NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462562000|ref|XP_054175348|]
View 

endothelial lipase isoform X1 [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 85-227 1.28e-57

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 cd00707:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 275  Bit Score: 184.37  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  85 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHIREkDANVVVVDWLPLAH 164
Cdd:cd00707     3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462562000 165 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA 227
Cdd:cd00707    80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITG 142
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 85-227 1.28e-57

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 184.37  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  85 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHIREkDANVVVVDWLPLAH 164
Cdd:cd00707     3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462562000 165 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA 227
Cdd:cd00707    80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITG 142
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
 86-226 6.41e-53

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 177.01  E-value: 6.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  86 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHIREKDANVVVVDWLPLAHQ 165
Cdd:TIGR03230   8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462562000 166 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRIT 226
Cdd:TIGR03230  88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRIT 148
Lipase pfam00151
Lipase;
60-227 1.47e-51

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 170.70  E-value: 1.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  60 AGPSVRRPRDKLHKPKAtqtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLH 139
Cdd:pfam00151  18 AGNTLVRPVKSLPWSPK-----DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000 140 KLVSALHIREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVK 219
Cdd:pfam00151  91 DMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN 169


                  ....*...
gi 2462562000 220 GTVGRITA 227
Cdd:pfam00151 170 GKLGRITG 177
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 118-211 3.89e-03

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: 37.67  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000 118 TAKTFFIIHGWTMSGifENWlHKLVSALhirEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 191
Cdd:COG0596    22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83

                          90       100
                  ....*....|....*....|
gi 2462562000 192 DDFSLGNVHLIGYSLGAHVA 211
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVA 103
 
Name Accession Description Interval E-value
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 85-227 1.28e-57

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 184.37  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  85 VRFNLRTSKDPEHeGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGiFENWLHKLVSALHIREkDANVVVVDWLPLAH 164
Cdd:cd00707     3 VRFLLYTRENPNC-PQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSG-EESWISDLRKAYLSRG-DYNVIVVDWGRGAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462562000 165 QLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITA 227
Cdd:cd00707    80 PNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITG 142
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
 86-226 6.41e-53

lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a eukaryotic triacylglycerol lipase active in plasma and similar to pancreatic and hepatic triacylglycerol lipases (EC 3.1.1.3). It is also called clearing factor. It cleaves chylomicron and VLDL triacylglycerols; it also has phospholipase A-1 activity.


Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 177.01  E-value: 6.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  86 RFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHIREKDANVVVVDWLPLAHQ 165
Cdd:TIGR03230   8 KFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQQ 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462562000 166 LYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRIT 226
Cdd:TIGR03230  88 HYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRIT 148
Lipase pfam00151
Lipase;
60-227 1.47e-51

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 170.70  E-value: 1.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000  60 AGPSVRRPRDKLHKPKAtqtevKPSVRFNLRTSKDPEheGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLH 139
Cdd:pfam00151  18 AGNTLVRPVKSLPWSPK-----DIDTRFLLYTNENPN--NCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000 140 KLVSALHIREkDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVK 219
Cdd:pfam00151  91 DMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTN 169


                  ....*...
gi 2462562000 220 GTVGRITA 227
Cdd:pfam00151 170 GKLGRITG 177
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 172-227 1.72e-07

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 49.42  E-value: 1.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462562000 172 NNTRVVGHSIARMLDWLQEK--DDFSLGNVHLIGYSLGAHVAGYAGNFVKGT----VGRITA 227
Cdd:cd00741     1 KGFYKAARSLANLVLPLLKSalAQYPDYKIHVTGHSLGGALAGLAGLDLRGRglgrLVRVYT 62
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 120-219 3.54e-05

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: 43.65  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000 120 KTFFIIHGWTMSGifENWlHKLVSALhiREKDANVVVVDWLplAHQLYTDAVNNTRVVGHSIARMLDWLQEKddFSLGNV 199
Cdd:pfam00561   1 PPVLLLHGLPGSS--DLW-RKLAPAL--ARDGFRVIALDLR--GFGKSSRPKAQDDYRTDDLAEDLEYILEA--LGLEKV 71

                          90       100
                  ....*....|....*....|.
gi 2462562000 200 HLIGYSLG-AHVAGYAGNFVK 219
Cdd:pfam00561  72 NLVGHSMGgLIALAYAAKYPD 92
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 118-211 3.89e-03

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: 37.67  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562000 118 TAKTFFIIHGWTMSGifENWlHKLVSALhirEKDANVVVVDWL-----PLAHQLYTdavnntrvvghsIARMLDWLQEK- 191
Cdd:COG0596    22 DGPPVVLLHGLPGSS--YEW-RPLIPAL---AAGYRVIAPDLRghgrsDKPAGGYT------------LDDLADDLAALl 83

                          90       100
                  ....*....|....*....|
gi 2462562000 192 DDFSLGNVHLIGYSLGAHVA 211
Cdd:COG0596    84 DALGLERVVLVGHSMGGMVA 103
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH