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Conserved domains on  [gi|33859532|ref|NP_034147|]
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dystroglycan 1 preproprotein [Mus musculus]

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 ...
 604-893 1.97e-154

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: 454.84  E-value: 1.97e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   604 ARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   684 GKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 33859532   844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 180-302 1.19e-73

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: 237.09  E-value: 1.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 33859532   260 LGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 302
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 60-161 1.17e-38

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: 139.03  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  60 PTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLgan 139
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77

                        90       100
                ....*....|....*....|..
gi 33859532 140 GSHVPQTSSVFSIEVYPEDHNE 161
Cdd:cd11303  78 GSAGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 496-600 1.23e-28

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: 110.14  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532 496 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 575
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                        90       100
                ....*....|....*....|....*..
gi 33859532 576 HATDKG--GLSAVDAFEIHVHKRPQGD 600
Cdd:cd11303  73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
301-414 2.06e-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: 45.15  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  301 KPTLPKRLRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 377
Cdd:PRK14971 376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 33859532  378 PTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAV 414
Cdd:PRK14971 453 KEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAP 489
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 604-893 1.97e-154

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: 454.84  E-value: 1.97e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   604 ARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   684 GKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 33859532   844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 180-302 1.19e-73

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: 237.09  E-value: 1.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 33859532   260 LGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 302
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 180-302 7.21e-63

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: 207.57  E-value: 7.21e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532 180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:cd11305   2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33859532 260 LGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 302
Cdd:cd11305  82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 60-161 1.17e-38

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: 139.03  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  60 PTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLgan 139
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77

                        90       100
                ....*....|....*....|..
gi 33859532 140 GSHVPQTSSVFSIEVYPEDHNE 161
Cdd:cd11303  78 GSAGSQASDVFSIDVHPEPHPE 99
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 496-600 1.23e-28

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: 110.14  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532 496 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 575
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                        90       100
                ....*....|....*....|....*..
gi 33859532 576 HATDKG--GLSAVDAFEIHVHKRPQGD 600
Cdd:cd11303  73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 499-594 1.74e-23

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: 95.49  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532    499 NHIDRVDAWVGTYFEVKIPSDTFYDNEdttTDKLKLTLKLREQQLVgeKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHAT 578
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTDAD---GDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTAT 76

                           90
                   ....*....|....*.
gi 33859532    579 DKGGLSAVDAFEIHVH 594
Cdd:smart00736  77 DSSGASASDTFTITVV 92
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 62-160 5.33e-18

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: 79.69  E-value: 5.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532     62 VVGIPDGTAVVGRSFRVSIPTDLIA-SSGEIIKVSAAGKE--ALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGA 138
Cdd:smart00736   1 ANAIGDQTATEGESFSYTIPSSTFTdADGDTLTYSATLSDgsALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSG 80

                           90       100
                   ....*....|....*....|..
gi 33859532    139 ngshvPQTSSVFSIEVYPEDHN 160
Cdd:smart00736  81 -----ASASDTFTITVVNTNDA 97
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
301-414 2.06e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.15  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  301 KPTLPKRLRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 377
Cdd:PRK14971 376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 33859532  378 PTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAV 414
Cdd:PRK14971 453 KEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAP 489
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 59-154 2.64e-03

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: 37.84  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532    59 VPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVS---AAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAAR 135
Cdd:pfam05345   1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTystTATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATD 80

                          90
                  ....*....|....*....
gi 33859532   136 LGANgshvpQTSSVFSIEV 154
Cdd:pfam05345  81 SSGL-----SSSTTFTLTV 94
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 604-893 1.97e-154

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: 454.84  E-value: 1.97e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   604 ARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   684 GKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 33859532   844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 180-302 1.19e-73

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: 237.09  E-value: 1.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 33859532   260 LGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 302
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 180-302 7.21e-63

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: 207.57  E-value: 7.21e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532 180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:cd11305   2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33859532 260 LGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKP 302
Cdd:cd11305  82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 60-161 1.17e-38

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: 139.03  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  60 PTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLgan 139
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77

                        90       100
                ....*....|....*....|..
gi 33859532 140 GSHVPQTSSVFSIEVYPEDHNE 161
Cdd:cd11303  78 GSAGSQASDVFSIDVHPEPHPE 99
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 65-160 8.62e-35

