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 2090126098 131 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNV 210
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLF---------------------------EKLEGEKLNV 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090126098 211 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDTVHAKSLVAILHLLVALSQYFRAPI 272
Cdd:cd21335    54 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 2090126098 131 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNV 210
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLF---------------------------EKLEGEKLNV 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090126098 211 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDTVHAKSLVAILHLLVALSQYFRAPI 272
Cdd:cd21335    54 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 2090126098 135 QELMKVLIDWINDVLV--GERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNVAE 212
Cdd:pfam00307   1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALL---------------------------NKLAPGLVDKKK 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2090126098 213 VTQSEIAQKQKLQTVLEKINETLKLPPRSIkWNVDTVHAKSLvAILHLLVALSQYFRA 270
Cdd:pfam00307  54 LNKSEFDKLENINLALDVAEKKLGVPKVLI-EPEDLVEGDNK-SVLTYLASLFRRFQA 109

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090126098 315 DAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNV 394
Cdd:cd21306     1 DAFDTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPTSFEQKVHNV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2090126098 395 SFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 435
Cdd:cd21306    81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121

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 2090126098 131 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNV 210
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLF---------------------------EKLEGEKLNV 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090126098 211 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDTVHAKSLVAILHLLVALSQYFRAPI 272
Cdd:cd21335    54 AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 2090126098 136 ELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNVAEVTQ 215
Cdd:cd21304     1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLL---------------------------EKLTGVKLEVAEVTQ 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2090126098 216 SEIAQKQKLQTVLEKINETLKLP-PRSIKWNVDTVHAKSLVAILHLLVALSQYF 268
Cdd:cd21304    54 SEVGQKQKLRTVLDKINRILNLPrWSQQKWSVDSIHSKNLVAILHLLVALARHF 107

first calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-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 2090126098 136 ELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNVAEVTQ 215
Cdd:cd21336     1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLL---------------------------EKLAGRKLNVAEVTQ 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090126098 216 SEIAQKQKLQTVLEKINETLKLPPRSIKWNVDTVHAKSLVAILHLLVALSQYF 268
Cdd:cd21336    54 SEIGQKQKLQTVLEAVNDLLRPQGWAIKWSVDSIHGKNLVAILHLLVALAMHF 106

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 2090126098 136 ELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNVAEVTQ 215
Cdd:cd21305     1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLL---------------------------VKLAGVKLEVEEIAL 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090126098 216 SEIAQKQKLQTVLEKINETLKLPPRSIKWNVDTVHAKSLVAILHLLVALSQYF 268
Cdd:cd21305    54 TENAQKRKLTVILEAVNQSLQLEESQLKWSVELIHNKDLLATLHLLVAIAKHF 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 2090126098 135 QELMKVLIDWINDVLV--GERIIVKDLAEDLYDGQVLQKLFggkpriphymqlsrllsfmtlallrrtEKLESEKLNVAE 212
Cdd:pfam00307   1 LELEKELLRWINSHLAeyGPGVRVTNFTTDLRDGLALCALL---------------------------NKLAPGLVDKKK 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2090126098 213 VTQSEIAQKQKLQTVLEKINETLKLPPRSIkWNVDTVHAKSLvAILHLLVALSQYFRA 270
Cdd:pfam00307  54 LNKSEFDKLENINLALDVAEKKLGVPKVLI-EPEDLVEGDNK-SVLTYLASLFRRFQA 109

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 2090126098 330 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGyfVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKP 409
Cdd:cd21215     4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGD--ESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLT 81

                          90       100
                  ....*....|....*....|....*.
gi 2090126098 410 KPRPEDIVNCDLKSTLRVLYNLFTKY 435
Cdd:cd21215    82 NIGAEDIVDGNLKLILGLLWTLILRF 107

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 2090126098 332 KKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLhsffltPDSFEQ---KVLNVSFAFELMQDGGLEK 408
Cdd:cd21214     7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK------PERGKMrfhKIANVNKALDFIASKGVKL 80

                          90
                  ....*....|....*..
gi 2090126098 409 PKPRPEDIVNCDLKSTL 425
Cdd:cd21214    81 VSIGAEEIVDGNLKMTL 97

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 2090126098 339 VNKHLNKL--------------NLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDG 404
Cdd:cd21223     1 LTRHLGYLgyvlshvqtpldefDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2090126098 405 GLEKPKP----RPEDIVNCDLKSTLRVLYNL 431
Cdd:cd21223    81 GVLRGGDgggiTAKDIVDGHREKTLALLWRI 111

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 2090126098 330 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLtpdSFeQKVLNVSFAFELMQDGGLEKP 409
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM---RF-HRLQNVQTALDFLKYRKIKLV 78

                          90
                  ....*....|....*.
gi 2090126098 410 KPRPEDIVNCDLKSTL 425
Cdd:cd21188    79 NIRAEDIVDGNPKLTL 94

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 2090126098 332 KKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYfvPLHSFFLTPDSFEQKVL-NVSFAFELMQDGGLEKPK 410
Cdd:cd21183     6 ANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTR--PLKRSYNRRPAFQQHYLeNVSTALKFIEADHIKLVN 83

                          90       100
                  ....*....|....*....|....*
gi 2090126098 411 PRPEDIVNCDLKSTLRVLYNLFTKY 435
Cdd:cd21183    84 IGSGDIVNGNIKLILGLIWTLILHY 108

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
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090126098 324 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVP 376
Cdd:cd21246    10 ADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLP 62

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 2090126098 330 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 409
Cdd:cd21235     6 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 81

                          90       100
                  ....*....|....*....|....*..
gi 2090126098 410 KPRPEDIVNCDLKSTLRVLYNLFTKYR 436
Cdd:cd21235    82 NIRNDDIADGNPKLTLGLIWTIILHFQ 108

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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 2090126098 330 VVKKTLITFVNKHLNKLNLE-VTELETQFADGVYLVLLMGLLEGYFVPlHSFFLTPDSFEQKVLNVSFAFELMQDGGLEK 408
Cdd:cd21225     4 VQIKAFTAWVNSVLEKRGIPkISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKNRIQMIQNLHLAMLFIEEDLKIR 82

                          90       100
                  ....*....|....*....|....*....
gi 2090126098 409 -PKPRPEDIVNCDLKSTLRVLYNLFTKYR 436
Cdd:cd21225    83 vQGIGAEDFVDNNKKLILGLLWTLYRKYR 111

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 2090126098 320 LFDHAPDKlNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVpLHSFFLTPDSFEQKVLNVSFAFE 399
Cdd:cd21309     8 LAEDAPWK-KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM-YRKYHQRPTFRQMQLENVSVALE 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2090126098 400 LMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 435
Cdd:cd21309    86 FLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHY 121