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Conserved domains on  [gi|27545299|ref|NP_775381|]
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dystroglycan 1 precursor [Danio rerio]

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 ...
 580-866 2.37e-143

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: 425.57  E-value: 2.37e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   580 VLFTAVFDGDARTVTNDIHKKILLVKKLSQSFGDRNSSTITLKSITKGSIIVEWTNNSLQQSPCPKDQIQQLSKKISDPE 659
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   660 GKPSSIFKFTMEPDFRPSNITVRGTASCRNYMFVP---LGEIPDPTPSPGTPAVGAGRQSTDDVYLHTVIPAVVVAAILL 736
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPtnqLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   737 IAGIIAMICYRKKRKGKLTIEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKPPLPPPEYPNMATPETTPLNQD 816
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 27545299   817 LLGEYTPLHDEDPNAPPYQPPPPFSTPMEGKGSRPKNMTPYRSPPPYVPP 866
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 192-314 4.70e-76

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: 242.86  E-value: 4.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   192 CGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 271
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 27545299   272 LGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKP 314
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 79-171 1.98e-33

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: 124.01  E-value: 1.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299  79 GFPDSSAVVGRVFRLQVPIKA-KDSGSIVKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNE-SKVSQS 156
Cdd:cd11303   5 GIPDLVAVVGRLFTYKIPPDTfSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDKgSAGSQA 84

                        90
                ....*....|....*
gi 27545299 157 PDVFSIEVHPEEHAE 171
Cdd:cd11303  85 SDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 476-570 1.74e-17

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: 78.15  E-value: 1.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299    476 NPIDQVNAYVGTYFEVKVPSDTFFDkEDGTTDKLRLTLRKGNdvvADDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATD 555
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTD-ADGDTLTYSATLSDGS---ALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATD 77

                           90
                   ....*....|....*
gi 27545299    556 KGGLYAMDAFEVRVS 570
Cdd:smart00736  78 SSGASASDTFTITVV 92
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 285-412 9.03e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   285 SSVQVPAKEG--TMSAQLGYPVVGWHIANKKPHVPKRVRRQlNNTPTPIPSLLPPT---TYPEP------PIRIVPTP-- 351
Cdd:pfam05109 456 TNLTAPASTGptVSTADVTSPTPAGTTSGASPVTPSPSPRD-NGTESKAPDMTSPTsavTTPTPnatsptPAVTTPTPna 534

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27545299   352 TSPSIAPTSESSAppVRGPVPLPVKPTIRNRDSAP--STPTLGPPLPTRVMVTTSTIAIQPTM 412
Cdd:pfam05109 535 TSPTLGKTSPTSA--VTTPTPNATSPTPAVTTPTPnaTIPTLGKTSPTSAVTTPTPNATSPTV 595
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 580-866 2.37e-143

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: 425.57  E-value: 2.37e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   580 VLFTAVFDGDARTVTNDIHKKILLVKKLSQSFGDRNSSTITLKSITKGSIIVEWTNNSLQQSPCPKDQIQQLSKKISDPE 659
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   660 GKPSSIFKFTMEPDFRPSNITVRGTASCRNYMFVP---LGEIPDPTPSPGTPAVGAGRQSTDDVYLHTVIPAVVVAAILL 736
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPtnqLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   737 IAGIIAMICYRKKRKGKLTIEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKPPLPPPEYPNMATPETTPLNQD 816
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 27545299   817 LLGEYTPLHDEDPNAPPYQPPPPFSTPMEGKGSRPKNMTPYRSPPPYVPP 866
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 192-314 4.70e-76

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: 242.86  E-value: 4.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   192 CGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 271
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 27545299   272 LGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKP 314
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 192-314 2.05e-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: 203.33  E-value: 2.05e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299 192 CGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 271
Cdd:cd11305   2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 27545299 272 LGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKP 314
Cdd:cd11305  82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 79-171 1.98e-33

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: 124.01  E-value: 1.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299  79 GFPDSSAVVGRVFRLQVPIKA-KDSGSIVKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNE-SKVSQS 156
Cdd:cd11303   5 GIPDLVAVVGRLFTYKIPPDTfSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDKgSAGSQA 84

                        90
                ....*....|....*
gi 27545299 157 PDVFSIEVHPEEHAE 171
Cdd:cd11303  85 SDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 476-570 1.74e-17

