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Conserved domains on  [gi|1958667463|ref|XP_038944884|]
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protein FAM131A isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAM131 super family cl20887
Putative cell signalling; The precise function of this protein family is unknown, however ...
 86-217 5.45e-89

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


The actual alignment was detected with superfamily member pfam15010:

Pssm-ID: 464442  Cd Length: 292  Bit Score: 267.21  E-value: 5.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667463  86 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPSDSPAALESAFSSYSDLSEGEQEA 165
Cdd:pfam15010   1 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958667463 166 RFAAGVAEQFAIAEAKLRAWSSVDGDDSTDDSYDEDFTGGADTDRRKETIQA 217
Cdd:pfam15010  81 RFAAGVAEQFAIAEAKLRAWSSVDGEDSNDDSYDEDFAPATEPTMQSQDNAA 132
 
Name Accession Description Interval E-value
FAM131 pfam15010
Putative cell signalling; The precise function of this protein family is unknown, however ...
 86-217 5.45e-89

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


Pssm-ID: 464442  Cd Length: 292  Bit Score: 267.21  E-value: 5.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667463  86 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPSDSPAALESAFSSYSDLSEGEQEA 165
Cdd:pfam15010   1 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958667463 166 RFAAGVAEQFAIAEAKLRAWSSVDGDDSTDDSYDEDFTGGADTDRRKETIQA 217
Cdd:pfam15010  81 RFAAGVAEQFAIAEAKLRAWSSVDGEDSNDDSYDEDFAPATEPTMQSQDNAA 132
 
Name Accession Description Interval E-value
FAM131 pfam15010
Putative cell signalling; The precise function of this protein family is unknown, however ...
 86-217 5.45e-89

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


Pssm-ID: 464442  Cd Length: 292  Bit Score: 267.21  E-value: 5.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958667463  86 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPSDSPAALESAFSSYSDLSEGEQEA 165
Cdd:pfam15010   1 MLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958667463 166 RFAAGVAEQFAIAEAKLRAWSSVDGDDSTDDSYDEDFTGGADTDRRKETIQA 217
Cdd:pfam15010  81 RFAAGVAEQFAIAEAKLRAWSSVDGEDSNDDSYDEDFAPATEPTMQSQDNAA 132
 
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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