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Conserved domains on  [gi|2786459525|ref|WP_369810476|]
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esterase/lipase family protein [Bacillus safensis]

Protein Classification

esterase/lipase family protein( domain architecture ID 10787203)

esterase/lipase family protein is an alpha/beta hydrolase, such as triacylglycerol lipase that catalyzes the hydrolysis of a triacylglycerol to form the corresponding diacylglycerol and a carboxylate

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787|GO:0016042

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
11-117 5.20e-31

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 108.76  E-value: 5.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  11 AAEHNPVVMVHGIGGASYNFFSIKSYLATQGWdrnQLYAIDFIDKTGNNRNNGPRLSRFVKDVLDKTGAKKVDIVAHSMG 90
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAGY---PVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMG 78
                          90       100
                  ....*....|....*....|....*..
gi 2786459525  91 GANTLYYIKNLDGGDKIENVVTIGGAN 117
Cdd:COG1075    79 GLVARYYLKRLGGAAKVARVVTLGTPH 105
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
11-117 5.20e-31

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 108.76  E-value: 5.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  11 AAEHNPVVMVHGIGGASYNFFSIKSYLATQGWdrnQLYAIDFIDKTGNNRNNGPRLSRFVKDVLDKTGAKKVDIVAHSMG 90
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAGY---PVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMG 78
                          90       100
                  ....*....|....*....|....*..
gi 2786459525  91 GANTLYYIKNLDGGDKIENVVTIGGAN 117
Cdd:COG1075    79 GLVARYYLKRLGGAAKVARVVTLGTPH 105
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
14-128 4.86e-16

Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.


Pssm-ID: 396304 [Multi-domain]  Cd Length: 218  Bit Score: 72.77  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  14 HNPVVMVHGIGG-ASYNFFSIKSYLATQGWDRNQLYAIDFIDKTGNNR-------NNGPRLSRFVKDVLDKTGAKKVDIV 85
Cdd:pfam01674   1 NQPVIFVHGNSGlAAGGWSKLSQYFKERGYTLAELYATTWGDGNESTSlqraekcEYVKQIRRFIEAVLGYTGAAKVDIV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2786459525  86 AHSMGGANTLYYIKNLDGGD-----------KIENVVTIGGANGLVSSRALPGT 128
Cdd:pfam01674  81 AHSMGVPIARKAILGGNCVDtnedlgppltsLVDTFVSVAGANYGICLCPSGDT 134
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
16-92 2.73e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  16 PVVMVHGIGGasynffSIKSYLATQ---GWDRnQLYAIDFIDKTGNNRNNGP----RLSRFVKDVLDKTGAKKVDIVAHS 88
Cdd:PRK14875  133 PVVLIHGFGG------DLNNWLFNHaalAAGR-PVIALDLPGHGASSKAVGAgsldELAAAVLAFLDALGIERAHLVGHS 205

                  ....
gi 2786459525  89 MGGA 92
Cdd:PRK14875  206 MGGA 209
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
11-117 5.20e-31

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 108.76  E-value: 5.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  11 AAEHNPVVMVHGIGGASYNFFSIKSYLATQGWdrnQLYAIDFIDKTGNNRNNGPRLSRFVKDVLDKTGAKKVDIVAHSMG 90
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAGY---PVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMG 78
                          90       100
                  ....*....|....*....|....*..
gi 2786459525  91 GANTLYYIKNLDGGDKIENVVTIGGAN 117
Cdd:COG1075    79 GLVARYYLKRLGGAAKVARVVTLGTPH 105
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
14-128 4.86e-16

Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.


Pssm-ID: 396304 [Multi-domain]  Cd Length: 218  Bit Score: 72.77  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  14 HNPVVMVHGIGG-ASYNFFSIKSYLATQGWDRNQLYAIDFIDKTGNNR-------NNGPRLSRFVKDVLDKTGAKKVDIV 85
Cdd:pfam01674   1 NQPVIFVHGNSGlAAGGWSKLSQYFKERGYTLAELYATTWGDGNESTSlqraekcEYVKQIRRFIEAVLGYTGAAKVDIV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2786459525  86 AHSMGGANTLYYIKNLDGGD-----------KIENVVTIGGANGLVSSRALPGT 128
Cdd:pfam01674  81 AHSMGVPIARKAILGGNCVDtnedlgppltsLVDTFVSVAGANYGICLCPSGDT 134
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
15-115 4.67e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 65.22  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  15 NPVVMVHGIGGASYNFFSIKSYLATQGWDrnqLYAIDF----IDKTGNNRNNGP--RLSRFVKDVLDKTGAKKVDIVAHS 88
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFR---VIALDLrgfgKSSRPKAQDDYRtdDLAEDLEYILEALGLEKVNLVGHS 77
                          90       100
                  ....*....|....*....|....*..
gi 2786459525  89 MGGANTLYYIknLDGGDKIENVVTIGG 115
Cdd:pfam00561  78 MGGLIALAYA--AKYPDRVKALVLLGA 102
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
16-116 1.83e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 55.01  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  16 PVVMVHGIGGASYNFFSIKSYLATQGWDrnqLYAIDF--IDKTGNNRNNGPRLSRFVKDV------LDKTGAKKVDIVAH 87
Cdd:COG2267    30 TVVLVHGLGEHSGRYAELAEALAAAGYA---VLAFDLrgHGRSDGPRGHVDSFDDYVDDLraaldaLRARPGLPVVLLGH 106
                          90       100
                  ....*....|....*....|....*....
gi 2786459525  88 SMGGANTLYYIknLDGGDKIENVVTIGGA 116
Cdd:COG2267   107 SMGGLIALLYA--ARYPDRVAGLVLLAPA 133
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
16-131 4.41e-09

