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.

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gi 2053612007 270 DELQSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKIL 323
Cdd:cd09516     7 EEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLL 60

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.

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gi 2053612007 270 DELQSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKIL 323
Cdd:cd09516     7 EEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLL 60

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.

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gi 2053612007  279 LQSLGLGKYSILFKAEEVD-MTALKQMGENDLKELGI-PMGPRKKILLAI 326
Cdd:smart00454  13 LESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGItKLGHRKKILKAI 62

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.

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                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053612007 270 DELQSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKIL 323
Cdd:cd09516     7 EEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLL 60

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.

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gi 2053612007 279 LQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGI-PMGPRKKILLAI 326
Cdd:cd09487     6 LESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGItSPGHRKKILRAI 54

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.

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gi 2053612007 269 GDELQSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKILLAIAPRSKR 332
Cdd:cd09584     6 EEDVPSLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVKEKAAK 69

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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gi 2053612007 279 LQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKILLAIAPR 329
Cdd:cd09517     9 LTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKR 59

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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gi 2053612007 271 ELQSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKILLAIAPR 329
Cdd:cd09586     1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRR 59

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.

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gi 2053612007 273 QSMDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIP-MGPRKKILLAIA 327
Cdd:cd09519     5 KDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITlFGPKRKMTSAIA 60

SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea.

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gi 2053612007 275 MDGLLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIPMGPRKKILLAIAPRSK--RQP 334
Cdd:cd09587     5 LEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQvlQQP 66

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.

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gi 2053612007 278 LLQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGIP-MGPRKKILLAI 326
Cdd:cd09521    11 FLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITqPGDQKKILDAI 60

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.

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gi 2053612007 286 KYSILFKAEEVDMTALKQMGENDLKELGIPMGP 318
Cdd:cd09528    20 KYAEILYEEEVTGAVLKELTEEDLVDMGLPHGP 52

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.

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gi 2053612007 279 LQSLGLGKYSILFKAEEVDMTALKQM-GENDLKELGI-PMGPRKKILLAI 326
Cdd:cd09505    14 LRSIGLEQYVEVFRANNIDGKELLNLtKESLSKDLKIeSLGHRNKILRKI 63

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.

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gi 2053612007 279 LQSLGLGKYSILFKAEEVDMTALKQMGENDLKELGI-PMGPRKKILLAI 326
Cdd:cd09533     6 LSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGItSVGHRLTILKAV 54