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Conserved domains on  [gi|523371100|gb|AGQ21328|]
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esterase [Psychrobacter sp. MCCC 1A004444]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
87-329 4.10e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.91  E-value: 4.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  87 DIYYPKPLAQamkaqstinnDYPMVVFVHGGSWESGNKDQYAFVGQSLA-QAGYVTAVINYRKVPEHVYPDYVNDTAQAI 165
Cdd:COG0657    2 DVYRPAGAKG----------PLPVVVYFHGGGWVSGSKDTHDPLARRLAaRAGAAVVSVDYRLAPEHPFPAALEDAYAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 166 AWSIENAASLHSDPSRVAVMGHSagafnavaavanedflA------PYGIKPTD-----VATVIGIAGPysYDFRkFSSA 234
Cdd:COG0657   72 RWLRANAAELGIDPDRIAVAGDS----------------AgghlaaALALRARDrggprPAAQVLIYPV--LDLT-ASPL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 235 SAFPSDAtpdqvmpdrqikgaqPPYLLLTAEKDKVVHptNALKMTQALKEAGVTVQTGEIEGASHATIigaMAPPLRWVN 314
Cdd:COG0657  133 RADLAGL---------------PPTLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGFG---LLAGLPEAR 192

                        250
                 ....*....|....*
gi 523371100 315 DVRAQVVTYLDTMLK 329
Cdd:COG0657  193 AALAEIAAFLRRALA 207
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
87-329 4.10e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.91  E-value: 4.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  87 DIYYPKPLAQamkaqstinnDYPMVVFVHGGSWESGNKDQYAFVGQSLA-QAGYVTAVINYRKVPEHVYPDYVNDTAQAI 165
Cdd:COG0657    2 DVYRPAGAKG----------PLPVVVYFHGGGWVSGSKDTHDPLARRLAaRAGAAVVSVDYRLAPEHPFPAALEDAYAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 166 AWSIENAASLHSDPSRVAVMGHSagafnavaavanedflA------PYGIKPTD-----VATVIGIAGPysYDFRkFSSA 234
Cdd:COG0657   72 RWLRANAAELGIDPDRIAVAGDS----------------AgghlaaALALRARDrggprPAAQVLIYPV--LDLT-ASPL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 235 SAFPSDAtpdqvmpdrqikgaqPPYLLLTAEKDKVVHptNALKMTQALKEAGVTVQTGEIEGASHATIigaMAPPLRWVN 314
Cdd:COG0657  133 RADLAGL---------------PPTLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGFG---LLAGLPEAR 192

                        250
                 ....*....|....*
gi 523371100 315 DVRAQVVTYLDTMLK 329
Cdd:COG0657  193 AALAEIAAFLRRALA 207
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 86-270 4.69e-24

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: 97.64  E-value: 4.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100   86 LDIYYPKplaqamkaqsTINNDYPMVVFVHGGSWESGNK----DQYAFVGQSLAQAGYVTAVINYRKVPEHVYPDYVNDT 161
Cdd:pfam20434   1 LDIYLPK----------NAKGPYPVVIWIHGGGWNSGDKeadmGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  162 AQAIAWSIENAASLHSDPSRVAVMGHSA----------GAFNAVAAVANEDFLAPYGIKPTDVATVIGIAGPysYDFRKF 231
Cdd:pfam20434  71 KAAIRFLRANAAKYGIDTNKIALMGFSAgghlallaglSNNNKEFEGNVGDYTPESSKESFKVNAVVDFYGP--TDLLDM 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523371100  232 SSASAFPSDATPDQVM--------PDR--------QIKGAQPPYLLLTAEKDKVV 270
Cdd:pfam20434 149 DSCGTHNDAKSPETLLlgapplenPDLaksaspitYVDKNDPPFLIIHGDKDPLV 203
PRK10162 PRK10162
acetyl esterase;
78-188 1.06e-06

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 49.72  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  78 YGDEPLQdldIYYPKPLAQAmkaqstinndypMVVFVHGGSWESGNKDQYAFVGQSLAQAGYVTAV-INYRKVPEHVYPD 156
Cdd:PRK10162  66 YGQVETR---LYYPQPDSQA------------TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIgIDYTLSPEARFPQ 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 523371100 157 YVNDTAQAIAWSIENAASLHSDPSRVAVMGHS 188
Cdd:PRK10162 131 AIEEIVAVCCYFHQHAEDYGINMSRIGFAGDS 162
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 73-188 4.67e-06

