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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQIRAFCT 121
Cdd:cd21255    81 DMVLLPIPDKLIVMTYLCQLRAHFT 105

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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQIRAFCT 121
Cdd:cd21255    81 DMVLLPIPDKLIVMTYLCQLRAHFT 105

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  17 SSSQSLLEWCQEVTNGY-RGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSL--DPLNIKQNNKQAFD-GFAALGVSR- 91
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDvAEKKLGVPKv 81

                          90       100
                  ....*....|....*....|....*
gi 1720394405  92 LLEPADMVLlsvPDKLIVMTYLCQI 116
Cdd:pfam00307  82 LIEPEDLVE---GDNKSVLTYLASL 103

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  22 LLEWCQEVTNGYR-GVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPL--NIKQNNKQAFD-GFAALGVSRLLEPAD 97
Cdd:COG5069   130 LLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFEnANKVIGIARLIGVED 209

                          90       100
                  ....*....|....*....|...
gi 1720394405  98 MVLLSVPDKLIVMTYLC-QIRAF 119
Cdd:COG5069   210 IVNVSIPDERSIMTYVSwYIIRF 232

exonuclease subunit SbcC; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  366 AELQALEQEQGQIDGRAAEVEKQLRSLM------ESGANRL--QEEVLIQEWFTLVNKKNALIRRQDQLQ-LLIEEQDLE 436
Cdd:PRK10246   530 SRLDALEKEVKKLGEEGAALRGQLDALTkqlqrdESEAQSLrqEEQALTQQWQAVCASLNITLQPQDDIQpWLDAQEEHE 609

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720394405  437 RRFELLSR--ELRAMLAIEEWQKTVAQQHREQ 466
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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQIRAFCT 121
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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80

                          90       100
                  ....*....|....*....|....*..
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQIRAFCTGQ 123
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 1720394405 367 ELQALEQEQGQIDGRAAEVEKQLRSLMEsgaNRLQEEVLIQEWFTLVNKKNALIRRQDQLQLLIEEQDLERRFELLSREL 446
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRGEMS---GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720394405 447 RAMLAIEEWQKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERL 500
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 1720394405  20 QSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPADM 98
Cdd:cd21197     3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRvAETSLGIPALLDAEDM 82

                          90
                  ....*....|....*...
gi 1720394405  99 VLLSVPDKLIVMTYLCQI 116
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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAA-LGVSRLLEP 95
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81

                          90
                  ....*....|....*...
gi 1720394405  96 ADmVLLSVPDKLIVMTYL 113
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 1720394405  16 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 94
Cdd:cd21251     4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDiAEKEFGISPIMT 83

                          90       100
                  ....*....|....*....|.
gi 1720394405  95 PADMVLLSVPDKLIVMTYLCQ 115
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 1720394405  16 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 94
Cdd:cd21195     3 DIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDvAEREFGIPPVTT 82

                          90       100
                  ....*....|....*....|.
gi 1720394405  95 PADMVLLSVPDKLIVMTYLCQ 115
Cdd:cd21195    83 GKEMASAQEPDKLSMVMYLSK 103

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 95
Cdd:cd21216    10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDvAEKHLDIPKMLDA 89

                          90       100
                  ....*....|....*....|....*
gi 1720394405  96 ADMVLLSVPDKLIVMTYL-CQIRAF 119
Cdd:cd21216    90 EDIVNTPRPDERSVMTYVsCYYHAF 114

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 1720394405  18 SSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEPA 96
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTvAHEHLGIEKLLDPE 80

                          90
                  ....*....|....*..
gi 1720394405  97 DmVLLSVPDKLIVMTYL 113
Cdd:cd21187    81 D-VNVEQPDKKSILMYV 96

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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 95
Cdd:cd21291    10 TAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQLLDV 89

                          90       100
                  ....*....|....*....|
gi 1720394405  96 ADMVLLSVPDKLIVMTYLCQ 115
Cdd:cd21291    90 EDVCDVAKPDERSIMTYVAY 109

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  17 SSSQSLLEWCQEVTNGY-RGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSL--DPLNIKQNNKQAFD-GFAALGVSR- 91
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDvAEKKLGVPKv 81

