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Conserved domains on  [gi|37537527|ref|NP_079374|]
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2-acylglycerol O-acyltransferase 2 [Homo sapiens]

Protein Classification

lysophospholipid acyltransferase family protein( domain architecture ID 106732)

lysophospholipid acyltransferase (LPLAT) family protein may act as an acyltransferase of a de novo or remodeling pathway of glycerophospholipid biosynthesis, catalyzing the incorporation of an acyl group from either acyl-CoAs or acyl-acyl carrier proteins (acyl-ACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LPLAT super family cl17185
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
41-333 3.04e-133

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


The actual alignment was detected with superfamily member pfam03982:

Pssm-ID: 473073 [Multi-domain]  Cd Length: 297  Bit Score: 381.01  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527    41 LLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN 120
Cdd:pfam03982   3 LFFTPQWSLLVLYALWLFYDWNSPKRGGYRSNWARNWRIWKWFANYFPVKLHKTAELPPNRNYLFGYHPHGILSVGAFSN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   121 LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFT 200
Cdd:pfam03982  83 FSTNATGFMDKFPGIRPNICTLAGQFYTPFRREILLSLGLIEVSRESIEYVLDKCGKGRAVVLVVGGAAEALEAHPGKHT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   201 LLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQ-YSFGLIPYRRP 279
Cdd:pfam03982 163 LTLKNRKGFVRIALKTGADLVPVYSFGENDVYKQWENPEGSRLRWVQEKLKRAIGFSPPIFHGRGVFNsYTFGLLPFRKP 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 37537527   280 ITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKFNIPADQHLEF 333
Cdd:pfam03982 243 ITTVVGAPIEVTKTLNPTQEQIDELHGQYMEALRELFEEHKTKFGVPPDTDLVL 296
 
Name Accession Description Interval E-value
DAGAT pfam03982
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is ...
41-333 3.04e-133

Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is catalyzed by the enzyme diacylglycerol acyltransferase (DAGAT).


Pssm-ID: 112781 [Multi-domain]  Cd Length: 297  Bit Score: 381.01  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527    41 LLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN 120
Cdd:pfam03982   3 LFFTPQWSLLVLYALWLFYDWNSPKRGGYRSNWARNWRIWKWFANYFPVKLHKTAELPPNRNYLFGYHPHGILSVGAFSN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   121 LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFT 200
Cdd:pfam03982  83 FSTNATGFMDKFPGIRPNICTLAGQFYTPFRREILLSLGLIEVSRESIEYVLDKCGKGRAVVLVVGGAAEALEAHPGKHT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   201 LLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQ-YSFGLIPYRRP 279
Cdd:pfam03982 163 LTLKNRKGFVRIALKTGADLVPVYSFGENDVYKQWENPEGSRLRWVQEKLKRAIGFSPPIFHGRGVFNsYTFGLLPFRKP 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 37537527   280 ITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKFNIPADQHLEF 333
Cdd:pfam03982 243 ITTVVGAPIEVTKTLNPTQEQIDELHGQYMEALRELFEEHKTKFGVPPDTDLVL 296
LPLAT_MGAT-like cd07987
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
83-320 1.99e-56

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.


Pssm-ID: 153249 [Multi-domain]  Cd Length: 212  Bit Score: 182.10  E-value: 1.99e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  83 MKDYFPISLVKTAELDPSRNYIAGFHPHGVLAV-GAFANLCtestgFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLV 161
Cdd:cd07987   1 HRKYFRVYEVRGLENIPDEGPALLVHPHGGLPIdGALLAAA-----FLLLFPGRLPRALADHFLFPLPGLRDLLRRLGAV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527 162 TSEKESAAHILNRkggGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGS 241
Cdd:cd07987  76 PGSRENCVRLLRE---GELVLIFPGGAREALKSKREEYYLLWKKRKGFARLALRAGAPIVPVFTFGEEELFRVLGDPDGP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527 242 WLRYIQNRLQkimgislplfhgrgvfqysfglIPYRRPITTVVGKPIEVQKT--LHPSEEEVNQLHQRYIKELCNLFEAH 319
Cdd:cd07987 153 VGKRLFRLLP----------------------LPRRLPLYPVFGEPIVVPRPpiPDPPDEDVEELHQKYIAALRELIEKH 210

                .
gi 37537527 320 K 320
Cdd:cd07987 211 K 211
PLN02783 PLN02783
diacylglycerol O-acyltransferase
24-323 1.33e-45

diacylglycerol O-acyltransferase


Pssm-ID: 178380  Cd Length: 315  Bit Score: 157.47  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   24 VFSFLALAE-ICTVGFIALL-------FTRFWLLTVLyAAWWYLD----RDKPRQGGRHIQAIRcwtiwKYMKDYFPISL 91
Cdd:PLN02783  16 VLSILAVAIwLGAIHFNVALvlaslffLPSPVALTVL-ALLLLLMfipaHPTSKLGRKIARFIC-----KYACAYFPVRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   92 VKTAE--LDPSRNYIAGFHPHGVL--AVGAFANLCtestGFssiFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKES 167
Cdd:PLN02783  90 HVEDEeaFDPNRAYVFGYEPHSVLpiGVIALADLS----GF---LPLPKIRALASSAVFYTPFLRHIWTWLGLDPASRKN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  168 AAHILNRkggGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFdqipnssgSWLR--- 244
Cdd:PLN02783 163 FTSLLKA---GYSCIIVPGGVQECLYMEHGSEVAYLKSRKGFVKIAMETGAPLVPVFCFGQTRAY--------KWWKpgg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  245 YIQNRLQKIMGISLPLFHGRgvfqysFGL-IPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKF 323
Cdd:PLN02783 232 PLVPKLSRAIGFTPIVFWGR------YGSpIPHRTPMHVVVGKPIEVKKNPQPSQEEVAEVLEQFVEALQDLFEKHKARA 305
 
Name Accession Description Interval E-value
DAGAT pfam03982
Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is ...
41-333 3.04e-133

Diacylglycerol acyltransferase; The terminal step of triacylglycerol (TAG) formation is catalyzed by the enzyme diacylglycerol acyltransferase (DAGAT).


