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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351457346  431 QTQEQNGILDWLRKLRLHKYYPVFKQLSMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 495
Cdd:cd09558      1 QTQEQNGILDWLRKLRLHKYYPVFKQLTMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 65

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351457346  255 FEVLWSDSSITSVTKSSSEVTEFISKLSQLYPEEN-----LEKLIPCLAGPDAF----YVERNHVDLDSGLRYLASLPSH 325
Cdd:cd06887     23 FLVKWQDLSEKLVYRRFTEIYEFHKTLKEMFPIEAgdinkENRIIPHLPAPKWFdgqrAAENRQGTLTEYCSTLLSLPPK 102

                           90
                   ....*....|...
gi 1351457346  326 VLKNDHVRRFLST 338
Cdd:cd06887    103 ISRCPHVLDFFKV 115

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351457346  431 QTQEQNGILDWLRKLRLHKYYPVFKQLSMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 495
Cdd:cd09558      1 QTQEQNGILDWLRKLRLHKYYPVFKQLTMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 65

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
                   ....*....|....*....|....*....|....*....|....*..
gi 1351457346  440 DWLRKLRLHKYYPVFKQ--LSMEKFLSLTEEDLNKFESLTMGAKKKL 484
Cdd:pfam00536   10 EWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKLGVTLLGHRKKI 56

The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351457346  255 FEVLWSDSSITSVTKSSSEVTEFISKLSQLYPEEN-----LEKLIPCLAGPDAF----YVERNHVDLDSGLRYLASLPSH 325
Cdd:cd06887     23 FLVKWQDLSEKLVYRRFTEIYEFHKTLKEMFPIEAgdinkENRIIPHLPAPKWFdgqrAAENRQGTLTEYCSTLLSLPPK 102

                           90
                   ....*....|...
gi 1351457346  326 VLKNDHVRRFLST 338
Cdd:cd06887    103 ISRCPHVLDFFKV 115

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351457346  431 QTQEQNGILDWLRKLRLHKYYPVFKQLSMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 495
Cdd:cd09558      1 QTQEQNGILDWLRKLRLHKYYPVFKQLTMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKS 65

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1351457346  437 GILDWLRKLRLHKYYPVFKQLSMEKFLSLTEEDLNKfESLTMGAKKKL 484
Cdd:cd09557      8 DVPAWLKSLRLHKYASLFSQMTYEEMLNLTEEQLEA-QGVTKGARHKI 54

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        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1351457346  438 ILDWLRKLRLHKYYPVFKQ--LSMEKFLSLTEEDLNKFESLTMGAKKKLKTQLE 489
Cdd:cd09487      2 VAEWLESLGLEQYADLFRKneIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1351457346  434 EQNGILdwlRKLRLHKYYPVF--KQLSMEKFLSLTEEDLNKfesltMGAKKKLKTQ 487
Cdd:cd09518      7 ELSGIL---RKLSLEKYQPIFeeQEVDMEAFLTLTDGDLKE-----LGIKTDGPRQ 54

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
                   ....*....|....*....|....*....|....*....|....*..
gi 1351457346  440 DWLRKLRLHKYYPVFKQ--LSMEKFLSLTEEDLNKFESLTMGAKKKL 484
Cdd:pfam00536   10 EWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKLGVTLLGHRKKI 56

The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351457346  255 FEVLWSDSSITSVTKSSSEVTEFISKLSQLYPEEN-----LEKLIPCLAGPDAF----YVERNHVDLDSGLRYLASLPSH 325
Cdd:cd06887     23 FLVKWQDLSEKLVYRRFTEIYEFHKTLKEMFPIEAgdinkENRIIPHLPAPKWFdgqrAAENRQGTLTEYCSTLLSLPPK 102

                           90
                   ....*....|...
gi 1351457346  326 VLKNDHVRRFLST 338
Cdd:cd06887    103 ISRCPHVLDFFKV 115

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
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1351457346   438 ILDWLRKLRLHKYYPVFKQ--LSMEKFLSLT-EEDLNKFESLTMGAKKKLKTQLE 489
Cdd:smart00454    9 VADWLESIGLEQYADNFRKngIDGALLLLLTsEEDLKELGITKLGHRKKILKAIQ 63