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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 540
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394403 541 DMVLLSVPDKLIVMTYLCQIRAFCT 565
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 1720394403  12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720394403  92 QYETKEWTFIIENESKGQRK-VLATVDVNLAHHAGPVPAQVPLRLRLKPKSVKvvHAELSLTLSGVLLREGRAT 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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 540
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394403 541 DMVLLSVPDKLIVMTYLCQIRAFCT 565
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 1720394403  12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720394403  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 1720394403  466 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDP----LNIKQNNKQAFDGFAALGVSR-LLEPA 540
Cdd:smart00033   3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVvLFEPE 82

                           90
                   ....*....|....*..
gi 1720394403  541 DMVLLSvPDKLIVMTYL 557
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 1720394403 810 AELQALEQEQGQIDGRAAEVEKQLRSLMESGANRLQEEV-LIQEWFTLVNKKNALIR-----RQDQLQLLIEEQDLERRF 883
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRaaaelAAQLEELEEAEEALLERL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394403 884 ELLSRELRAMLAIEEwqKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERLERGLEQRRRKVSRQLSRRE 963
Cdd:COG1196   417 ERLEEELEELEEALA--ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494

transcription termination factor Rho; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394403 269 RAFRGQGSEPAAITGGQVGPETPEPPPSPPETRSTGQPgqtmvPTPAPRLRKGSDAPSSPVPCSGDEVPNTSEDPPTGMG 348
Cdd:PRK12678   56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQP-----AAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARER 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394403 349 SSGETQAQISSQEgtEAHEARPEPDIEVRGSKDSLGGERSKVEEEDTGDRPGASGAGNREKNTKKSDTTAGEAGESSELH 428
Cdd:PRK12678  131 RERGEAARRGAAR--KAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208

                         170
                  ....*....|....*..
gi 1720394403 429 QvDAEHKSKVQHRATEG 445
Cdd:PRK12678  209 R-EQGDRREERGRRDGG 224

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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 540
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394403 541 DMVLLSVPDKLIVMTYLCQIRAFCT 565
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 540
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80

                          90       100
                  ....*....|....*....|....*..
gi 1720394403 541 DMVLLSVPDKLIVMTYLCQIRAFCTGQ 567
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 1720394403 811 ELQALEQEQGQIDGRAAEVEKQLRSLMEsgaNRLQEEVLIQEWFTLVNKKNALIRRQDQLQLLIEEQDLERRFELLSREL 890
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRGEMS---GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720394403 891 RAMLAIEEWQKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERL 944
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 1720394403 464 QSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPADM 542
Cdd:cd21197     3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRvAETSLGIPALLDAEDM 82

                          90
                  ....*....|....*...
gi 1720394403 543 VLLSVPDKLIVMTYLCQI 560
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 539
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81

                          90
                  ....*....|....*...
gi 1720394403 540 ADmVLLSVPDKLIVMTYL 557
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 1720394403 462 SSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPA 540
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEvAERELGIPALLDPE 80

                          90
                  ....*....|....*....
gi 1720394403 541 DMVLLSVPDKLIVMTYLCQ 559
Cdd:cd21252    81 DMVSMKVPDCLSIMTYVSQ 99

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 1720394403 460 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 538
Cdd:cd21195     3 DIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDvAEREFGIPPVTT 82

                          90       100
                  ....*....|....*....|.
gi 1720394403 539 PADMVLLSVPDKLIVMTYLCQ 559
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 1720394403  12 GKRAAKFQFVACYHELVLECTkkwQPDKLVVVWTRRNrricSKAHSWQPGIQNPYRGTVVWmvPENVDISVTLYRDPHVD 91
Cdd:pfam10358   1 KKRKPKFQFVLTIHELQNLPL---VGGELFVKWRRGD----KKGSSGTTEKALVNNGRAIF--NEEFSIPVTLFLDKKGG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720394403  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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDgfAA---LGVSRLL 537
Cdd:cd21248     2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFN--VAeqkLGLTKLL 79

                          90
                  ....*....|....*....
gi 1720394403 538 EPADmVLLSVPDKLIVMTY 556
Cdd:cd21248    80 DPED-VNVEQPDEKSIITY 97

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. 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 1720394403 462 SSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPA 540
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTvAHEHLGIEKLLDPE 80

                          90
                  ....*....|....*..
gi 1720394403 541 DmVLLSVPDKLIVMTYL 557
Cdd:cd21187    81 D-VNVEQPDKKSILMYV 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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAAL-GVSRLLEP 539
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                          90
                  ....*....|....*....
gi 1720394403 540 ADMVLLS-VPDKLIVMTYL 557
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 1720394403 466 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPADMVL 544
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDvAEREFGIPPVTTGKEMAS 88

                          90
                  ....*....|...
gi 1720394403 545 LSVPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALG-VSRLLEP 539
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80

                          90
                  ....*....|....*...
gi 1720394403 540 ADMVLLSVPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALG-VSRLLEP 539
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLAdCVPLVEV 80

                          90
                  ....*....|....*....
gi 1720394403 540 ADMVLL-SVPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 539
Cdd:cd21322    17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLDP 96

                          90
                  ....*....|....*...
gi 1720394403 540 ADmVLLSVPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 539
Cdd:cd21192     3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRiAEQHLNIPRLLEV 82

                          90       100
                  ....*....|....*....|
gi 1720394403 540 ADmVLLSVPDKLIVMTYLCQ 559
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 539
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNvAEKELGLTKLLDP 84

                          90
                  ....*....|....*...
gi 1720394403 540 ADmVLLSVPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 539
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNlAEQHLGLTKLLDP 81

                          90
                  ....*....|....*...
gi 1720394403 540 ADmVLLSVPDKLIVMTYL 557
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 1720394403  466 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDP----LNIKQNNKQAFDGFAALGVSR-LLEPA 540
Cdd:smart00033   3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVvLFEPE 82

                           90
                   ....*....|....*..
gi 1720394403  541 DMVLLSvPDKLIVMTYL 557
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSL---DPLNikqNNKQAFD-GFAALGVSRL 536
Cdd:cd21287    10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLrkdDPLT---NLNTAFDvAEKYLDIPKM 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720394403 537 LEPADMVLLSVPDKLIVMTYLCQI-RAFCTGQEL 569
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 1720394403 461 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSL---DPLNikqNNKQAFD-GFAALGVSRL 536
Cdd:cd21289    10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLrkdDPIG---NLNTAFEvAEKYLDIPKM 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720394403 537 LEPADMVLLSVPDKLIVMTYL-CQIRAFCTGQELQ 570
Cdd:cd21289    87 LDAEDIVNTPKPDEKAIMTYVsCFYHAFAGAEQAE 121