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: 78.15  E-value: 1.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299    476 NPIDQVNAYVGTYFEVKVPSDTFFDkEDGTTDKLRLTLRKGNdvvADDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATD 555
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTD-ADGDTLTYSATLSDGS---ALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATD 77

                           90
                   ....*....|....*
gi 27545299    556 KGGLYAMDAFEVRVS 570
Cdd:smart00736  78 SSGASASDTFTITVV 92
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 478-569 3.03e-13

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: 66.23  E-value: 3.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299 478 IDQVNAYVGTYFEVKVPSDTFFDKEDgttdKLRLTLRKGNDVvadDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATDKG 557
Cdd:cd11303   6 IPDLVAVVGRLFTYKIPPDTFSGNGD----TYQVSEAGKDDL---PSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDKG 78

                        90
                ....*....|....
gi 27545299 558 --GLYAMDAFEVRV 569
Cdd:cd11303  79 saGSQASDVFSIDV 92
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 78-170 1.47e-11

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: 61.59  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299     78 SGFPDSSAVVGRVFRLQVP---IKAKDSGSI-VKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNESKV 153
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPsstFTDADGDTLtYSATLSDGSALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSGA 81

                           90
                   ....*....|....*..
gi 27545299    154 SQSpDVFSIEVHPEEHA 170
Cdd:smart00736  82 SAS-DTFTITVVNTNDA 97
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 285-412 9.03e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   285 SSVQVPAKEG--TMSAQLGYPVVGWHIANKKPHVPKRVRRQlNNTPTPIPSLLPPT---TYPEP------PIRIVPTP-- 351
Cdd:pfam05109 456 TNLTAPASTGptVSTADVTSPTPAGTTSGASPVTPSPSPRD-NGTESKAPDMTSPTsavTTPTPnatsptPAVTTPTPna 534

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27545299   352 TSPSIAPTSESSAppVRGPVPLPVKPTIRNRDSAP--STPTLGPPLPTRVMVTTSTIAIQPTM 412
Cdd:pfam05109 535 TSPTLGKTSPTSA--VTTPTPNATSPTPAVTTPTPnaTIPTLGKTSPTSAVTTPTPNATSPTV 595
PHA03247 PHA03247
large tegument protein UL36; Provisional
 321-462 1.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   321 RRQLNNTPTPIPSLL---PPTTYPEPP----IRIVPTPTSPSIAPTSESSAPPVRGPVPLPVKPTIRNRDSAPSTP--TL 391
Cdd:PHA03247 2685 RRAARPTVGSLTSLAdppPPPPTPEPAphalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPptTA 2764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   392 GPPLPTRVMVTTSTiaIQPTMTRPVYVGASVT---------PATPTTRKPTKRPPKKPKTTPIPREPKTTTTKPPRRSTP 462
Cdd:PHA03247 2765 GPPAPAPPAAPAAG--PPRRLTRPAVASLSESreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 81-164 6.03e-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: 39.76  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299    81 PDSSAVVGRVFRLQVP---IKAKDSGSIVKITE-ASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNESKVSQS 156
Cdd:pfam05345   8 ADQTATVGTPYSFTLSasgGSDPYGGSTVTYSTtATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATDSSGLSSS 87


                  ....*...
gi 27545299   157 pDVFSIEV 164
Cdd:pfam05345  88 -TTFTLTV 94
 
Name Accession Description Interval E-value
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
 580-866 2.37e-143

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: 425.57  E-value: 2.37e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   580 VLFTAVFDGDARTVTNDIHKKILLVKKLSQSFGDRNSSTITLKSITKGSIIVEWTNNSLQQSPCPKDQIQQLSKKISDPE 659
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   660 GKPSSIFKFTMEPDFRPSNITVRGTASCRNYMFVP---LGEIPDPTPSPGTPAVGAGRQSTDDVYLHTVIPAVVVAAILL 736
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPtnqLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   737 IAGIIAMICYRKKRKGKLTIEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKPPLPPPEYPNMATPETTPLNQD 816
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 27545299   817 LLGEYTPLHDEDPNAPPYQPPPPFSTPMEGKGSRPKNMTPYRSPPPYVPP 866
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290
a_DG1_N2 pfam18424
Alpha-Dystroglycan N-terminal domain 2; This is the second N-terminal domain found in ...
 192-314 4.70e-76

