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 4102751   29 EGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQ 108
Cdd:cd21246   3 RSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQ 82

                        90       100
                ....*....|....*....|....*
gi 4102751  109 FLKEQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21246  83 FLKEQRVHLENMGSHDIVDGNHRLT 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 4102751   29 EGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQ 108
Cdd:cd21246   3 RSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQ 82

                        90       100
                ....*....|....*....|....*
gi 4102751  109 FLKEQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21246  83 FLKEQRVHLENMGSHDIVDGNHRLT 107

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 4102751      45 KTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLPK--PTKGRMRIHCLENVDKALQFLKEQRVHLENMG 121
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKkkVAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|.
gi 4102751     122 SHDIVDGNHR----LTTLELL 138
Cdd:smart00033  81 PEDLVEGPKLilgvIWTLISL 101

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 4102751   29 EGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQ 108
Cdd:cd21246   3 RSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQ 82

                        90       100
                ....*....|....*....|....*
gi 4102751  109 FLKEQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21246  83 FLKEQRVHLENMGSHDIVDGNHRLT 107

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) 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. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 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 4102751   31 RFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFL 110
Cdd:cd21318  27 RIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRMRIHSLENVDKALQFL 106

                        90       100
                ....*....|....*....|...
gi 4102751  111 KEQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21318 107 KEQRVHLENVGSHDIVDGNHRLT 129

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   29 EGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQ 108
Cdd:cd21193   3 KGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRLRVQKIENVNKALA 82

                        90       100
                ....*....|....*....|....*
gi 4102751  109 FLKEQrVHLENMGSHDIVDGNHRLT 133
Cdd:cd21193  83 FLKTK-VRLENIGAEDIVDGNPRLI 106

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 4102751   42 VQKKTFTKWVNSHLARVSCR-ITDLYTDLRDGRMLIKLLEVLSGERLpKPTKGRMRIHCLENVDKALQFLKEQRVHLENM 120
Cdd:cd21186   2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKL-KPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80

                        90
                ....*....|...
gi 4102751  121 GSHDIVDGNHRLT 133
Cdd:cd21186  81 SSNDIVDGNPKLT 93

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 4102751   29 EGRFKQLQDEREAVQKKTFTKWVNSHLARVSCRI--TDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKA 106
Cdd:cd21247   7 KGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRPSRGKMRVHFLENNSKA 86

                        90       100
                ....*....|....*....|....*.
gi 4102751  107 LQFLKeQRVHLENMGSHDIVDGNHRL 132
Cdd:cd21247  87 ITFLK-TKVPVKLIGPENIVDGDRTL 111

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   32 FKQLQDEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 111
Cdd:cd21236   7 LERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLK 85

                        90       100
                ....*....|....*....|..
gi 4102751  112 EQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21236  86 RRQVKLVNIRNDDITDGNPKLT 107

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 4102751   40 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPK-PTKGRMRIHCLENVDKALQFLKEQRVHLE 118
Cdd:cd21215   2 VDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRyNKNPKMRVQKLENVNKALEFIKSRGVKLT 81

                        90
                ....*....|....*
gi 4102751  119 NMGSHDIVDGNHRLT 133
Cdd:cd21215  82 NIGAEDIVDGNLKLI 96

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; 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. MACF1 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 4102751   37 DEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 116
Cdd:cd21237   1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR-EKGRMRFHRLQNVQIALDFLKQRQVK 79

                        90
                ....*....|....*..
gi 4102751  117 LENMGSHDIVDGNHRLT 133
Cdd:cd21237  80 LVNIRNDDITDGNPKLT 96

first calponin homology (CH) domain found in utrophin and similar proteins; 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. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   41 AVQKKTFTKWVNSHLARV-SCRITDLYTDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVHLEN 119
Cdd:cd21232   1 DVQKKTFTKWINARFSKSgKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVN 79

                        90
                ....*....|....
gi 4102751  120 MGSHDIVDGNHRLT 133
Cdd:cd21232  80 IGGTDIVDGNHKLT 93

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 4102751   42 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLKEQRVHLENM 120
Cdd:cd21227   4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKpLNQHQKLENVTLALKAMAEDGIKLVNI 83

                        90
                ....*....|..
gi 4102751  121 GSHDIVDGNHRL 132
Cdd:cd21227  84 GNEDIVNGNLKL 95

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   38 EREAVQKKTFTKWVNSHLARVS--CRITDLYTDLRDGRMLIKLLEVLSGERLPKPTK-GRMRIHCLENVDKALQFLKEQR 114
Cdd:cd21191   1 ERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKpSSHRIFRLNNIAKALKFLEDSN 80

