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Conserved domains on  [gi|56961643|ref|NP_036729|]
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hepatic triacylglycerol lipase precursor [Rattus norvegicus]

Protein Classification

Pancreat_lipase_like and PLAT_LPL domain-containing protein( domain architecture ID 11988341)

Pancreat_lipase_like and PLAT_LPL domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
18-350 4.49e-180

Lipase;


:

Pssm-ID: 395099  Cd Length: 336  Bit Score: 507.75  E-value: 4.49e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    18 QSSACGQGVG------TEPFGRNLGATEERKPLQKPEIRFLLFKDESDrLGCQLRPQHPETLQECGFNSSHPLVMIIHGW 91
Cdd:pfam00151   1 KEVCYGQLGCfgdkipWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENP-NNCQLITGDPETIRNSNFNTSRKTRFIIHGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    92 SVDGLLETWIWKIVGALKSRQsqPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLG 171
Cdd:pfam00151  80 IDKGYEESWLSDMCKALFQVE--DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   172 AHVSGFAGSSMGGKrkIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSF 251
Cdd:pfam00151 158 AHVAGEAGRRTNGK--LGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   252 QPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSNlQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRR 331
Cdd:pfam00151 236 QPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADK 314
                         330       340
                  ....*....|....*....|..
gi 56961643   332 DRPRKSK---TLFLITRAQSPF 350
Cdd:pfam00151 315 FPGKTSKleqTFYLNTGSSSPF 336
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
353-488 8.34e-64

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: 203.39  E-value: 8.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 353 YHYQFKIQFINQMEKP-IEPTFTMTLLGTKEEIKKIPITLGEGITSNKTYSLLITLDKDIGELIMLKFKWENSAVWANVW 431
Cdd:cd01758   1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56961643 432 NTVQTIMLWDTEPHYAGLILKTIWVKAGETQQRMTFCPDNVDDLQLHPTQEKVFVKC 488
Cdd:cd01758  81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
18-350 4.49e-180

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 507.75  E-value: 4.49e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    18 QSSACGQGVG------TEPFGRNLGATEERKPLQKPEIRFLLFKDESDrLGCQLRPQHPETLQECGFNSSHPLVMIIHGW 91
Cdd:pfam00151   1 KEVCYGQLGCfgdkipWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENP-NNCQLITGDPETIRNSNFNTSRKTRFIIHGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    92 SVDGLLETWIWKIVGALKSRQsqPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLG 171
Cdd:pfam00151  80 IDKGYEESWLSDMCKALFQVE--DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   172 AHVSGFAGSSMGGKrkIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSF 251
Cdd:pfam00151 158 AHVAGEAGRRTNGK--LGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   252 QPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSNlQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRR 331
Cdd:pfam00151 236 QPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADK 314
                         330       340
                  ....*....|....*....|..
gi 56961643   332 DRPRKSK---TLFLITRAQSPF 350
Cdd:pfam00151 315 FPGKTSKleqTFYLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
56-488 1.47e-144

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: 421.61  E-value: 1.47e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    56 DESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLLETWIWKIVGALKSRQSQPvNVGLVDWISLAYQHYAIAV 135
Cdd:TIGR03230  15 EEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSA-NVIVVDWLSRAQQHYPTSA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   136 RNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMggKRKIGRITGLDPAGPMFEGTSPNERLSPDDA 215
Cdd:TIGR03230  94 AYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLT--KHKVNRITGLDPAGPTFEYADAPSTLSPDDA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   216 NFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSN 295
Cdd:TIGR03230 172 DFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   296 LQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRRDRPRKSKTLFLITRAQSPFKVYHYQFKIQFI--NQMEKPIEPtF 373
Cdd:TIGR03230 252 NPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFgkTSLSHTDQP-M 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   374 TMTLLGTKEEIKKIPITLGEgITSNKTYSLLITLDKDIGELIMLKFKWENSAV--WANVWNTvqtimlwdtephyAGLIL 451
Cdd:TIGR03230 331 KISLYGTHGEKENIPFTLPE-VSTNKTYSFLITTDVDIGELLMVKLKWEKDTYisWSDWWSS-------------PGFHI 396
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 56961643   452 KTIWVKAGETQQRMTFCPDNVDDLQLHPTQEK-VFVKC 488
Cdd:TIGR03230 397 RKLRIKSGETQSKVIFSAKEGEFSYLQRGGEAaVFVKC 434
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
47-346 2.20e-113