Pssm-ID: 112781 [Multi-domain]  Cd Length: 297  Bit Score: 381.01  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527    41 LLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN 120
Cdd:pfam03982   3 LFFTPQWSLLVLYALWLFYDWNSPKRGGYRSNWARNWRIWKWFANYFPVKLHKTAELPPNRNYLFGYHPHGILSVGAFSN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   121 LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFT 200
Cdd:pfam03982  83 FSTNATGFMDKFPGIRPNICTLAGQFYTPFRREILLSLGLIEVSRESIEYVLDKCGKGRAVVLVVGGAAEALEAHPGKHT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   201 LLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQ-YSFGLIPYRRP 279
Cdd:pfam03982 163 LTLKNRKGFVRIALKTGADLVPVYSFGENDVYKQWENPEGSRLRWVQEKLKRAIGFSPPIFHGRGVFNsYTFGLLPFRKP 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 37537527   280 ITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKFNIPADQHLEF 333
Cdd:pfam03982 243 ITTVVGAPIEVTKTLNPTQEQIDELHGQYMEALRELFEEHKTKFGVPPDTDLVL 296
LPLAT_MGAT-like cd07987
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
83-320 1.99e-56

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.


Pssm-ID: 153249 [Multi-domain]  Cd Length: 212  Bit Score: 182.10  E-value: 1.99e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  83 MKDYFPISLVKTAELDPSRNYIAGFHPHGVLAV-GAFANLCtestgFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLV 161
Cdd:cd07987   1 HRKYFRVYEVRGLENIPDEGPALLVHPHGGLPIdGALLAAA-----FLLLFPGRLPRALADHFLFPLPGLRDLLRRLGAV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527 162 TSEKESAAHILNRkggGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGS 241
Cdd:cd07987  76 PGSRENCVRLLRE---GELVLIFPGGAREALKSKREEYYLLWKKRKGFARLALRAGAPIVPVFTFGEEELFRVLGDPDGP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527 242 WLRYIQNRLQkimgislplfhgrgvfqysfglIPYRRPITTVVGKPIEVQKT--LHPSEEEVNQLHQRYIKELCNLFEAH 319
Cdd:cd07987 153 VGKRLFRLLP----------------------LPRRLPLYPVFGEPIVVPRPpiPDPPDEDVEELHQKYIAALRELIEKH 210

                .
gi 37537527 320 K 320
Cdd:cd07987 211 K 211
PLN02783 PLN02783
diacylglycerol O-acyltransferase
24-323 1.33e-45

diacylglycerol O-acyltransferase


Pssm-ID: 178380  Cd Length: 315  Bit Score: 157.47  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   24 VFSFLALAE-ICTVGFIALL-------FTRFWLLTVLyAAWWYLD----RDKPRQGGRHIQAIRcwtiwKYMKDYFPISL 91
Cdd:PLN02783  16 VLSILAVAIwLGAIHFNVALvlaslffLPSPVALTVL-ALLLLLMfipaHPTSKLGRKIARFIC-----KYACAYFPVRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527   92 VKTAE--LDPSRNYIAGFHPHGVL--AVGAFANLCtestGFssiFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKES 167
Cdd:PLN02783  90 HVEDEeaFDPNRAYVFGYEPHSVLpiGVIALADLS----GF---LPLPKIRALASSAVFYTPFLRHIWTWLGLDPASRKN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  168 AAHILNRkggGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFdqipnssgSWLR--- 244
Cdd:PLN02783 163 FTSLLKA---GYSCIIVPGGVQECLYMEHGSEVAYLKSRKGFVKIAMETGAPLVPVFCFGQTRAY--------KWWKpgg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  245 YIQNRLQKIMGISLPLFHGRgvfqysFGL-IPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKF 323
Cdd:PLN02783 232 PLVPKLSRAIGFTPIVFWGR------YGSpIPHRTPMHVVVGKPIEVKKNPQPSQEEVAEVLEQFVEALQDLFEKHKARA 305
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
92-237 6.66e-08

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 52.03  E-value: 6.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37537527  92 VKTAELDPSRNYIAGFHPHGVLAVGAFANLCTE-STGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAH 170
Cdd:cd06551  16 VKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLErGLRRDVYGLMDEELLERYPFFTRLGAFSVDRDSPRSAAKSLKYVAR 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37537527 171 ILnrKGGGNLLGIIVGGAQEALDARPgsftllLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPN 237
Cdd:cd06551  96 LL--SKPGSVVWIFPEGTRTRRDKRP------LQFKPGVAHLAEKAGVPIVPVALRYTFELFEQFPE 154
 
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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