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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 334
Cdd:cd21198    1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80

                         90       100
                 ....*....|....*....|....*
gi 167736347 335 DMVLLSVPDKLIVMTYLCQIRAFCT 359
Cdd:cd21198   81 DMVLLSVPDKLSVMTYLHQIRAHFT 105

N-terminal C2 in EEIG1 and EHBP1 proteins; This version of the C2 domain was initally identified in the vertebrate estrogen early-induced gene 1 (EEIG1), and its Drosophila ortholog required for uptake of dsRNA via the endocytotic machinery to induce RNAi silencing. It is also in C.elegans ortholog Sym-3 (SYnthetic lethal with Mec-3) and the mammalian protein EHBP1 (EH domain Binding Protein-1) that regulates endocytotic recycling and two plant proteins, RPG that regulates Rhizobium-directed polar growth and PMI1 (Plastid Movement Impaired 1) that is essential for intracellular movement of chloroplasts in response to blue light.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347   12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167736347   92 QYETKEWTFIIENESKGQRK-VLATVDVNLAHHAGPVPAQVPLRLRLKPKSVKvvHAELSLTLSGVLLREGRAT 164
Cdd:pfam10358  72 KYEEKLLEFSVYKVTKKGKKkVLGKASIDLAEYANLKKKPTTVRFLLKKSSKK--NATLSLSIQVLPLGEDPND 143

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 334
Cdd:cd21198    1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80

                         90       100
                 ....*....|....*....|....*
gi 167736347 335 DMVLLSVPDKLIVMTYLCQIRAFCT 359
Cdd:cd21198   81 DMVLLSVPDKLSVMTYLHQIRAHFT 105

N-terminal C2 in EEIG1 and EHBP1 proteins; This version of the C2 domain was initally identified in the vertebrate estrogen early-induced gene 1 (EEIG1), and its Drosophila ortholog required for uptake of dsRNA via the endocytotic machinery to induce RNAi silencing. It is also in C.elegans ortholog Sym-3 (SYnthetic lethal with Mec-3) and the mammalian protein EHBP1 (EH domain Binding Protein-1) that regulates endocytotic recycling and two plant proteins, RPG that regulates Rhizobium-directed polar growth and PMI1 (Plastid Movement Impaired 1) that is essential for intracellular movement of chloroplasts in response to blue light.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347   12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167736347   92 QYETKEWTFIIENESKGQRK-VLATVDVNLAHHAGPVPAQVPLRLRLKPKSVKvvHAELSLTLSGVLLREGRAT 164
Cdd:pfam10358  72 KYEEKLLEFSVYKVTKKGKKkVLGKASIDLAEYANLKKKPTTVRFLLKKSSKK--NATLSLSIQVLPLGEDPND 143

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 167736347   260 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDP----LNIKQNNKQAFDGFAALGVSR-LLEPA 334
Cdd:smart00033   3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVvLFEPE 82

                           90
                   ....*....|....*..
gi 167736347   335 DMVLLSvPDKLIVMTYL 351
Cdd:smart00033  83 DLVEGP-KLILGVIWTL 98

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 604 AELQALEQEQGQIDGRAAEVEKQLRSLMESGANRLQEEV-LIQEWFTLVNKKNALIR-----RQDQLQLLIEEQDLERRF 677
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRaaaelAAQLEELEEAEEALLERL 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 678 ELLSRELRAMLAIEEwqKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERLERGLEQRRRKVSRQLSRRE 757
Cdd:COG1196  417 ERLEEELEELEEALA--ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 334
Cdd:cd21198    1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80

                         90       100
                 ....*....|....*....|....*
gi 167736347 335 DMVLLSVPDKLIVMTYLCQIRAFCT 359
Cdd:cd21198   81 DMVLLSVPDKLSVMTYLHQIRAHFT 105

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 334
Cdd:cd21254    1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80

                         90       100
                 ....*....|....*....|....*..
gi 167736347 335 DMVLLSVPDKLIVMTYLCQIRAFCTGQ 361
Cdd:cd21254   81 DMVLLAVPDKLTVMTYLYQIRAHFSGQ 107

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347  605 ELQALEQEQGQIDGRAAEVEKQLRSLMEsgaNRLQEEVLIQEWFTLVNKKNALIRRQDQLQLLIEEQDLERRFELLSREL 684
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRGEMS---GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 167736347  685 RAMLAIEEWQKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERL 738
Cdd:pfam12130  78 RELMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. 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 family 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 167736347 258 QSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPADM 336
Cdd:cd21197    3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRvAETSLGIPALLDAEDM 82

                         90
                 ....*....|....*...
gi 167736347 337 VLLSVPDKLIVMTYLCQI 354
Cdd:cd21197   83 VTMHVPDRLSIITYVSQY 100

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 333
Cdd:cd21194    2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81

                         90
                 ....*....|....*...
gi 167736347 334 ADmVLLSVPDKLIVMTYL 351
Cdd:cd21194   82 ED-VDVARPDEKSIMTYV 98

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains 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 167736347 254 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 332
Cdd:cd21251    4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDiAEKEFGISPIMT 83

                         90       100
                 ....*....|....*....|.
gi 167736347 333 PADMVLLSVPDKLIVMTYLCQ 353
Cdd:cd21251   84 GKEMASVGEPDKLSMVMYLTQ 104

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 254 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 332
Cdd:cd21195    3 DIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDvAEREFGIPPVTT 82

