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Conserved domains on  [gi|736413614|ref|WP_034436086|]
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MULTISPECIES: triacylglycerol lipase [Acinetobacter]

Protein Classification

esterase/lipase family protein( domain architecture ID 10787203)

esterase/lipase family protein is an alpha/beta hydrolase, such as triacylglycerol lipase that catalyzes the hydrolysis of a triacylglycerol to form the corresponding diacylglycerol and a carboxylate

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787|GO:0016042

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 ...
377-521 4.94e-16

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


:

Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 74.10  E-value: 4.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614 377 YNPDKKVLVLIHGLASSPEAWIRLTNDIMgdpvlRENFQVWQVFY-STNMPILESRFQINALVQQgfaqVANNAPAKKdA 455
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLR-----AAGYPVYALNYpSTNGSIEDSAEQLAAFVDA----VLAATGAEK-V 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736413614 456 VLVGHSMGGVIARLMVSQADitqdafklvqntriaqfkdnplfkarlqmrPIPNFTRAIFLATPHR 521
Cdd:COG1075   71 DLVGHSMGGLVARYYLKRLG------------------------------GAAKVARVVTLGTPHH 106
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
377-521 4.94e-16

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 74.10  E-value: 4.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614 377 YNPDKKVLVLIHGLASSPEAWIRLTNDIMgdpvlRENFQVWQVFY-STNMPILESRFQINALVQQgfaqVANNAPAKKdA 455
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLR-----AAGYPVYALNYpSTNGSIEDSAEQLAAFVDA----VLAATGAEK-V 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736413614 456 VLVGHSMGGVIARLMVSQADitqdafklvqntriaqfkdnplfkarlqmrPIPNFTRAIFLATPHR 521
Cdd:COG1075   71 DLVGHSMGGLVARYYLKRLG------------------------------GAAKVARVVTLGTPHH 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
382-545 1.33e-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: 44.03  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614  382 KVLVLIHGLASSPEAWIRLtndimGDPVLRENFQVWqVF------YSTNmPILESRFQINALVQQgFAQVANNAPAKKdA 455
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKL-----APALARDGFRVI-ALdlrgfgKSSR-PKAQDDYRTDDLAED-LEYILEALGLEK-V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614  456 VLVGHSMGGVIARLMVSQADI---------TQDAFKLVQNTRIAQFKDNPLFkARLQMRPIPNFTRAIFLATPHRGTEYA 526
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPDrvkalvllgALDPPHELDEADRFILALFPGF-FDGFVADFAPNPLGRLVAKLLALLLLR 150
                         170
                  ....*....|....*....
gi 736413614  527 DRWHTKLARKIIRIPGAFL 545
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDY 169
 
Name Accession Description Interval E-value
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
377-521 4.94e-16

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 74.10  E-value: 4.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614 377 YNPDKKVLVLIHGLASSPEAWIRLTNDIMgdpvlRENFQVWQVFY-STNMPILESRFQINALVQQgfaqVANNAPAKKdA 455
Cdd:COG1075    1 YAATRYPVVLVHGLGGSAASWAPLAPRLR-----AAGYPVYALNYpSTNGSIEDSAEQLAAFVDA----VLAATGAEK-V 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736413614 456 VLVGHSMGGVIARLMVSQADitqdafklvqntriaqfkdnplfkarlqmrPIPNFTRAIFLATPHR 521
Cdd:COG1075   71 DLVGHSMGGLVARYYLKRLG------------------------------GAAKVARVVTLGTPHH 106
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
377-474 3.65e-06

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: 48.46  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614 377 YNPDKKVLVLIHGLASSPEAWIRLTndimgdPVLRENFQVWQV----FYSTNMPilESRFQINALVQQgFAQVANNAPAK 452
Cdd:COG0596   19 AGPDGPPVVLLHGLPGSSYEWRPLI------PALAAGYRVIAPdlrgHGRSDKP--AGGYTLDDLADD-LAALLDALGLE 89
                         90       100
                 ....*....|....*....|..
gi 736413614 453 KdAVLVGHSMGGVIARLMVSQA 474
Cdd:COG0596   90 R-VVLVGHSMGGMVALELAARH 110
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
382-545 1.33e-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: 44.03  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614  382 KVLVLIHGLASSPEAWIRLtndimGDPVLRENFQVWqVF------YSTNmPILESRFQINALVQQgFAQVANNAPAKKdA 455
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKL-----APALARDGFRVI-ALdlrgfgKSSR-PKAQDDYRTDDLAED-LEYILEALGLEK-V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614  456 VLVGHSMGGVIARLMVSQADI---------TQDAFKLVQNTRIAQFKDNPLFkARLQMRPIPNFTRAIFLATPHRGTEYA 526
Cdd:pfam00561  72 NLVGHSMGGLIALAYAAKYPDrvkalvllgALDPPHELDEADRFILALFPGF-FDGFVADFAPNPLGRLVAKLLALLLLR 150
                         170
                  ....*....|....*....
gi 736413614  527 DRWHTKLARKIIRIPGAFL 545
Cdd:pfam00561 151 LRLLKALPLLNKRFPSGDY 169
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
384-531 5.93e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 41.69  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736413614  384 LVLIHGLASSPEAWIRLtndimgdpvLRENFQVWQV-FYSTNMPiLESRFQINALVQqgFAQVANNAPAKKDAVLVGHSM 462
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL---------LAAGVAVLAPdLPGHGSS-SPPPLDLADLAD--LAALLDELGAARPVVLVGHSL 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736413614  463 GGVIARLMVSQAD-----ITQDAFKLVQNTRIAQFKDNPLFKARLQMRPIPNFTRAIFLATPHRGTEYADRWHT 531
Cdd:pfam12697  69 GGAVALAAAAAALvvgvlVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALAR 142
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
446-476 1.64e-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: 40.43  E-value: 1.64e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 736413614  446 ANNAPAKKDAVLVGHSMGGVIARLMVSQADI 476
Cdd:pfam07819  84 ASGRPGPTSVILIGHSMGGIVARAALTLPNY 114
 
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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