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Conserved domains on  [gi|2232488649|gb|UPQ63661|]
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lecithin-cholesterol acyl transferase, partial [Orientallactaga balikunica]

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, ...
1-135 4.48e-48

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 pfam02450:

Pssm-ID: 451272  Cd Length: 383  Bit Score: 158.48  E-value: 4.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649   1 REEQRITTTSPWMFPSRQ-------VWPEDHVFISTPSFNYTGHDFQRFFTD-----------LHFEEGWYMWLQSRDLL 62
Cdd:pfam02450 183 RGLQRSFSSSPWMLPKGKyvlwsdvAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLD 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649  63 AGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHS---------FPYKDPVAALYEDGDDTV 109
Cdd:pfam02450 263 GGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGktsspilsrIDYEDPVGIVSGDGDGTV 342
                         170       180
                  ....*....|....*....|....*..
gi 2232488649 110 ATRSMELCGQWQG-RQSQPVHLLPLNG 135
Cdd:pfam02450 343 PKRSLELCKNWQGlPAGQNVTVHELKH 369
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
1-135 4.48e-48

Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved in extracellular metabolism of plasma lipoproteins, including cholesterol.


Pssm-ID: 396835  Cd Length: 383  Bit Score: 158.48  E-value: 4.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649   1 REEQRITTTSPWMFPSRQ-------VWPEDHVFISTPSFNYTGHDFQRFFTD-----------LHFEEGWYMWLQSRDLL 62
Cdd:pfam02450 183 RGLQRSFSSSPWMLPKGKyvlwsdvAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLD 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649  63 AGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHS---------FPYKDPVAALYEDGDDTV 109
Cdd:pfam02450 263 GGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGktsspilsrIDYEDPVGIVSGDGDGTV 342
                         170       180
                  ....*....|....*....|....*..
gi 2232488649 110 ATRSMELCGQWQG-RQSQPVHLLPLNG 135
Cdd:pfam02450 343 PKRSLELCKNWQGlPAGQNVTVHELKH 369
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
58-88 5.56e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 44.36  E-value: 5.56e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2232488649  58 SRDLLAGLP-APGVEVYCLYGVGLPTPRTYIY 88
Cdd:PLN02517  476 SNPLETKLPnAPEMEIYSLYGVGIPTERSYVY 507
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
1-135 4.48e-48

Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved in extracellular metabolism of plasma lipoproteins, including cholesterol.


Pssm-ID: 396835  Cd Length: 383  Bit Score: 158.48  E-value: 4.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649   1 REEQRITTTSPWMFPSRQ-------VWPEDHVFISTPSFNYTGHDFQRFFTD-----------LHFEEGWYMWLQSRDLL 62
Cdd:pfam02450 183 RGLQRSFSSSPWMLPKGKyvlwsdvAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLNTLDGWYMWKVSRDLD 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232488649  63 AGLP------------------------APGVEVYCLYGVGLPTPRTYIYDHS---------FPYKDPVAALYEDGDDTV 109
Cdd:pfam02450 263 GGLPyleaelakndikywvnpeetplpvAPGVKVYCIYGVGLPTERGYYYTPGktsspilsrIDYEDPVGIVSGDGDGTV 342
                         170       180
                  ....*....|....*....|....*..
gi 2232488649 110 ATRSMELCGQWQG-RQSQPVHLLPLNG 135
Cdd:pfam02450 343 PKRSLELCKNWQGlPAGQNVTVHELKH 369
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
58-88 5.56e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 44.36  E-value: 5.56e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2232488649  58 SRDLLAGLP-APGVEVYCLYGVGLPTPRTYIY 88
Cdd:PLN02517  476 SNPLETKLPnAPEMEIYSLYGVGIPTERSYVY 507
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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