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Conserved domains on  [gi|126723006|ref|NP_032535|]
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lipoprotein lipase precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lipo_lipase super family cl31319
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
33-472 0e+00

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.


The actual alignment was detected with superfamily member TIGR03230:

Pssm-ID: 132274 [Multi-domain]  Cd Length: 442  Bit Score: 880.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   33 DFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  113 WLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  273 HLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  353 EDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 126723006  433 VKAGETQKKVIFCAREKV-SHLQKGKDSAVFVKCHDKSLKK 472
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSR 441
 
Name Accession Description Interval E-value
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
33-472 0e+00

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: 880.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   33 DFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  113 WLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  273 HLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  353 EDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 126723006  433 VKAGETQKKVIFCAREKV-SHLQKGKDSAVFVKCHDKSLKK 472
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSR 441
Lipase pfam00151
Lipase;
30-338 1.41e-168

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 477.70  E-value: 1.41e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   30 AGRDFSDIESKFALRTPEDTaeDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREpDSNVI 109
Cdd:pfam00151  29 LPWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  110 VVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNF 189
Cdd:pfam00151 106 CVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  190 EYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHE 269
Cdd:pfam00151 186 QGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHL 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723006  270 RSIHLFIDSLLNeENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 266 RSVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
37-334 8.10e-127

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  Cd Length: 275  Bit Score: 369.26  E-value: 8.10e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  37 IESKFALRTPEDtAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLYR 116
Cdd:cd00707    1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 117 AQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707   78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707  158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126723006 277 DSLLNeENPSKAYRCNSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 334
Cdd:cd00707  222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
341-452 4.29e-17

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 76.53  E-value: 4.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   341 FHYQVKIHFSGtEDGKQHNQAFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWisdsyfsw 417
Cdd:smart00308   1 GKYKVTVTTGG-LDFAGTTASVSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKN-------- 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 126723006   418 pdWWSSPSFVIERIRVKAGETQKKVIFCAREKVSH 452
Cdd:smart00308  72 --EHRHPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
77-197 2.56e-04

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 42.69  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  77 VVIHGWTVTGMYESWVPKLVAALYKRepdSNVIVVDWlyRAQQHYPVSAGYTKLVGNDVARFINwmeeefNYPLDNVHLL 156
Cdd:COG0596   25 VLLHGFPGSSSVWRPVFKVLPALAAR---YRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------ALGLEKVVLV 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126723006 157 GYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSR 197
Cdd:COG0596   94 GHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
 
Name Accession Description Interval E-value
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
33-472 0e+00

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: 880.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   33 DFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVD 112
Cdd:TIGR03230   1 DFTDIESKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  113 WLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYA 192
Cdd:TIGR03230  81 WLSRAQQHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLTKHKVNRITGLDPAGPTFEYA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  193 EAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSI 272
Cdd:TIGR03230 161 DAPSTLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  273 HLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGT 352
Cdd:TIGR03230 241 HLFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  353 EDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIR 432
Cdd:TIGR03230 321 TSLSHTDQPMKISLYGTHGEKENIPFTLPEVSTNKTYSFLITTDVDIGELLMVKLKWEKDTYISWSDWWSSPGFHIRKLR 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 126723006  433 VKAGETQKKVIFCAREKV-SHLQKGKDSAVFVKCHDKSLKK 472
Cdd:TIGR03230 401 IKSGETQSKVIFSAKEGEfSYLQRGGEAAVFVKCKEKSLSR 441
Lipase pfam00151
Lipase;
30-338 1.41e-168

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 477.70  E-value: 1.41e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   30 AGRDFSDIESKFALRTPEDTaeDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREpDSNVI 109
Cdd:pfam00151  29 LPWSPKDIDTRFLLYTNENP--NNCQLITGDPETIRNSNFNTSRKTRFIIHGFIDKGYEESWLSDMCKALFQVE-DVNVI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  110 VVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNF 189
Cdd:pfam00151 106 CVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAHVAGEAGRRTNGKLGRITGLDPAGPYF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  190 EYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHE 269
Cdd:pfam00151 186 QGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQPGCQKNILSQIIDIDGIWEGTQFVACNHL 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126723006  270 RSIHLFIDSLLNeENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSS---KMYLKTRSQMPY 338
Cdd:pfam00151 266 RSVHYYIDSLLN-PRGFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
37-334 8.10e-127

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  Cd Length: 275  Bit Score: 369.26  E-value: 8.10e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  37 IESKFALRTPEDtAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMyESWVPKLVAALYKREpDSNVIVVDWLYR 116
Cdd:cd00707    1 IDVRFLLYTREN-PNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRG-DYNVIVVDWGRG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 117 AQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPS 196
Cdd:cd00707   78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNGKLGRITGLDPAGPLFSGADPED 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 197 RLSPDDADFVDVLHTFtrgspGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRviaerglgdvdQLVKCSHERSIHLFI 276
Cdd:cd00707  158 RLDPSDAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPKDILSS-----------DFVACSHQRAVHYFA 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126723006 277 DSLLNeENPSKAYRCNSKEAFEKGLCLSCRKnRCNNLGYEINkvRAKRSSKMYLKTRS 334
Cdd:cd00707  222 ESILS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
341-465 2.27e-62

PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs) and has therefeore has a profound influence on triglyceride and high-density lipoprotein (HDL) cholesterol levels in the blood. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238856  Cd Length: 137  Bit Score: 199.15  E-value: 2.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVST-NKTYSFLIYTEVDIGELLMMKLKWISDSYFSWP- 418
Cdd:cd01758    1 FHYQLKIHFFNQTNRIETDPTFTISLYGTLGESENLPLTLPEGITgNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSw 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 126723006 419 ----------DWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKC 465
Cdd:cd01758   81 wtvqtiipwsGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
341-465 2.67e-47

PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major subgroups, the lipoprotein lipase (LPL) and the pancreatic triglyceride lipase. LPL is a key enzyme in catabolism of plasma lipoprotein triglycerides (TGs). The central role of triglyceride lipases is in energy production. In general, PLAT/LH2 domain's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238853  Cd Length: 120  Bit Score: 159.00  E-value: 2.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 341 FHYQVKIHFSGTEDGKQhNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPdW 420
Cdd:cd01755    1 WHYQVKVHLSGKKNLEV-DGTFTVSLYGTKGETEQLPIVLGELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNS-G 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 126723006 421 WSSPSFVIERIRVKAGETQKKVIFCAREKVSHLqkgKDSAVFVKC 465
Cdd:cd01755   79 ETLPKLGARKIRVKSGETQKKFTFCSQDTVREL---EVLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
127-271 2.01e-27

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: 107.20  E-value: 2.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 127 YTKLVGNDVARFINWMEEEF--NYPLDNVHLLGYSLGAHAAGVAGSLTNK----KVNRITGLDPAGPNFEyAEAPSRLSP 200
Cdd:cd00741    2 GFYKAARSLANLVLPLLKSAlaQYPDYKIHVTGHSLGGALAGLAGLDLRGrglgRLVRVYTFGPPRVGNA-AFAEDRLDP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126723006 201 DDADFVDVLHT----FTRGSPGrsiGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERS 271
Cdd:cd00741   81 SDALFVDRIVNdndiVPRLPPG---GEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRY 152
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
343-463 8.11e-25

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 98.66  E-value: 8.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  343 YQVKIHfSGTEDGKQHNQAFEISLYGTVAESENIPFTL--PEVSTNKTYSFLIYTEVDIGELLMMKLKWISdsyfswpdW 420
Cdd:pfam01477   1 YQVKVV-TGDELGAGTDADVYISLYGKVGESAQLEITLdnPDFERGAEDSFEIDTDWDVGAILKINLHWDN--------N 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 126723006  421 WSSPSFVIERIRV-KAGETQKKVIFCAREKVSHLQKGKDSAVFV 463
Cdd:pfam01477  72 GLSDEWFLKSITVeVPGETGGKYTFPCNSWVYGSKKYKETRVFF 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
341-452 4.29e-17

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 76.53  E-value: 4.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   341 FHYQVKIHFSGtEDGKQHNQAFEISLYGTVA---ESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWisdsyfsw 417
Cdd:smart00308   1 GKYKVTVTTGG-LDFAGTTASVSLSLVGAEGdgkESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKN-------- 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 126723006   418 pdWWSSPSFVIERIRVKAGETQKKVIFCAREKVSH 452
Cdd:smart00308  72 --EHRHPEWFLKSITVKDLPTGGKYHFPCNSWVYP 104
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
342-445 1.33e-10

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 58.50  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 342 HYQVKIHFSGTEDGKQHNQaFEISLYGTVAESENIPFTLPEVS--TNKTYSFLIYTEVDIGELLMMKLKWisDSYFSWPD 419
Cdd:cd00113    2 RYTVTIKTGDKKGAGTDSN-ISLALYGENGNSSDIPILDGPGSfeRGSTDTFQIDLKLDIGDITKVYLRR--DGSGLSDG 78
                         90       100
                 ....*....|....*....|....*.
gi 126723006 420 WwsspsfVIERIRVKAGETQKKVIFC 445
Cdd:cd00113   79 W------YCESITVQALGTKKVYTFP 98
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
74-207 3.93e-08

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: 54.05  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006   74 KTFVVIHGWTvtGMYESWvPKLVAALYKREPDsnVIVVDWLYRAQ-QHYPVSAGYTKLvgnDVARFINWMEEEFnyPLDN 152
Cdd:pfam00561   1 PPVLLLHGLP--GSSDLW-RKLAPALARDGFR--VIALDLRGFGKsSRPKAQDDYRTD---DLAEDLEYILEAL--GLEK 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 126723006  153 VHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVD 207
Cdd:pfam00561  71 VNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFD 125
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
343-451 8.31e-05

PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and triglycerides to generate fatty acids for energy production or for storage and to release inositol phosphates that act as second messengers. The central role of triglyceride lipases is in energy production. The proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238857  Cd Length: 113  Bit Score: 41.97  E-value: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006 343 YQVKIHFSGTEDGKQHnqaFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKW----ISDSYfswp 418
Cdd:cd01759    3 YKVSVTLSGKKKVTGT---ILVSLYGNKGNTRQYEIFKGTLKPGNTYSAFIDVDVDVGPLTKVKFIWnnnvINITL---- 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 126723006 419 dwwssPSFVIERIRVKAGETQKKVIFCAREKVS 451
Cdd:cd01759   76 -----PKVGAEKITVQSGKDGKVFNFCSSETVR 103
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
77-197 2.56e-04

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 42.69  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723006  77 VVIHGWTVTGMYESWVPKLVAALYKRepdSNVIVVDWlyRAQQHYPVSAGYTKLVGNDVARFINwmeeefNYPLDNVHLL 156
Cdd:COG0596   25 VLLHGFPGSSSVWRPVFKVLPALAAR---YRVIAPDL--RGHGRSDPAGYSLSAYADDLAALLD------ALGLEKVVLV 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126723006 157 GYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSR 197
Cdd:COG0596   94 GHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQ 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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