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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 115
Cdd:cd21336    1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                         90       100
                 ....*....|....*....|....*.
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21336   81 KWSVDSIHGKNLVAILHLLVALAMHF 106

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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 115
Cdd:cd21336    1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                         90       100
                 ....*....|....*....|....*.
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21336   81 KWSVDSIHGKNLVAILHLLVALAMHF 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 343432588   35 KELVKVLLDWINDVLVE--ERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRG 112
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 343432588  113 WaLRWSVDSIHGKNLvAILHLLVSLAMHFRA 143
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343432588    39 KVLLDWINDVLVEE-RIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQ--SEIGQKQKLQTVLEAVHDLL 108
Cdd:smart00033   1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLG 73

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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 115
Cdd:cd21336    1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                         90       100
                 ....*....|....*....|....*.
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21336   81 KWSVDSIHGKNLVAILHLLVALAMHF 106

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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLR-PRGWA 114
Cdd:cd21304    1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNlPRWSQ 80

                         90       100
                 ....*....|....*....|....*..
gi 343432588 115 LRWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21304   81 QKWSVDSIHSKNLVAILHLLVALARHF 107

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343432588 184 RFERDAFDTLFDHAPDKLSVVKK-----------------------FADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQK 240
Cdd:cd21337    1 RHERDAFDTLFDHAPDKLNVVKKtlitfvnkhlnklnlevteletqFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 343432588 241 VHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 289
Cdd:cd21337   81 VLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE 129

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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 115
Cdd:cd21221    1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                         90       100
                 ....*....|....*....|....*.
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21221   81 RWTVDGIYNKDLVSILHLLVALAHHY 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 343432588  36 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 115
Cdd:cd21305    1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                         90       100
                 ....*....|....*....|....*.
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21305   81 KWSVELIHNKDLLATLHLLVAIAKHF 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 343432588   35 KELVKVLLDWINDVLVE--ERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRG 112
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 343432588  113 WaLRWSVDSIHGKNLvAILHLLVSLAMHFRA 143
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109

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 343432588  207 FADGVYLVLLMGLLEDYFVPLHHFYLTPEsfdQKVHNVSFAFEL-MLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 285
Cdd:pfam00307  31 LRDGLALCALLNKLAPGLVDKKKLNKSEF---DKLENINLALDVaEKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107

                  .
gi 343432588  286 K 286
Cdd:pfam00307 108 Q 108

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 343432588  39 KVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLnvaevtQSEIGQKQ--KLQTVLEAVhDLLRPRGWAL- 115
Cdd:cd21188    6 KTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL------PRERGRMRfhRLQNVQTAL-DFLKYRKIKLv 78

                         90       100
                 ....*....|....*....|....*..
gi 343432588 116 RWSVDSIHGKNLVAILHLLVSLAMHFR 142
Cdd:cd21188   79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. 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. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343432588  43 DWINDVLVEE--RIIVKQLEEDLYDGQVLQKLLEKLAGCKlnVAEVTQSEIGQKQKLQ------TVLEA----VHDLlrp 110
Cdd:cd21212    7 DWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEK--VPGIHSRPKTRAQKLEniqaclQFLAAlgvdVQGI--- 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 343432588 111 rgwalrwSVDSIHGKNLVAILHLLVSLAMHF 141
Cdd:cd21212   82 -------TAEDIVDGNLKAILGLFFSLSRYK 105

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 343432588  35 KELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKL 81
Cdd:cd21214    4 KQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL 50

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
                 ....*....|....*....|....*....|....*....|...
gi 343432588  39 KVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKL 81
Cdd:cd21246   19 KTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL 61