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Conserved domains on  [gi|24656084|ref|NP_725942|]
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Hormone-sensitive lipase, isoform C [Drosophila melanogaster]

Protein Classification

HSL_N and Abhydrolase domain-containing protein( domain architecture ID 12070005)

protein containing domains HSL_N, Abhydrolase, and Aes

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 ...
51-376 3.63e-164

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: 479.83  E-value: 3.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084    51 YGTLYAACQDHAAFFARDHTEFGQRLHAAHIAWQDFIVLANRLVQQIDAFAHEYDFDEQTPGNGYRSFIYVTNACIAHGI 130
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   131 SICQQLTATRSTIFFRKKFYMKEVEACSQLLSSLCTCLQYLLILRQWSaSTGDLFACGNHTAEQLFELGDTINQYCFYGR 210
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   211 CLGFQYGDSIRGVLRFLGISMASYSESYYSQegDGPIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 290
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   291 ESEMMHKLPSIVGSSIKVNRLIELPAEPLKLPrrknfkasdnlssdvnqNQGDGDFVEIPVPTAHLGPGlPVSVRLLSAR 370
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-----------------LSDDGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 24656084   371 RRSGML 376
Cdd:pfam06350 301 LREGQD 306
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
395-539 8.55e-34

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam07859:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 208  Bit Score: 128.87  E-value: 8.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   395 LFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAERVVCAGDSA 474
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24656084   475 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 539
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
767-838 1.98e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 49.49  E-value: 1.98e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656084 767 DPFLSPYWASdewLSQLPETKILTLNMDPCLDDCVMFAKKLKRLGRQVDLEILEGLPHGFLNFTML--SNEAME 838
Cdd:COG0657 126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLpeARAALA 196
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
51-376 3.63e-164

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: 479.83  E-value: 3.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084    51 YGTLYAACQDHAAFFARDHTEFGQRLHAAHIAWQDFIVLANRLVQQIDAFAHEYDFDEQTPGNGYRSFIYVTNACIAHGI 130
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   131 SICQQLTATRSTIFFRKKFYMKEVEACSQLLSSLCTCLQYLLILRQWSaSTGDLFACGNHTAEQLFELGDTINQYCFYGR 210
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   211 CLGFQYGDSIRGVLRFLGISMASYSESYYSQegDGPIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 290
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   291 ESEMMHKLPSIVGSSIKVNRLIELPAEPLKLPrrknfkasdnlssdvnqNQGDGDFVEIPVPTAHLGPGlPVSVRLLSAR 370
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-----------------LSDDGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 24656084   371 RRSGML 376
Cdd:pfam06350 301 LREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
395-539 8.55e-34

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: 128.87  E-value: 8.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   395 LFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAERVVCAGDSA 474
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24656084   475 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 539
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
386-514 3.22e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 121.52  E-value: 3.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084 386 KPIPPSPSILFhCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAE 465
Cdd:COG0657   8 GAKGPLPVVVY-FHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24656084 466 RVVCAGDSAGANLSIGVALKCIEQGVRVPDGLFLAYcPtLVSFVPSPAR 514
Cdd:COG0657  87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIY-P-VLDLTASPLR 133
PRK10162 PRK10162
acetyl esterase;
387-484 3.02e-20

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 92.47  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084  387 PIPPSPSILFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAER 466
Cdd:PRK10162  76 PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155
                         90
                 ....*....|....*...
gi 24656084  467 VVCAGDSAGANLSIGVAL 484
Cdd:PRK10162 156 IGFAGDSAGAMLALASAL 173
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
767-838 1.98e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 49.49  E-value: 1.98e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656084 767 DPFLSPYWASdewLSQLPETKILTLNMDPCLDDCVMFAKKLKRLGRQVDLEILEGLPHGFLNFTML--SNEAME 838
Cdd:COG0657 126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLpeARAALA 196
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
51-376 3.63e-164

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: 479.83  E-value: 3.63e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084    51 YGTLYAACQDHAAFFARDHTEFGQRLHAAHIAWQDFIVLANRLVQQIDAFAHEYDFDEQTPGNGYRSFIYVTNACIAHGI 130
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   131 SICQQLTATRSTIFFRKKFYMKEVEACSQLLSSLCTCLQYLLILRQWSaSTGDLFACGNHTAEQLFELGDTINQYCFYGR 210
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   211 CLGFQYGDSIRGVLRFLGISMASYSESYYSQegDGPIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 290
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   291 ESEMMHKLPSIVGSSIKVNRLIELPAEPLKLPrrknfkasdnlssdvnqNQGDGDFVEIPVPTAHLGPGlPVSVRLLSAR 370
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLP-----------------LSDDGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 24656084   371 RRSGML 376
Cdd:pfam06350 301 LREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
395-539 8.55e-34

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: 128.87  E-value: 8.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   395 LFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAERVVCAGDSA 474
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24656084   475 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 539
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
386-514 3.22e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 121.52  E-value: 3.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084 386 KPIPPSPSILFhCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAE 465
Cdd:COG0657   8 GAKGPLPVVVY-FHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24656084 466 RVVCAGDSAGANLSIGVALKCIEQGVRVPDGLFLAYcPtLVSFVPSPAR 514
Cdd:COG0657  87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIY-P-VLDLTASPLR 133
PRK10162 PRK10162
acetyl esterase;
387-484 3.02e-20

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 92.47  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084  387 PIPPSPSILFHCHGGGFVAQSSKSHELYLRDWAVALDCPILSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELLGTTAER 466
Cdd:PRK10162  76 PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSR 155
                         90
                 ....*....|....*...
gi 24656084  467 VVCAGDSAGANLSIGVAL 484
Cdd:PRK10162 156 IGFAGDSAGAMLALASAL 173
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
390-479 2.04e-08

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: 55.65  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   390 PSPsILFHCHGGGFVAQSSKS---------HELYLRDWAVAldcpilSVDYSLAPEAPFPRALQEVYYAYCWLLNNTELL 460
Cdd:pfam20434  12 PYP-VVIWIHGGGWNSGDKEAdmgfmtntvKALLKAGYAVA------SINYRLSTDAKFPAQIQDVKAAIRFLRANAAKY 84
                          90
                  ....*....|....*....
gi 24656084   461 GTTAERVVCAGDSAGANLS 479
Cdd:pfam20434  85 GIDTNKIALMGFSAGGHLA 103
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
767-838 1.98e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 49.49  E-value: 1.98e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24656084 767 DPFLSPYWASdewLSQLPETKILTLNMDPCLDDCVMFAKKLKRLGRQVDLEILEGLPHGFLNFTML--SNEAME 838
Cdd:COG0657 126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLpeARAALA 196
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
385-486 1.47e-03

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: 41.74  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24656084   385 HKPIPPSPSILFHCHGGGFVAQSSKSHELYLRDWAVAL-DCPILSVDYSLAPEAP----FPRALQEVYYAYCWLlnnTEL 459
Cdd:pfam10340 115 ETFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFpDMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYL---TLT 191
                          90       100
                  ....*....|....*....|....*..
gi 24656084   460 LGTTaeRVVCAGDSAGANLSIGVALKC 486
Cdd:pfam10340 192 KGCK--NVTLMGDSAGGNLVLNILLYL 216
 
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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