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: 242.86  E-value: 4.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   192 CGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 271
Cdd:pfam18424   1 CGPEEPVTVLTVILDADLTKMTPKQRVDLLHRMRKFSEVPLHHMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 27545299   272 LGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKP 314
Cdd:pfam18424  81 LGCALDQSSIPDISSVEAPAKEGTMSAQLGYPVVGWHIANKKP 123
alpha_DG_C cd11305
C-terminal domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely distributed in ...
 192-314 2.05e-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: 203.33  E-value: 2.05e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299 192 CGNEEPVTVLTVILDADLTKMSSKQRVELLAKMKKFSGMGLQHMKILPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 271
Cdd:cd11305   2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 27545299 272 LGCSLDQSSIPDISSVQVPAKEGTMSAQLGYPVVGWHIANKKP 314
Cdd:cd11305  82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 79-171 1.98e-33

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: 124.01  E-value: 1.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299  79 GFPDSSAVVGRVFRLQVPIKA-KDSGSIVKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNE-SKVSQS 156
Cdd:cd11303   5 GIPDLVAVVGRLFTYKIPPDTfSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDKgSAGSQA 84

                        90
                ....*....|....*
gi 27545299 157 PDVFSIEVHPEEHAE 171
Cdd:cd11303  85 SDVFSIDVHPEPHPE 99
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 476-570 1.74e-17

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: 78.15  E-value: 1.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299    476 NPIDQVNAYVGTYFEVKVPSDTFFDkEDGTTDKLRLTLRKGNdvvADDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATD 555
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTD-ADGDTLTYSATLSDGS---ALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATD 77

                           90
                   ....*....|....*
gi 27545299    556 KGGLYAMDAFEVRVS 570
Cdd:smart00736  78 SSGASASDTFTITVV 92
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 81-169 3.25e-15

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: 71.99  E-value: 3.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299  81 PDSSAVVGR---VFRLQVPI-KAKDSGSIVKITEASKDVLPAWLHWDAESGTLQGL--PLETDKGVHYISVS-VSNESKV 153
Cdd:cd00031   2 PDGSAVEGRsrgSFRVSIPTdLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLekLDREDKGVHYISVSaASLGANV 81

                        90
                ....*....|....*.
gi 27545299 154 SQSPDVFSIEVHPEEH 169
Cdd:cd00031  82 PQTSSVFSIEVYDEND 97
Dystroglycan_repeat cd11303
Cadherin-like repeat domain of alpha dystroglycan; Dystroglycan is a glycoprotein widely ...
 478-569 3.03e-13

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: 66.23  E-value: 3.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299 478 IDQVNAYVGTYFEVKVPSDTFFDKEDgttdKLRLTLRKGNDVvadDSWIQFNSTSQLLYGLPDQEHAGKHEYFMQATDKG 557
Cdd:cd11303   6 IPDLVAVVGRLFTYKIPPDTFSGNGD----TYQVSEAGKDDL---PSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDKG 78

                        90
                ....*....|....
gi 27545299 558 --GLYAMDAFEVRV 569
Cdd:cd11303  79 saGSQASDVFSIDV 92
CADG smart00736
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
 78-170 1.47e-11

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: 61.59  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299     78 SGFPDSSAVVGRVFRLQVP---IKAKDSGSI-VKITEASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNESKV 153
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPsstFTDADGDTLtYSATLSDGSALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSGA 81

                           90
                   ....*....|....*..
gi 27545299    154 SQSpDVFSIEVHPEEHA 170
Cdd:smart00736  82 SAS-DTFTITVVNTNDA 97
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 285-412 9.03e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   285 SSVQVPAKEG--TMSAQLGYPVVGWHIANKKPHVPKRVRRQlNNTPTPIPSLLPPT---TYPEP------PIRIVPTP-- 351
Cdd:pfam05109 456 TNLTAPASTGptVSTADVTSPTPAGTTSGASPVTPSPSPRD-NGTESKAPDMTSPTsavTTPTPnatsptPAVTTPTPna 534

