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Conserved domains on  [gi|2217305368|ref|XP_047289843|]
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lysosomal phospholipase A and acyltransferase isoform X3 [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

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
61-246 4.84e-44

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 pfam02450:

Pssm-ID: 473884  Cd Length: 383  Bit Score: 153.09  E-value: 4.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368  61 QPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NYTWSPEKVFV 133
Cdd:pfam02450 137 VAEAWKDQHIDAFISLGAPLLGSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFI 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 134 QTPTINYTLRDYRKFFQD-----------IGFEDGWLMRQDTEGL------------------------VEATMPPGVQL 178
Cdd:pfam02450 217 QTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKV 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 179 HCLYGTGVPTPDSFYYES-----------FPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQ-VLLQELP----GSEH 242
Cdd:pfam02450 297 YCIYGVGLPTERGYYYTPgktsspilsriDYEDPVGIVSGDGDGTVPKRSLELCKNWQGLPAGQnVTVHELKhgsrSAEH 376

                  ....
gi 2217305368 243 IEML 246
Cdd:pfam02450 377 VDIL 380
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
61-246 4.84e-44

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: 153.09  E-value: 4.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368  61 QPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NYTWSPEKVFV 133
Cdd:pfam02450 137 VAEAWKDQHIDAFISLGAPLLGSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFI 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 134 QTPTINYTLRDYRKFFQD-----------IGFEDGWLMRQDTEGL------------------------VEATMPPGVQL 178
Cdd:pfam02450 217 QTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKV 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 179 HCLYGTGVPTPDSFYYES-----------FPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQ-VLLQELP----GSEH 242
Cdd:pfam02450 297 YCIYGVGLPTERGYYYTPgktsspilsriDYEDPVGIVSGDGDGTVPKRSLELCKNWQGLPAGQnVTVHELKhgsrSAEH 376

                  ....
gi 2217305368 243 IEML 246
Cdd:pfam02450 377 VDIL 380
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
167-218 5.25e-03

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 37.69  E-value: 5.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217305368 167 LVEATMPPGVQLHCLYGTGVPTPDSFYY--ESFPDRD--------PKICFGDGDGTVNLKSA 218
Cdd:PLN02733  324 LSSAKLPKGVKFYNIYGTSLDTPFDVCYgsEKSPIEDlseilhtePEYTYVDGDGTVPVESA 385
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
61-246 4.84e-44

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: 153.09  E-value: 4.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368  61 QPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NYTWSPEKVFV 133
Cdd:pfam02450 137 VAEAWKDQHIDAFISLGAPLLGSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFI 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 134 QTPTINYTLRDYRKFFQD-----------IGFEDGWLMRQDTEGL------------------------VEATMPPGVQL 178
Cdd:pfam02450 217 QTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKV 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217305368 179 HCLYGTGVPTPDSFYYES-----------FPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQ-VLLQELP----GSEH 242
Cdd:pfam02450 297 YCIYGVGLPTERGYYYTPgktsspilsriDYEDPVGIVSGDGDGTVPKRSLELCKNWQGLPAGQnVTVHELKhgsrSAEH 376

                  ....
gi 2217305368 243 IEML 246
Cdd:pfam02450 377 VDIL 380
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
167-218 5.25e-03

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 37.69  E-value: 5.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217305368 167 LVEATMPPGVQLHCLYGTGVPTPDSFYY--ESFPDRD--------PKICFGDGDGTVNLKSA 218
Cdd:PLN02733  324 LSSAKLPKGVKFYNIYGTSLDTPFDVCYgsEKSPIEDlseilhtePEYTYVDGDGTVPVESA 385
 
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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