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Conserved domains on  [gi|41056195|ref|NP_957316|]
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hepatic triacylglycerol lipase precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lipase super family cl28163
Lipase;
44-488 6.22e-160

Lipase;


The actual alignment was detected with superfamily member TIGR03230:

Pssm-ID: 332983  Cd Length: 442  Bit Score: 465.91  E-value: 6.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    44 SVFRVYTDGEYTEDTCALELFQPHTLDACGFNSSLPLAIIIHGWSVDGMMEKWISRLASALKSSEGNINVLIADWLTLAH 123
Cdd:TIGR03230   7 SKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   124 QHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSnlaMSGRTLGRITGLDPAGPMFEGMSHT 203
Cdd:TIGR03230  87 QHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGS---LTKHKVNRITGLDPAGPTFEYADAP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   204 DRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQPGCQLhmQNIYAHLAQHGIMGFEQTVKCAHERAVH 283
Cdd:TIGR03230 164 STLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDI--QETLLVIAEKGLGNMDQLVKCSHERSIH 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   284 LFIDSLLNKDKQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDIKKVRTGKSKRLFLKTRSHMPYKLFHYQFRIQFI--N 361
Cdd:TIGR03230 242 LFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFgkT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   362 QIDKIDPTLTVSLSGTLGESENLPITLvEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNpvwanmwntvkTIIPWGKKS 441
Cdd:TIGR03230 322 SLSHTDQPMKISLYGTHGEKENIPFTL-PEVSTNKTYSFLITTDVDIGELLMVKLKWEKD-----------TYISWSDWW 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 41056195   442 KGPQLTFGKITVKSGESQRKTTFCPQTDEGMSIEMLQEK-VFVRCEKQ 488
Cdd:TIGR03230 390 SSPGFHIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEAaVFVKCKEK 437
 
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 ...
44-488 6.22e-160

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  Cd Length: 442  Bit Score: 465.91  E-value: 6.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    44 SVFRVYTDGEYTEDTCALELFQPHTLDACGFNSSLPLAIIIHGWSVDGMMEKWISRLASALKSSEGNINVLIADWLTLAH 123
Cdd:TIGR03230   7 SKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   124 QHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSnlaMSGRTLGRITGLDPAGPMFEGMSHT 203
Cdd:TIGR03230  87 QHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGS---LTKHKVNRITGLDPAGPTFEYADAP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   204 DRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQPGCQLhmQNIYAHLAQHGIMGFEQTVKCAHERAVH 283
Cdd:TIGR03230 164 STLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDI--QETLLVIAEKGLGNMDQLVKCSHERSIH 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   284 LFIDSLLNKDKQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDIKKVRTGKSKRLFLKTRSHMPYKLFHYQFRIQFI--N 361
Cdd:TIGR03230 242 LFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFgkT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   362 QIDKIDPTLTVSLSGTLGESENLPITLvEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNpvwanmwntvkTIIPWGKKS 441
Cdd:TIGR03230 322 SLSHTDQPMKISLYGTHGEKENIPFTL-PEVSTNKTYSFLITTDVDIGELLMVKLKWEKD-----------TYISWSDWW 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 41056195   442 KGPQLTFGKITVKSGESQRKTTFCPQTDEGMSIEMLQEK-VFVRCEKQ 488
Cdd:TIGR03230 390 SSPGFHIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEAaVFVKCKEK 437
Lipase pfam00151
Lipase;
9-348 1.83e-127

Lipase;


Pssm-ID: 278576  Cd Length: 336  Bit Score: 379.09  E-value: 1.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195     9 LCFLMISQLTDGATFQGNRADTEPEARMKMRYEPKSVFRVYTDGEytEDTCALELFQPHTLDACGFNSSLPLAIIIHGWS 88
Cdd:pfam00151   3 VCYGQLGCFGDKIPWAGNTLVRPVKSLPWSPKDIDTRFLLYTNEN--PNNCQLITGDPETIRNSNFNTSRKTRFIIHGFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    89 VDGMMEKWISRLASALKSSEgNINVLIADWLTLAHQHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAH 168
Cdd:pfam00151  81 DKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   169 ISGFAGSNLamsGRTLGRITGLDPAGPMFEGMSHTDRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQ 248
Cdd:pfam00151 160 VAGEAGRRT---NGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   249 PGCQlhmQNI-YAHLAQHGIMGFEQTVKCAHERAVHLFIDSLLNKDkQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDI 327
Cdd:pfam00151 237 PGCQ---KNIlSQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
                         330       340
                  ....*....|....*....|....
gi 41056195   328 KKVRTGKSK---RLFLKTRSHMPY 348
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
54-344 1.95e-105

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: 319.96  E-value: 1.95e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195  54 YTEDT--CALELFQ--PHTLDACGFNSSLPLAIIIHGWSVDGMmEKWISRLASALKSsEGNINVLIADWLTLAHQHYPIA 129
Cdd:cd00707   8 YTRENpnCPQLLFAddPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLS-RGDYNVIVVDWGRGANPNYPQA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 130 AQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSNLamsGRTLGRITGLDPAGPMFEGMSHTDRLSPE 209
Cdd:cd00707  86 VNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRL---NGKLGRITGLDPAGPLFSGADPEDRLDPS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 210 DAKFVDAIHTFtlqrmGLSVGIKQPVAHFDFYPNGGSFQPGCQLhmqNIYAHlaqhgimgfeQTVKCAHERAVHLFIDSL 289
Cdd:cd00707 163 DAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPK---DILSS----------DFVACSHQRAVHYFAESI 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41056195 290 LNkDKQIMAYKCSDNTAFDKGNCLDCRKnRCNTLGYDIKkvRTGKSKRLFLKTRS 344
Cdd:cd00707 225 LS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
351-465 5.56e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608  Cd Length: 105  Bit Score: 48.79  E-value: 5.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    351 FHYQFRIQFINQI-DKIDPTLTVSLSGTLGESENLPITLVEE--ISGNKTFTFLITLDTDIGDLMIMRFTWEGNpvwanm 427
Cdd:smart00308   1 GKYKVTVTTGGLDfAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHR------ 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 41056195    428 wntvktiipwgkkskGPQLTFGKITVKSGESQRKTTFC 465
Cdd:smart00308  75 ---------------HPEWFLKSITVKDLPTGGKYHFP 97
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
79-190 4.37e-03

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


Pssm-ID: 223669  Cd Length: 282  Bit Score: 38.84  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195  79 PLAIIIHGWSVDGMMEKWISRLASALkssEGNINVLIADWLtlAHQHYPIAAQNTRIVGQDIAHLLswledfKQFPLGKV 158
Cdd:COG0596  22 PPLVLLHGFPGSSSVWRPVFKVLPAL---AARYRVIAPDLR--GHGRSDPAGYSLSAYADDLAALL------DALGLEKV 90
                        90       100       110
                ....*....|....*....|....*....|..
gi 41056195 159 HLIGYSLGAHISgfagsnLAMSGRTLGRITGL 190
Cdd:COG0596  91 VLVGHSMGGAVA------LALALRHPDRVRGL 116
 
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 ...
44-488 6.22e-160

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  Cd Length: 442  Bit Score: 465.91  E-value: 6.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    44 SVFRVYTDGEYTEDTCALELFQPHTLDACGFNSSLPLAIIIHGWSVDGMMEKWISRLASALKSSEGNINVLIADWLTLAH 123
Cdd:TIGR03230   7 SKFSLRTPEEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSANVIVVDWLSRAQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   124 QHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSnlaMSGRTLGRITGLDPAGPMFEGMSHT 203
Cdd:TIGR03230  87 QHYPTSAAYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGS---LTKHKVNRITGLDPAGPTFEYADAP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   204 DRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQPGCQLhmQNIYAHLAQHGIMGFEQTVKCAHERAVH 283
Cdd:TIGR03230 164 STLSPDDADFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDI--QETLLVIAEKGLGNMDQLVKCSHERSIH 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   284 LFIDSLLNKDKQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDIKKVRTGKSKRLFLKTRSHMPYKLFHYQFRIQFI--N 361
Cdd:TIGR03230 242 LFIDSLLNEENPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFgkT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   362 QIDKIDPTLTVSLSGTLGESENLPITLvEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNpvwanmwntvkTIIPWGKKS 441
Cdd:TIGR03230 322 SLSHTDQPMKISLYGTHGEKENIPFTL-PEVSTNKTYSFLITTDVDIGELLMVKLKWEKD-----------TYISWSDWW 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 41056195   442 KGPQLTFGKITVKSGESQRKTTFCPQTDEGMSIEMLQEK-VFVRCEKQ 488
Cdd:TIGR03230 390 SSPGFHIRKLRIKSGETQSKVIFSAKEGEFSYLQRGGEAaVFVKCKEK 437
Lipase pfam00151
Lipase;
9-348 1.83e-127

