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Conserved domains on  [gi|1622916630|ref|XP_014981935|]
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phosphatidylcholine-sterol acyltransferase isoform X4 [Macaca mulatta]

Protein Classification

alpha/beta hydrolase; tannase/feruloyl esterase family alpha/beta hydrolase( domain architecture ID 11131495)

uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds| tannase/feruloyl esterase family alpha/beta hydrolase similar to Aspergillus oryzae tannase and Aspergillus niger feruloyl esterase B

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
11-336 3.44e-161

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: 456.63  E-value: 3.44e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  11 TIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVP-GFgktYSVEYLDSSKLAGY--LHTLVQNLVNNGYVR 87
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  88 DETVRAAPYDWRLEPGQQEEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLR-QPQAWKDRFIDGFISLGAPWG 166
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 167 GSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSR-------MAWPEDHVFISTPSFNYTGRDFQRFFAD--- 236
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKGkyvlwsdVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 237 --------LHFEEGWYMWLQSRDLLAGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHG-- 282
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916630 283 -------FPYTDPVDVLYEDGDDTVATRSTELCGLWQG-RQPQPVHLLPL----RGIQHLNMVFSN 336
Cdd:pfam02450 318 sspilsrIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELkhgsRSAEHVDILGSN 383
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
11-336 3.44e-161

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: 456.63  E-value: 3.44e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  11 TIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVP-GFgktYSVEYLDSSKLAGY--LHTLVQNLVNNGYVR 87
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  88 DETVRAAPYDWRLEPGQQEEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLR-QPQAWKDRFIDGFISLGAPWG 166
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 167 GSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSR-------MAWPEDHVFISTPSFNYTGRDFQRFFAD--- 236
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKGkyvlwsdVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 237 --------LHFEEGWYMWLQSRDLLAGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHG-- 282
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916630 283 -------FPYTDPVDVLYEDGDDTVATRSTELCGLWQG-RQPQPVHLLPL----RGIQHLNMVFSN 336
Cdd:pfam02450 318 sspilsrIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELkhgsRSAEHVDILGSN 383
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
70-165 3.37e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 50.39  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  70 AGYLHTLVQNLVNNGYvrdeTVRAapYDWR---LEPGQQ------EEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLL 140
Cdd:COG2267    41 SGRYAELAEALAAAGY----AVLA--FDLRghgRSDGPRghvdsfDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAL 114
                          90       100
                  ....*....|....*....|....*
gi 1622916630 141 YFLLRQPQAwkdrfIDGFIsLGAPW 165
Cdd:COG2267   115 LYAARYPDR-----VAGLV-LLAPA 133
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
35-167 9.93e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 47.32  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  35 YNRSSG-LVSNAPGVQIRVPG--FGkTYSVEYLDSSKLAG-----YLHTLVQNLVNNGYVRDETVRAAPYDWRlEPGQQE 106
Cdd:PLN02733   65 YDPKTGkTVSLDPKTEIVVPDdrYG-LYAIDILDPDVIIRldevyYFHDMIEQLIKWGYKEGKTLFGFGYDFR-QSNRLP 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916630 107 EYYHKLAGLVEEMH-AAYGKPVFLIGHSLGCLHLLYFLLRQPQAWkDRFIDGFISLGAPWGG 167
Cdd:PLN02733  143 ETMDGLKKKLETVYkASGGKKVNIISHSMGGLLVKCFMSLHSDVF-EKYVNSWIAIAAPFQG 203
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
11-336 3.44e-161