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: 48.10  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  73 SKDILYgdeplqdLDIYYPKPlaqamkaqSTINNDYPMVVFVHGGSWESG-----NKDQYAFVGQSLAqagYVTavINYR 147
Cdd:cd00312   75 SEDCLY-------LNVYTPKN--------TKPGNSLPVMVWIHGGGFMFGsgslyPGDGLAREGDNVI---VVS--INYR 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 523371100 148 KVP-------EHVYPDyvN----DTAQAIAWSIENAASLHSDPSRVAVMGHS 188
Cdd:cd00312  135 LGVlgflstgDIELPG--NyglkDQRLALKWVQDNIAAFGGDPDSVTIFGES 184
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
87-329 4.10e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.91  E-value: 4.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  87 DIYYPKPLAQamkaqstinnDYPMVVFVHGGSWESGNKDQYAFVGQSLA-QAGYVTAVINYRKVPEHVYPDYVNDTAQAI 165
Cdd:COG0657    2 DVYRPAGAKG----------PLPVVVYFHGGGWVSGSKDTHDPLARRLAaRAGAAVVSVDYRLAPEHPFPAALEDAYAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 166 AWSIENAASLHSDPSRVAVMGHSagafnavaavanedflA------PYGIKPTD-----VATVIGIAGPysYDFRkFSSA 234
Cdd:COG0657   72 RWLRANAAELGIDPDRIAVAGDS----------------AgghlaaALALRARDrggprPAAQVLIYPV--LDLT-ASPL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 235 SAFPSDAtpdqvmpdrqikgaqPPYLLLTAEKDKVVHptNALKMTQALKEAGVTVQTGEIEGASHATIigaMAPPLRWVN 314
Cdd:COG0657  133 RADLAGL---------------PPTLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGFG---LLAGLPEAR 192

                        250
                 ....*....|....*
gi 523371100 315 DVRAQVVTYLDTMLK 329
Cdd:COG0657  193 AALAEIAAFLRRALA 207
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 86-270 4.69e-24

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: 97.64  E-value: 4.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100   86 LDIYYPKplaqamkaqsTINNDYPMVVFVHGGSWESGNK----DQYAFVGQSLAQAGYVTAVINYRKVPEHVYPDYVNDT 161
Cdd:pfam20434   1 LDIYLPK----------NAKGPYPVVIWIHGGGWNSGDKeadmGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  162 AQAIAWSIENAASLHSDPSRVAVMGHSA----------GAFNAVAAVANEDFLAPYGIKPTDVATVIGIAGPysYDFRKF 231
Cdd:pfam20434  71 KAAIRFLRANAAKYGIDTNKIALMGFSAgghlallaglSNNNKEFEGNVGDYTPESSKESFKVNAVVDFYGP--TDLLDM 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523371100  232 SSASAFPSDATPDQVM--------PDR--------QIKGAQPPYLLLTAEKDKVV 270
Cdd:pfam20434 149 DSCGTHNDAKSPETLLlgapplenPDLaksaspitYVDKNDPPFLIIHGDKDPLV 203
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
108-329 9.16e-21

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 89.31  E-value: 9.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 108 YPMVVFVHGGSWESGnkDQYAFVGQSLAQAGYVTAVINYR---KVPEHVYPDYVNDTAQAIAWSIENAaslHSDPSRVAV 184
Cdd:COG1506   23 YPVVVYVHGGPGSRD--DSFLPLAQALASRGYAVLAPDYRgygESAGDWGGDEVDDVLAAIDYLAARP---YVDPDRIGI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 185 MGHSagafnavaavanedflapYG---------IKPTDVATVIGIAGPYsyDFRKFSSASAF--------PSDATP--DQ 245
Cdd:COG1506   98 YGHS------------------YGgymallaaaRHPDRFKAAVALAGVS--DLRSYYGTTREyterlmggPWEDPEayAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 246 VMPDRQIKGAQPPYLLLTAEKDKVVHPTNALKMTQALKEAGVTVQTGEIEGASHAtIIGAMAPplrwvnDVRAQVVTYLD 325
Cdd:COG1506  158 RSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHG-FSGAGAP------DYLERILDFLD 230


                 ....
gi 523371100 326 TMLK 329
Cdd:COG1506  231 RHLK 234
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 111-300 4.35e-14

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: 69.93  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  111 VVFVHGGSWESGNKDQY-AFVGQSLAQAGYVTAVINYRKVPEHVYPDYVNDTAQAIAWSIENAASLHSDPSRVAVMGHSA 189
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHdRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  190 ---GAFNAVAAVANEDFLAPYG---IKP-TDVATvigiaGPYSYDFRKFSSASAFPSDATP---DQVMPDRQIK------ 253
Cdd:pfam07859  81 ggnLAAAVALRARDEGLPKPAGqvlIYPgTDLRT-----ESPSYLAREFADGPLLTRAAMDwfwRLYLPGADRDdplasp 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 523371100  254 ------GAQPPYLLLTAEKDkVVHPtNALKMTQALKEAGVTVQTGEIEGASHA 300
Cdd:pfam07859 156 lfasdlSGLPPALVVVAEFD-PLRD-EGEAYAERLRAAGVPVELIEYPGMPHG 206
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
40-329 8.45e-09

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 55.88  E-value: 8.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  40 LALGSIALATQSAQALSPLGFVNGITSSGGVGVSKdilyGDEPLqDLDIYYPkplaQAMKAQSTINNDYPMVVFVHGGSw 119
Cdd:COG4188    3 ALLALLLAAAAAASPLRQPGPFAVGVQTLTLRDPS----RDRPL-PVDVWYP----ATAPADAPAGGPFPLVVLSHGLG- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 120 esGNKDQYAFVGQSLAQAGYVTAVinyrkvPEHVYPDYVNDTAQAIAWSIENAASL------------------------ 175
Cdd:COG4188   73 --GSREGYAYLAEHLASHGYVVAA------PDHPGSNAADLSAALDGLADALDPEElwerpldlsfvldqllalnksdpp 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 176 ---HSDPSRVAVMGHS--------------------AGAFNAVAAVANEDFLAPYGIKPTD--VATVIGIAGPYSYDFRK 230
Cdd:COG4188  145 lagRLDLDRIGVIGHSlggytalalagarldfaalrQYCGKNPDLQCRALDLPRLAYDLRDprIKAVVALAPGGSGLFGE 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 231 FSsasafpsdatpdqvmpdrqIKGAQPPYLLLTAEKDKVV-HPTNALKMTQALKEAGVTVQTgeIEGASHATIIGAMAPP 309
Cdd:COG4188  225 EG-------------------LAAITIPVLLVAGSADDVTpAPDEQIRPFDLLPGADKYLLT--LEGATHFSFLDPCTPG 283

                        330       340       350
                 ....*....|....*....|....*....|....
gi 523371100 310 LRWVND--------------VRAQVVTYLDTMLK 329
Cdd:COG4188  284 AAILPEpdppgpdraaiheyLNALSLAFFDAYLK 317
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
108-300 8.52e-09

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 54.97  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 108 YPMVVFVHGgSWesGNKDQYAFVGQSLAQAGYVTAVIN-YRKVPEHVYPD-------------YVNDTAQAIAWsienAA 173
Cdd:COG0412   29 RPGVVVLHE-IF--GLNPHIRDVARRLAAAGYVVLAPDlYGRGGPGDDPDearalmgaldpelLAADLRAALDW----LK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 174 SL-HSDPSRVAVMGHSagafnavaavanedflapYG--------IKPTDVATVIGIAGpysydfrkfssasAFPSDATPD 244
Cdd:COG0412  102 AQpEVDAGRVGVVGFC------------------FGgglallaaARGPDLAAAVSFYG-------------GLPADDLLD 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 523371100 245 QVmpdRQIKGaqpPYLLLTAEKDKVVHPTNALKMTQALKEAGVTVQTGEIEGASHA 300
Cdd:COG0412  151 LA---ARIKA---PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHG 200
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
109-325 3.02e-08

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 53.47  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 109 PMVVFVHGGSwesGNKDQYAFVGQSLAQAGYVTAVINYR------KVPEHV--YPDYVNDTAQAIAWsienaasLHSDPS 180
Cdd:COG2267   29 GTVVLVHGLG---EHSGRYAELAEALAAAGYAVLAFDLRghgrsdGPRGHVdsFDDYVDDLRAALDA-------LRARPG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 181 -RVAVMGHS------AgafnavaavaneDFLAPYgikPTDVATVIGIAGPYSYDFRKFSSASAFpsdatpDQVMPDRQIK 253
Cdd:COG2267   99 lPVVLLGHSmggliaL------------LYAARY---PDRVAGLVLLAPAYRADPLLGPSARWL------RALRLAEALA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523371100 254 GAQPPYLLLTAEKDKVVHPTNALKMTQALKEAGVTVqtgEIEGASHATIIGAMAPplrwvnDVRAQVVTYLD 325
Cdd:COG2267  158 RIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELV---LLPGARHELLNEPARE------EVLAAILAWLE 220
COesterase pfam00135
Carboxylesterase family;
65-188 7.64e-08

