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Conserved domains on  [gi|1174097918|ref|NP_001337012|]
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sterile alpha motif domain-containing protein 9-like [Homo sapiens]

Protein Classification

SAM domain-containing protein( domain architecture ID 10175783)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 12-76 6.54e-27

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.


:

Pssm-ID: 188927  Cd Length: 64  Bit Score: 104.81  E-value: 6.54e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1174097918   12 KDWTKEHVKKWVNEDlKINEQYGQILLSEEVTGLVLQELTEKDLVEMGLPWGPALLIKRSYNKLN 76
Cdd:cd09528      1 DDWTKEHVKQWLIED-LIDKKYAEILYEEEVTGAVLKELTEEDLVDMGLPHGPALLIIHSFNELN 64
 
Name Accession Description Interval E-value
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 12-76 6.54e-27

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.


Pssm-ID: 188927  Cd Length: 64  Bit Score: 104.81  E-value: 6.54e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1174097918   12 KDWTKEHVKKWVNEDlKINEQYGQILLSEEVTGLVLQELTEKDLVEMGLPWGPALLIKRSYNKLN 76
Cdd:cd09528      1 DDWTKEHVKQWLIED-LIDKKYAEILYEEEVTGAVLKELTEEDLVDMGLPHGPALLIIHSFNELN 64
 
Name Accession Description Interval E-value
SAM_Samd9_Samd9L cd09528
SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L ...
 12-76 6.54e-27

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.


Pssm-ID: 188927  Cd Length: 64  Bit Score: 104.81  E-value: 6.54e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1174097918   12 KDWTKEHVKKWVNEDlKINEQYGQILLSEEVTGLVLQELTEKDLVEMGLPWGPALLIKRSYNKLN 76
Cdd:cd09528      1 DDWTKEHVKQWLIED-LIDKKYAEILYEEEVTGAVLKELTEEDLVDMGLPHGPALLIIHSFNELN 64
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 14-68 1.26e-03

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 38.61  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1174097918   14 WTKEHVKKWVNEdLKINEQYGQILLSEEVTGLVLQELTEKDLVE-MGLPWGPALLI 68
Cdd:cd09509      4 WSVDDVAQFIKS-LDGCAEYAEVFREQEIDGQALLLLTEDDLLKgMGLKLGPALKI 58
 
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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