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27545299   352 TSPSIAPTSESSAppVRGPVPLPVKPTIRNRDSAP--STPTLGPPLPTRVMVTTSTIAIQPTM 412
Cdd:pfam05109 535 TSPTLGKTSPTSA--VTTPTPNATSPTPAVTTPTPnaTIPTLGKTSPTSAVTTPTPNATSPTV 595
PHA03247 PHA03247
large tegument protein UL36; Provisional
 321-462 1.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   321 RRQLNNTPTPIPSLL---PPTTYPEPP----IRIVPTPTSPSIAPTSESSAPPVRGPVPLPVKPTIRNRDSAPSTP--TL 391
Cdd:PHA03247 2685 RRAARPTVGSLTSLAdppPPPPTPEPAphalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPptTA 2764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   392 GPPLPTRVMVTTSTiaIQPTMTRPVYVGASVT---------PATPTTRKPTKRPPKKPKTTPIPREPKTTTTKPPRRSTP 462
Cdd:PHA03247 2765 GPPAPAPPAAPAAG--PPRRLTRPAVASLSESreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 336-425 2.57e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.80  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299  336 PPTTYPEPPIRIVPTPTSPSIAPTSESSAPPVRGPVPLPVKPTIRNRDSAPSTPTLGPPLPTRVMVTTSTIAIQPTMTRP 415
Cdd:PRK14950 363 VPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKP 442

                         90
                 ....*....|
gi 27545299  416 VYVGASVTPA 425
Cdd:PRK14950 443 KYTPPAPPKE 452
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 329-487 3.46e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   329 TPIPSLLPPTTYPEPPIRIVPTPTSPSIAPTSESSAPPVRGPVPLPVKPTI--RNRDSAPSTPTLGPPLPTRVMVTTSTI 406
Cdd:pfam05109 489 TPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLgkTSPTSAVTTPTPNATSPTPAVTTPTPN 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   407 AIQPTMTRPVYVGASVTPATPTTrkptkrppkkpkttpiprEPKTTTTKPPRRSTPAVIGDSNIKPELRNPIDQVNAYVG 486
Cdd:pfam05109 569 ATIPTLGKTSPTSAVTTPTPNAT------------------SPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVT 630


                  .
gi 27545299   487 T 487
Cdd:pfam05109 631 T 631
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 81-164 6.03e-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: 39.76  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299    81 PDSSAVVGRVFRLQVP---IKAKDSGSIVKITE-ASKDVLPAWLHWDAESGTLQGLPLETDKGVHYISVSVSNESKVSQS 156
Cdd:pfam05345   8 ADQTATVGTPYSFTLSasgGSDPYGGSTVTYSTtATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTATDSSGLSSS 87


                  ....*...
gi 27545299   157 pDVFSIEV 164
Cdd:pfam05345  88 -TTFTLTV 94
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 328-396 8.37e-04

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 40.06  E-value: 8.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27545299   328 PTPIPSLLPPTTYPEPPIRIVPTPTSP--SIAPTSESSAPPVrGPVPLPVKPTIRNRDSAPSTPTLGPPLP 396
Cdd:pfam12526  33 ESAHPDPPPPVGDPRPPVVDTPPPVSAvwVLPPPSEPAAPEP-DLVPPVTGPAGPPSPLAPPAPAQKPPLP 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 317-479 1.78e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   317 PKRVRRqlnntPTPIPSLLPPTTYPEPPIRIVPTPTSPSIAPTSESSAPPVRGPVPLPvkptiRNRDSAPSTPTLGPPLP 396
Cdd:PHA03247 2658 PGRVSR-----PRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEP-----APHALVSATPLPPGPAA 2727

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   397 TRVMVTTSTIAIQPtmtrPVYVGASVTPATPTTRKPTKRPPKKPKttpiPREPKTTTTKPPRRST-PAVIGDSNIKPELR 475
Cdd:PHA03247 2728 ARQASPALPAAPAP----PAVPAGPATPGGPARPARPPTTAGPPA----PAPPAAPAAGPPRRLTrPAVASLSESRESLP 2799


                  ....
gi 27545299   476 NPID 479
Cdd:PHA03247 2800 SPWD 2803
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 310-421 9.17e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545299   310 ANKKPHVPKR---VRRQLNNTPTPIPSLLPPTTYPEPpirivptPTSPSIAPtSESSAPPVRgpvPLPVKPTIRNRDSAP 386
Cdd:pfam17380  56 LDSRVFKPMRkyeTAKTIITTPAPIPSSYPVSAEVSP-------PGAPAAAP-EEFVFSTIR---PKSRKPKARTRGKKR 124

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 27545299   387 STPTLGPPLPTRVMVTTSTIAIQPTMTRPVYVGAS 421
Cdd:pfam17380 125 KTTTTMIQTTTPMMVTTSSSALEMTTTPKIVIFAS 159
 
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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