                        90
                ....*....|....*....
gi 4102751  115 VHLENMGSHDIVDGNHRLT 133
Cdd:cd21191  81 VKLVSIDAAEIADGNPSLV 99

first calponin homology (CH) domain found in filamins; 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. Members of this family contain two copies of the CH domain. The 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 4102751   42 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHLEN 119
Cdd:cd21228   4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRptFRQMKLENVSVALEFLERESIKLVS 83

                        90
                ....*....|...
gi 4102751  120 MGSHDIVDGNHRL 132
Cdd:cd21228  84 IDSSAIVDGNLKL 96

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 4102751     41 AVQKKTFTKWVNSHLAR--VSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFL-KEQRVHL 117
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPK 80

                          90
                  ....*....|....*.
gi 4102751    118 ENMGSHDIVDGNHRLT 133
Cdd:pfam00307  81 VLIEPEDLVEGDNKSV 96

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (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. FLN-C 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 4102751   42 VQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERL-----PKPTKGRMRihcLENVDKALQFLKEQRVH 116
Cdd:cd21310  16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkyhPRPNFRQMK---LENVSVALEFLDREHIK 92

                        90
                ....*....|....*.
gi 4102751  117 LENMGSHDIVDGNHRL 132
Cdd:cd21310  93 LVSIDSKAIVDGNLKL 108

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   44 KKTFTKWVNSHLA-RVSCRITDLYTDLRDGRMLIKLLEVLSGERLPK-PTKGRMRIHCLENVDKALQFLKEQRVH-LENM 120
Cdd:cd00014   1 EEELLKWINEVLGeELPVSITDLFESLRDGVLLCKLINKLSPGSIPKiNKKPKSPFKKRENINLFLNACKKLGLPeLDLF 80

                        90
                ....*....|....*...
gi 4102751  121 GSHDIVDGNHRLTTLELL 138
Cdd:cd00014  81 EPEDLYEKGNLKKVLGTL 98

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   34 QLQDEREAVQKKTFTKWVNSHLARVSC-RITDLYTDLRDGRMLIKLLEVLSGERL----PKPtkgRMRIHCLENVDKALQ 108
Cdd:COG5069   1 MEAKKWQKVQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAgeynETP---ETRIHVMENVSGRLE 77

                        90       100
                ....*....|....*....|....
gi 4102751  109 FLKEQRVHLENMGSHDIVDGNHRL 132
Cdd:COG5069  78 FIKGKGVKLFNIGPQDIVDGNPKL 101

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (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 anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A 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 4102751   40 EAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGR--MRIHCLENVDKALQFLKEQRVHL 117
Cdd:cd21308  18 KKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRptFRQMQLENVSVALEFLDRESIKL 97

                        90
                ....*....|....*
gi 4102751  118 ENMGSHDIVDGNHRL 132
Cdd:cd21308  98 VSIDSKAIVDGNLKL 112

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. 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 4102751   61 RITDLYTDLRDGRMLIKLLEVLSGERLPK-----PTKGRMR-IHcleNVDKALQFLKEQRVHLENMGSH----DIVDGnH 130
Cdd:cd21223  25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLsklrvPAISRLQkLH---NVEVALKALKEAGVLRGGDGGGitakDIVDG-H 100

                ....*...
gi 4102751  131 RLTTLELL 138
Cdd:cd21223 101 REKTLALL 108

third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   38 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLE------VLSGERLPKPTKGRMRIHCLENVDKALQFLK 111
Cdd:cd21298   2 IEETREEKTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDkikpgvVDWSRVNKPFKKLGANMKKIENCNYAVELGK 79

                        90       100
                ....*....|....*....|..
gi 4102751  112 EQRVHLENMGSHDIVDGNHRLT 133
Cdd:cd21298  80 KLKFSLVGIGGKDIYDGNRTLT 101

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four 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 4102751   49 KWVNSHLARVSC---RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRM--RIHCLENVDKALQFLKE--QRVHLEnmg 121
Cdd:cd21218  17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVlsEEDLEKRAEKVLQAAEKlgCKYFLT--- 93

                        90
                ....*....|....
gi 4102751  122 SHDIVDGNHRLTTL 135
Cdd:cd21218  94 PEDIVSGNPRLNLA 107

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   41 AVQKKTFTKWVNSHLARVSCR--ITDLYTDLRDGRMLIKLLEVLSGERL------PKPtkgrmRIHCLENVDKALQFLKE 112
Cdd:cd21285   9 GFDKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIedingcPKN-----RSQMIENIDACLSFLAA 83

                        90
                ....*....|....*..
gi 4102751  113 QRVHLENMGSHDIVDGN 129
Cdd:cd21285  84 KGINIQGLSAEEIRNGN 100

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   36 QDEREavqKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLE-----VLSGERLPKPTKgRMRIHCLENVDKALQFL 110
Cdd:cd21299   1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDkvspgSVNWKHANKPPI-KMPFKKVENCNQVVKIG 74

                        90       100
                ....*....|....*....|..
gi 4102751  111 KEQRVHLENMGSHDIVDGNHRL 132
Cdd:cd21299  75 KQLKFSLVNVAGNDIVQGNKKL 96

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four 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 4102751   37 DEREAvqkktFTKWVNSHLAR---VSCRIT------DLYTDLRDGRMLIKLLE-------VLSGERLPKPtkgrMRIH-C 99
Cdd:cd21217   1 EEKEA-----FVEHINSLLADdpdLKHLLPidpdgdDLFEALRDGVLLCKLINkivpgtiDERKLNKKKP----KNIFeA 71

                        90       100       110
                ....*....|....*....|....*....|
gi 4102751  100 LENVDKALQFLKEQRVHLENMGSHDIVDGN 129
Cdd:cd21217  72 TENLNLALNAAKKIGCKVVNIGPQDILDGN 101

third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   38 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLEVLS----GERLPKPTKGRM--RIHCLENVDKALQFLK 111
Cdd:cd21330   9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIKvpvdWNRVNKPPYPKLgeNMKKLENCNYAVELGK 86

                        90       100
                ....*....|....*....|...
gi 4102751  112 EQ-RVHLENMGSHDIVDGNHRLT 133
Cdd:cd21330  87 NKaKFSLVGIAGQDLNEGNRTLT 109

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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 4102751   45 KTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPT--------KGRMRIhCLENVDKALQFL--KEQR 114
Cdd:cd21304   4 KVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEvtqsevgqKQKLRT-VLDKINRILNLPrwSQQK 82

                        90       100
                ....*....|....*....|.
gi 4102751  115 VHLENMGSHDIVDGNHRLTTL 135
Cdd:cd21304  83 WSVDSIHSKNLVAILHLLVAL 103

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4102751   38 EREAVQKKTFTKWVNShlARVSCRITDLYTDLRDGRMLIKLLEV----LSGERLPKPT----KGRMRIhcLENVDKALQF 109
Cdd:cd21329   2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpVDWGHVNKPPypalGGNMKK--IENCNYAVEL 77

                        90       100
                ....*....|....*....|....*
gi 4102751  110 LKEQ-RVHLENMGSHDIVDGNHRLT 133
Cdd:cd21329  78 GKNKaKFSLVGIAGSDLNEGNKTLT 102

first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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
                ....*....|....*....|....*....|....*....|...
gi 4102751   45 KTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERL 87
Cdd:cd21335   9 KVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKL 51

Hook domain found in nuclear mitotic apparatus protein (NuMA) and similar proteins; NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles, and the alignment and segregation of chromosomes during mitotic cell division. The model corresponds to the N-terminal conserved globular Hook domain of NuMA, which folds as a variant of the helical calponin homology (CH) domain. It directly binds dynein light intermediate chains LIC1 and LIC2 through a conserved hydrophobic patch shared among other Hook adaptors.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4102751   49 KWVNS-HLARvscRITDLyTDLRDGRMLIKLLEVLSGERLPK-----PTKGRMRI 97
Cdd:cd22224   9 SWVNSlKLDD---PIESI-SQLQDGTILLKIIYKLKGEEEEEqildlSVEERLEF 59

second calponin homology (CH) domain found in the family of plastin; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four 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 4102751   49 KWVNSHLARVSC--RITDLYTDLRDGRMLIKLLEVLSGERLPKPTKG------RMRIHC-LENVDK--ALQFLKEQrvhl 117
Cdd:cd21295  19 RWVNYHLERAGCdrRIKNFSGDIKDSEAYTHLLKQIAPKDAGVDTSAlresdlLQRAELmLQNADKigCRKFVTPK---- 94

                        90
                ....*....|....*
gi 4102751  118 enmgshDIVDGNHRL 132
Cdd:cd21295  95 ------DVVTGNPKL 103