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Conserved domains on  [gi|880808860|ref|WP_048661025|]
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triacylglycerol lipase [Vibrio crassostreae]

Protein Classification

lipase family alpha/beta hydrolase( domain architecture ID 18498059)

lipase family alpha/beta hydrolase similar to triacylglycerol lipase that catalyzes the hydrolysis of triacylglycerol

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917|37582413

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 ...
 31-138 5.00e-34

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 120.32  E-value: 5.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  31 YTETKYPIVLVHGLFGFDTLagvdyFYGVPESLTKDGASVYVAQVSATNSS-EVRGEQLLAQVETLIAATGASKVNLVGH 109
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAAS-----WAPLAPRLRAAGYPVYALNYPSTNGSiEDSAEQLAAFVDAVLAATGAEKVDLVGH 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808860 110 SHGGPTARYVASV--RPDLVASVTSIGGVHK 138
Cdd:COG1075   76 SMGGLVARYYLKRlgGAAKVARVVTLGTPHH 106
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 36-282 2.86e-19

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 85.25  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   36 YPIVLVHGLFGfdtlaGVDYFYGVPESLTKDGASVYVAQVSATNSSEVRGEQ-------LLAQVETLIAATGASKVNLVG 108
Cdd:pfam00561   1 PPVLLLHGLPG-----SSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQddyrtddLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  109 HSHGGPTARYVASVRPDLVASVTSIGGVHKGSK--VADLVRGTVPEGSATEGIAVKLADGLTTLINLLSGGTDLDQDGLA 186
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALVLLGALDPPHEldEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  187 SLEALTtegSLAFNQFYPEGVPTSECGDGEWQASNGVYYYSWTGS--STFTNLLDPTDGAMTILGLAFtepndgLVGACS 264
Cdd:pfam00561 156 ALPLLN---KRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRldEPTLIIWGDQDPLVPPQALEK------LAQLFP 226

                         250
                  ....*....|....*...
gi 880808860  265 AHLGKVIGDDYKMNHLDE 282
Cdd:pfam00561 227 NARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 31-138 5.00e-34

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 120.32  E-value: 5.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  31 YTETKYPIVLVHGLFGFDTLagvdyFYGVPESLTKDGASVYVAQVSATNSS-EVRGEQLLAQVETLIAATGASKVNLVGH 109
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAAS-----WAPLAPRLRAAGYPVYALNYPSTNGSiEDSAEQLAAFVDAVLAATGAEKVDLVGH 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808860 110 SHGGPTARYVASV--RPDLVASVTSIGGVHK 138
Cdd:COG1075   76 SMGGLVARYYLKRlgGAAKVARVVTLGTPHH 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 36-282 2.86e-19

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: 85.25  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   36 YPIVLVHGLFGfdtlaGVDYFYGVPESLTKDGASVYVAQVSATNSSEVRGEQ-------LLAQVETLIAATGASKVNLVG 108
Cdd:pfam00561   1 PPVLLLHGLPG-----SSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQddyrtddLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  109 HSHGGPTARYVASVRPDLVASVTSIGGVHKGSK--VADLVRGTVPEGSATEGIAVKLADGLTTLINLLSGGTDLDQDGLA 186
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALVLLGALDPPHEldEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  187 SLEALTtegSLAFNQFYPEGVPTSECGDGEWQASNGVYYYSWTGS--STFTNLLDPTDGAMTILGLAFtepndgLVGACS 264
Cdd:pfam00561 156 ALPLLN---KRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRldEPTLIIWGDQDPLVPPQALEK------LAQLFP 226

                         250
                  ....*....|....*...
gi 880808860  265 AHLGKVIGDDYKMNHLDE 282
Cdd:pfam00561 227 NARLVVIPDAGHFAFLEG 244
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
 37-119 4.67e-07

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: 49.66  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   37 PIVLVHGLFGfdtLAGVDYFYGVPESLTKDgasVYVAQVSATN-------SSEVRGE--QLLAQVETLIAA----TGASK 103
Cdd:pfam01674   3 PVIFVHGNSG---LAAGGWSKLSQYFKERG---YTLAELYATTwgdgnesTSLQRAEkcEYVKQIRRFIEAvlgyTGAAK 76

                          90
                  ....*....|....*.
gi 880808860  104 VNLVGHSHGGPTARYV 119
Cdd:pfam01674  77 VDIVAHSMGVPIARKA 92
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 37-150 3.04e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 44.93  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  37 PIVLVHG--------LFGFDTLAGVDYFYGVpeSLTKDGASVYVAQVSATnssevrgEQLLAQVETLIAATGASKVNLVG 108
Cdd:PRK14875 133 PVVLIHGfggdlnnwLFNHAALAAGRPVIAL--DLPGHGASSKAVGAGSL-------DELAAAVLAFLDALGIERAHLVG 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 880808860 109 HSHGGPTARYVASVRPDLVASVTSIGGVHKGSKV-ADLVRGTV 150
Cdd:PRK14875 204 HSMGGAVALRLAARAPQRVASLTLIAPAGLGPEInGDYIDGFV 246
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 89-133 1.33e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 39.90  E-value: 1.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 880808860  89 LAQVETLIAATGAS------KVNLVGHSHGGPTARYVASVRPDLVASVTSI 133
Cdd:cd12809  152 LAEQEALVRAAGCAlldiigPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 31-138 5.00e-34

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 120.32  E-value: 5.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  31 YTETKYPIVLVHGLFGFDTLagvdyFYGVPESLTKDGASVYVAQVSATNSS-EVRGEQLLAQVETLIAATGASKVNLVGH 109
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAAS-----WAPLAPRLRAAGYPVYALNYPSTNGSiEDSAEQLAAFVDAVLAATGAEKVDLVGH 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808860 110 SHGGPTARYVASV--RPDLVASVTSIGGVHK 138
Cdd:COG1075   76 SMGGLVARYYLKRlgGAAKVARVVTLGTPHH 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 36-282 2.86e-19

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: 85.25  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   36 YPIVLVHGLFGfdtlaGVDYFYGVPESLTKDGASVYVAQVSATNSSEVRGEQ-------LLAQVETLIAATGASKVNLVG 108
Cdd:pfam00561   1 PPVLLLHGLPG-----SSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQddyrtddLAEDLEYILEALGLEKVNLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  109 HSHGGPTARYVASVRPDLVASVTSIGGVHKGSK--VADLVRGTVPEGSATEGIAVKLADGLTTLINLLSGGTDLDQDGLA 186
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALVLLGALDPPHEldEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  187 SLEALTtegSLAFNQFYPEGVPTSECGDGEWQASNGVYYYSWTGS--STFTNLLDPTDGAMTILGLAFtepndgLVGACS 264
Cdd:pfam00561 156 ALPLLN---KRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRldEPTLIIWGDQDPLVPPQALEK------LAQLFP 226

                         250
                  ....*....|....*...
gi 880808860  265 AHLGKVIGDDYKMNHLDE 282
Cdd:pfam00561 227 NARLVVIPDAGHFAFLEG 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 37-138 2.01e-08

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: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  37 PIVLVHGLFGfdtlaGVDYFYGVPESLTKDGASVYVAQV----SATNSSEVRGEQLLAQVETLIAATGASKVNLVGHSHG 112
Cdd:COG0596   25 PVVLLHGLPG-----SSYEWRPLIPALAAGYRVIAPDLRghgrSDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100
                 ....*....|....*....|....*.
gi 880808860 113 GPTARYVASVRPDLVASVTSIGGVHK 138
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVDEVLA 125
Lipase_2 pfam01674
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ...
 37-119 4.67e-07

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: 49.66  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   37 PIVLVHGLFGfdtLAGVDYFYGVPESLTKDgasVYVAQVSATN-------SSEVRGE--QLLAQVETLIAA----TGASK 103
Cdd:pfam01674   3 PVIFVHGNSG---LAAGGWSKLSQYFKERG---YTLAELYATTwgdgnesTSLQRAEkcEYVKQIRRFIEAvlgyTGAAK 76

                          90
                  ....*....|....*.
gi 880808860  104 VNLVGHSHGGPTARYV 119
Cdd:pfam01674  77 VDIVAHSMGVPIARKA 92
Palm_thioest pfam02089
Palmitoyl protein thioesterase;
37-145 1.15e-05

Palmitoyl protein thioesterase;


