calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain 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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                         90       100
                 ....*....|....*....|....*..
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213   81 TSAKDIVDGNLKAIMRLILALAAHFKP 107

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain 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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                         90       100
                 ....*....|....*....|....*..
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213   81 TSAKDIVDGNLKAIMRLILALAAHFKP 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 513126889    24 AYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMHQTS 102
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKiENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 513126889   103 AKDIVDGNlKSIMRLVLALAAH 124
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain 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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                         90       100
                 ....*....|....*....|....*..
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213   81 TSAKDIVDGNLKAIMRLILALAAHFKP 107

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 513126889   23 QAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgNQQEMKNNVEKVLQFvASKKIRMHQTS 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-SEFDKLENINLALDV-AEKKLGVPKVL 82

                          90       100
                  ....*....|....*....|....*.
gi 513126889  103 --AKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:pfam00307  83 iePEDLVEGDNKSVLTYLASLFRRFQ 108

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 513126889  20 QQLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKK 95
Cdd:cd21214    5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVISGE-----RLPKPERGKMRfhkiANVNKALDFIASKG 77

                         90       100
                 ....*....|....*....|...
gi 513126889  96 IRMHQTSAKDIVDGNLKSIMRLV 118
Cdd:cd21214   78 VKLVSIGAEEIVDGNLKMTLGMI 100

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 513126889  21 QLQAYVAWVNAQLKKRPavKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21215    5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTN 82

                         90       100
                 ....*....|....*....|....*
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21215   83 IGAEDIVDGNLKLILGLLWTLILRF 107

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 513126889  22 LQAYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKI-RMHQ 100
Cdd:cd00014    1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79

                         90       100
                 ....*....|....*....|...
gi 513126889 101 TSAKDIV-DGNLKSIMRLVLALA 122
Cdd:cd00014   80 FEPEDLYeKGNLKKVLGTLWALA 102

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 513126889  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21188    4 QKKTFTKWVNKHLIK--ARRRVVDLFEDLRDGHNLISLLEVLSGESL------PRERGRMRfhrlQNVQTALDFLKYRKI 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 513126889  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21188   76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 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-2 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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSpgNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21242    6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGH--NVFQCRSNIETALSFLKNKSIKLIN 83

                         90       100
                 ....*....|....*....|....*
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21242   84 IHVPDIIEGKPSIILGLIWTIILHF 108

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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21190    6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85

                         90       100
                 ....*....|....*....|....*.
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21190   86 INSTDIVDGKPSIVLGLIWTIILYFQ 111

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 513126889  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21246   17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEVLSGERLP-----KPTKGKMRihclENVDKALQFLKEQRV 89

                         90       100
                 ....*....|....*....|....*
gi 513126889  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21246   90 HLENMGSHDIVDGN----HRLTLGL 110

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 513126889    24 AYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMHQTS 102
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKiENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 513126889   103 AKDIVDGNlKSIMRLVLALAAH 124
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101

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 513126889  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21228    5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLV 82

                         90       100
                 ....*....|....*....|....*.
gi 513126889 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21228   83 SIDSSAIVDGNLKLILGLIWTLILHY 108

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 513126889  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVAS-KKIRMH 99
Cdd:cd21311   16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIV 93

                         90       100
                 ....*....|....*....|....*.
gi 513126889 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21311   94 NIDSSDIVDGKLKLILGLIWTLILHY 119

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 513126889  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21191    6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVS 85

                         90       100
                 ....*....|....*....|....*.
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21191   86 IDAAEIADGNPSLVLGLIWNIILFFQ 111

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 513126889  26 VAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGV---QLSPGNQQEMKNNVEKVLQFVASKKIRMHQTS 102
Cdd:cd21304    7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLEVAevtQSEVGQKQKLRTVLDKINRILNLPRWSQQKWS 84

                         90       100
                 ....*....|....*....|...
gi 513126889 103 AKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21304   85 VDSIHSKNLVAILHLLVALARHF 107

first calponin homology (CH) domain found in dystrophin and similar proteins; 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. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by 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, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513126889  21 QLQAYVAWVNAQLKKrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21231    7 QKKTFTKWINAQFAK-FGKPPIEDLFTDLQDGRRLLELLEGLTGQKL--VKEKGSTRVHALNNVNKALQVLQKNNVDLVN 83

                         90       100
                 ....*....|....*....|....*.
gi 513126889 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21231   84 IGSADIVDGNHKLTLGLIWSIILHWQ 109

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 513126889   1 MGTQVVMRFNNSllptEPSQQLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEM 80
Cdd:cd21236    2 AYENVLERYKDE----RDKVQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRM 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 513126889  81 K----NNVEKVLQFVASKKIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21236   70 RfhrlQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-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. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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 513126889  27 AWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLsgvQLSPGNQQEM--KNNVEKVLQFVaSKKIRMHQTSAK 104
Cdd:cd21221    8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLEKLANEKL---EVPEVAQSEEgqKQKLAVVLACV-NFLLGLEEDEAR 81

