calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may 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 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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPA 529
Cdd:cd21255    1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                         90       100
                 ....*....|....*....|....*
gi 530396516 530 DMVLLSVPDKLIVMTYLCQIRAFCT 554
Cdd:cd21255   81 DMVLLPIPDKLIVMTYLCQLRAHFT 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 530396516   12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530396516   92 QYEAKEWTFIIENESKGQRK-VLATAEVDLARHAGPVPVQVPVRLRLKPKSVKvvQAELSLTLSGVLLREGRAT 164
Cdd:pfam10358  72 KYEEKLLEFSVYKVTKKGKKkVLGKASIDLAEYANLKKKPTTVRFLLKKSSKK--NATLSLSIQVLPLGEDPND 143

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may 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 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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPA 529
Cdd:cd21255    1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                         90       100
                 ....*....|....*....|....*
gi 530396516 530 DMVLLSVPDKLIVMTYLCQIRAFCT 554
Cdd:cd21255   81 DMVLLPIPDKLIVMTYLCQLRAHFT 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 530396516   12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530396516   92 QYEAKEWTFIIENESKGQRK-VLATAEVDLARHAGPVPVQVPVRLRLKPKSVKvvQAELSLTLSGVLLREGRAT 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 530396516   455 LLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDY----ASLDPLNIKQNNKQAFDGFAALGVSR-LLEPA 529
Cdd:smart00033   3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVvLFEPE 82

                           90
                   ....*....|....*..
gi 530396516   530 DMVLLSvPDKLIVMTYL 546
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 530396516 777 AELQALEQEQRQIDGRAAEVEMQLRSLMESGANKLQEEV-LIQEWFTLVNKKNALIR-----RQDQLQLLMEEQDLERRF 850
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRaaaelAAQLEELEEAEEALLERL 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396516 851 ELLSRELRAMLAIEdwQKTSAQQHREQLLLEELVSLVNQRDELVRDLDHKERIALEEDERLERGLEQRRRKLSRQLSRRE 930
Cdd:COG1196  417 ERLEEELEELEEAL--AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494

exonuclease subunit SbcC; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396516  777 AELQALEQEQRQIDGRAAEVEMQLRSLM------ESGANKL--QEEVLIQEWFTLVNKKNALIRRQDQLQLLMEEQ-DLE 847
Cdd:PRK10246  530 SRLDALEKEVKKLGEEGAALRGQLDALTkqlqrdESEAQSLrqEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQeEHE 609

                          90       100       110
                  ....*....|....*....|....*....|..
gi 530396516  848 RRFELLSR--ELRAMLAIEDWQKTSAQQHREQ 877
Cdd:PRK10246  610 RQLRLLSQrhELQGQIAAHNQQIIQYQQQIEQ 641

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may 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 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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPA 529
Cdd:cd21255    1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                         90       100
                 ....*....|....*....|....*
gi 530396516 530 DMVLLSVPDKLIVMTYLCQIRAFCT 554
Cdd:cd21255   81 DMVLLPIPDKLIVMTYLCQLRAHFT 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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPA 529
Cdd:cd21254    1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80

                         90       100
                 ....*....|....*....|....*..
gi 530396516 530 DMVLLSVPDKLIVMTYLCQIRAFCTGQ 556
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 530396516  778 ELQALEQEQRQIDGRAAEVEMQLRSLMEsgaNKLQEEVLIQEWFTLVNKKNALIRRQDQLQLLMEEQDLERRFELLSREL 857
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRGEMS---GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530396516  858 RAMLAIEDWQKTSAQQHREQLLLEELVSLVNQRDELVRDLDHKERIALEEDERL 911
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 530396516 453 QSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEPADM 531
Cdd:cd21197    3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRvAETSLGIPALLDAEDM 82

                         90
                 ....*....|....*...
gi 530396516 532 VLLSVPDKLIVMTYLCQI 549
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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 528
Cdd:cd21194    2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81

                         90
                 ....*....|....*...
gi 530396516 529 ADmVLLSVPDKLIVMTYL 546
Cdd:cd21194   82 ED-VDVARPDEKSIMTYV 98

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (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. 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 530396516 451 SSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEPA 529
Cdd:cd21252    1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEvAERELGIPALLDPE 80

