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Conserved domains on  [gi|30689883|ref|NP_850428|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

lipase family alpha/beta hydrolase( domain architecture ID 18498059)

lipase family alpha/beta hydrolase similar to triacylglycerol lipase that catalyzes the hydrolysis of triacylglycerol

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
214-306 4.66e-08

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 50.98  E-value: 4.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883 214 LLVPGLFSNhgPLYFVDTKTKFSKMGLACHIAKIHS-ESSVEKNAREIKEYIEELCWGS-NKRVLLLGHSKGGIDAAAAL 291
Cdd:COG1075   9 VLVHGLGGS--AASWAPLAPRLRAAGYPVYALNYPStNGSIEDSAEQLAAFVDAVLAATgAEKVDLVGHSMGGLVARYYL 86
                        90
                ....*....|....*
gi 30689883 292 SLYwpELKDKVAGLV 306
Cdd:COG1075  87 KRL--GGAAKVARVV 99
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
272-356 1.03e-03

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 pfam07819:

Pssm-ID: 473884  Cd Length: 233  Bit Score: 40.81  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883   272 NKRVLLLGHSKGGIDAAAALSL--YWPelkDKVAGLVLAQSPYGGSPIATDilregqlGDYVNLRKMME-ILISKVIKGD 348
Cdd:pfam07819  90 PTSVILIGHSMGGIVARAALTLpnYIP---QSVNTIITLSSPHAKPPLTFD-------GDILKFYERLNaFWRKLYNDGD 159

                  ....*...
gi 30689883   349 IQALEDLT 356
Cdd:pfam07819 160 SNNLSNVL 167
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
214-306 4.66e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 50.98  E-value: 4.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883 214 LLVPGLFSNhgPLYFVDTKTKFSKMGLACHIAKIHS-ESSVEKNAREIKEYIEELCWGS-NKRVLLLGHSKGGIDAAAAL 291
Cdd:COG1075   9 VLVHGLGGS--AASWAPLAPRLRAAGYPVYALNYPStNGSIEDSAEQLAAFVDAVLAATgAEKVDLVGHSMGGLVARYYL 86
                        90
                ....*....|....*
gi 30689883 292 SLYwpELKDKVAGLV 306
Cdd:COG1075  87 KRL--GGAAKVARVV 99
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
272-356 1.03e-03

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 40.81  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883   272 NKRVLLLGHSKGGIDAAAALSL--YWPelkDKVAGLVLAQSPYGGSPIATDilregqlGDYVNLRKMME-ILISKVIKGD 348
Cdd:pfam07819  90 PTSVILIGHSMGGIVARAALTLpnYIP---QSVNTIITLSSPHAKPPLTFD-------GDILKFYERLNaFWRKLYNDGD 159

                  ....*...
gi 30689883   349 IQALEDLT 356
Cdd:pfam07819 160 SNNLSNVL 167
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
214-306 4.66e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 50.98  E-value: 4.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883 214 LLVPGLFSNhgPLYFVDTKTKFSKMGLACHIAKIHS-ESSVEKNAREIKEYIEELCWGS-NKRVLLLGHSKGGIDAAAAL 291
Cdd:COG1075   9 VLVHGLGGS--AASWAPLAPRLRAAGYPVYALNYPStNGSIEDSAEQLAAFVDAVLAATgAEKVDLVGHSMGGLVARYYL 86
                        90
                ....*....|....*
gi 30689883 292 SLYwpELKDKVAGLV 306
Cdd:COG1075  87 KRL--GGAAKVARVV 99
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
272-356 1.03e-03

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 40.81  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689883   272 NKRVLLLGHSKGGIDAAAALSL--YWPelkDKVAGLVLAQSPYGGSPIATDilregqlGDYVNLRKMME-ILISKVIKGD 348
Cdd:pfam07819  90 PTSVILIGHSMGGIVARAALTLpnYIP---QSVNTIITLSSPHAKPPLTFD-------GDILKFYERLNaFWRKLYNDGD 159

                  ....*...
gi 30689883   349 IQALEDLT 356
Cdd:pfam07819 160 SNNLSNVL 167
 
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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