C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. This C-terminal domain of the alpha-subunit appears to contact neighboring cadherin-like repeats of alpha dystroglycan, and may also be involved in interactions with other components of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with extracellular matrix components such as laminin, perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298683721    1 LVPVVNN*LFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 78
Cdd:pfam18424  46 LVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298683721  380 ARFKARLAGDPAPVLNDIHKKIALVKKLAF*FGDRNCSSITLQNITRGSIVV 431
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIV 52

Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in alpha-Dystroglycan (DG). The murine skeletal muscle N-terminal alpha-DG region, contains two autonomous domains; the first identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. This domain is similar to the small subunit ribosomal protein S6 of Thermus thermophilus (S6 domain). It is suggested that the S6 domain may be of functional relevance for LARGE (like-acetylglucosaminyltransferase) recognition along the alpha-DG maturation pathway.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298683721    1 LVPVVNN*LFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 78
Cdd:pfam18424  46 LVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298683721 272 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdkfkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 351
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                         90       100
                 ....*....|....*....|....*..
gi 298683721 352 HATDKG--GLSAVDAFEIHVHKRPQGD 376
Cdd:cd11303   73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298683721  380 ARFKARLAGDPAPVLNDIHKKIALVKKLAF*FGDRNCSSITLQNITRGSIVV 431
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIV 52

Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in alpha-Dystroglycan (DG). The murine skeletal muscle N-terminal alpha-DG region, contains two autonomous domains; the first identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. This domain is similar to the small subunit ribosomal protein S6 of Thermus thermophilus (S6 domain). It is suggested that the S6 domain may be of functional relevance for LARGE (like-acetylglucosaminyltransferase) recognition along the alpha-DG maturation pathway.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298683721    1 LVPVVNN*LFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 78
Cdd:pfam18424  46 LVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123

Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in skeletal muscle and other tissues; the pre-protein is cleaved into two subunits (alpha and beta) that form a complex which links the extracellular matrix to the cytoskeleton. Cadherin-like dystroglycan repeats are present in the extracellular alpha-dystroglycan subunit, which binds to the alpha-2-laminin G-domain in the basement membrane as part of the dystrophin-dystroglycan-complex (DGC). DGC has been shown to interact with other etxtracellular matrix components as well, such as perlecan and m-agrin, suggesting that the complex may play various different roles depending on the extracellular ligand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298683721 272 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdkfkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 351
Cdd:cd11303    1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                         90       100
                 ....*....|....*....|....*..
gi 298683721 352 HATDKG--GLSAVDAFEIHVHKRPQGD 376
Cdd:cd11303   73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298683721  380 ARFKARLAGDPAPVLNDIHKKIALVKKLAF*FGDRNCSSITLQNITRGSIVV 431
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIV 52

DNA polymerase III subunits gamma and tau; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298683721  91 TPTPVTAIGPPTTAIQEP--PSRIVPTPTSPAIAPPTETmAPPVRDPVPgKPTVTIRTrgaiiQTPTLGPIQPTRVSEAG 168
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPvrPTPAPSTRPKAAAAANIPP-KEPVRETAT-PPPVPPRP-----VAPPVPHTPESAPKLTR 433

                         90
                 ....*....|....
gi 298683721 169 TTVPGQIRPTLTIP 182
Cdd:PRK14950 434 AAIPVDEKPKYTPP 447