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Conserved domains on  [gi|1401585379|ref|NP_001351190|]
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lipid droplet-associated hydrolase isoform 1 [Mus musculus]

Protein Classification

lipid droplet-associated hydrolase family protein( domain architecture ID 10562972)

lipid droplet-associated hydrolase (LDAH) family protein is a lipid hydrolase associated with lipid droplets; similar to Saccharomyces cerevisiae lipid droplet-associated triacylglycerol lipase that shows both triacylglycerol (TAG) lipase and ester hydrolase activities

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
43-304 3.81e-112

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


:

Pssm-ID: 370901  Cd Length: 261  Bit Score: 325.79  E-value: 3.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  43 PKQLIFIIPGNPGYSAFYVPFAKALYTLMKSRFPVWIISHAGFSVTPKDkkvlaapqeesNAQKIEDVYGLNGQIEHKIA 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN-----------DAKENGRVFSLQDQIEHKID 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 123 FLRAHVP----KDVKLILIGHSVGTYMTLHVMKRVPELPVAHAFLLFPTIERMSESPNGKFATPFLCQFRYLLYATSYLL 198
Cdd:pfam10230  70 FIRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGIIKCVLLFPTIEDMARSPNGRILTRLLCYIPFLALVAGFLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 199 --FKPCPEVIKSFIIQKLMGQMNI---KLELPLTDILQPFCLANAAYLGSQEMVQIVKRDD-DIIKEFLPKLKFYYGKTD 272
Cdd:pfam10230 150 rvFKLLPESVKSLLIRKVMGGMSSpphAVQTTLKFLLNPHCVRNALHMARDEMREVREDDDeDFIKANQERLWFYYGTTD 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1401585379 273 GWCPVKYYEDMKKDFPEGNIYLCEKGIPHAFV 304
Cdd:pfam10230 230 HWVPVSTRDELKELYPDGDLVVDEDGIPHAFV 261
 
Name Accession Description Interval E-value
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
43-304 3.81e-112

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 325.79  E-value: 3.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  43 PKQLIFIIPGNPGYSAFYVPFAKALYTLMKSRFPVWIISHAGFSVTPKDkkvlaapqeesNAQKIEDVYGLNGQIEHKIA 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN-----------DAKENGRVFSLQDQIEHKID 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 123 FLRAHVP----KDVKLILIGHSVGTYMTLHVMKRVPELPVAHAFLLFPTIERMSESPNGKFATPFLCQFRYLLYATSYLL 198
Cdd:pfam10230  70 FIRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGIIKCVLLFPTIEDMARSPNGRILTRLLCYIPFLALVAGFLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 199 --FKPCPEVIKSFIIQKLMGQMNI---KLELPLTDILQPFCLANAAYLGSQEMVQIVKRDD-DIIKEFLPKLKFYYGKTD 272
Cdd:pfam10230 150 rvFKLLPESVKSLLIRKVMGGMSSpphAVQTTLKFLLNPHCVRNALHMARDEMREVREDDDeDFIKANQERLWFYYGTTD 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1401585379 273 GWCPVKYYEDMKKDFPEGNIYLCEKGIPHAFV 304
Cdd:pfam10230 230 HWVPVSTRDELKELYPDGDLVVDEDGIPHAFV 261
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-164 1.85e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 41.91  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  41 SKPKQLIFIIPGNPGYSAFYVPFAKALYtlmKSRFPVWIISHAGFSVTPKDKKVLAAPQEEsnaqkIEDVYGLngqiehk 120
Cdd:COG2267    25 GSPRGTVVLVHGLGEHSGRYAELAEALA---AAGYAVLAFDLRGHGRSDGPRGHVDSFDDY-----VDDLRAA------- 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1401585379 121 IAFLRAHvpKDVKLILIGHSVGTYMTLHVMKRVPElPVAHAFLL 164
Cdd:COG2267    90 LDALRAR--PGLPVVLLGHSMGGLIALLYAARYPD-RVAGLVLL 130
 
Name Accession Description Interval E-value
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
43-304 3.81e-112

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 325.79  E-value: 3.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  43 PKQLIFIIPGNPGYSAFYVPFAKALYTLMKSRFPVWIISHAGFSVTPKDkkvlaapqeesNAQKIEDVYGLNGQIEHKIA 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN-----------DAKENGRVFSLQDQIEHKID 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 123 FLRAHVP----KDVKLILIGHSVGTYMTLHVMKRVPELPVAHAFLLFPTIERMSESPNGKFATPFLCQFRYLLYATSYLL 198
Cdd:pfam10230  70 FIRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGIIKCVLLFPTIEDMARSPNGRILTRLLCYIPFLALVAGFLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379 199 --FKPCPEVIKSFIIQKLMGQMNI---KLELPLTDILQPFCLANAAYLGSQEMVQIVKRDD-DIIKEFLPKLKFYYGKTD 272
Cdd:pfam10230 150 rvFKLLPESVKSLLIRKVMGGMSSpphAVQTTLKFLLNPHCVRNALHMARDEMREVREDDDeDFIKANQERLWFYYGTTD 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1401585379 273 GWCPVKYYEDMKKDFPEGNIYLCEKGIPHAFV 304
Cdd:pfam10230 230 HWVPVSTRDELKELYPDGDLVVDEDGIPHAFV 261
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-164 1.85e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 41.91  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  41 SKPKQLIFIIPGNPGYSAFYVPFAKALYtlmKSRFPVWIISHAGFSVTPKDKKVLAAPQEEsnaqkIEDVYGLngqiehk 120
Cdd:COG2267    25 GSPRGTVVLVHGLGEHSGRYAELAEALA---AAGYAVLAFDLRGHGRSDGPRGHVDSFDDY-----VDDLRAA------- 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1401585379 121 IAFLRAHvpKDVKLILIGHSVGTYMTLHVMKRVPElPVAHAFLL 164
Cdd:COG2267    90 LDALRAR--PGLPVVLLGHSMGGLIALLYAARYPD-RVAGLVLL 130
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
46-164 4.02e-04

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 41.34  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585379  46 LIFIIPGNPGYSAFYVPFAKALYtlmKSRFPVWIISHAGFSvtpkdkkvlaapqeESNAQKIEDVYGLNGQIEHkIAFLR 125
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALA---RDGFRVIALDLRGFG--------------KSSRPKAQDDYRTDDLAED-LEYIL 63
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1401585379 126 AHVPKDvKLILIGHSVGTYMTLHVMKRVPElPVAHAFLL 164
Cdd:pfam00561  64 EALGLE-KVNLVGHSMGGLIALAYAAKYPD-RVKALVLL 100
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
121-175 5.37e-03

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 37.45  E-value: 5.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1401585379 121 IAFLRAHVPKdvKLILIGHSVGTYMTLHVMKRVPElpVAHAFLLFPTIERMSESP 175
Cdd:COG2945    87 LDWLRAQNPL--PLWLAGFSFGAYVALQLAMRLPE--VEGLILVAPPVNRYDFSF 137
 
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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