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Conserved domains on  [gi|158262015|ref|NP_058720|]
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phosphatidylcholine-sterol acyltransferase precursor [Rattus norvegicus]

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, ...
83-408 1.26e-144

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: 417.72  E-value: 1.26e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015   83 TIWLDFNMFLPLGVDCWIDNTRVVYNRSSGHMSNAPGVQIRVP-GFgktYSVEYLDDNKLAGY--LHTLVQNLVNNGYVR 159
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  160 DETVRAAPYDWRLAPRQQDEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLR-QPQSWKDHFIDGFISLGAPWG 238
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  239 GSIKPMRILASGDNQGIPIMSNIKLREEQRITTTSPWMFPA-------HHVWPEDHVFISTPNFNYTGQDFERFFAD--- 308
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  309 --------LHFEEGWHMFLQSRDLLAGLP------------------------APGVEVYCLYGVGMPTAHTYIYDH--- 353
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPgkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262015  354 ------NFPYKDPVAALYEDGDDTVATRSTELCGQWQG-RQSQAVHLLPMN----GTDHLNMVFSN 408
Cdd:pfam02450 318 sspilsRIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDILGSN 383
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
83-408 1.26e-144

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: 417.72  E-value: 1.26e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015   83 TIWLDFNMFLPLGVDCWIDNTRVVYNRSSGHMSNAPGVQIRVP-GFgktYSVEYLDDNKLAGY--LHTLVQNLVNNGYVR 159
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  160 DETVRAAPYDWRLAPRQQDEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLR-QPQSWKDHFIDGFISLGAPWG 238
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  239 GSIKPMRILASGDNQGIPIMSNIKLREEQRITTTSPWMFPA-------HHVWPEDHVFISTPNFNYTGQDFERFFAD--- 308
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  309 --------LHFEEGWHMFLQSRDLLAGLP------------------------APGVEVYCLYGVGMPTAHTYIYDH--- 353
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPgkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262015  354 ------NFPYKDPVAALYEDGDDTVATRSTELCGQWQG-RQSQAVHLLPMN----GTDHLNMVFSN 408
Cdd:pfam02450 318 sspilsRIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDILGSN 383
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
48-239 1.77e-07

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 53.10  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  48 PVILVPGCMGNRLEAKlDKPNvvnwlcyRKTEdffTIW-------LDFNMFLplgvdcWidntrVVYNRSSGH-MSNAPG 119
Cdd:PLN02733  21 PVLLVPGIGGSILNAV-DKDG-------GNEE---RVWvrifaadHEFRKKL------W-----SRYDPKTGKtVSLDPK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 120 VQIRVPG--FGkTYSVEYLDDNKLAG-----YLHTLVQNLVNNGYVRDETVRAAPYDWRLAPRQqDEYYQKLAGLVEEMY 192
Cdd:PLN02733  79 TEIVVPDdrYG-LYAIDILDPDVIIRldevyYFHDMIEQLIKWGYKEGKTLFGFGYDFRQSNRL-PETMDGLKKKLETVY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 158262015 193 -AAYGKPVFLIGHSLGCLHVLHFLLRQPQSWKDHfIDGFISLGAPWGG 239
Cdd:PLN02733 157 kASGGKKVNIISHSMGGLLVKCFMSLHSDVFEKY-VNSWIAIAAPFQG 203
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
142-237 2.03e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 142 AGYLHTLVQNLVNNGYvrdeTVRAapYDWR---LAPRQQ------DEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVL 212
Cdd:COG2267   41 SGRYAELAEALAAAGY----AVLA--FDLRghgRSDGPRghvdsfDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAL 114
                         90       100
                 ....*....|....*....|....*
gi 158262015 213 HFLLRQPQSwkdhfIDGFIsLGAPW 237
Cdd:COG2267  115 LYAARYPDR-----VAGLV-LLAPA 133
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
83-408 1.26e-144

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: 417.72  E-value: 1.26e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015   83 TIWLDFNMFLPLGVDCWIDNTRVVYNRSSGHMSNAPGVQIRVP-GFgktYSVEYLDDNKLAGY--LHTLVQNLVNNGYVR 159
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  160 DETVRAAPYDWRLAPRQQDEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLR-QPQSWKDHFIDGFISLGAPWG 238
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  239 GSIKPMRILASGDNQGIPIMSNIKLREEQRITTTSPWMFPA-------HHVWPEDHVFISTPNFNYTGQDFERFFAD--- 308
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  309 --------LHFEEGWHMFLQSRDLLAGLP------------------------APGVEVYCLYGVGMPTAHTYIYDH--- 353
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPgkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262015  354 ------NFPYKDPVAALYEDGDDTVATRSTELCGQWQG-RQSQAVHLLPMN----GTDHLNMVFSN 408
Cdd:pfam02450 318 sspilsRIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDILGSN 383
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
48-239 1.77e-07