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 53.47  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100   65 TSSGGVGVSKDILYgdeplqdLDIYYPKPLAQAmkaqstiNNDYPMVVFVHGGSWESGNKDQYAfvGQSLAQAGYVTAV- 143
Cdd:pfam00135  74 PGSSGLEGSEDCLY-------LNVYTPKELKEN-------KNKLPVMVWIHGGGFMFGSGSLYD--GSYLAAEGDVIVVt 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 523371100  144 INYRKVP--------EHVyPDyvN----DTAQAIAWSIENAASLHSDPSRVAVMGHS 188
Cdd:pfam00135 138 INYRLGPlgflstgdDEA-PG--NygllDQVLALRWVQENIASFGGDPNRVTLFGES 191
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 87-188 9.98e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.14  E-value: 9.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  87 DIYYPKPlaqamkaqstINNDYPMVVFVHGGSwesGNKDQYAFVGQSLAQAGYVTAVINYR-------KVPEHVYPDYvN 159
Cdd:COG1073   26 DLYLPAG----------ASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFDYRgygesegEPREEGSPER-R 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 523371100 160 DTAQAIAWsienaASLHS--DPSRVAVMGHS 188
Cdd:COG1073   92 DARAAVDY-----LRTLPgvDPERIGLLGIS 117
PRK10162 PRK10162
acetyl esterase;
78-188 1.06e-06

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 49.72  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  78 YGDEPLQdldIYYPKPLAQAmkaqstinndypMVVFVHGGSWESGNKDQYAFVGQSLAQAGYVTAV-INYRKVPEHVYPD 156
Cdd:PRK10162  66 YGQVETR---LYYPQPDSQA------------TLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIgIDYTLSPEARFPQ 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 523371100 157 YVNDTAQAIAWSIENAASLHSDPSRVAVMGHS 188
Cdd:PRK10162 131 AIEEIVAVCCYFHQHAEDYGINMSRIGFAGDS 162
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
132-290 2.41e-06

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 47.61  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  132 QSLAQAGYVTAVINYR-------KVPEHVYPDY-VNDTAQAIAWSIENAASLHSDPSRVAVMGHSA--GAFNAVAAVANE 201
Cdd:pfam00326   8 QLLADRGYVVAIANGRgsggygeAFHDAGKGDLgQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYggYLTGAALNQRPD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  202 DF---LAPYGIkpTDV-----ATVIGIA--------GPYSYD-FRKFSSASafpsdatpdqvmpDRQIKGAQPPYLLLTA 264
Cdd:pfam00326  88 LFkaaVAHVPV--VDWlaymsDTSLPFTerymewgnPWDNEEgYDYLSPYS-------------PADNVKVYPPLLLIHG 152

                         170       180
                  ....*....|....*....|....*.
gi 523371100  265 EKDKVVHPTNALKMTQALKEAGVTVQ 290
Cdd:pfam00326 153 LLDDRVPPWQSLKLVAALQRKGVPFL 178
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 73-188 4.67e-06

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: 48.10  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100  73 SKDILYgdeplqdLDIYYPKPlaqamkaqSTINNDYPMVVFVHGGSWESG-----NKDQYAFVGQSLAqagYVTavINYR 147
Cdd:cd00312   75 SEDCLY-------LNVYTPKN--------TKPGNSLPVMVWIHGGGFMFGsgslyPGDGLAREGDNVI---VVS--INYR 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 523371100 148 KVP-------EHVYPDyvN----DTAQAIAWSIENAASLHSDPSRVAVMGHS 188
Cdd:cd00312  135 LGVlgflstgDIELPG--NyglkDQRLALKWVQDNIAAFGGDPDSVTIFGES 184
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
109-188 2.39e-04

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 42.57  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100 109 PMVVFVHGGSWESGNKDQYAFVGQSLAQAG--YVTavINYR----------KVPEHVYPDYVN----DTAQAIAWSIENA 172
Cdd:COG2272  106 PVMVWIHGGGFVSGSGSEPLYDGAALARRGvvVVT--INYRlgalgflalpALSGESYGASGNygllDQIAALRWVRDNI 183

                         90
                 ....*....|....*.
gi 523371100 173 ASLHSDPSRVAVMGHS 188
Cdd:COG2272  184 AAFGGDPDNVTIFGES 199
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 91-188 3.09e-03

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 38.67  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523371100   91 PKPLaqaMKAQSTINNDYPMVVFVHGGSWEsgNKDqYAFVGQSLAQAGY-VTAVINYRKVPEHVYPDYVNDTAQAIAWSI 169
Cdd:pfam07224  32 PKPL---IIITPKEAGTYPVVLFLHGTMLS--NEF-YSLFFNHIASHGFiVVAPQLYRLFPPPSQQDEIDSAAEVANWLP 105

                          90       100
                  ....*....|....*....|....
gi 523371100  170 EN-----AASLHSDPSRVAVMGHS 188
Cdd:pfam07224 106 LGlqvvlPTGVEANLSKLALSGHS 129
 
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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