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: 127.85  E-value: 8.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  65 IPDGTAVVGR---SFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGL--PLDTDKGVHYISVSAARLGAN 139
Cdd:cd00031   1 IPDGSAVEGRsrgSFRVSIPTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLekLDREDKGVHYISVSAASLGAN 80

                        90       100
                ....*....|....*....|.
gi 33859532 140 gshVPQTSSVFSIEVYPEDHN 160
Cdd:cd00031  81 ---VPQTSSVFSIEVYDENDN 98
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 496-600 1.23e-28

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: 110.14  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532 496 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 575
Cdd:cd11303   1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                        90       100
                ....*....|....*....|....*..
gi 33859532 576 HATDKG--GLSAVDAFEIHVHKRPQGD 600
Cdd:cd11303  73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 499-594 1.74e-23

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: 95.49  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532    499 NHIDRVDAWVGTYFEVKIPSDTFYDNEdttTDKLKLTLKLREQQLVgeKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHAT 578
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTDAD---GDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTAT 76

                           90
                   ....*....|....*.
gi 33859532    579 DKGGLSAVDAFEIHVH 594
Cdd:smart00736  77 DSSGASASDTFTITVV 92
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 62-160 5.33e-18

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: 79.69  E-value: 5.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532     62 VVGIPDGTAVVGRSFRVSIPTDLIA-SSGEIIKVSAAGKE--ALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGA 138
Cdd:smart00736   1 ANAIGDQTATEGESFSYTIPSSTFTdADGDTLTYSATLSDgsALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSG 80

                           90       100
                   ....*....|....*....|..
gi 33859532    139 ngshvPQTSSVFSIEVYPEDHN 160
Cdd:smart00736  81 -----ASASDTFTITVVNTNDA 97
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
301-414 2.06e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.15  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  301 KPTLPKRLRRQIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQT 377
Cdd:PRK14971 376 KQHIKPVFTQPAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQF 452

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 33859532  378 PTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAV 414
Cdd:PRK14971 453 KEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAP 489
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-494 2.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   277 TPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPT-TAIQEPPSRIVPTPTSPAIAPPTETM--A 353
Cdd:PHA03247 2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESResL 2798

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   354 PPVRDPVPGKPTVTIRTRG-AIIQTP-TLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEP------------TAVITPPT 419
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAAlPPAASPaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrppsrsPAAKPAAP 2878

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   420 TTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIR----------TTTSGVPRGG 489
Cdd:PHA03247 2879 ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRpqpplapttdPAGAGEPSGA 2958


                  ....*
gi 33859532   490 EPNQR 494
Cdd:PHA03247 2959 VPQPW 2963
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 59-154 2.64e-03

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: 37.84  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532    59 VPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVS---AAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAAR 135
Cdd:pfam05345   1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTystTATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATD 80

                          90
                  ....*....|....*....
gi 33859532   136 LGANgshvpQTSSVFSIEV 154
Cdd:pfam05345  81 SSGL-----SSSTTFTLTV 94
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 315-406 3.63e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532  315 TPTPVTAIGPPTTAIQEP--PSRIVPTPTSPAIAPPTETmAPPVRDPVPgKPTVTIRTrgaiiQTPTLGPIQPTRVSEAG 392
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPvrPTPAPSTRPKAAAAANIPP-KEPVRETAT-PPPVPPRP-----VAPPVPHTPESAPKLTR 433

                         90
                 ....*....|....
gi 33859532  393 TTVPGQIRPTLTIP 406
Cdd:PRK14950 434 AAIPVDEKPKYTPP 447
PHA03247 PHA03247
large tegument protein UL36; Provisional
 270-491 6.13e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   270 PDIRGVETPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPTTAIQePPSRIVPTPTSPAIAPPT 349
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR-PTVGSLTSLADPPPPPPT 2707

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859532   350 ETMAPPVRDPVPGKPTVTIRTRGAIIQTPtLGPIQPTrvSEAGTTVPGQIRPTLTIPGYVEPTAVITPPTTTTKKPRVST 429
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALP-AAPAPPA--VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33859532   430 PKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSGVPRGGEP 491
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846
 
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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