Lipase;


Pssm-ID: 278576  Cd Length: 336  Bit Score: 379.09  E-value: 1.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195     9 LCFLMISQLTDGATFQGNRADTEPEARMKMRYEPKSVFRVYTDGEytEDTCALELFQPHTLDACGFNSSLPLAIIIHGWS 88
Cdd:pfam00151   3 VCYGQLGCFGDKIPWAGNTLVRPVKSLPWSPKDIDTRFLLYTNEN--PNNCQLITGDPETIRNSNFNTSRKTRFIIHGFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    89 VDGMMEKWISRLASALKSSEgNINVLIADWLTLAHQHYPIAAQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAH 168
Cdd:pfam00151  81 DKGYEESWLSDMCKALFQVE-DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLGAH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   169 ISGFAGSNLamsGRTLGRITGLDPAGPMFEGMSHTDRLSPEDAKFVDAIHTFTLQRMGLSVGIKQPVAHFDFYPNGGSFQ 248
Cdd:pfam00151 160 VAGEAGRRT---NGKLGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSEQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   249 PGCQlhmQNI-YAHLAQHGIMGFEQTVKCAHERAVHLFIDSLLNKDkQIMAYKCSDNTAFDKGNCLDCRKNRCNTLGYDI 327
Cdd:pfam00151 237 PGCQ---KNIlSQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYA 312
                         330       340
                  ....*....|....*....|....
gi 41056195   328 KKVRTGKSK---RLFLKTRSHMPY 348
Cdd:pfam00151 313 DKFPGKTSKleqTFYLNTGSSSPF 336
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
54-344 1.95e-105

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: 319.96  E-value: 1.95e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195  54 YTEDT--CALELFQ--PHTLDACGFNSSLPLAIIIHGWSVDGMmEKWISRLASALKSsEGNINVLIADWLTLAHQHYPIA 129
Cdd:cd00707   8 YTRENpnCPQLLFAddPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLS-RGDYNVIVVDWGRGANPNYPQA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 130 AQNTRIVGQDIAHLLSWLEDFKQFPLGKVHLIGYSLGAHISGFAGSNLamsGRTLGRITGLDPAGPMFEGMSHTDRLSPE 209
Cdd:cd00707  86 VNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRL---NGKLGRITGLDPAGPLFSGADPEDRLDPS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 210 DAKFVDAIHTFtlqrmGLSVGIKQPVAHFDFYPNGGSFQPGCQLhmqNIYAHlaqhgimgfeQTVKCAHERAVHLFIDSL 289
Cdd:cd00707 163 DAQFVDVIHTD-----GGLLGFSQPIGHADFYPNGGRDQPGCPK---DILSS----------DFVACSHQRAVHYFAESI 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41056195 290 LNkDKQIMAYKCSDNTAFDKGNCLDCRKnRCNTLGYDIKkvRTGKSKRLFLKTRS 344
Cdd:cd00707 225 LS-PCGFVAYPCSSYDEFLAGKCFPCGS-GCVRMGYHAD--RFRREGKFYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
351-485 6.08e-71

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: 225.73  E-value: 6.08e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 351 FHYQFRIQFINQIDK--IDPTLTVSLSGTLGESENLPITLVEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNPVWANMW 428
Cdd:cd01758   1 FHYQLKIHFFNQTNRieTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41056195 429 NTVKTIIPWGKKSKGPQLTFGKITVKSGESQRKTTFCPQTDEGMSIEMLQEKVFVRC 485
Cdd:cd01758  81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
351-485 1.36e-42

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: 149.37  E-value: 1.36e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 351 FHYQFRIQFINQID-KIDPTLTVSLSGTLGESENLPITLvEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNPVWANMWN 429
Cdd:cd01755   1 WHYQVKVHLSGKKNlEVDGTFTVSLYGTKGETEQLPIVL-GELKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSGE 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41056195 430 TvktiipwgkkskGPQLTFGKITVKSGESQRKTTFCPQTDEGmsiEMLQEKVFVRC 485
Cdd:cd01755  80 T------------LPKLGARKIRVKSGETQKKFTFCSQDTVR---ELEVLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
131-282 4.16e-26