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 53.85  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  16 PVVMVHGIGGASYNFFSIKSYLAtqgwDRNQLYAIDFI-----DKTGNNRNnGPRLSRFVKDVLDKTGAKKVDIVAHSMG 90
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLIPALA----AGYRVIAPDLRghgrsDKPAGGYT-LDDLADDLAALLDALGLERVVLVGHSMG 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2786459525  91 GANTLYYIknLDGGDKIENVVTIGGA-NGLVSSRALPGTDPN 131
Cdd:COG0596   100 GMVALELA--ARHPERVAGLVLVDEVlAALAEPLRRPGLAPE 139
COG4782 COG4782
Esterase/lipase superfamily enzyme [General function prediction only];
63-111 2.03e-05

Esterase/lipase superfamily enzyme [General function prediction only];


Pssm-ID: 443812  Cd Length: 357  Bit Score: 43.79  E-value: 2.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2786459525  63 GPRLSRFVKDVLDKTGAKKVDIVAHSMGGANTLY-----YIKNLDG-GDKIENVV 111
Cdd:COG4782   181 RDALEELLRDLARDPGAERIHIVAHSMGNWLTMEalrqlAIRGRGRvLRKIGQVV 235
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
8-98 6.56e-05

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 42.20  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525   8 EAKAAehnpVVMVHGIGGASYNFFSIKSYLATQGWDrnqLYAIDFID--KTGNNRNNGPRLSRFVKDV---LDKTGA--- 79
Cdd:pfam12146   2 EPRAV----VVLVHGLGEHSGRYAHLADALAAQGFA---VYAYDHRGhgRSDGKRGHVPSFDDYVDDLdtfVDKIREehp 74
                          90       100
                  ....*....|....*....|
gi 2786459525  80 -KKVDIVAHSMGGANTLYYI 98
Cdd:pfam12146  75 gLPLFLLGHSMGGLIAALYA 94
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
16-92 2.73e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  16 PVVMVHGIGGasynffSIKSYLATQ---GWDRnQLYAIDFIDKTGNNRNNGP----RLSRFVKDVLDKTGAKKVDIVAHS 88
Cdd:PRK14875  133 PVVLIHGFGG------DLNNWLFNHaalAAGR-PVIALDLPGHGASSKAVGAgsldELAAAVLAFLDALGIERAHLVGHS 205

                  ....
gi 2786459525  89 MGGA 92
Cdd:PRK14875  206 MGGA 209
COG4814 COG4814
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
58-122 9.89e-04

Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];


Pssm-ID: 443842  Cd Length: 286  Bit Score: 38.77  E-value: 9.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786459525  58 NNRNNGPRLSRFVKDVL----DKTGAKKVDIVAHSMGGANTLYYIKNlDGGDK----IENVVTIGGA-NGLVSS 122
Cdd:COG4814   108 DNRDSIKKQAKWLKKVLkylkKKYGFKKFNAVGHSMGGLALTYYLEK-YGNDKslpkLNKLVTIGGPfNGIENE 180
DUF900 pfam05990
Alpha/beta hydrolase of unknown function (DUF900); This family consists of several ...
17-111 4.28e-03

Alpha/beta hydrolase of unknown function (DUF900); This family consists of several hypothetical proteins of unknown function mostly found in Rhizobium species. Members of this family have an alpha/beta hydrolase fold.


Pssm-ID: 399172  Cd Length: 236  Bit Score: 36.64  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  17 VVMVHGIG----GASYNFFSIKSYLATQG------W-DRNQLYAIDfIDKTGNNRNNgPRLSRFVKDVLDKTGAKKVDIV 85
Cdd:pfam05990  22 LVFVHGYNnsfeDAVFRFAQIAHDLGNQGvpvvftWpSRGSVFDYN-YDKESANYSR-PALEHLLRYLANDPPVKKIYLI 99
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2786459525  86 AHSMGGANTLYYIKNL-------DGGDKIENVV 111
Cdd:pfam05990 100 AHSMGTWLVMEALRQLaieadepGVEAKIDNVI 132
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
30-115 4.81e-03

Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved in extracellular metabolism of plasma lipoproteins, including cholesterol.


Pssm-ID: 396835  Cd Length: 383  Bit Score: 36.76  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  30 FFSIKSYLATQGWDRNQ-LYAIDFIDKTGNNRNN--GPRLSRFVKDVLdKTGAKKVDIVAHSMGGANTLYYIKNLDG--- 103
Cdd:pfam02450  63 WHKVVQNLVNIGYERNKtVRAAPYDWRLSLEERDkyFHKLKQLIEEAH-KLYGKKVVLIGHSMGNLLVLYFLLWVVAeaw 141
                          90
                  ....*....|...
gi 2786459525 104 -GDKIENVVTIGG 115
Cdd:pfam02450 142 kDQHIDAFISLGA 154
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
17-96 9.75e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 35.76  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786459525  17 VVMVHGIGGASYNFFSIK-SYLATQGwdrnqlYAIDFIDKTGNNRNNGPRLSRFVKDVLD---------KTGAKKVDIVA 86
Cdd:COG1506    26 VVYVHGGPGSRDDSFLPLaQALASRG------YAVLAPDYRGYGESAGDWGGDEVDDVLAaidylaarpYVDPDRIGIYG 99
                          90
                  ....*....|
gi 2786459525  87 HSMGGANTLY 96
Cdd:COG1506   100 HSYGGYMALL 109
 
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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