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Conserved domains on  [gi|8923526|ref|NP_060348|]
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phospholipase A and acyltransferase 2 [Homo sapiens]

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 ...
 19-125 1.08e-53

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: 165.16  E-value: 1.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923526     19 FGYAHWAIYVGDGYVVHLAPASEIAGAGAASVLSALTNKAIVKKELLSVVAGGDNYRVNNKHDDRYTPLPSNKIVKRAEE 98
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDSEKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKDDDKYEPLPPDEVIQRAEE 80

                          90       100
                  ....*....|....*....|....*..
gi 8923526     99 LVGQeLPYSLTSDNCEHFVNHLRYGVS 125
Cdd:pfam04970  81 LVGF-VPYSLLSNNCEHFVTYCRYGLS 106
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 19-125 1.08e-53

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: 165.16  E-value: 1.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923526     19 FGYAHWAIYVGDGYVVHLAPASEIAGAGAASVLSALTNKAIVKKELLSVVAGGDNYRVNNKHDDRYTPLPSNKIVKRAEE 98
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDSEKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKDDDKYEPLPPDEVIQRAEE 80

                          90       100
                  ....*....|....*....|....*..
gi 8923526     99 LVGQeLPYSLTSDNCEHFVNHLRYGVS 125
Cdd:pfam04970  81 LVGF-VPYSLLSNNCEHFVTYCRYGLS 106
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 19-125 1.08e-53

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: 165.16  E-value: 1.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923526     19 FGYAHWAIYVGDGYVVHLAPASEIAGAGAASVLSALTNKAIVKKELLSVVAGGDNYRVNNKHDDRYTPLPSNKIVKRAEE 98
Cdd:pfam04970   1 TLYTHHGIYVGDGYVVHLAPDSEKVVSNSRSILGVLSNKAGVRKSTLEDFAGGDKYRVNNKDDDKYEPLPPDEVIQRAEE 80

                          90       100
                  ....*....|....*....|....*..
gi 8923526     99 LVGQeLPYSLTSDNCEHFVNHLRYGVS 125
Cdd:pfam04970  81 LVGF-VPYSLLSNNCEHFVTYCRYGLS 106
 
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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