                         90       100
                 ....*....|....*....|....*
gi 513126889 105 DIVDG----NLKSIMRLVLALAAHF 125
Cdd:cd21221   82 WTVDGiynkDLVSILHLLVALAHHY 106

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-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. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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 513126889  26 VAWVNAQLkkRPAVKPVQDLRQDLRDGVILAYLIEIVAG--EKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSA 103
Cdd:cd21222   22 LQFVNKHL--AKLNIEVTDLATQFHDGVYLILLIGLLEGffVPLHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRP 99

                         90       100
                 ....*....|....*....|..
gi 513126889 104 KDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21222  100 EDIVNGDLKSILRVLYSLFSKY 121

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 513126889  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21237    7 QKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEVLSGVKL------PREKGRMRfhrlQNVQIALDFLKQRQV 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 513126889  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21237   79 KLVNIRNDDITDGNPKLTLGLIWTIILHFQ 108

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (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. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B 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 513126889  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21309   18 QQNTFTRWCNEHLKC--VNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLV 95

                         90       100
                 ....*....|....*....|....*.
gi 513126889 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21309   96 SIDSKAIVDGNLKLILGLVWTLILHY 121

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513126889  28 WVNAQLKKRPavkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgnqQEMKNNVEKVLQfvASKKIRM-HQTSAKDI 106
Cdd:cd21185    9 WVRQLLPDVD----VNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDP---EESENNIQRGLE--AGKSLGVePVLTAEEM 79

                         90       100
                 ....*....|....*....|
gi 513126889 107 VDGNLKSIMrlVLALAAHFK 126
Cdd:cd21185   80 ADPEVEHLG--IMAYAAQLQ 97

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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 513126889  28 WVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKL--SGVQLSPGNQqemKNNVEKVLQFVaSKKIRMHQTSAK- 104
Cdd:cd21305    9 WINTTLKQEHIV--VKSLEEDLYDGLVLHHLLVKLAGVKLevEEIALTENAQ---KRKLTVILEAV-NQSLQLEESQLKw 82

                         90       100
                 ....*....|....*....|....
gi 513126889 105 ---DIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21305   83 sveLIHNKDLLATLHLLVAIAKHF 106

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 513126889  24 AYVAWVNAQLKKRPAVK-------PVQDLRQDLRDGVILAYLIE-IVAG----EKLSGVqlSPGNQQEMKNNVEKVLQfv 91
Cdd:cd21217    5 AFVEHINSLLADDPDLKhllpidpDGDDLFEALRDGVLLCKLINkIVPGtideRKLNKK--KPKNIFEATENLNLALN-- 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 513126889  92 ASKKIRMHQTS--AKDIVDGNLKsimrLVLAL 121
Cdd:cd21217   81 AAKKIGCKVVNigPQDILDGNPH----LVLGL 108

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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513126889  22 LQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSP---GNQQEMKNNVEKVlqfvaSKKIRM 98
Cdd:cd21335    8 MKVLIDWINDVLVGERII--VKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQseiAQKQKLQTVLEKI-----NETLKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 513126889  99 HQTSAKDIVDG----NLKSIMRLVLALAAHFK 126
Cdd:cd21335   81 PPRSIKWNVDSvhakSLVAILHLLVALSQYFR 112

third 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. 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. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) 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. 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513126889  17 EPSQQLQAYVAWVNAQLKKRPavkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLS---PGNQQEMKNNVEKVLQFVAS 93
Cdd:cd21219    1 EGSREERAFRMWLNSLGLDPL----INNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNkpkPLNKFKKVENCNYAVDLAKK 76

                         90       100
                 ....*....|....*....|....*
gi 513126889  94 KKIRMHQTSAKDIVDGNLKSIMRLV 118
Cdd:cd21219   77 LGFSLVGIGGKDIADGNRKLTLALV 101

Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. 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 the segregation of chromosomes during mitotic cell division.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513126889  22 LQAYVAWVNAQlkkrPAVKPVQDLrQDLRDGVILAYLIEIVAGEKLSGVQL----SPGNQQEMKNNVEKVLQFVAS--KK 95
Cdd:cd22211    1 EAALLAWINTF----PLSSPVESL-DDLSDGVVLAEILSQIDPSYFDSEWLesrdSSDNWVLKLNNLKKLYRSLSKyyRE 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 513126889  96 IRMHQTSAKDIVDgnLKSI------------MRLVLALA 122
Cdd:cd22211   76 VLGQQLSDLPLPD--LSAIardgdeeeivklLELVLGAA 112