PHAT; The PHAT (pseudo-HEAT analogous topology) domain assumes a structure consisting of a layer of three parallel helices packed against a layer of two antiparallel helices, into a cylindrical shaped five-helix bundle. It is found in the RNA-binding protein Smaug, where it is essential for high-affinity RNA binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681114  656 RANILNRVEQELLTGQ-MELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYA-VQDDETLGVL 733
Cdd:pfam09246   1 RAGILLQLEKDLIGGQkAELGTALEELTNIVLTPMKPIEMDGPPEEDIAAQFAKVIDIVGNILQMDPVAsQQDDETLGIF 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 300681114  734 MWILDRSIHNEAFMNHASQLKDLKFKLSKM 763
Cdd:pfam09246  81 LWILDRAIHNDAFIAHAAQLKDHKFKLSKI 110

PHAT; The PHAT (pseudo-HEAT analogous topology) domain assumes a structure consisting of a layer of three parallel helices packed against a layer of two antiparallel helices, into a cylindrical shaped five-helix bundle. It is found in the RNA-binding protein Smaug, where it is essential for high-affinity RNA binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681114  656 RANILNRVEQELLTGQ-MELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYA-VQDDETLGVL 733
Cdd:pfam09246   1 RAGILLQLEKDLIGGQkAELGTALEELTNIVLTPMKPIEMDGPPEEDIAAQFAKVIDIVGNILQMDPVAsQQDDETLGIF 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 300681114  734 MWILDRSIHNEAFMNHASQLKDLKFKLSKM 763
Cdd:pfam09246  81 LWILDRAIHNDAFIAHAAQLKDHKFKLSKI 110

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300681114  601 IGLWLKSLRLHKYIELFKN--MTYEEMLLITEDFLQSVGVTK-GASHKLALCIDKLK 654
Cdd:pfam00536   8 VGEWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKLGVTLlGHRKKILYAIQRLK 64

PHAT; The PHAT (pseudo-HEAT analogous topology) domain assumes a structure consisting of a layer of three parallel helices packed against a layer of two antiparallel helices, into a cylindrical shaped five-helix bundle. It is found in the RNA-binding protein Smaug, where it is essential for high-affinity RNA binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681114  656 RANILNRVEQELLTGQ-MELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYA-VQDDETLGVL 733
Cdd:pfam09246   1 RAGILLQLEKDLIGGQkAELGTALEELTNIVLTPMKPIEMDGPPEEDIAAQFAKVIDIVGNILQMDPVAsQQDDETLGIF 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 300681114  734 MWILDRSIHNEAFMNHASQLKDLKFKLSKM 763
Cdd:pfam09246  81 LWILDRAIHNDAFIAHAAQLKDHKFKLSKI 110

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300681114 600 GIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGV-TKGASHKLALCIDKLKE 655
Cdd:cd09489    1 GIPMWLKSLRLHKYSDAFKGTTWEELLYLTEETLEKKGVlTLGARRKLLKAFGIVKE 57

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 300681114 604 WLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGV-TKGASHKL 646
Cdd:cd09556   12 WLRSLRLHKYTDNLKDLSWKELIELDDEDLEDKGVsALGARRKL 55

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681114   601 IGLWLKSLRLHKYIELFKNMTY--EEML-LITEDFLQSVGVTK-GASHKLALCIDKLKER 656
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIdgALLLlLTSEEDLKELGITKlGHRKKILKAIQKLKEQ 68

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300681114 605 LKSLRLHKYIELFKN--MTYEEMLLITEDFLQSVGVTK-GASHKLALCIDKLKER 656
Cdd:cd09520   11 LAKLGLEKYIDLFAQqeIDLQTFLTLTDQDLKELGITAfGARRKMLLAISELNKR 65

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 300681114 604 WLKSLRLHKYIELFK--NMTYEEMLLITEDFLQSVGVTK 640
Cdd:cd09487    5 WLESLGLEQYADLFRknEIDGDALLLLTDEDLKELGITS 43