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Conserved domains on  [gi|1972267158|ref|NP_001379105|]
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Transthyretin-like family protein [Caenorhabditis elegans]

Protein Classification

transthyretin-like family protein( domain architecture ID 2821)

transthyretin-like family protein similar to Caenorhabditis elegans transthyretin-like protein 52 (TTR-52) that functions as a bridging molecule that mediates recognition and engulfment of apoptotic cells by cross-linking the surface-exposed phosphatidylserine with the extracellular domain of the phagocyte receptor ced-1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF6795 super family cl03084
Domain of unknown function (DUF6795); This domain, mainly found in bacteria and eukaryotes, is ...
28-106 3.24e-07

Domain of unknown function (DUF6795); This domain, mainly found in bacteria and eukaryotes, is functionally uncharacterized. This domain is approximately 100 amino acids in length and, based on structure prediction and overlaps with other families, belongs to the transthyretin superfamily. It is likely to have a seven stranded beta sandwich fold.


The actual alignment was detected with superfamily member pfam01060:

Pssm-ID: 470730  Cd Length: 79  Bit Score: 44.88  E-value: 3.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972267158  28 GQLQCtDTSKLENVVVEIWDKDRSFFpitlfvdDDLAGRTITsaDDNGTFKVEGCASDLdflfikNEPEFYLKIRHYCK 106
Cdd:pfam01060   2 GRLMC-GGKPASNVKVKLWEKDTLDP-------DDLLDETKT--DEDGNFELSGSTDEI------TTIDPYLKIYHDCN 64
 
Name Accession Description Interval E-value
TTR-52 pfam01060
Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to ...
28-106 3.24e-07

Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to transthyretin (formerly called pre-albumin) which transports thyroid hormones. The specific function of this protein is as a bridging molecule in apoptosis cross-linking dying cells to phagocytes. TTR-52 bridges by cross-linking surface-exposed phosphatidylserine (PtdSer) on apoptotic cells to the CED-1 receptor, a transmembrane receptor, on phagocytes. TTR-52 has an open beta-barrel-like structure.


Pssm-ID: 460046  Cd Length: 79  Bit Score: 44.88  E-value: 3.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972267158  28 GQLQCtDTSKLENVVVEIWDKDRSFFpitlfvdDDLAGRTITsaDDNGTFKVEGCASDLdflfikNEPEFYLKIRHYCK 106
Cdd:pfam01060   2 GRLMC-GGKPASNVKVKLWEKDTLDP-------DDLLDETKT--DEDGNFELSGSTDEI------TTIDPYLKIYHDCN 64
 
Name Accession Description Interval E-value
TTR-52 pfam01060
Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to ...
28-106 3.24e-07

Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to transthyretin (formerly called pre-albumin) which transports thyroid hormones. The specific function of this protein is as a bridging molecule in apoptosis cross-linking dying cells to phagocytes. TTR-52 bridges by cross-linking surface-exposed phosphatidylserine (PtdSer) on apoptotic cells to the CED-1 receptor, a transmembrane receptor, on phagocytes. TTR-52 has an open beta-barrel-like structure.


Pssm-ID: 460046  Cd Length: 79  Bit Score: 44.88  E-value: 3.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972267158  28 GQLQCtDTSKLENVVVEIWDKDRSFFpitlfvdDDLAGRTITsaDDNGTFKVEGCASDLdflfikNEPEFYLKIRHYCK 106
Cdd:pfam01060   2 GRLMC-GGKPASNVKVKLWEKDTLDP-------DDLLDETKT--DEDGNFELSGSTDEI------TTIDPYLKIYHDCN 64
 
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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