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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 604 ARFKAKLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIVGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 684 GKPRPAFSNALEPDFKALSVAVAGSGSCRHLQFIPVAPPSPGTSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958794263 844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263  60 PTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLgan 139
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDTYQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISVTAEDK--- 77

                          90       100
                  ....*....|....*....|..
gi 1958794263 140 GSHVPQTASVFSIEVYPEDHSE 161
Cdd:cd11303    78 GSAGSQASDVFSIDVHPEPHPE 99

DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 311 QIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQTPTLGPIPPTR 387
Cdd:PRK14971  386 PAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQFKEEKKIPVSK 462

                          90
                  ....*....|....*
gi 1958794263 388 VSEAGTTVPGQIRPT 402
Cdd:PRK14971  463 VSSLGPSTLRPIQEK 477

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 604 ARFKAKLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIVGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 684 GKPRPAFSNALEPDFKALSVAVAGSGSCRHLQFIPVAPPSPGTSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958794263 844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELNNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:cd11305     2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958794263 260 LGCSLNQNSVPDIRGVETPAREGTMSAHLGYPVVGWHIANKKP 302
Cdd:cd11305    82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 496 ELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTttdklkltLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFM 575
Cdd:cd11303     1 SPLWGIPDLVAVVGRLFTYKIPPDTFSGNGDT--------YQVSEAGKDDLPSWLQFDSSSRTLYGLPLSDDVGVHYISV 72

                          90       100
                  ....*....|....*....|....*..
gi 1958794263 576 HATDKG--GLSAVDAFEIHVHKRPQGD 600
Cdd:cd11303    73 TAEDKGsaGSQASDVFSIDVHPEPHPE 99

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263   62 VVGIPDGTAVVGRSFRVSIPTDLIA-SSGEIIKVSAAGKE--ALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGA 138
Cdd:smart00736   1 ANAIGDQTATEGESFSYTIPSSTFTdADGDTLTYSATLSDgsALPSWLSFDSDTGTLSGTPTNSDVGSLSLKVTATDSSG 80

                           90       100
                   ....*....|....*....|...
gi 1958794263  139 ngshvpQTAS-VFSIEVYPEDHS 160
Cdd:smart00736  81 ------ASASdTFTITVVNTNDA 97

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263  277 TPAREGTMSAHLGYPVVGWHIANKKPTLPKRIRRQIHATPTPVTAIGPPT-TAIQEPPSRIVPTPTSPAIAPPTETM--A 353
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPApAPPAAPAAGPPRRLTRPAVASLSESResL 2798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263  354 PPVRDPVPGKPTVTIRTRG-AIIQTP-TLGPIPPTRVSEAGTTVPGQIRPTLTIPGYV------------EPTAVVTPPT 419
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAAlPPAASPaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAP 2878

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794263  420 TTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSAVPRGGEANQ 493
Cdd:PHA03247  2879 ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 604 ARFKAKLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIVGLSRRIADEN 683
Cdd:pfam05454   1 VFFKAKFSGDHERVNNDIHKKILLVKKLAFAFGDRNSSTITLRSITKGSIIVEWTNNTLPHEPCPKEQVAGLSKKILDSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 684 GKPRPAFSNALEPDFKALSVAVAGSGSCRHLQFIPVAPPSPGTSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILL 763
Cdd:pfam05454  81 GSPREAFKNALEPEFKLTNISVVGSGSCRHTEFIPTNQLDYIPSRTPPTGTPDRPTEKSSEDDVYLHTVIPAVVVAAILL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 764 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQD 843
Cdd:pfam05454 161 IAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILKEEKPPLPPPEYPNQNVPETTPLNQD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958794263 844 TVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 893
Cdd:pfam05454 241 LLGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP 290

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 180 CAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELNNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWK 259
Cdd:cd11305     2 CPNGEPVTVLTVILDADLSKLTPKQRVHLLNKLAKFLGLPLDAFKLLPVSNNGLFDMSALMAGPGNVKKANEAGTLLSWQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958794263 260 LGCSLNQNSVPDIRGVETPAREGTMSAHLGYPVVGWHIANKKP 302
Cdd:cd11305    82 VGCGGDLNHLPLVSQLEEQAKDGTLAEVLGLPVIGWHVANKKP 124

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263  65 IPDGTAVVGR---SFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGL--PLDTDKGVHYISVSAARLGAN 139
Cdd:cd00031     1 IPDGSAVEGRsrgSFRVSIPTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLekLDREDKGVHYISVSAASLGAN 80

                          90       100
                  ....*....|....*....|
gi 1958794263 140 gshVPQTASVFSIEVYPEDH 159
Cdd:cd00031    81 ---VPQTSSVFSIEVYDEND 97

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263  499 NHIDRVDAWVGTYFEVKIPSDTFYDNEdttTDKLKLTLKLREQQLVgeKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHAT 578
Cdd:smart00736   2 NAIGDQTATEGESFSYTIPSSTFTDAD---GDTLTYSATLSDGSAL--PSWLSFDSDTGTLSGTPTNSDVGSLSLKVTAT 76

                           90
                   ....*....|....*.
gi 1958794263  579 DKGGLSAVDAFEIHVH 594
Cdd:smart00736  77 DSSGASASDTFTITVV 92

DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794263 311 QIHATPTPVTAIG---PPTTAIQEPPSrIVPTPTSPAIAPPTETMAPPvrDPVPGKPTVTIRTRGAIIQTPTLGPIPPTR 387
Cdd:PRK14971  386 PAAAPQPSAAAAAspsPSQSSAAAQPS-APQSATQPAGTPPTVSVDPP--AAVPVNPPSTAPQAVRPAQFKEEKKIPVSK 462

                          90
                  ....*....|....*
gi 1958794263 388 VSEAGTTVPGQIRPT 402
Cdd:PRK14971  463 VSSLGPSTLRPIQEK 477

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794263  59 VPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVS---AAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSA 133
Cdd:pfam05345   1 PPVVTSPADQTATVGTPYSFTLSASGGSDPYGGSTVTystTATGGALPSGLTLNSSTGTISGTPTSVQPGTYTFTVTA 78