NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2465246881|ref|WP_276324420|]
View 

lecithin retinol acyltransferase family protein [Fibrobacter succinogenes]

Protein Classification

C40 family peptidase( domain architecture ID 229557)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NLPC_P60 super family cl21534
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 2-100 7.21e-10

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


The actual alignment was detected with superfamily member pfam04970:

Pssm-ID: 473902  Cd Length: 106  Bit Score: 51.91  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465246881   2 HFAAPNGDMDAEKAYIhettLSHFSEGSDIhIMTFNEEYESGSVLRNFFKGD-EYELQSPRQTVARARSMLGRkgidnAG 80
Cdd:pfam04970  17 HLAPDSEKVVSNSRSI----LGVLSNKAGV-RKSTLEDFAGGDKYRVNNKDDdKYEPLPPDEVIQRAEELVGF-----VP 86

                          90       100
                  ....*....|....*....|
gi 2465246881  81 YNVLFNNCEDFAIWCKTNVA 100
Cdd:pfam04970  87 YSLLSNNCEHFVTYCRYGLS 106
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 2-100 7.21e-10

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: 51.91  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465246881   2 HFAAPNGDMDAEKAYIhettLSHFSEGSDIhIMTFNEEYESGSVLRNFFKGD-EYELQSPRQTVARARSMLGRkgidnAG 80
Cdd:pfam04970  17 HLAPDSEKVVSNSRSI----LGVLSNKAGV-RKSTLEDFAGGDKYRVNNKDDdKYEPLPPDEVIQRAEELVGF-----VP 86

                          90       100
                  ....*....|....*....|
gi 2465246881  81 YNVLFNNCEDFAIWCKTNVA 100
Cdd:pfam04970  87 YSLLSNNCEHFVTYCRYGLS 106
 
Name Accession Description Interval E-value
LRAT pfam04970
Lecithin retinol acyltransferase; The full-length members of this family, eg Swiss:P53816, are ...
 2-100 7.21e-10

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: 51.91  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465246881   2 HFAAPNGDMDAEKAYIhettLSHFSEGSDIhIMTFNEEYESGSVLRNFFKGD-EYELQSPRQTVARARSMLGRkgidnAG 80
Cdd:pfam04970  17 HLAPDSEKVVSNSRSI----LGVLSNKAGV-RKSTLEDFAGGDKYRVNNKDDdKYEPLPPDEVIQRAEELVGF-----VP 86

                          90       100
                  ....*....|....*....|
gi 2465246881  81 YNVLFNNCEDFAIWCKTNVA 100
Cdd:pfam04970  87 YSLLSNNCEHFVTYCRYGLS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH