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Conserved domains on  [gi|672035710|ref|XP_008757365|]
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protein Smaug homolog 2 isoform X1 [Rattus norvegicus]

Protein Classification

Smaug family SAM domain-containing protein( domain architecture ID 10175959)

Smaug family sterile alpha motif (SAM) domain-containing protein such as mammalian Smaug which is a translational repressor that forms cytoplasmic foci similar to stress granules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM_Smaug cd09557
SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA ...
296-358 1.32e-40

SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA recognition domain. It binds a specific RNA motif known as Smaug recognition element (SRE). Among members of this group are invertebrate Smaug (Smg) proteins and vertebrate Smaug1 and Smaug2 proteins. They are involved in post-transcriptional control during early embryogenesis in animals. In Drosophila, Smaug protein is a translational repressor of mRNA of Nanos (Nos) protein. Gradient of Nanos is required for proper abdominal segmentation. SAM domain interacts specifically with the Nanos mRNA regulatory regions. Moreover, Smaug protein is involved in regulation of specific maternal transcripts degradation in Drosophila early embryo via recruitment of the CCR4/POP2/NOT deadenylase.


:

Pssm-ID: 188956  Cd Length: 63  Bit Score: 142.47  E-value: 1.32e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710 296 EDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRE 358
Cdd:cd09557    1 EEGSGMKDVPAWLKSLRLHKYASLFSQMTYEEMLNLTEEQLEAQGVTKGARHKIALSIQKLKE 63
 
Name Accession Description Interval E-value
SAM_Smaug cd09557
SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA ...
296-358 1.32e-40

SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA recognition domain. It binds a specific RNA motif known as Smaug recognition element (SRE). Among members of this group are invertebrate Smaug (Smg) proteins and vertebrate Smaug1 and Smaug2 proteins. They are involved in post-transcriptional control during early embryogenesis in animals. In Drosophila, Smaug protein is a translational repressor of mRNA of Nanos (Nos) protein. Gradient of Nanos is required for proper abdominal segmentation. SAM domain interacts specifically with the Nanos mRNA regulatory regions. Moreover, Smaug protein is involved in regulation of specific maternal transcripts degradation in Drosophila early embryo via recruitment of the CCR4/POP2/NOT deadenylase.


Pssm-ID: 188956  Cd Length: 63  Bit Score: 142.47  E-value: 1.32e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710 296 EDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRE 358
Cdd:cd09557    1 EEGSGMKDVPAWLKSLRLHKYASLFSQMTYEEMLNLTEEQLEAQGVTKGARHKIALSIQKLKE 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
297-357 9.64e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 60.75  E-value: 9.64e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672035710  297 DGSGMKDVPSWLKSLRLHKYAALFSQ--MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQKLR 357
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKLGVTLlGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
301-359 3.92e-08

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: 50.37  E-value: 3.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710   301 MKDVPSWLKSLRLHKYAALFSQMSY--EEMMTLTEQ-HLESQNVTK-GARHKIALSIQKLRER 359
Cdd:smart00454   6 PESVADWLESIGLEQYADNFRKNGIdgALLLLLTSEeDLKELGITKlGHRKKILKAIQKLKEQ 68
 
Name Accession Description Interval E-value
SAM_Smaug cd09557
SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA ...
296-358 1.32e-40

SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA recognition domain. It binds a specific RNA motif known as Smaug recognition element (SRE). Among members of this group are invertebrate Smaug (Smg) proteins and vertebrate Smaug1 and Smaug2 proteins. They are involved in post-transcriptional control during early embryogenesis in animals. In Drosophila, Smaug protein is a translational repressor of mRNA of Nanos (Nos) protein. Gradient of Nanos is required for proper abdominal segmentation. SAM domain interacts specifically with the Nanos mRNA regulatory regions. Moreover, Smaug protein is involved in regulation of specific maternal transcripts degradation in Drosophila early embryo via recruitment of the CCR4/POP2/NOT deadenylase.


Pssm-ID: 188956  Cd Length: 63  Bit Score: 142.47  E-value: 1.32e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710 296 EDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRE 358
Cdd:cd09557    1 EEGSGMKDVPAWLKSLRLHKYASLFSQMTYEEMLNLTEEQLEAQGVTKGARHKIALSIQKLKE 63
SAM_Smaug-like cd09489
SAM (Sterile alpha motif ); SAM (sterile alpha motif) domain of Smaug-like subfamily proteins ...
304-358 3.43e-16

SAM (Sterile alpha motif ); SAM (sterile alpha motif) domain of Smaug-like subfamily proteins is an RNA binding domain. SAM interacts with stem-loop structures in target mRNAs. Proteins of this subfamily are post-transcriptional regulators involved in mRNA silencing and deadenylation; they can be implicated in transcript stability regulation and vacuolar protein transport as well. SAM_Smaug-like domain-containing proteins are found in metazoa from yeast to human. In animals they are active during early embryogenesis.


Pssm-ID: 188888  Cd Length: 57  Bit Score: 72.97  E-value: 3.43e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672035710 304 VPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNV-TKGARHKIALSIQKLRE 358
Cdd:cd09489    2 IPMWLKSLRLHKYSDAFKGTTWEELLYLTEETLEKKGVlTLGARRKLLKAFGIVKE 57
SAM_VTS1_fungal cd09556
SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily ...
301-362 6.47e-13

SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding.


Pssm-ID: 188955  Cd Length: 69  Bit Score: 64.24  E-value: 6.47e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710 301 MKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNV-TKGARHKIALSIQKLRERQSV 362
Cdd:cd09556    6 LKDIPAWLRSLRLHKYTDNLKDLSWKELIELDDEDLEDKGVsALGARRKLLKAFEIVREYKER 68
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
297-357 9.64e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 60.75  E-value: 9.64e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672035710  297 DGSGMKDVPSWLKSLRLHKYAALFSQ--MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQKLR 357
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKLGVTLlGHRKKILYAIQRLK 64
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
302-359 2.63e-08

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: 50.76  E-value: 2.63e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672035710 302 KDVPSWLKSLRLHKYAALFSQ--MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQKLRER 359
Cdd:cd09520    5 SDLPELLAKLGLEKYIDLFAQqeIDLQTFLTLTDQDLKELGITAfGARRKMLLAISELNKR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
301-359 3.92e-08

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: 50.37  E-value: 3.92e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672035710   301 MKDVPSWLKSLRLHKYAALFSQMSY--EEMMTLTEQ-HLESQNVTK-GARHKIALSIQKLRER 359
Cdd:smart00454   6 PESVADWLESIGLEQYADNFRKNGIdgALLLLLTSEeDLKELGITKlGHRKKILKAIQKLKEQ 68
SAM_ZCCH14 cd09558
SAM domain of ZCCH14 subfamily; SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC ...
307-359 1.67e-07

SAM domain of ZCCH14 subfamily; SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC domain 14) protein subfamily (also known as BDG-29 or KIAA0579) is a putative RNA binding domain. Members of this group are believed to be involved in post-translational regulation during early embryogenesis.


Pssm-ID: 188957  Cd Length: 65  Bit Score: 48.54  E-value: 1.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672035710 307 WLKSLRLHKYAALFSQMSYEEMMTLTEQHLES-QNVTKGARHKIALSIQKLRER 359
Cdd:cd09558   11 WLRKLRLHKYYPVFKQLTMEKFLSLTEEDLNKfESLTMGAKKKLKTQLELEKEK 64
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
303-355 2.03e-06

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: 45.31  E-value: 2.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672035710 303 DVPSWLKSLRLHKYAALFSQ--MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQK 355
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKneIDGDALLLLTDEDLKELGITSpGHRKKILRAIQR 56
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
302-357 4.50e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 4.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672035710  302 KDVPSWLKSLRLHKYAALFSQ---MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQKLR 357
Cdd:pfam07647   7 ESVADWLRSIGLEQYTDNFRDqgiTGAELLLRLTLEDLKRLGITSvGHRRKILKKIQELK 66
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
297-366 5.57e-04

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 38.83  E-value: 5.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672035710 297 DGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTE-QHLESQNVtkgarhkiaLSIQKLRERQSVLKSL 366
Cdd:cd09500    1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRiWEVELTNV---------LEINKLGHRKRILASL 62
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
302-357 3.58e-03

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 36.42  E-value: 3.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672035710 302 KDVPSWLKSLRLHKYAALFSQ--MSYEEMMTLTEQHLESQNVTK-GARHKIALSIQKLR 357
Cdd:cd09534    4 EFVEEWLNELNCGQYLDIFEKnlITGDLLLELDKEALKELGITKvGDRIRLLRAIKSLR 62
 
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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