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 53.10  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  48 PVILVPGCMGNRLEAKlDKPNvvnwlcyRKTEdffTIW-------LDFNMFLplgvdcWidntrVVYNRSSGH-MSNAPG 119
Cdd:PLN02733  21 PVLLVPGIGGSILNAV-DKDG-------GNEE---RVWvrifaadHEFRKKL------W-----SRYDPKTGKtVSLDPK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 120 VQIRVPG--FGkTYSVEYLDDNKLAG-----YLHTLVQNLVNNGYVRDETVRAAPYDWRLAPRQqDEYYQKLAGLVEEMY 192
Cdd:PLN02733  79 TEIVVPDdrYG-LYAIDILDPDVIIRldevyYFHDMIEQLIKWGYKEGKTLFGFGYDFRQSNRL-PETMDGLKKKLETVY 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 158262015 193 -AAYGKPVFLIGHSLGCLHVLHFLLRQPQSWKDHfIDGFISLGAPWGG 239
Cdd:PLN02733 157 kASGGKKVNIISHSMGGLLVKCFMSLHSDVFEKY-VNSWIAIAAPFQG 203
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
142-237 2.03e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 142 AGYLHTLVQNLVNNGYvrdeTVRAapYDWR---LAPRQQ------DEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVL 212
Cdd:COG2267   41 SGRYAELAEALAAAGY----AVLA--FDLRghgRSDGPRghvdsfDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAL 114
                         90       100
                 ....*....|....*....|....*
gi 158262015 213 HFLLRQPQSwkdhfIDGFIsLGAPW 237
Cdd:COG2267  115 LYAARYPDR-----VAGLV-LLAPA 133
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
142-237 1.31e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 46.75  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 142 AGYLHTLVQNLVNNGYvrdeTVRAAPYDWRLAPRqqDEYYQKLAGLVEEMYAAYG-KPVFLIGHSLGCL---HVLHFLLR 217
Cdd:COG1075   18 AASWAPLAPRLRAAGY----PVYALNYPSTNGSI--EDSAEQLAAFVDAVLAATGaEKVDLVGHSMGGLvarYYLKRLGG 91
                         90       100
                 ....*....|....*....|
gi 158262015 218 QPQswkdhfIDGFISLGAPW 237
Cdd:COG1075   92 AAK------VARVVTLGTPH 105
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
33-215 2.79e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 49.76  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  33 PPHTTPKAELSNHTRPVILVPGCMGNRLEAkldkpnvvnWLCYRKTEDFFTIWLDFNMF-----LPLgvdCWIDntrvvy 107
Cdd:PLN02517  61 PPGVKLRKEGLTAKHPVVFVPGIVTGGLEL---------WEGHQCAEGLFRKRLWGGTFgevykRPL---CWVE------ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 108 nrssgHMS-------NAPGVQIR-VPGFgktYSVEYLddnkLAGYL--HTLVQNLVNNGYvRDETVRAAPYDWRLAPRQ- 176
Cdd:PLN02517 123 -----HMSldnetglDPPGIRVRaVSGL---VAADYF----APGYFvwAVLIANLARIGY-EEKNMYMAAYDWRLSFQNt 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 158262015 177 --QDEYYQKLAGLVEEMYAAYG-KPVFLIGHSLGCLHVLHFL 215
Cdd:PLN02517 190 evRDQTLSRLKSNIELMVATNGgKKVVVVPHSMGVLYFLHFM 231
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
144-236 2.75e-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: 45.28  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015  144 YLHtLVQNLVNNGYVrdetVRAapYDWR---LAPRQQ------DEYYQKLAGLVEEMYAAY-GKPVFLIGHSLGCLHVLH 213
Cdd:pfam12146  20 YAH-LADALAAQGFA----VYA--YDHRghgRSDGKRghvpsfDDYVDDLDTFVDKIREEHpGLPLFLLGHSMGGLIAAL 92
                          90       100
                  ....*....|....*....|...
gi 158262015  214 FLLRQPQSWkdhfiDGFIsLGAP 236
Cdd:pfam12146  93 YALRYPDKV-----DGLI-LSAP 109
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
184-220 3.53e-04

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 40.99  E-value: 3.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 158262015 184 LAGLVEEMyAAYGKPVFLIGHSLGCLHVLHFLLRQPQ 220
Cdd:COG3545   42 LAALDAAV-AAADGPVVLVAHSLGCLAVAHWAARLPR 77
Ser_hydrolase pfam06821
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ...
175-218 8.84e-04

Serine hydrolase; Members of this family have serine hydrolase activity. They contain a conserved serine hydrolase motif, GXSXG/A, where the serine is a putative nucleophile. This family has an alpha-beta hydrolase fold. Eukaryotic members of this family have a conserved LXCXE motif, which binds to retinoblastomas. This motif is absent from prokaryotic members of this family.


Pssm-ID: 399658 [Multi-domain]  Cd Length: 171  Bit Score: 40.01  E-value: 8.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 158262015  175 RQQDEYYQKL----AGLVEEMYAAyGKPVFLIGHSLGCLHVLHFLLRQ 218
Cdd:pfam06821  30 EQDDWLQPVLddwvAALSRAVAAL-PGPVILVAHSLGCLAVAHWAALQ 76
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
321-386 1.13e-03

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 41.28  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262015 321 SRDLLAGLP-APGVEVYCLYGVGMPTAHTYIY---------------------DHNFPYKDPVaaLYEDGDDTVATRSTE 378
Cdd:PLN02517 476 SNPLETKLPnAPEMEIYSLYGVGIPTERSYVYklspsdecsipfqidtsadggDEDSCLKGGV--YFVDGDETVPVLSAG 553
                         90
                 ....*....|
gi 158262015 379 -LCGQ-WQGR 386
Cdd:PLN02517 554 fMCAKgWRGK 563
 
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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