                          90       100
                  ....*....|....*....|....*
gi 1720394405  92 LLEPADMVLlsvPDKLIVMTYLCQI 116
Cdd:pfam00307  82 LIEPEDLVE---GDNKSVLTYLASL 103

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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21257     8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87

                          90       100
                  ....*....|....*....|
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQI 116
Cdd:cd21257    88 EMMYTDRPDWQSVMQYVAQI 107

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 95
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNvAERQLGITKLLDP 84

                          90
                  ....*....|....*...
gi 1720394405  96 ADmVLLSVPDKLIVMTYL 113
Cdd:cd21319    85 ED-VFTENPDEKSIITYV 101

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 95
Cdd:cd21249     4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLvAEQELGISQLLDP 83

                          90
                  ....*....|....*...
gi 1720394405  96 ADmVLLSVPDKLIVMTYL 113
Cdd:cd21249    84 ED-VAVPHPDERSIMTYV 100

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A 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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21256    14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKSTLDIN 93

                          90       100
                  ....*....|....*....|...
gi 1720394405  97 DMVLLSVPDKLIVMTYLCQIRAF 119
Cdd:cd21256    94 EMVRTERPDWQSVMTYVTAIYKY 116

second calponin homology (CH) domain found in dystonin and similar proteins; 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. Dystonin 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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPA 96
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80

                          90
                  ....*....|....*..
gi 1720394405  97 DmVLLSVPDKLIVMTYL 113
Cdd:cd21239    81 D-VDVSSPDEKSVITYV 96

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; 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. MACF1 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 1720394405  16 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEP 95
Cdd:cd21240     3 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDA 82

                          90       100
                  ....*....|....*....|.
gi 1720394405  96 ADMVLLSvPDKLIVMTYLCQI 116
Cdd:cd21240    83 EDVDVPS-PDEKSVITYVSSI 102

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 1720394405  17 SSSQSLLEWCQEVTNGYRgvcITNFTTSWRNGLAFCAILHRFYPDKI-DYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 94
Cdd:cd21184     1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDiAEEELGIPKIIT 77

                          90       100
                  ....*....|....*....|...
gi 1720394405  95 PADMVLLSVpDKLIVMTYLCQIR 117
Cdd:cd21184    78 PEDMVSPNV-DELSVMTYLSYFR 99

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  22 LLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYF---SLDPLNIKQNNKQAFDGFAALGVSR--LLEPA 96
Cdd:cd00014     4 LLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkkPKSPFKKRENINLFLNACKKLGLPEldLFEPE 83

                          90       100
                  ....*....|....*....|.
gi 1720394405  97 DmvLLSVPDKLIVMTYLCQIR 117
Cdd:cd00014    84 D--LYEKGNLKKVLGTLWALA 102

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 1720394405  16 VSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLE 94
Cdd:cd21244     4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRiAEQELKIPRLLE 83

                          90       100
                  ....*....|....*....|.
gi 1720394405  95 PADmVLLSVPDKLIVMTYLCQ 115
Cdd:cd21244    84 PED-VDVVNPDEKSIMTYVAQ 103

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; 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, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 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-1 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 1720394405  20 QSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDgfAA---LGVSRLLEPA 96
Cdd:cd21243     8 KALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFT--VAekeLGIPRLLDPE 85

                          90
                  ....*....|....*....
gi 1720394405  97 DmVLLSVPDKLIVMTYLCQ 115
Cdd:cd21243    86 D-VDVDKPDEKSIMTYVAQ 103

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. 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 1720394405  17 SSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFD-GFAALGVSRLLEP 95
Cdd:cd21288    10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEiAEKHLDIPKMLDA 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720394405  96 ADMVLLSVPDKLIVMTYL-CQIRAFCTGQELQ 126
Cdd:cd21288    90 EDIVNTPKPDERAIMTYVsCFYHAFAGAEQAE 121

second calponin homology (CH) domain found in utrophin and similar proteins; 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. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720394405  18 SSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDgFAA--LGVSRLLEP 95
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFS-KAKnhLGIEKLLDP 79

                          90
                  ....*....|....*...
gi 1720394405  96 ADmVLLSVPDKLIVMTYL 113
Cdd:cd21234    80 ED-VAVQLPDKKSIIMYL 96