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: 456.63  E-value: 3.44e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  11 TIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVP-GFgktYSVEYLDSSKLAGY--LHTLVQNLVNNGYVR 87
Cdd:pfam02450   1 RIWLDLNMLLPLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYwiWHKVVQNLVNIGYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  88 DETVRAAPYDWRLEPGQQEEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLR-QPQAWKDRFIDGFISLGAPWG 166
Cdd:pfam02450  78 NKTVRAAPYDWRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 167 GSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSR-------MAWPEDHVFISTPSFNYTGRDFQRFFAD--- 236
Cdd:pfam02450 158 GSPKAVRALASGYNFGIPILSEITLRGLQRSFSSSPWMLPKGkyvlwsdVAWPSDEIFIQTPSINYTYGALVRFFDDeti 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630 237 --------LHFEEGWYMWLQSRDLLAGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHG-- 282
Cdd:pfam02450 238 nvdalgftLNTLDGWYMWKVSRDLDGGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGkt 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916630 283 -------FPYTDPVDVLYEDGDDTVATRSTELCGLWQG-RQPQPVHLLPL----RGIQHLNMVFSN 336
Cdd:pfam02450 318 sspilsrIDYEDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELkhgsRSAEHVDILGSN 383
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
70-165 3.37e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 50.39  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  70 AGYLHTLVQNLVNNGYvrdeTVRAapYDWR---LEPGQQ------EEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLL 140
Cdd:COG2267    41 SGRYAELAEALAAAGY----AVLA--FDLRghgRSDGPRghvdsfDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAL 114
                          90       100
                  ....*....|....*....|....*
gi 1622916630 141 YFLLRQPQAwkdrfIDGFIsLGAPW 165
Cdd:COG2267   115 LYAARYPDR-----VAGLV-LLAPA 133
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
70-165 3.84e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 45.21  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  70 AGYLHTLVQNLVNNGYvrdeTVRAAPYDWRLEPgqQEEYYHKLAGLVEEMHAAYG-KPVFLIGHSLGCLHLLYFLLRQPQ 148
Cdd:COG1075    18 AASWAPLAPRLRAAGY----PVYALNYPSTNGS--IEDSAEQLAAFVDAVLAATGaEKVDLVGHSMGGLVARYYLKRLGG 91
                          90
                  ....*....|....*..
gi 1622916630 149 AwkdRFIDGFISLGAPW 165
Cdd:COG1075    92 A---AKVARVVTLGTPH 105
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
35-167 9.93e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 47.32  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  35 YNRSSG-LVSNAPGVQIRVPG--FGkTYSVEYLDSSKLAG-----YLHTLVQNLVNNGYVRDETVRAAPYDWRlEPGQQE 106
Cdd:PLN02733   65 YDPKTGkTVSLDPKTEIVVPDdrYG-LYAIDILDPDVIIRldevyYFHDMIEQLIKWGYKEGKTLFGFGYDFR-QSNRLP 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916630 107 EYYHKLAGLVEEMH-AAYGKPVFLIGHSLGCLHLLYFLLRQPQAWkDRFIDGFISLGAPWGG 167
Cdd:PLN02733  143 ETMDGLKKKLETVYkASGGKKVNIISHSMGGLLVKCFMSLHSDVF-EKYVNSWIAIAAPFQG 203
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
249-279 8.46e-05

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 44.36  E-value: 8.46e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622916630 249 SRDLLAGLP-APGVEVYCLYGVGLPTPRTYIY 279
Cdd:PLN02517  476 SNPLETKLPnAPEMEIYSLYGVGIPTERSYVY 507
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
72-180 2.83e-04

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: 41.82  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  72 YLHtLVQNLVNNGYVrdetVRAapYDWR---LEPGQQ------EEYYHKLAGLVEEMHAAY-GKPVFLIGHSLGCLHLLY 141
Cdd:pfam12146  20 YAH-LADALAAQGFA----VYA--YDHRghgRSDGKRghvpsfDDYVDDLDTFVDKIREEHpGLPLFLLGHSMGGLIAAL 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622916630 142 FLLRQPQAW------------KDRFIDGFISLGAPWGGSIKPMLVLASGDN 180
Cdd:pfam12146  93 YALRYPDKVdglilsapalkiKPYLAPPILKLLAKLLGKLFPRLRVPNNLL 143
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
26-143 3.70e-04

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 42.44  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916630  26 CWIDNTRVvyNRSSGLvsNAPGVQIR-VPGFgktYSVEYLdsskLAGYL--HTLVQNLVNNGYvRDETVRAAPYDWRLEP 102
Cdd:PLN02517  119 CWVEHMSL--DNETGL--DPPGIRVRaVSGL---VAADYF----APGYFvwAVLIANLARIGY-EEKNMYMAAYDWRLSF 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622916630 103 GQQEEYYHKLAGL---VEEMHAAYG-KPVFLIGHSLGCLHLLYFL 143
Cdd:PLN02517  187 QNTEVRDQTLSRLksnIELMVATNGgKKVVVVPHSMGVLYFLHFM 231
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
112-148 2.17e-03

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 38.68  E-value: 2.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622916630 112 LAGLVEEMHAAyGKPVFLIGHSLGCLHLLYFLLRQPQ 148
Cdd:COG3545    42 LAALDAAVAAA-DGPVVLVAHSLGCLAVAHWAARLPR 77
Ser_hydrolase pfam06821
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ...
112-149 6.77e-03

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: 36.93  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622916630 112 LAGLVEEMHAAyGKPVFLIGHSLGCLHLLYFLLRQPQA 149
Cdd:pfam06821  43 VAALSRAVAAL-PGPVILVAHSLGCLAVAHWAALQLRA 79
 
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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