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Conserved domains on  [gi|1622900752|ref|XP_028699080|]
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dystroglycan isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
605-894 1.73e-161

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.


:

Pssm-ID: 461655  Cd Length: 290  Bit Score: 472.94  E-value: 1.73e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 605 VRFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTVTLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDD 684
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 685 GKPRPAFSNALEPDFKATSIAVMGSGSCRHLQFIPVAPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 764
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 765 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 844
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622900752 845 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 894
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
181-303 8.98e-75

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.


:

Pssm-ID: 465761  Cd Length: 123  Bit Score: 240.17  E-value: 8.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 181 CAVDEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 260
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622900752 261 LGCSLNQNSVPDIRGVEAPAREGAMSAQLGYPVVGWHIANKKP 303
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
61-162 4.37e-40

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.


:

Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 142.89  E-value: 4.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  61 PTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLgan 140
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77
                          90       100
                  ....*....|....*....|..
gi 1622900752 141 GSHIPQTSSVFSIEVYPEDHSE 162
Cdd:cd11303    78 GSAGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
497-601 3.17e-29

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.


:

Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 112.07  E-value: 3.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 497 ELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 576
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72
                          90       100
                  ....*....|....*....|....*..
gi 1622900752 577 HATDKG--GLSAVDAFEIHVHRRPQGD 601
Cdd:cd11303    73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
302-403 3.57e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14971:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 614  Bit Score: 44.38  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 302 KPPLPKRIRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 378
Cdd:PRK14971  376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452
                          90       100
                  ....*....|....*....|....*
gi 1622900752 379 PTLGPIQPTRVSEAGTTVPGQIRPT 403
Cdd:PRK14971  453 KEEKKIPVSKVSSLGPSTLRPIQEK 477
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
605-894 1.73e-161

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.


Pssm-ID: 461655  Cd Length: 290  Bit Score: 472.94  E-value: 1.73e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 605 VRFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTVTLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDD 684
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 685 GKPRPAFSNALEPDFKATSIAVMGSGSCRHLQFIPVAPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 764
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 765 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 844
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622900752 845 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 894
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
181-303 8.98e-75

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.


Pssm-ID: 465761  Cd Length: 123  Bit Score: 240.17  E-value: 8.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 181 CAVDEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 260
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622900752 261 LGCSLNQNSVPDIRGVEAPAREGAMSAQLGYPVVGWHIANKKP 303
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
181-303 1.55e-61

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.


Pssm-ID: 206765  Cd Length: 124  Bit Score: 204.10  E-value: 1.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 181 CAVDEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 260
Cdd:cd11305     2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622900752 261 LGCSLNQNSVPDIRGVEAPAREGAMSAQLGYPVVGWHIANKKP 303
Cdd:cd11305    82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
61-162 4.37e-40

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.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 142.89  E-value: 4.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  61 PTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLgan 140
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77
                          90       100
                  ....*....|....*....|..
gi 1622900752 141 GSHIPQTSSVFSIEVYPEDHSE 162
Cdd:cd11303    78 GSAGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
497-601 3.17e-29

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.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 112.07  E-value: 3.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 497 ELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 576
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72
                          90       100
                  ....*....|....*....|....*..
gi 1622900752 577 HATDKG--GLSAVDAFEIHVHRRPQGD 601
Cdd:cd11303    73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
500-598 3.37e-24

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 97.41  E-value: 3.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  500 NHIDRVDAWVGTYFEVKIPSDTFYDHEdttTDKLKLTLKLREQQLVgeKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHAT 579
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTDAD---GDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTAT 76
                           90
                   ....*....|....*....
gi 1622900752  580 DKGGLSAVDAFEIHVHRRP 598
Cdd:smart00736  77 DSSGASASDTFTITVVNTN 95
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
63-161 1.37e-20

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 87.40  E-value: 1.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752   63 VVGIPDGTAVVGRSFRVTIPTDLIA-SSGDIIKVSAAGKE--ALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGA 139
Cdd:smart00736   1 ANAIGDQTATEGESFSYTIPSSTFTdADGDTLTYSATLSDgsALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSG 80
                           90       100
                   ....*....|....*....|..
gi 1622900752  140 ngshiPQTSSVFSIEVYPEDHS 161
Cdd:smart00736  81 -----ASASDTFTITVVNTNDA 97
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
60-155 3.54e-04

Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.


Pssm-ID: 398814 [Multi-domain]  Cd Length: 95  Bit Score: 40.53  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  60 VPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVS---AAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAAR 136
Cdd:pfam05345   1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTystTATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATD 80
                          90
                  ....*....|....*....
gi 1622900752 137 LGANgshipQTSSVFSIEV 155
Cdd:pfam05345  81 SSGL-----SSSTTFTLTV 94
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
302-403 3.57e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.38  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 302 KPPLPKRIRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 378
Cdd:PRK14971  376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452
                          90       100
                  ....*....|....*....|....*
gi 1622900752 379 PTLGPIQPTRVSEAGTTVPGQIRPT 403
Cdd:PRK14971  453 KEEKKIPVSKVSSLGPSTLRPIQEK 477
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
605-894 1.73e-161

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.


