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Conserved domains on  [gi|1879298499|ref|NP_001372595|]
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serum amyloid A-2 protein isoform a preproprotein [Homo sapiens]

Protein Classification

SAA domain-containing protein( domain architecture ID 10447209)

SAA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAA pfam00277
Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate ...
 25-122 4.77e-58

Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate amphipathic alpha-helical apolipoproteins that associate predominantly with high density lipoproteins (HDL). They play a role in the mobilization of cholesterol for tissue repair and regeneration. The synthesis of these proteins is greatly increased (as much as a 1000 fold) in inflammation, being a major acute phase reactant together with C-reactive protein. They act as cytokine-like proteins that are involved in cell-cell communication and in inflammatory, immunologic, neoplastic and protective pathways. Prolonged elevation of plasma SAA levels, as in chronic inflammation, results in a pathological condition, called amyloidosis, which is characterized by the highly insoluble accumulation of SAA in several tissues. During chronic inflammation, SAA association with HDL can change its protein and lipid composition which abrogates the HDL anti-atherogenic properties, contributing to a pro-atherogenic state.


:

Pssm-ID: 459744  Cd Length: 102  Bit Score: 174.43  E-value: 4.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298499  25 LGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLT-GRGAEDSLADQAANKW 103
Cdd:pfam00277   4 FKEAAQGAGDMWRAYWDMREANYKNSDKYFHARGNYDAAQRGPGGVWAAKVISDAREYLQGHVsGRGLEDSAADQEANEW 83

                          90
                  ....*....|....*....
gi 1879298499 104 GRSGRDPNHFRPAGLPEKY 122
Cdd:pfam00277  84 GRSGKDPNHFRPRGLPDKY 102
 
Name Accession Description Interval E-value
SAA pfam00277
Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate ...
 25-122 4.77e-58

Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate amphipathic alpha-helical apolipoproteins that associate predominantly with high density lipoproteins (HDL). They play a role in the mobilization of cholesterol for tissue repair and regeneration. The synthesis of these proteins is greatly increased (as much as a 1000 fold) in inflammation, being a major acute phase reactant together with C-reactive protein. They act as cytokine-like proteins that are involved in cell-cell communication and in inflammatory, immunologic, neoplastic and protective pathways. Prolonged elevation of plasma SAA levels, as in chronic inflammation, results in a pathological condition, called amyloidosis, which is characterized by the highly insoluble accumulation of SAA in several tissues. During chronic inflammation, SAA association with HDL can change its protein and lipid composition which abrogates the HDL anti-atherogenic properties, contributing to a pro-atherogenic state.


Pssm-ID: 459744  Cd Length: 102  Bit Score: 174.43  E-value: 4.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298499  25 LGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLT-GRGAEDSLADQAANKW 103
Cdd:pfam00277   4 FKEAAQGAGDMWRAYWDMREANYKNSDKYFHARGNYDAAQRGPGGVWAAKVISDAREYLQGHVsGRGLEDSAADQEANEW 83

                          90
                  ....*....|....*....
gi 1879298499 104 GRSGRDPNHFRPAGLPEKY 122
Cdd:pfam00277  84 GRSGKDPNHFRPRGLPDKY 102
SAA smart00197
Serum amyloid A proteins; Serum amyloid A proteins are induced during the acute-phase response. ...
 25-122 1.44e-55

Serum amyloid A proteins; Serum amyloid A proteins are induced during the acute-phase response. Secondary amyloidosis is characterised by the extracellular accumulation in tissues of SAA proteins. SAA proteins are apolipoproteins.


Pssm-ID: 214552  Cd Length: 103  Bit Score: 168.46  E-value: 1.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298499   25 LGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLT-GRGAEDSLADQAANKW 103
Cdd:smart00197   5 FKEALQGAWDMWRAYRDMKEANHQNADKYFHARGNYDAAQRGPGGVWAAKVISDAREYFQGLIsGRGLEDSKADQKANEW 84

                           90
                   ....*....|....*....
gi 1879298499  104 GRSGRDPNHFRPAGLPEKY 122
Cdd:smart00197  85 GRSGKDPNRFRPPGLPEKY 103
 
Name Accession Description Interval E-value
SAA pfam00277
Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate ...
 25-122 4.77e-58

Serum amyloid A protein; The serum amyloid A (SAA) proteins comprise a family of vertebrate amphipathic alpha-helical apolipoproteins that associate predominantly with high density lipoproteins (HDL). They play a role in the mobilization of cholesterol for tissue repair and regeneration. The synthesis of these proteins is greatly increased (as much as a 1000 fold) in inflammation, being a major acute phase reactant together with C-reactive protein. They act as cytokine-like proteins that are involved in cell-cell communication and in inflammatory, immunologic, neoplastic and protective pathways. Prolonged elevation of plasma SAA levels, as in chronic inflammation, results in a pathological condition, called amyloidosis, which is characterized by the highly insoluble accumulation of SAA in several tissues. During chronic inflammation, SAA association with HDL can change its protein and lipid composition which abrogates the HDL anti-atherogenic properties, contributing to a pro-atherogenic state.


Pssm-ID: 459744  Cd Length: 102  Bit Score: 174.43  E-value: 4.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298499  25 LGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLT-GRGAEDSLADQAANKW 103
Cdd:pfam00277   4 FKEAAQGAGDMWRAYWDMREANYKNSDKYFHARGNYDAAQRGPGGVWAAKVISDAREYLQGHVsGRGLEDSAADQEANEW 83

                          90
                  ....*....|....*....
gi 1879298499 104 GRSGRDPNHFRPAGLPEKY 122
Cdd:pfam00277  84 GRSGKDPNHFRPRGLPDKY 102
SAA smart00197
Serum amyloid A proteins; Serum amyloid A proteins are induced during the acute-phase response. ...
 25-122 1.44e-55

Serum amyloid A proteins; Serum amyloid A proteins are induced during the acute-phase response. Secondary amyloidosis is characterised by the extracellular accumulation in tissues of SAA proteins. SAA proteins are apolipoproteins.


Pssm-ID: 214552  Cd Length: 103  Bit Score: 168.46  E-value: 1.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298499   25 LGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVISNARENIQRLT-GRGAEDSLADQAANKW 103
Cdd:smart00197   5 FKEALQGAWDMWRAYRDMKEANHQNADKYFHARGNYDAAQRGPGGVWAAKVISDAREYFQGLIsGRGLEDSKADQKANEW 84

                           90
                   ....*....|....*....
gi 1879298499  104 GRSGRDPNHFRPAGLPEKY 122
Cdd:smart00197  85 GRSGKDPNRFRPPGLPEKY 103
 
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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