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 [Multi-domain]  Cd Length: 275  Bit Score: 335.75  E-value: 2.20e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643  47 PEIRFLLFKDESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLlETWIWKIVGALKSRQSqpVNVGLVDWISL 126
Cdd:cd00707   1 IDVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRGD--YNVIVVDWGRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 127 AYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMGGkrKIGRITGLDPAGPMFEGTSP 206
Cdd:cd00707  78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNG--KLGRITGLDPAGPLFSGADP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 207 NERLSPDDANFVDAIHTFTREhmglsVGIKQPIAHYDFYPNGGSFQPGCHFlelykhiaehgLNAITQTIKCAHERSVHL 286
Cdd:cd00707 156 EDRLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPK-----------DILSSDFVACSHQRAVHY 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56961643 287 FIDSL-QHSNLqnTGFQCSNMDSFSQGLCLNCKKGrCNSLGYDIrrDRPRKSKTLFLITRA 346
Cdd:cd00707 220 FAESIlSPCGF--VAYPCSSYDEFLAGKCFPCGSG-CVRMGYHA--DRFRREGKFYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
353-488 8.34e-64

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: 203.39  E-value: 8.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 353 YHYQFKIQFINQMEKP-IEPTFTMTLLGTKEEIKKIPITLGEGITSNKTYSLLITLDKDIGELIMLKFKWENSAVWANVW 431
Cdd:cd01758   1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56961643 432 NTVQTIMLWDTEPHYAGLILKTIWVKAGETQQRMTFCPDNVDDLQLHPTQEKVFVKC 488
Cdd:cd01758  81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
355-486 4.32e-13

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: 65.53  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   355 YQFKIQFINQMEKPIEPTFTMTLLGTKEEIKKIPITLGEG-ITSNKTYSLLITLDKDIGELIMLKFKWENSavwanvwnt 433
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDNN--------- 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56961643   434 vqtimlwdtePHYAGLILKTIWV-KAGETQQRMTFCP-DNVDDLQlHPTQEKVFV 486
Cdd:pfam01477  72 ----------GLSDEWFLKSITVeVPGETGGKYTFPCnSWVYGSK-KYKETRVFF 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
353-468 2.52e-12

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 63.04  E-value: 2.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    353 YHYQFKIQFINQMEKPIEPTFTMTLLGTKEEIKK-IPITLGEGITS-NKTYSLLITLDKDIGELIMLKFKWENSAVwanv 430
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKEsKLDYLFKGIFArGSTYEFTFDVDEDFGELGAVKIKNEHRHP---- 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 56961643    431 wntvqtimlwdtephyaGLILKTIWVKAGETQQRMTFC 468
Cdd:smart00308  77 -----------------EWFLKSITVKDLPTGGKYHFP 97
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
82-199 3.72e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.12  E-value: 3.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643  82 HPLVMIiHGWSVDGllETWiWKIVGALKSRQSQPVNVGLvDWISLAYQHYAiavrntRVVGQEVAALLlwleesMKFSRS 161
Cdd:COG1075   6 YPVVLV-HGLGGSA--ASW-APLAPRLRAAGYPVYALNY-PSTNGSIEDSA------EQLAAFVDAVL------AATGAE 68
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 56961643 162 KVHLIGYSLGAHVSGFAGSSMGGKRKIGRITGLdpAGP 199
Cdd:COG1075  69 KVDLVGHSMGGLVARYYLKRLGGAAKVARVVTL--GTP 104
 
Name Accession Description Interval E-value
Lipase pfam00151
Lipase;
18-350 4.49e-180

Lipase;


Pssm-ID: 395099  Cd Length: 336  Bit Score: 507.75  E-value: 4.49e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    18 QSSACGQGVG------TEPFGRNLGATEERKPLQKPEIRFLLFKDESDrLGCQLRPQHPETLQECGFNSSHPLVMIIHGW 91
Cdd:pfam00151   1 KEVCYGQLGCfgdkipWAGNTLVRPVKSLPWSPKDIDTRFLLYTNENP-NNCQLITGDPETIRNSNFNTSRKTRFIIHGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    92 SVDGLLETWIWKIVGALKSRQsqPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLG 171
Cdd:pfam00151  80 IDKGYEESWLSDMCKALFQVE--DVNVICVDWKSGSRTHYTQAVQNIRVVGAEVANLLQWLSNELNYSPSNVHLIGHSLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   172 AHVSGFAGSSMGGKrkIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSF 251
Cdd:pfam00151 158 AHVAGEAGRRTNGK--LGRITGLDPAGPYFQGTPEEVRLDPGDADFVDAIHTDTRPIPGLGFGISQPVGHVDFFPNGGSE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   252 QPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSNlQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRR 331
Cdd:pfam00151 236 QPGCQKNILSQIIDIDGIWEGTQFVACNHLRSVHYYIDSLLNPR-GFPGYPCSSYDAFSQNKCLPCPKGGCPQMGHYADK 314
                         330       340
                  ....*....|....*....|..
gi 56961643   332 DRPRKSK---TLFLITRAQSPF 350
Cdd:pfam00151 315 FPGKTSKleqTFYLNTGSSSPF 336
lipo_lipase TIGR03230
lipoprotein lipase; Members of this protein family are lipoprotein lipase (EC 3.1.1.34), a ...
56-488 1.47e-144

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: 421.61  E-value: 1.47e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    56 DESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLLETWIWKIVGALKSRQSQPvNVGLVDWISLAYQHYAIAV 135
Cdd:TIGR03230  15 EEPDDDTCYIVPGQPDSIADCNFNHETKTFIVIHGWTVTGMFESWVPKLVAALYEREPSA-NVIVVDWLSRAQQHYPTSA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   136 RNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMggKRKIGRITGLDPAGPMFEGTSPNERLSPDDA 215
Cdd:TIGR03230  94 AYTKLVGKDVAKFVNWMQEEFNYPWDNVHLLGYSLGAHVAGIAGSLT--KHKVNRITGLDPAGPTFEYADAPSTLSPDDA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   216 NFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSN 295
Cdd:TIGR03230 172 DFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDIQETLLVIAEKGLGNMDQLVKCSHERSIHLFIDSLLNEE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   296 LQNTGFQCSNMDSFSQGLCLNCKKGRCNSLGYDIRRDRPRKSKTLFLITRAQSPFKVYHYQFKIQFI--NQMEKPIEPtF 373
Cdd:TIGR03230 252 NPSMAYRCSSKEAFNKGLCLSCRKNRCNKLGYEINKVRTKRSSKMYLKTREMMPYKVFHYQVKVHFFgkTSLSHTDQP-M 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   374 TMTLLGTKEEIKKIPITLGEgITSNKTYSLLITLDKDIGELIMLKFKWENSAV--WANVWNTvqtimlwdtephyAGLIL 451
Cdd:TIGR03230 331 KISLYGTHGEKENIPFTLPE-VSTNKTYSFLITTDVDIGELLMVKLKWEKDTYisWSDWWSS-------------PGFHI 396
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 56961643   452 KTIWVKAGETQQRMTFCPDNVDDLQLHPTQEK-VFVKC 488
Cdd:TIGR03230 397 RKLRIKSGETQSKVIFSAKEGEFSYLQRGGEAaVFVKC 434
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
47-346 2.20e-113

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 [Multi-domain]  Cd Length: 275  Bit Score: 335.75  E-value: 2.20e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643  47 PEIRFLLFKDESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLlETWIWKIVGALKSRQSqpVNVGLVDWISL 126
Cdd:cd00707   1 IDVRFLLYTRENPNCPQLLFADDPSSLKNSNFNPSRPTRFIIHGWTSSGE-ESWISDLRKAYLSRGD--YNVIVVDWGRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 127 AYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMGGkrKIGRITGLDPAGPMFEGTSP 206
Cdd:cd00707  78 ANPNYPQAVNNTRVVGAELAKFLDFLVDNTGLSLENVHLIGHSLGAHVAGFAGKRLNG--KLGRITGLDPAGPLFSGADP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 207 NERLSPDDANFVDAIHTFTREhmglsVGIKQPIAHYDFYPNGGSFQPGCHFlelykhiaehgLNAITQTIKCAHERSVHL 286
Cdd:cd00707 156 EDRLDPSDAQFVDVIHTDGGL-----LGFSQPIGHADFYPNGGRDQPGCPK-----------DILSSDFVACSHQRAVHY 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56961643 287 FIDSL-QHSNLqnTGFQCSNMDSFSQGLCLNCKKGrCNSLGYDIrrDRPRKSKTLFLITRA 346
Cdd:cd00707 220 FAESIlSPCGF--VAYPCSSYDEFLAGKCFPCGSG-CVRMGYHA--DRFRREGKFYLKTNA 275
PLAT_LPL cd01758
PLAT/ LH2 domain present in lipoprotein lipase (LPL). LPL is a key enzyme in catabolism of ...
353-488 8.34e-64

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: 203.39  E-value: 8.34e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 353 YHYQFKIQFINQMEKP-IEPTFTMTLLGTKEEIKKIPITLGEGITSNKTYSLLITLDKDIGELIMLKFKWENSAVWANVW 431
Cdd:cd01758   1 FHYQLKIHFFNQTNRIeTDPTFTISLYGTLGESENLPLTLPEGITGNKTNSFLITTEKDIGDLLMLKLKWEGSSLWSNSW 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56961643 432 NTVQTIMLWDTEPHYAGLILKTIWVKAGETQQRMTFCPDNVDDLQLHPTQEKVFVKC 488
Cdd:cd01758  81 WTVQTIIPWSGWWRGSGLTIRKIRVKAGETQKKMTFCAEDPESSLLRPGQEKVFVKC 137
PLAT_lipase cd01755
PLAT/ LH2 domain present in connection with a lipase domain. This family contains two major ...
353-488 2.34e-38

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: 135.89  E-value: 2.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 353 YHYQFKIQFINQMEKPIEPTFTMTLLGTKEEIKKIPITLGEgITSNKTYSLLITLDKDIGELIMLKFKWENSAVWANVWN 432
Cdd:cd01755   1 WHYQVKVHLSGKKNLEVDGTFTVSLYGTKGETEQLPIVLGE-LKPNKTYSFLIDTEVDIGDLLKVKFKWENNVINSNSGE 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 56961643 433 TvqtimlwdtephYAGLILKTIWVKAGETQQRMTFCPDNVDDlqlHPTQEKVFVKC 488
Cdd:cd01755  80 T------------LPKLGARKIRVKSGETQKKFTFCSQDTVR---ELEVLQTLVKC 120
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
136-284 5.91e-28

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: 108.74  E-value: 5.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 136 RNTRVVGQEVAALLLWLEESMK--FSRSKVHLIGYSLGAHVSGFAGSSM--GGKRKIGRITGLDPAGPMFEGTSPnERLS 211
Cdd:cd00741   1 KGFYKAARSLANLVLPLLKSALaqYPDYKIHVTGHSLGGALAGLAGLDLrgRGLGRLVRVYTFGPPRVGNAAFAE-DRLD 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56961643 212 PDDANFVDAIHTFTREHMGLS-VGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSV 284
Cdd:cd00741  80 PSDALFVDRIVNDNDIVPRLPpGGEGYPHGGAEFYINGGKSQPGCCKNVLEAVDIDFGNIGLSGNGLCDHLRYF 153
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
355-486 4.32e-13

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: 65.53  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643   355 YQFKIQFINQMEKPIEPTFTMTLLGTKEEIKKIPITLGEG-ITSNKTYSLLITLDKDIGELIMLKFKWENSavwanvwnt 433
Cdd:pfam01477   1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPdFERGAEDSFEIDTDWDVGAILKINLHWDNN--------- 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56961643   434 vqtimlwdtePHYAGLILKTIWV-KAGETQQRMTFCP-DNVDDLQlHPTQEKVFV 486
Cdd:pfam01477  72 ----------GLSDEWFLKSITVeVPGETGGKYTFPCnSWVYGSK-KYKETRVFF 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
353-468 2.52e-12

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 63.04  E-value: 2.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643    353 YHYQFKIQFINQMEKPIEPTFTMTLLGTKEEIKK-IPITLGEGITS-NKTYSLLITLDKDIGELIMLKFKWENSAVwanv 430
Cdd:smart00308   1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKEsKLDYLFKGIFArGSTYEFTFDVDEDFGELGAVKIKNEHRHP---- 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 56961643    431 wntvqtimlwdtephyaGLILKTIWVKAGETQQRMTFC 468
Cdd:smart00308  77 -----------------EWFLKSITVKDLPTGGKYHFP 97
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
353-468 4.04e-12

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: 62.74  E-value: 4.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643 353 YHYQFKIQFINQMEKPIEPTFTMTLLGTKEEIKKIPITLGEG-ITSNKTYSLLITLDKDIGELIMLKFKWENSAVWanvw 431
Cdd:cd00113   1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGPGsFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLS---- 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 56961643 432 ntvqtimlwdtephyAGLILKTIWVKAGETQQRMTFC 468
Cdd:cd00113  77 ---------------DGWYCESITVQALGTKKVYTFP 98
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
82-199 3.72e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.12  E-value: 3.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56961643  82 HPLVMIiHGWSVDGllETWiWKIVGALKSRQSQPVNVGLvDWISLAYQHYAiavrntRVVGQEVAALLlwleesMKFSRS 161
Cdd:COG1075   6 YPVVLV-HGLGGSA--ASW-APLAPRLRAAGYPVYALNY-PSTNGSIEDSA------EQLAAFVDAVL------AATGAE 68
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 56961643 162 KVHLIGYSLGAHVSGFAGSSMGGKRKIGRITGLdpAGP 199
Cdd:COG1075  69 KVDLVGHSMGGLVARYYLKRLGGAAKVARVVTL--GTP 104
 
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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