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Conserved domains on  [gi|564326511|ref|XP_006228456|]
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hormone-sensitive lipase isoform X4 [Rattus norvegicus]

Protein Classification

hormone-sensitive lipase( domain architecture ID 10533829)

hormone-sensitive lipase displays broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters; belongs to the alpha/beta hydrolase superfamily

EC:  3.1.1.-
Gene Symbol:  LIPE
Gene Ontology:  GO:0016787|GO:0016298

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314 3.80e-157

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


:

Pssm-ID: 461882  Cd Length: 306  Bit Score: 458.26  E-value: 3.80e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511    6 MTQSLVALAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511   86 LLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDeGLSADFLQDYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564326511  246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 8.52e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 8.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511 334 RPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGST 413
Cdd:COG0657    5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564326511 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314 3.80e-157

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 458.26  E-value: 3.80e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511    6 MTQSLVALAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511   86 LLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDeGLSADFLQDYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564326511  246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 8.52e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 8.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511 334 RPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGST 413
Cdd:COG0657    5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564326511 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
345-493 9.31e-36

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 134.26  E-value: 9.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  345 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGSTGERICLAGDSA 424
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564326511  425 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTETEDH 493
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
334-434 1.14e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 90.55  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511 334 RPQqaPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGST 413
Cdd:PRK10162  75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
                         90       100
                 ....*....|....*....|.
gi 564326511 414 GERICLAGDSAGGNLCITVSL 434
Cdd:PRK10162 153 MSRIGFAGDSAGAMLALASAL 173
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314 3.80e-157

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 458.26  E-value: 3.80e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511    6 MTQSLVALAEDNMAFFSSqGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAH 85
Cdd:pfam06350   1 VFETLRSLCEDNAAYFEG-DSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511   86 LLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDeGLSADFLQDYVTLHKGCFY 165
Cdd:pfam06350  80 IIKLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWSEPGDLFPSED-HSSEELLREYETINQYCFY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  166 GRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNIT 245
Cdd:pfam06350 159 GRCLGFQFCPSLRPILKTISISMASFSEGYYNNGGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564326511  246 EIEVLSSLANMASTTVRVSRLLSLPPEAFEMPlTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQD 314
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-LSDDGEMVTIPPPSAHIGPGPVHVRLISYELREGQD 306
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
334-464 8.52e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 137.31  E-value: 8.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511 334 RPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGST 413
Cdd:COG0657    5 RPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGID 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564326511 414 GERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqsSASPSR 464
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDL--TASPLR 133
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
345-493 9.31e-36

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 134.26  E-value: 9.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  345 VVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGSTGERICLAGDSA 424
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564326511  425 GGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLqSSASPSRLLSLM--DPLLPLSVLSKCVSAYSGTETEDH 493
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWFWRLYLPGADRDD 150
PRK10162 PRK10162
acetyl esterase;
334-434 1.14e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 90.55  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511 334 RPQqaPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGST 413
Cdd:PRK10162  75 YPQ--PDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGIN 152
                         90       100
                 ....*....|....*....|.
gi 564326511 414 GERICLAGDSAGGNLCITVSL 434
Cdd:PRK10162 153 MSRIGFAGDSAGAMLALASAL 173
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
335-428 2.43e-13

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 69.90  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  335 PQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQEL---GVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLG 411
Cdd:pfam20434   6 PKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALlkaGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAAKYG 85
                          90
                  ....*....|....*..
gi 564326511  412 STGERICLAGDSAGGNL 428
Cdd:pfam20434  86 IDTNKIALMGFSAGGHL 102
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
339-428 7.98e-04

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 42.52  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326511  339 PRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELG-VPIISIDYSLAPEAP----FPRALEECFFAYCWAVkhcELLGST 413
Cdd:pfam10340 119 PKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPdMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYLT---LTKGCK 195
                          90
                  ....*....|....*
gi 564326511  414 geRICLAGDSAGGNL 428
Cdd:pfam10340 196 --NVTLMGDSAGGNL 208
 
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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