e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  37 PEVDTPLGRVRGRqvgvkdTDRMVNVFLGIPFAQAPVGPLRFSAPLPPQPWEGVRDASINPPMCLQDvekMINSRFGLNE 116
Cdd:COG2272   13 PVVRTEAGRVRGV------VEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQP---PRPGDPGGPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 117 kikifPISEDCLTLNIYSPtEITAGDKRPVMVWIHGGSLLVGSSTS--QDGSALAAYGdVVVVTVQYRLGIFGF-----L 189
Cdd:COG2272   84 -----PGSEDCLYLNVWTP-ALAAGAKLPVMVWIHGGGFVSGSGSEplYDGAALARRG-VVVVTINYRLGALGFlalpaL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 190 STGDKHMPGNRGFLDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSLFLSPISAGLFHRAISQSGIVTTIMmedm 269
Cdd:COG2272  157 SGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVL---- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 270 kPWPEAQ----NFANSVACGSASPAelvqCLLQKEGKDLIK-QKNVNISY--------IVNDSFFPQRPEKLLADQQFPT 336
Cdd:COG2272  233 -TLAEAEavgaAFAAALGVAPATLA----ALRALPAEELLAaQAALAAEGpgglpfgpVVDGDVLPEDPLEAFAAGRAAD 307

                        330       340
                 ....*....|....*....|....*.
gi 568956102 337 VPYLLGVTNHEFGWLLLKAPPSSAIS 362
Cdd:COG2272  308 VPLLIGTNRDEGRLFAALLGDLGPLT 333
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
132-241 1.66e-20

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 88.39  E-value: 1.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 132 IYSPTEitAGDKRPVMVWIHGGSLLVGSSTSQDG--SALAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GFLDVV 206
Cdd:COG0657    3 VYRPAG--AKGPLPVVVYFHGGGWVSGSKDTHDPlaRRLAARAGAAVVSVDYRLA------------PEHPfpaALEDAY 68

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568956102 207 AALRWVQGNIAPFGGDPNCVTIFGNSAGGMIVSSL 241
Cdd:COG0657   69 AALRWLRANAAELGIDPDRIAVAGDSAGGHLAAAL 103
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 147-241 3.31e-16

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: 76.48  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  147 MVWIHGGSLLVGSSTSQDG--SALAAYGDVVVVTVQYRLGifgflstgdkhmPGNR---GFLDVVAALRWVQGNIAPFGG 221
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRlcRRLAAEAGAVVVSVDYRLA------------PEHPfpaAYDDAYAALRWLAEQAAELGA 68

                          90       100
                  ....*....|....*....|
gi 568956102  222 DPNCVTIFGNSAGGMIVSSL 241
Cdd:pfam07859  69 DPSRIAVAGDSAGGNLAAAV 88
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 130-235 6.94e-12

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: 64.12  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  130 LNIYSPTeiTAGDKRPVMVWIHGGSLLVGSSTSQDG------SALAAYGdVVVVTVQYRLgifgflsTGDKHMPG--Nrg 201
Cdd:pfam20434   1 LDIYLPK--NAKGPYPVVIWIHGGGWNSGDKEADMGfmtntvKALLKAG-YAVASINYRL-------STDAKFPAqiQ-- 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568956102  202 flDVVAALRWVQGNIAPFGGDPNCVTIFGNSAGG 235
Cdd:pfam20434  69 --DVKAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
124-279 3.95e-08

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 124 SEDCLTLN--IYSPTEitaGDKRPVMVWIHGGSLLVGSSTSQDGSALAAYGdVVVVTVQYRlgifGF-LSTGDkhmPGNR 200
Cdd:COG1506    4 SADGTTLPgwLYLPAD---GKKYPVVVYVHGGPGSRDDSFLPLAQALASRG-YAVLAPDYR----GYgESAGD---WGGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 201 GFLDVVAALRWV--QGNIapfggDPNCVTIFGNSAGGMIVssLFLSPISAGLFHRAISQSGIVT-TIMMEDMKPWPEAQN 277
Cdd:COG1506   73 EVDDVLAAIDYLaaRPYV-----DPDRIGIYGHSYGGYMA--LLAAARHPDRFKAAVALAGVSDlRSYYGTTREYTERLM 145