Pssm-ID: 461655  Cd Length: 290  Bit Score: 472.94  E-value: 1.73e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 605 VRFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTVTLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDD 684
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 685 GKPRPAFSNALEPDFKATSIAVMGSGSCRHLQFIPVAPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 764
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 765 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 844
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622900752 845 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 894
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
181-303 8.98e-75

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.


Pssm-ID: 465761  Cd Length: 123  Bit Score: 240.17  E-value: 8.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 181 CAVDEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 260
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622900752 261 LGCSLNQNSVPDIRGVEAPAREGAMSAQLGYPVVGWHIANKKP 303
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
181-303 1.55e-61

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.


Pssm-ID: 206765  Cd Length: 124  Bit Score: 204.10  E-value: 1.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 181 CAVDEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 260
Cdd:cd11305     2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622900752 261 LGCSLNQNSVPDIRGVEAPAREGAMSAQLGYPVVGWHIANKKP 303
Cdd:cd11305    82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
61-162 4.37e-40

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.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 142.89  E-value: 4.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  61 PTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLgan 140
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77
                          90       100
                  ....*....|....*....|..
gi 1622900752 141 GSHIPQTSSVFSIEVYPEDHSE 162
Cdd:cd11303    78 GSAGSQASDVFSIDVHPEPHPE 99
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
66-160 1.37e-31

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 118.60  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  66 IPDGTAVVGR---SFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDPQSHTLEGL--PLDTDKGVHYISVSAARLGAN 140
Cdd:cd00031     1 IPDGSAVEGRsrgSFRVSIPTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLekLDREDKGVHYISVSAASLGAN 80
                          90       100
                  ....*....|....*....|
gi 1622900752 141 gshIPQTSSVFSIEVYPEDH 160
Cdd:cd00031    81 ---VPQTSSVFSIEVYDEND 97
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
497-601 3.17e-29

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.


Pssm-ID: 206636 [Multi-domain]  Cd Length: 99  Bit Score: 112.07  E-value: 3.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 497 ELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 576
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72
                          90       100
                  ....*....|....*....|....*..
gi 1622900752 577 HATDKG--GLSAVDAFEIHVHRRPQGD 601
Cdd:cd11303    73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
500-598 3.37e-24

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 97.41  E-value: 3.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  500 NHIDRVDAWVGTYFEVKIPSDTFYDHEdttTDKLKLTLKLREQQLVgeKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHAT 579
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTDAD---GDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTAT 76
                           90
                   ....*....|....*....
gi 1622900752  580 DKGGLSAVDAFEIHVHRRP 598
Cdd:smart00736  77 DSSGASASDTFTITVVNTN 95
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
63-161 1.37e-20

Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.


Pssm-ID: 214795 [Multi-domain]  Cd Length: 97  Bit Score: 87.40  E-value: 1.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752   63 VVGIPDGTAVVGRSFRVTIPTDLIA-SSGDIIKVSAAGKE--ALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGA 139
Cdd:smart00736   1 ANAIGDQTATEGESFSYTIPSSTFTdADGDTLTYSATLSDgsALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSG 80
                           90       100
                   ....*....|....*....|..
gi 1622900752  140 ngshiPQTSSVFSIEVYPEDHS 161
Cdd:smart00736  81 -----ASASDTFTITVVNTNDA 97
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
60-155 3.54e-04

Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.


Pssm-ID: 398814 [Multi-domain]  Cd Length: 95  Bit Score: 40.53  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752  60 VPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVS---AAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAAR 136
Cdd:pfam05345   1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTystTATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATD 80
                          90
                  ....*....|....*....
gi 1622900752 137 LGANgshipQTSSVFSIEV 155
Cdd:pfam05345  81 SSGL-----SSSTTFTLTV 94
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
302-403 3.57e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.38  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 302 KPPLPKRIRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 378
Cdd:PRK14971  376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452
                          90       100
                  ....*....|....*....|....*
gi 1622900752 379 PTLGPIQPTRVSEAGTTVPGQIRPT 403
Cdd:PRK14971  453 KEEKKIPVSKVSSLGPSTLRPIQEK 477
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
316-407 3.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900752 316 TPTPVTAIGPPTTAIQEP--PSRIVPTPTSPAIAPPTETmAPPVRDPVPgKPTVTIRTrgaiiQTPTLGPIQPTRVSEAG 393
Cdd:PRK14950  361 VPVPAPQPAKPTAAAPSPvrPTPAPSTRPKAAAAANIPP-KEPVRETAT-PPPVPPRP-----VAPPVPHTPESAPKLTR 433
                          90
                  ....*....|....
gi 1622900752 394 TTVPGQIRPTMTIP 407
Cdd:PRK14950  434 AAIPVDEKPKYTPP 447
 
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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