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  Cd Length: 153  Bit Score: 104.89  E-value: 4.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 131 QNTRIVGQDIAHLLSWLED--FKQFPLGKVHLIGYSLGAHISGFAGSNLA-MSGRTLGRITGLDPAGPMFEGMShTDRLS 207
Cdd:cd00741   1 KGFYKAARSLANLVLPLLKsaLAQYPDYKIHVTGHSLGGALAGLAGLDLRgRGLGRLVRVYTFGPPRVGNAAFA-EDRLD 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41056195 208 PEDAKFVDAIHTFT-LQRMGLSVGIKQPVAHFDFYPNGGSFQPGCqlHMQNIYAHLAQHGIMGFEQTVKCAHERAV 282
Cdd:cd00741  80 PSDALFVDRIVNDNdIVPRLPPGGEGYPHGGAEFYINGGKSQPGC--CKNVLEAVDIDFGNIGLSGNGLCDHLRYF 153
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
353-465 1.20e-11

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: 307568  Cd Length: 115  Bit Score: 62.84  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195   353 YQFRIQFINQIDK-IDPTLTVSLSGTLGESENLPITLV-EEISGNKTFTFLITLDTDIGDLMIMRFTWEGNPVWAnmwnt 430
Cdd:pfam01477   1 YQVKVVTGDELGAgTDADVYISLYGKVGESAQLEITLDnPDFERGAEDSFEIDTDWDVGAILKINLHWDNNGLSD----- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 41056195   431 vktiiPWGKKSkgpqltfgkITV-KSGESQRKTTFC 465
Cdd:pfam01477  76 -----EWFLKS---------ITVeVPGETGGKYTFP 97
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
352-465 1.04e-08

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: 54.27  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 352 HYQFRIQFINQID-KIDPTLTVSLSGTLGESENLPIT-LVEEISGNKTFTFLITLDTDIGDLMIMRFTWEGNPVWANmwn 429
Cdd:cd00113   2 RYTVTIKTGDKKGaGTDSNISLALYGENGNSSDIPILdGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDG--- 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 41056195 430 tvktiipWGKKSkgpqltfgkITVKSGESQRKTTFC 465
Cdd:cd00113  79 -------WYCES---------ITVQALGTKKVYTFP 98
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
351-465 5.56e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608  Cd Length: 105  Bit Score: 48.79  E-value: 5.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195    351 FHYQFRIQFINQI-DKIDPTLTVSLSGTLGESENLPITLVEE--ISGNKTFTFLITLDTDIGDLMIMRFTWEGNpvwanm 427
Cdd:smart00308   1 GKYKVTVTTGGLDfAGTTASVSLSLVGAEGDGKESKLDYLFKgiFARGSTYEFTFDVDEDFGELGAVKIKNEHR------ 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 41056195    428 wntvktiipwgkkskGPQLTFGKITVKSGESQRKTTFC 465
Cdd:smart00308  75 ---------------HPEWFLKSITVKDLPTGGKYHFP 97
PLAT_PL cd01759
PLAT/LH2 domain of pancreatic triglyceride lipase. Lipases hydrolyze phospholipids and ...
369-478 3.66e-06

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: 46.59  E-value: 3.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195 369 TLTVSLSGTLGESENLPITLVEEISGNkTFTFLITLDTDIGDLMIMRFTWEgnpvwanmwNTVKTIIPwgkkskgPQLTF 448
Cdd:cd01759  18 TILVSLYGNKGNTRQYEIFKGTLKPGN-TYSAFIDVDVDVGPLTKVKFIWN---------NNVINITL-------PKVGA 80
                        90       100       110
                ....*....|....*....|....*....|
gi 41056195 449 GKITVKSGESQRKTTFCPQtdEGMSIEMLQ 478
Cdd:cd01759  81 EKITVQSGKDGKVFNFCSS--ETVRENVLQ 108
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
79-190 4.37e-03

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


Pssm-ID: 223669  Cd Length: 282  Bit Score: 38.84  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056195  79 PLAIIIHGWSVDGMMEKWISRLASALkssEGNINVLIADWLtlAHQHYPIAAQNTRIVGQDIAHLLswledfKQFPLGKV 158
Cdd:COG0596  22 PPLVLLHGFPGSSSVWRPVFKVLPAL---AARYRVIAPDLR--GHGRSDPAGYSLSAYADDLAALL------DALGLEKV 90
                        90       100       110
                ....*....|....*....|....*....|..
gi 41056195 159 HLIGYSLGAHISgfagsnLAMSGRTLGRITGL 190
Cdd:COG0596  91 VLVGHSMGGAVA------LALALRHPDRVRGL 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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