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Conserved domains on  [gi|392900336|ref|NP_001255460|]
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Transthyretin-like family protein [Caenorhabditis elegans]

Protein Classification

transthyretin-like family protein( domain architecture ID 10470959)

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

Gene Ontology:  GO:0009986
PubMed:  22713871

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTR-52 pfam01060
Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to ...
64-142 7.86e-39

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: 127.31  E-value: 7.86e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392900336   64 KGKLMCGGRPVRNATVKLWDNDMFDPDDLIAETHVNEDGTFEVSGFAISITAIDPQLRIYHNCRSSSKVCRRKITFTVP 142
Cdd:pfam01060   1 KGRLMCGGKPASNVKVKLWEKDTLDPDDLLDETKTDEDGNFELSGSTDEITTIDPYLKIYHDCNDGVKPCQRKIKIPIP 79
 
Name Accession Description Interval E-value
TTR-52 pfam01060
Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to ...
64-142 7.86e-39

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: 127.31  E-value: 7.86e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392900336   64 KGKLMCGGRPVRNATVKLWDNDMFDPDDLIAETHVNEDGTFEVSGFAISITAIDPQLRIYHNCRSSSKVCRRKITFTVP 142
Cdd:pfam01060   1 KGRLMCGGKPASNVKVKLWEKDTLDPDDLLDETKTDEDGNFELSGSTDEITTIDPYLKIYHDCNDGVKPCQRKIKIPIP 79
 
Name Accession Description Interval E-value
TTR-52 pfam01060
Transthyretin-like family; TTR-52 was called family 2 in, and has weak similarity to ...
64-142 7.86e-39

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: 127.31  E-value: 7.86e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392900336   64 KGKLMCGGRPVRNATVKLWDNDMFDPDDLIAETHVNEDGTFEVSGFAISITAIDPQLRIYHNCRSSSKVCRRKITFTVP 142
Cdd:pfam01060   1 KGRLMCGGKPASNVKVKLWEKDTLDPDDLLDETKTDEDGNFELSGSTDEITTIDPYLKIYHDCNDGVKPCQRKIKIPIP 79
 
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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