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Conserved domains on  [gi|544186006|ref|NP_001269652|]
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lipid droplet-associated hydrolase isoform e [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
43-162 1.61e-46

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 pfam10230:

Pssm-ID: 473884  Cd Length: 261  Bit Score: 152.45  E-value: 1.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006   43 PKLLIFIIPGNPGFSAFYVPFAKALYSLTNRRFPVWTISHAGHALAPKDkkilttsedsNAQEIKDIYGLNGQIEHKLAF 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN----------DAKENGRVFSLQDQIEHKIDF 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 544186006  123 LRTHVP----KDMKLVLIGHSIGSYFTLQMLKRVPELP-----LMLPTL 162
Cdd:pfam10230  71 IRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGiikcvLLFPTI 119
 
Name Accession Description Interval E-value
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
43-162 1.61e-46

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: 152.45  E-value: 1.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006   43 PKLLIFIIPGNPGFSAFYVPFAKALYSLTNRRFPVWTISHAGHALAPKDkkilttsedsNAQEIKDIYGLNGQIEHKLAF 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN----------DAKENGRVFSLQDQIEHKIDF 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 544186006  123 LRTHVP----KDMKLVLIGHSIGSYFTLQMLKRVPELP-----LMLPTL 162
Cdd:pfam10230  71 IRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGiikcvLLFPTI 119
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-154 3.81e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.99  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006  41 KRPKLLIFIIPGNPGFSAFYVPFAKALyslTNRRFPVWTISHAGHALAPKDKKILTTSEDSnaqeIKDIYGLngqiehkL 120
Cdd:COG2267   25 GSPRGTVVLVHGLGEHSGRYAELAEAL---AAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY----VDDLRAA-------L 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 544186006 121 AFLRTHVPKdmKLVLIGHSIGSYFTLQMLKRVPE 154
Cdd:COG2267   91 DALRARPGL--PVVLLGHSMGGLIALLYAARYPD 122
 
Name Accession Description Interval E-value
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
43-162 1.61e-46

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: 152.45  E-value: 1.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006   43 PKLLIFIIPGNPGFSAFYVPFAKALYSLTNRRFPVWTISHAGHALAPKDkkilttsedsNAQEIKDIYGLNGQIEHKLAF 122
Cdd:pfam10230   1 PRPLIVVIPGNPGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRN----------DAKENGRVFSLQDQIEHKIDF 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 544186006  123 LRTHVP----KDMKLVLIGHSIGSYFTLQMLKRVPELP-----LMLPTL 162
Cdd:pfam10230  71 IRAFLPansdKDVKLILIGHSIGAYIALEVLKRLSERGiikcvLLFPTI 119
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
41-154 3.81e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.99  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006  41 KRPKLLIFIIPGNPGFSAFYVPFAKALyslTNRRFPVWTISHAGHALAPKDKKILTTSEDSnaqeIKDIYGLngqiehkL 120
Cdd:COG2267   25 GSPRGTVVLVHGLGEHSGRYAELAEAL---AAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY----VDDLRAA-------L 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 544186006 121 AFLRTHVPKdmKLVLIGHSIGSYFTLQMLKRVPE 154
Cdd:COG2267   91 DALRARPGL--PVVLLGHSMGGLIALLYAARYPD 122
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
46-154 1.13e-03

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: 38.25  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006   46 LIFIIPGNPGFSAFYVPFAKALYSltnRRFPVWTISHAGHAlapKDKKILTTSEDSNAQEIKDIYglngqiehklaFLRT 125
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALAR---DGFRVIALDLRGFG---KSSRPKAQDDYRTDDLAEDLE-----------YILE 64
                          90       100
                  ....*....|....*....|....*....
gi 544186006  126 HVPKDmKLVLIGHSIGSYFTLQMLKRVPE 154
Cdd:pfam00561  65 ALGLE-KVNLVGHSMGGLIALAYAAKYPD 92
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
47-155 2.40e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 36.90  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186006  47 IFIIPGNPGFSAFYVPFAKALysltNRRFPVWTISHAGHALAPKDKKILTTsedsnAQEIKDIyglngqiehkLAFLRtH 126
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPAL----AAGYRVIAPDLRGHGRSDKPAGGYTL-----DDLADDL----------AALLD-A 85
                         90       100
                 ....*....|....*....|....*....
gi 544186006 127 VPKDmKLVLIGHSIGSYFTLQMLKRVPEL 155
Cdd:COG0596   86 LGLE-RVVLVGHSMGGMVALELAARHPER 113
 
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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