second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  186 QRKTIRALLAWVQRKTRKYGVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLE 265
Cdd:cd21245      1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  266 PEDVMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245     81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  186 QRKTIRALLAWVQRKTRKYGVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLE 265
Cdd:cd21245      1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  266 PEDVMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245     81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  191 RALLAWVQRKTRKYG--VAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQ--ALEDSMRENLEKAFSIAHDALHIPR-LLE 265
Cdd:pfam00307    5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  266 PEDvMVDtPDEQSIVTYVAQFLEHFP 291
Cdd:pfam00307   85 PED-LVE-GDNKSVLTYLASLFRRFQ 108

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555    36 RTFTRWINLHLEKcNPPLEVKDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033    1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 1823878555   115 DAAEIADGNPsLVLGLIWNIILF 137
Cdd:smart00033   80 EPEDLVEGPK-LILGVIWTLISL 101

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  186 QRKTIRALLAWVQRKTRKYGVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLE 265
Cdd:cd21245      1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  266 PEDVMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245     81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   29 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1823878555  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   29 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1823878555  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21190     81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   32 NVQKRTFTRWINLHLEKCNPPLeVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21186      1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKL 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1823878555  112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21186     78 VNISSNDIVDGNPKLTLGLVWSIILHWQVK 107

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   22 RVQNLQVERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21246      5 RIKALADEREAVQKKTFTKWVNSHLARVG--CRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKM-RIHCLENVDKAL 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1823878555  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21246     82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   33 VQKRTFTRWINLHLEKCNPPleVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21188      3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRE--RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                           90       100
                   ....*....|....*....|....*..
gi 1823878555  113 SIDAAEIADGNPSLVLGLIWNIILFFQ 139
Cdd:cd21188     79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  182 SVKDqrktirALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHI 260
Cdd:cd21194      2 SAKD------ALLLWCQRKTAGYpGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGI 75

                           90       100       110
                   ....*....|....*....|....*....|
gi 1823878555  261 PRLLEPEDVMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21194     76 AKLLDAEDVDVARPDEKSIMTYVASYYHYF 105

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   31 ENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAG--TQIENIEEDFRDGLKLMLLLEVISGERLPKPERGKM-RFHKIANVNKALDFIASKGVK 79

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  111 LVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21214     80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  186 QRKTIRALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLL 264
Cdd:cd21249      2 LRSAKEALLIWCQRKTAGYtNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81

                           90       100
                   ....*....|....*....|....*.
gi 1823878555  265 EPEDVMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21249     82 DPEDVAVPHPDERSIMTYVSLYYHYF 107

second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  182 SVKDqrktirALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHI 260
Cdd:cd21248      2 SAKD------ALLLWCQMKTAGYpNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGL 75

                           90       100       110
                   ....*....|....*....|....*....|
gi 1823878555  261 PRLLEPEDVMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21248     76 TKLLDPEDVNVEQPDEKSIITYVVTYYHYF 105

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   31 ENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21215      2 VDVQKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVK 79

                           90       100
                   ....*....|....*....|....*...
gi 1823878555  111 LVSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21215     80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   29 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21235      2 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1823878555  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21235     78 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDI 112

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   33 VQKRTFTRWINLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE-DSNVKL 111
Cdd:cd21311     15 IQQNTFTRWANEHLKTANKHIA--DLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEeDEGIKI 92

                           90       100
                   ....*....|....*....|....*....
gi 1823878555  112 VSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21311     93 VNIDSSDIVDGKLKLILGLIWTLILHYSI 121

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  192 ALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLEPEDVM 270
Cdd:cd21216     14 GLLLWCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIV 93

                           90       100
                   ....*....|....*....|.
gi 1823878555  271 -VDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21216     94 nTPRPDERSVMTYVSCYYHAF 114

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  191 RALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLEPEDV 269
Cdd:cd21187      3 KTLLAWCRQSTRGYeQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82

                           90       100
                   ....*....|....*....|..
gi 1823878555  270 MVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21187     83 NVEQPDKKSILMYVTSLFQVLP 104

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   33 VQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21183      4 IQANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLSTRPLKRSYnRRPAFQQHYLENVSTALKFIEADHIKL 81

                           90       100
                   ....*....|....*....|....*..
gi 1823878555  112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21183     82 VNIGSGDIVNGNIKLILGLIWTLILHY 108

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   33 VQKRTFTRWINLHLEkcNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21227      4 IQKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLV 81

                           90       100
                   ....*....|....*....|....*...
gi 1823878555  113 SIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21227     82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  193 LLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAhDALHIPRLLEPEDVMV 271
Cdd:cd21239      6 LLLWSQQMTEGYtGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKLGVTRLLDPEDVDV 84

                           90       100
                   ....*....|....*....|
gi 1823878555  272 DTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21239     85 SSPDEKSVITYVSSLYDVFP 104

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555  190 IRALLAWVQRKTRKY-GVAVQDFASSWRSGLAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHDALHIPRLLEPED 268
Cdd:cd21197      2 IQALLRWCRRQCEGYpGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAED 81

                           90       100
                   ....*....|....*....|...
gi 1823878555  269 -VMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21197     82 mVTMHVPDRLSIITYVSQYYNHF 104

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   22 RVQNLQVERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21316     42 RIKALADEREAVQKKTFTKWVNSHLARVS--CRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRM-RIHCLENVDKAL 118

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1823878555  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21316    119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823878555   16 GQISDIRVQNLQVERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLlheyKSSSHRIFR-- 93
Cdd:cd21247      3 TEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL----PRPSRGKMRvh 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1823878555   94 -LNNIAKALKFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21247     79 fLENNSKAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125