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Conserved domains on  [gi|12963753|ref|NP_076113|]
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lecithin retinol acyltransferase [Mus musculus]

Protein Classification

lecithin retinol acyltransferase family protein( domain architecture ID 10523089)

lecithin retinol acyltransferase family protein which may catalyze transacylation and/or phospholipase (PL)A1/2-type hydrolysis of glycerophospholipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 56-171 2.93e-47

Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are representatives of a novel class II tumour-suppressor family, designated as H-REV107-like. This domain is the catalytic N-terminal proline-rich region of the protein. The downstream region is a putative C-terminal transmembrane domain which is found to be crucial for cellular localization, but not necessary for the enzyme activity. H-REV107-like proteins are homologous to lecithin retinol acyltransferase (LRAT), an enzyme that catalyzes the transfer of the sn-1 acyl group of phosphatidylcholine to all-trans-retinol and forming a retinyl ester.


:

Pssm-ID: 398571  Cd Length: 106  Bit Score: 151.68  E-value: 2.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963753    56 THFIHYGIYLGENRVAHLMPDIllaltndkertQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDgTLKKKS 135
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDS-----------EKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKD-DDKYEP 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 12963753   136 LLNEEVARRAEQQLGLTPYSLLWNNCEHFVTYCRYG 171
Cdd:pfam04970  69 LPPDEVIQRAEELVGFVPYSLLSNNCEHFVTYCRYG 104
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 56-171 2.93e-47

Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are representatives of a novel class II tumour-suppressor family, designated as H-REV107-like. This domain is the catalytic N-terminal proline-rich region of the protein. The downstream region is a putative C-terminal transmembrane domain which is found to be crucial for cellular localization, but not necessary for the enzyme activity. H-REV107-like proteins are homologous to lecithin retinol acyltransferase (LRAT), an enzyme that catalyzes the transfer of the sn-1 acyl group of phosphatidylcholine to all-trans-retinol and forming a retinyl ester.


Pssm-ID: 398571  Cd Length: 106  Bit Score: 151.68  E-value: 2.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963753    56 THFIHYGIYLGENRVAHLMPDIllaltndkertQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDgTLKKKS 135
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDS-----------EKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKD-DDKYEP 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 12963753   136 LLNEEVARRAEQQLGLTPYSLLWNNCEHFVTYCRYG 171
Cdd:pfam04970  69 LPPDEVIQRAEELVGFVPYSLLSNNCEHFVTYCRYG 104
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 56-171 2.93e-47

Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are representatives of a novel class II tumour-suppressor family, designated as H-REV107-like. This domain is the catalytic N-terminal proline-rich region of the protein. The downstream region is a putative C-terminal transmembrane domain which is found to be crucial for cellular localization, but not necessary for the enzyme activity. H-REV107-like proteins are homologous to lecithin retinol acyltransferase (LRAT), an enzyme that catalyzes the transfer of the sn-1 acyl group of phosphatidylcholine to all-trans-retinol and forming a retinyl ester.


Pssm-ID: 398571  Cd Length: 106  Bit Score: 151.68  E-value: 2.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963753    56 THFIHYGIYLGENRVAHLMPDIllaltndkertQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDgTLKKKS 135
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDS-----------EKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKD-DDKYEP 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 12963753   136 LLNEEVARRAEQQLGLTPYSLLWNNCEHFVTYCRYG 171
Cdd:pfam04970  69 LPPDEVIQRAEELVGFVPYSLLSNNCEHFVTYCRYG 104
 
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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