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Conserved domains on  [gi|24660919|ref|NP_648223|]
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matrimony [Drosophila melanogaster]

Protein Classification

SAM domain-containing protein( domain architecture ID 12211438)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation; similar to Drosophila melanogaster protein matrimony, a polo kinase inhibitor required to maintain G2 arrest in the meiotic cell cycle in females

CATH:  1.10.150.50
Gene Ontology:  GO:0005515
SCOP:  4001022

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
154-217 1.13e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


:

Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.29  E-value: 1.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24660919    154 YVVNHAANVEQILMHMGLENYVTNFEEAHIDLVELASL-ERADLVKIGLNTDEDCNRIMDVLHTL 217
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKL 65
 
Name Accession Description Interval E-value
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
154-217 1.13e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.29  E-value: 1.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24660919    154 YVVNHAANVEQILMHMGLENYVTNFEEAHIDLVELASL-ERADLVKIGLNTDEDCNRIMDVLHTL 217
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
162-210 1.21e-04

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 39.17  E-value: 1.21e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24660919 162 VEQILMHMGLENYVTNFEEAHIDLVELASLERADLVKIGLNTDEDCNRI 210
Cdd:cd09512  12 VCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLL 60
 
Name Accession Description Interval E-value
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
154-217 1.13e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 47.29  E-value: 1.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24660919    154 YVVNHAANVEQILMHMGLENYVTNFEEAHIDLVELASL-ERADLVKIGLNTDEDCNRIMDVLHTL 217
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
162-210 1.21e-04

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 39.17  E-value: 1.21e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24660919 162 VEQILMHMGLENYVTNFEEAHIDLVELASLERADLVKIGLNTDEDCNRI 210
Cdd:cd09512  12 VCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLL 60
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
165-211 7.46e-04

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 36.78  E-value: 7.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24660919 165 ILMHMGLENYVTNFEEAHIDLVELASLERADLVKIGLNTDEDCNRIM 211
Cdd:cd09518  11 ILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQIL 57
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
162-211 1.04e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 36.06  E-value: 1.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24660919 162 VEQILMHMGLENYVTNFEEAHIDLVELASLERADLVKIGLNTDEDCNRIM 211
Cdd:cd09487   2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKIL 51
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
157-203 1.29e-03

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 36.12  E-value: 1.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24660919 157 NHAANVEQILMHMGLENYVTNFEEAHIDLVELASLERADLVKIGLNT 203
Cdd:cd09520   2 AKYSDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITA 48
 
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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