                         90
                 ....*....|....*....
gi 530396516 530 DMVLLSVPDKLIVMTYLCQ 548
Cdd:cd21252   81 DMVSMKVPDCLSIMTYVSQ 99

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 530396516 449 VSSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLE 527
Cdd:cd21251    4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDiAEKEFGISPIMT 83

                         90       100
                 ....*....|....*....|.
gi 530396516 528 PADMVLLSVPDKLIVMTYLCQ 548
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 530396516 449 VSSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLE 527
Cdd:cd21195    3 DIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDvAEREFGIPPVTT 82

                         90       100
                 ....*....|....*....|.
gi 530396516 528 PADMVLLSVPDKLIVMTYLCQ 548
Cdd:cd21195   83 GKEMASAQEPDKLSMVMYLSK 103

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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDgfAA---LGVSRLL 526
Cdd:cd21248    2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFN--VAeqkLGLTKLL 79

                         90
                 ....*....|....*....
gi 530396516 527 EPADmVLLSVPDKLIVMTY 545
Cdd:cd21248   80 DPED-VNVEQPDEKSIITY 97

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEP 528
Cdd:cd21291   10 TAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQLLDV 89

                         90       100
                 ....*....|....*....|
gi 530396516 529 ADMVLLSVPDKLIVMTYLCQ 548
Cdd:cd21291   90 EDVCDVAKPDERSIMTYVAY 109

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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAAL-GVSRLLEP 528
Cdd:cd21261    1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                         90
                 ....*....|....*....
gi 530396516 529 ADMVLLS-VPDKLIVMTYL 546
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 530396516 455 LLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEPADMVL 533
Cdd:cd21250    9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDvAEREFGIPPVTTGKEMAS 88

                         90
                 ....*....|...
gi 530396516 534 LSVPDKLIVMTYL 546
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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALG-VSRLLEP 528
Cdd:cd21259    1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80

                         90
                 ....*....|....*...
gi 530396516 529 ADMVLLSVPDKLIVMTYL 546
Cdd:cd21259   81 EDMVRMREPDWKCVYTYI 98

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that 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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPA 529
Cdd:cd21257    8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87

                         90       100
                 ....*....|....*....|
gi 530396516 530 DMVLLSVPDKLIVMTYLCQI 549
Cdd:cd21257   88 EMMYTDRPDWQSVMQYVAQI 107

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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 528
Cdd:cd21322   17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLDP 96

                         90
                 ....*....|....*...
gi 530396516 529 ADmVLLSVPDKLIVMTYL 546
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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEP 528
Cdd:cd21192    3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRiAEQHLNIPRLLEV 82

                         90       100
                 ....*....|....*....|
gi 530396516 529 ADmVLLSVPDKLIVMTYLCQ 548
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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEP 528
Cdd:cd21321    5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNvAEKELGLTKLLDP 84

                         90
                 ....*....|....*...
gi 530396516 529 ADmVLLSVPDKLIVMTYL 546
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 530396516 450 SSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLEP 528
Cdd:cd21320    2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNlAEQHLGLTKLLDP 81

                         90
                 ....*....|....*...
gi 530396516 529 ADmVLLSVPDKLIVMTYL 546
Cdd:cd21320   82 ED-ISVDHPDEKSIITYV 98

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396516 450 SSSQSLLEWCQEVTTGYRgvrITNFTTSWRNGLAFCAILHRFYPDKI-DYASLDPLNIKQNNKQAFD-GFAALGVSRLLE 527
Cdd:cd21184    1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDiAEEELGIPKIIT 77

                         90       100
                 ....*....|....*....|...
gi 530396516 528 PADMVLLSVpDKLIVMTYLCQIR 550
Cdd:cd21184   78 PEDMVSPNV-DELSVMTYLSYFR 99

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396516 449 VSSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFD-GFAALGVSRLLE 527
Cdd:cd21244    4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRiAEQELKIPRLLE 83

                         90       100
                 ....*....|....*....|.
gi 530396516 528 PADmVLLSVPDKLIVMTYLCQ 548
Cdd:cd21244   84 PED-VDVVNPDEKSIMTYVAQ 103

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).