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Conserved domains on  [gi|228312406|pdb|3H19|A]
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Chain A, Esterase/lipase

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
83-284 6.03e-70

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: 216.31  E-value: 6.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A         83 ILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQHLSISGDSA 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        159 GGGLVLAVLVSARDQGLPMPASAIPISPWADMTCTNDSFKTRAEAD-PMVAPGGINKMAARYLNGADAKHPYASPNFA-N 236
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
3H19_A        237 LKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWH 284
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
83-284 6.03e-70

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: 216.31  E-value: 6.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A         83 ILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQHLSISGDSA 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        159 GGGLVLAVLVSARDQGLPMPASAIPISPWADMTCTNDSFKTRAEAD-PMVAPGGINKMAARYLNGADAKHPYASPNFA-N 236
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
3H19_A        237 LKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWH 284
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
74-308 1.62e-63

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 199.71  E-value: 1.62e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       74 APGCQAGKAILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQ 149
Cdd:COG0657   7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaaelGIDPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A      150 HLSISGDSAGGGLVLAVLVSARDQGLPMPASAIPISPWADMTctndsfktraeadpmvapgginkmaarylngadakhpy 229
Cdd:COG0657  87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT-------------------------------------- 128
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3H19_A      230 ASPNFANLKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWHAFHPmLPEGKQAIVRVGEFMREQW 308
Cdd:COG0657 129 ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
75-307 8.59e-23

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 96.33  E-value: 8.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        75 PGCQAGKAILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQGFK----PQH 150
Cdd:PRK10162  76 PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDyginMSR 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       151 LSISGDSAGGGLVLAVLVSARDQGLPMpASAIPISPWADMTCTNDSFKTR---AEADPMVAPGGINKMAARYLNGADAKH 227
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIDC-GKVAGVLLWYGLYGLRDSVSRRllgGVWDGLTQQDLQMYEEAYLSNDADRES 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       228 PYASPnFAN--LKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWHAFHPMLPEGKQAIVRVGEFMR 305
Cdd:PRK10162 235 PYYCL-FNNdlTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQFFT 313

                 ..
3H19_A       306 EQ 307
Cdd:PRK10162 314 AQ 315
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
83-284 6.03e-70

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: 216.31  E-value: 6.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A         83 ILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQHLSISGDSA 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQaaelGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        159 GGGLVLAVLVSARDQGLPMPASAIPISPWADMTCTNDSFKTRAEAD-PMVAPGGINKMAARYLNGADAKHPYASPNFA-N 236
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
3H19_A        237 LKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWH 284
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
74-308 1.62e-63

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 199.71  E-value: 1.62e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       74 APGCQAGKAILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQ 149
Cdd:COG0657   7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaaelGIDPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A      150 HLSISGDSAGGGLVLAVLVSARDQGLPMPASAIPISPWADMTctndsfktraeadpmvapgginkmaarylngadakhpy 229
Cdd:COG0657  87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT-------------------------------------- 128
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3H19_A      230 ASPNFANLKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWHAFHPmLPEGKQAIVRVGEFMREQW 308
Cdd:COG0657 129 ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
75-307 8.59e-23

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 96.33  E-value: 8.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        75 PGCQAGKAILYLHGGGYVMGSINTHRSMVGEISRASQAAALLLDYRLAPEHPFPAAVEDGVAAYRWLLDQGFK----PQH 150
Cdd:PRK10162  76 PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDyginMSR 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       151 LSISGDSAGGGLVLAVLVSARDQGLPMpASAIPISPWADMTCTNDSFKTR---AEADPMVAPGGINKMAARYLNGADAKH 227
Cdd:PRK10162 156 IGFAGDSAGAMLALASALWLRDKQIDC-GKVAGVLLWYGLYGLRDSVSRRllgGVWDGLTQQDLQMYEEAYLSNDADRES 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       228 PYASPnFAN--LKGLPPLLIHVGRDEVLLDDSIKLDAKAKADGVKSTLEIWDDMIHVWHAFHPMLPEGKQAIVRVGEFMR 305
Cdd:PRK10162 235 PYYCL-FNNdlTRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMDTADDALRDGAQFFT 313

                 ..
3H19_A       306 EQ 307
Cdd:PRK10162 314 AQ 315
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
81-260 3.78e-15

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: 75.26  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A         81 KAILYLHGGGYVMGSINTHRSMVGEISRA-SQAAALLLDYRLAPEHP----FPAAVEDGVAAYRWL-LDQGFKpqHLSIS 154
Cdd:pfam10340 123 PILLYYHGGGFALKLIPVTLVFLNNLGKYfPDMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLtLTKGCK--NVTLM 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A        155 GDSAGGGLVLAVLVSARDQGLPM-PASAIPISPWADMTCTNDSFKTRAEAD---PMVAPGGINKMAARYLNGADAKHPYA 230
Cdd:pfam10340 201 GDSAGGNLVLNILLYLHKCNKVVlPKKAIAISPWLNLTDRNEKEKEYMKANdklDGLCYKGLNMFGKLYVPNVEPEESLF 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
3H19_A        231 SPNFANL--------------KGlpPLLIHVGRDEVlLDDSIKL 260
Cdd:pfam10340 281 TDPFVNIemnfdietwskileKC--KLLITYGDDEI-LSDQIKS 321
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
51-306 3.11e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.56  E-value: 3.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A       51 FKAADDIQVEqvtvagcaAEWVRAPGCQAGKAILYLHGGGYvmgsiNTHRSMVGEISRASQA--AALLLDYR---LAPEH 125
Cdd:COG1506   2 FKSADGTTLP--------GWLYLPADGKKYPVVVYVHGGPG-----SRDDSFLPLAQALASRgyAVLAPDYRgygESAGD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A      126 PFPAAVEDGVAAYRWLLDQGF-KPQHLSISGDSAGGGLVLAVLVSARDqglpMPASAIPISPWADMtctnDSFKTRAEAD 204
Cdd:COG1506  69 WGGDEVDDVLAAIDYLAARPYvDPDRIGIYGHSYGGYMALLAAARHPD----RFKAAVALAGVSDL----RSYYGTTREY 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A      205 PMVAPGGINKMAARYlngaDAKHPYAspNFANLKGlPPLLIHVGRDE-VLLDDSIKLDAKAKADGVKSTLEIWDDMIHVW 283
Cdd:COG1506 141 TERLMGGPWEDPEAY----AARSPLA--YADKLKT-PLLLIHGEADDrVPPEQAERLYEALKKAGKPVELLVYPGEGHGF 213
                       250       260
                ....*....|....*....|...
3H19_A      284 HAfhpmlPEGKQAIVRVGEFMRE 306
Cdd:COG1506 214 SG-----AGAPDYLERILDFLDR 231
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
81-164 3.64e-09

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: 56.03  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H19_A         81 KAILYLHGGGYVMGS----INTHRSMVGEISRASQAAALLlDYRLAPEHPFPAAVEDGVAAYRWLLDQ----GFKPQHLS 152
Cdd:pfam20434  14 PVVIWIHGGGWNSGDkeadMGFMTNTVKALLKAGYAVASI-NYRLSTDAKFPAQIQDVKAAIRFLRANaakyGIDTNKIA 92
                          90
                  ....*....|..
3H19_A        153 ISGDSAGGGLVL 164
Cdd:pfam20434  93 LMGFSAGGHLAL 104
 
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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