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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 128 IQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKE 207
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 66827249 208 LDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66827249 733 EFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYM 794
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62

Ca2+ insensitive EF hand; EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66827249   801 TDSVESTKAAFKVMAEDKDFITEAQIRAAISdSKQIDYLLASMP--------AVEGGFDYNSFAEKLYQ 861
Cdd:pfam08726   2 TDTAEQVEASFRALAGGKPYVTEEDLRRELT-PDQAEYCIARMPpysgpdgdSVPGAYDYVSFSEALFG 69

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 128 IQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKE 207
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 66827249 208 LDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115

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 66827249  19 AWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKtPKLRIHNIQNVGLCLKHIESHGVK 98
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIASKGVK 79

                        90       100
                ....*....|....*....|....*.
gi 66827249  99 LVGIGAEELVDKNLKMTLGMIWTIIL 124
Cdd:cd21214  80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105

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 66827249    140 EALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKD----DKAGNLQLAFDIAEKELDIPKMLD 215
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 66827249    216 VSDMLDvVRPDERSVMTYVAQY 237
Cdd:smart00033  81 PEDLVE-GPKLILGVIWTLISL 101

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66827249 733 EFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYM 794
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62

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 66827249    24 QKKTFTAWCNSHLRKLG--SSIEQIDTDFTDGIKLAQLLEVISNDpVFKVNKTPKLRIHNIQNVGLCLKHIESH-GVKLV 100
Cdd:pfam00307   3 LEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKSEFDKLENINLALDVAEKKlGVPKV 81

                          90       100
                  ....*....|....*....|....*...
gi 66827249   101 GIGAEELVDKNLKMTLGMIWTIILRFAI 128
Cdd:pfam00307  82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109

EF-hand domain pair;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66827249   732 SEFKACFSHFDKDNDNKLNRLEFSSCLKSI--GDELTEEQLNQVISKIDTDGNGTISFEEFIDYM 794
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66827249 717 EILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGdeLTEEQLNQVISKIDTDGNGTISFEEFIDYM 794
Cdd:COG5126  54 EFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249   504 LVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISY 583
Cdd:pfam00435   3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82

                          90       100
                  ....*....|....*....|...
gi 66827249   584 DELSAKWNNLLAGIEERKVQLAN 606
Cdd:pfam00435  83 EELNERWEQLLELAAERKQKLEE 105

XopAW family type III secretion system calcium-binding effector;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 66827249  738 FSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEF 790
Cdd:NF041410  33 FAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDEL 85

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 128 IQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKE 207
Cdd:cd21216   1 IQDISVEELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKH 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 66827249 208 LDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21216  81 LDIPKMLDAEDIVNTPRPDERSVMTYVSCYYHAFA 115

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 66827249  19 AWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKtPKLRIHNIQNVGLCLKHIESHGVK 98
Cdd:cd21214   1 AWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIASKGVK 79

                        90       100
                ....*....|....*....|....*.
gi 66827249  99 LVGIGAEELVDKNLKMTLGMIWTIIL 124
Cdd:cd21214  80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDV 216
Cdd:cd21194   2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81

                        90       100
                ....*....|....*....|....*
gi 66827249 217 SDmLDVVRPDERSVMTYVAQYYHHF 241
Cdd:cd21194  82 ED-VDVARPDEKSIMTYVASYYHYF 105

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It 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 66827249 128 IQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKE 207
Cdd:cd21289   1 IQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 66827249 208 LDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAG 251
Cdd:cd21289  81 LDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAA 124

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It 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 66827249 128 IQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKE 207
Cdd:cd21287   1 IQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKY 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 66827249 208 LDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRK 246
Cdd:cd21287  81 LDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQK 119

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDV 216
Cdd:cd21253   1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                        90       100
                ....*....|....*....|....*
gi 66827249 217 SDMLDVVRPDERSVMTYVAQYYHHF 241
Cdd:cd21253  81 EDMVALKVPDKLSILTYVSQYYNYF 105

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 136 LSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLD 215
Cdd:cd21249   3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82

                        90       100
                ....*....|....*....|....*..
gi 66827249 216 VSDMLdVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21249  83 PEDVA-VPHPDERSIMTYVSLYYHYFS 108

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) 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. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB 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 66827249 134 EELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKM 213
Cdd:cd21319   2 ETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKL 81

                        90       100
                ....*....|....*....|....*....
gi 66827249 214 LDVSDMLdVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21319  82 LDPEDVF-TENPDEKSIITYVVAFYHYFS 109

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDV 216
Cdd:cd21189   1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                        90       100
                ....*....|....*....|....*
gi 66827249 217 SDmLDVVRPDERSVMTYVAQYYHHF 241
Cdd:cd21189  81 ED-VDVPEPDEKSIITYVSSLYDVF 104

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 66827249  20 WEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKL 99
Cdd:cd21215   1 WVDVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                        90       100
                ....*....|....*....|....*..
gi 66827249 100 VGIGAEELVDKNLKMTLGMIWTIILRF 126
Cdd:cd21215  81 TNIGAEDIVDGNLKLILGLLWTLILRF 107

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKeLDIPKMLDV 216
Cdd:cd21198   1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79

                        90       100
                ....*....|....*....|....*.
gi 66827249 217 SDMLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21198  80 ADMVLLSVPDKLSVMTYLHQIRAHFT 105

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDV 216
Cdd:cd21320   2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81

                        90       100
                ....*....|....*....|....*.
gi 66827249 217 SDmLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21320  82 ED-ISVDHPDEKSIITYVVTYYHYFS 106

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDV 216
Cdd:cd21200   1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80

                        90       100
                ....*....|....*....|....*..
gi 66827249 217 SDMLDV-VRPDERSVMTYVAQYYHHFS 242
Cdd:cd21200  81 EDMVRMgNRPDWKCVFTYVQSLYRHLR 107

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66827249 137 SAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKeLDIPKMLDV 216
Cdd:cd21254   1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79

                        90       100
                ....*....|....*....|....*.
gi 66827249 217 SDMLDVVRPDERSVMTYVAQYYHHFS 242
Cdd:cd21254  80 SDMVLLAVPDKLTVMTYLYQIRAHFS 105