Pssm-ID: 460441 [Multi-domain]  Cd Length: 248  Bit Score: 45.69  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860   37 PIVLVHGLF------GFDTLAgvdyfygvpESLTK--DGASVYVAQVSATNSSEVRG-------EQLLAQVETLIAATGA 101
Cdd:pfam02089   1 PVVIWHGLGdscaspGMQSLA---------ELIKEahPGTYVHSIDIGDGPSEDRKAsffgnmnEQVEAVCEQLKPELPA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 880808860  102 SKVNLVGHSHGGPTARYVASVRPDL-VASVTSIGGVHKGskVADL 145
Cdd:pfam02089  72 NGFNAIGFSQGGLFLRGLVERCPDPpVHNLISLGGPHMG--VFGL 114
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 37-150 3.04e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 44.93  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  37 PIVLVHG--------LFGFDTLAGVDYFYGVpeSLTKDGASVYVAQVSATnssevrgEQLLAQVETLIAATGASKVNLVG 108
Cdd:PRK14875 133 PVVLIHGfggdlnnwLFNHAALAAGRPVIAL--DLPGHGASSKAVGAGSL-------DELAAAVLAFLDALGIERAHLVG 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 880808860 109 HSHGGPTARYVASVRPDLVASVTSIGGVHKGSKV-ADLVRGTV 150
Cdd:PRK14875 204 HSMGGAVALRLAARAPQRVASLTLIAPAGLGPEInGDYIDGFV 246
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
21-137 6.93e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.47  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  21 TSASALEVSGY-----TETKYP-IVLVHGLFGfdtlAGVDYFYGVPESLTKDGasvY-VAQVSATNSSEVRGEQLLAQVE 93
Cdd:COG1506    3 KSADGTTLPGWlylpaDGKKYPvVVYVHGGPG----SRDDSFLPLAQALASRG---YaVLAPDYRGYGESAGDWGGDEVD 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 880808860  94 TLIAAT---------GASKVNLVGHSHGGPTARYVASVRPDLVASVTSIGGVH 137
Cdd:COG1506   76 DVLAAIdylaarpyvDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS 128
PRK10673 PRK10673
esterase;
37-133 2.99e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 41.64  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  37 PIVLVHGLFG-FDTLaGVdyfygvpesLTKDGASVY-VAQVSATN-SSEVRGEQL----LAQ-VETLIAATGASKVNLVG 108
Cdd:PRK10673  18 PIVLVHGLFGsLDNL-GV---------LARDLVNDHdIIQVDMRNhGLSPRDPVMnypaMAQdLLDTLDALQIEKATFIG 87

                         90       100
                 ....*....|....*....|....*
gi 880808860 109 HSHGGPTARYVASVRPDLVASVTSI 133
Cdd:PRK10673  88 HSMGGKAVMALTALAPDRIDKLVAI 112
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-147 9.51e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 9.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  21 TSASALEVSGY-----TETKYPIVLV-HGLFGF--------DTLAGVDYFYGVPESLTKDGASVYVAQVSATnSSEVRGE 86
Cdd:COG0412    9 PTPDGVTLPGYlarpaGGGPRPGVVVlHEIFGLnphirdvaRRLAAAGYVVLAPDLYGRGGPGDDPDEARAL-MGALDPE 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 880808860  87 QLLAQVETLIAA------TGASKVNLVGHSHGGPTARYVASVRPDLVASVtSIGGVHKGSKVADLVR 147
Cdd:COG0412   88 LLAADLRAALDWlkaqpeVDAGRVGVVGFCFGGGLALLAAARGPDLAAAV-SFYGGLPADDLLDLAA 153
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 89-133 1.33e-03

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214008  Cd Length: 280  Bit Score: 39.90  E-value: 1.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 880808860  89 LAQVETLIAATGAS------KVNLVGHSHGGPTARYVASVRPDLVASVTSI 133
Cdd:cd12809  152 LAEQEALVRAAGCAlldiigPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
33-134 2.94e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 38.44  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808860  33 ETKYPIVLVHGLFGFdtlagVDYFYGVPESLTKDGASVYVA------QVSATNSSEVRGEQLLAQVETLIA---ATGASK 103
Cdd:COG2267   26 SPRGTVVLVHGLGEH-----SGRYAELAEALAAAGYAVLAFdlrghgRSDGPRGHVDSFDDYVDDLRAALDalrARPGLP 100

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808860 104 VNLVGHSHGGPTARYVASVRPDLVASVTSIG 134
Cdd:COG2267  101 VVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
 
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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