                 ..
gi 568956102 278 FA 279
Cdd:COG1506  146 GG 147
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 129-261 1.38e-04

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: 42.83  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  129 TLNIYSPTEITAGDKRPVMVWIHggsllvGSSTSQDGSALAAYG---------DVVVVTV----QYRLGIFGFLSTGDKH 195
Cdd:pfam00756   9 KVQVYLPEDYPPGRKYPVLYLLD------GTGWFQNGPAKEGLDrlaasgeipPVIIVGSprggEVSFYSDWDRGLNATE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956102  196 MPGNRGFLDVVAA--LRWVQGNiapFGGDPNCVTIFGNSAGGmiVSSLFLSPISAGLFHRAISQSGIV 261
Cdd:pfam00756  83 GPGAYAYETFLTQelPPLLDAN---FPTAPDGRALAGQSMGG--LGALYLALKYPDLFGSVSSFSPIL 145
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
129-276 5.33e-04

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 41.38  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 129 TLNIYSPTEITAGDKR-PVMVWIHGGSllvGSSTS--QDGSA------LAAYGDV---VVVTVQYRLGifgflSTGDKHM 196
Cdd:COG2382   96 RVWVYLPPGYDNPGKKyPVLYLLDGGG---GDEQDwfDQGRLptildnLIAAGKIppmIVVMPDGGDG-----GDRGTEG 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 197 PGNRGFLDVVAA--LRWVQGNiAPFGGDPNCVTIFGNSAGGMivSSLFLSPISAGLFHRAISQSGIVTTIMMEDMKPWPE 274
Cdd:COG2382  168 PGNDAFERFLAEelIPFVEKN-YRVSADPEHRAIAGLSMGGL--AALYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWA 244


                 ..
gi 568956102 275 AQ 276
Cdd:COG2382  245 EL 246
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
173-266 2.57e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 38.75  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102  173 DVVVVTVQYR-LGIFG--FLSTGDKHMpGNRGFLDVVAALRWVqgnIAPFGGDPNCVTIFGNSAGG-MIVSSLFLSPisa 248
Cdd:pfam00326  14 GYVVAIANGRgSGGYGeaFHDAGKGDL-GQNEFDDFIAAAEYL---IEQGYTDPDRLAIWGGSYGGyLTGAALNQRP--- 86

                          90
                  ....*....|....*...
gi 568956102  249 GLFHRAISQSGIVTTIMM 266
Cdd:pfam00326  87 DLFKAAVAHVPVVDWLAY 104
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 116-259 3.42e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 38.74  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 116 EKIKIfpISEDCLTL--NIYSPTeiTAGDKRPVMVWIHG-GSllVGSSTSQDGSALAAYGdVVVVTVQYRlgifGF-LST 191
Cdd:COG1073   11 EDVTF--KSRDGIKLagDLYLPA--GASKKYPAVVVAHGnGG--VKEQRALYAQRLAELG-FNVLAFDYR----GYgESE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956102 192 GDKHMPGNRGFLDVVAALRWVQGNIapfGGDPNCVTIFGNSAGGMIVSSLflspisAGLFHRA---ISQSG 259
Cdd:COG1073   80 GEPREEGSPERRDARAAVDYLRTLP---GVDPERIGLLGISLGGGYALNA------AATDPRVkavILDSP 141
COG4099 COG4099
Predicted peptidase [General function prediction only];
131-236 6.14e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 38.02  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956102 131 NIYSPTEITAGDKRPVMVWIHGgsllvGSSTSQDGSALAAYGDVVVVTVQYRlGIFGFL-----STGDKHMPGNRGFLDV 205
Cdd:COG4099   36 RLYLPKGYDPGKKYPLVLFLHG-----AGERGTDNEKQLTHGAPKFINPENQ-AKFPAIvlapqCPEDDYWSDTKALDAV 109

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568956102 206 VAALRWVQGNiapFGGDPNCVTIFGNSAGGM 236
Cdd:COG4099  110 LALLDDLIAE---YRIDPDRIYLTGLSMGGY 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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