                         90       100
                 ....*....|....*....|.
gi 167736347 333 PADMVLLSVPDKLIVMTYLCQ 353
Cdd:cd21195   83 GKEMASAQEPDKLSMVMYLSK 103

N-terminal C2 in EEIG1 and EHBP1 proteins; This version of the C2 domain was initally identified in the vertebrate estrogen early-induced gene 1 (EEIG1), and its Drosophila ortholog required for uptake of dsRNA via the endocytotic machinery to induce RNAi silencing. It is also in C.elegans ortholog Sym-3 (SYnthetic lethal with Mec-3) and the mammalian protein EHBP1 (EH domain Binding Protein-1) that regulates endocytotic recycling and two plant proteins, RPG that regulates Rhizobium-directed polar growth and PMI1 (Plastid Movement Impaired 1) that is essential for intracellular movement of chloroplasts in response to blue light.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347   12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167736347   92 QYETKEWTFIIENESKGQRK-VLATVDVNLAHHAGPVPAQVPLRLRLKPKSVKvvHAELSLTLSGVLLREGRAT 164
Cdd:pfam10358  72 KYEEKLLEFSVYKVTKKGKKkVLGKASIDLAEYANLKKKPTTVRFLLKKSSKK--NATLSLSIQVLPLGEDPND 143

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDgfAA---LGVSRLL 331
Cdd:cd21248    2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFN--VAeqkLGLTKLL 79

                         90
                 ....*....|....*....
gi 167736347 332 EPADmVLLSVPDKLIVMTY 350
Cdd:cd21248   80 DPED-VNVEQPDEKSIITY 97

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDgfAA---LGVSRLL 331
Cdd:cd21189    1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFN--VAekeFGVTRLL 78

                         90
                 ....*....|....*....
gi 167736347 332 EPADmVLLSVPDKLIVMTY 350
Cdd:cd21189   79 DPED-VDVPEPDEKSIITY 96

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains 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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAAL-GVSRLLEP 333
Cdd:cd21261    1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                         90
                 ....*....|....*....
gi 167736347 334 ADMVLLS-VPDKLIVMTYL 351
Cdd:cd21261   81 EDMMVMGrKPDPMCVFTYV 99

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains 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 167736347 260 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPADMVL 338
Cdd:cd21250    9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDvAEREFGIPPVTTGKEMAS 88

                         90
                 ....*....|...
gi 167736347 339 LSVPDKLIVMTYL 351
Cdd:cd21250   89 AEEPDKLSMVMYL 101

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALG-VSRLLEP 333
Cdd:cd21259    1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80

                         90
                 ....*....|....*...
gi 167736347 334 ADMVLLSVPDKLIVMTYL 351
Cdd:cd21259   81 EDMVRMREPDWKCVYTYI 98

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALG-VSRLLEP 333
Cdd:cd21258    1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLAdCVPLVEV 80

                         90
                 ....*....|....*....
gi 167736347 334 ADMVLL-SVPDKLIVMTYL 351
Cdd:cd21258   81 EDMMIMgKKPDSKCVFTYV 99

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 333
Cdd:cd21322   17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLDP 96

                         90
                 ....*....|....*...
gi 167736347 334 ADmVLLSVPDKLIVMTYL 351
Cdd:cd21322   97 ED-VNMEAPDEKSIITYV 113

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 333
Cdd:cd21192    3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRiAEQHLNIPRLLEV 82

                         90       100
                 ....*....|....*....|
gi 167736347 334 ADmVLLSVPDKLIVMTYLCQ 353
Cdd:cd21192   83 ED-VLVDKPDERSIMTYVSQ 101

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) 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. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 333
Cdd:cd21321    5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNvAEKELGLTKLLDP 84

                         90
                 ....*....|....*...
gi 167736347 334 ADmVLLSVPDKLIVMTYL 351
Cdd:cd21321   85 ED-VNVDQPDEKSIITYV 101

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 333
Cdd:cd21320    2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNlAEQHLGLTKLLDP 81

                         90
                 ....*....|....*...
gi 167736347 334 ADmVLLSVPDKLIVMTYL 351
Cdd:cd21320   82 ED-ISVDHPDEKSIITYV 98

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 167736347   260 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDP----LNIKQNNKQAFDGFAALGVSR-LLEPA 334
Cdd:smart00033   3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVvLFEPE 82

                           90
                   ....*....|....*..
gi 167736347   335 DMVLLSvPDKLIVMTYL 351
Cdd:smart00033  83 DLVEGP-KLILGVIWTL 98

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSL---DPLNikqNNKQAFD-GFAALGVSRL 330
Cdd:cd21287   10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLrkdDPLT---NLNTAFDvAEKYLDIPKM 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 167736347 331 LEPADMVLLSVPDKLIVMTYLCQI-RAFCTGQEL 363
Cdd:cd21287   87 LDAEDIVGTARPDEKAIMTYVSSFyHAFSGAQKA 120

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 167736347 255 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 333
Cdd:cd21289   10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEvAEKYLDIPKMLDA 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 167736347 334 ADMVLLSVPDKLIVMTYL-CQIRAFCTGQELQ 364
Cdd:cd21289   90 EDIVNTPKPDEKAIMTYVsCFYHAFAGAEQAE 121

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736347 260 LLEWCQEVTNGYR-GVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPL--NIKQNNKQAFD-GFAALGVSRLLEPAD 335
Cdd:COG5069  130 LLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFEnANKVIGIARLIGVED 209