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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*
gi 15292293   91 ADMVSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYF 105

LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15292293  146 RRDKCQKCNLPVFLAERVLVGKRAYHRTCLKCARCSSLLTPGSFYETEvNNIYCCETCPDEE 207
Cdd:cd09400    1 RREPCASCGLPVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSFYETE-YGSYCCETCPDEE 61

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*
gi 15292293   91 ADMVSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYF 105

LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15292293  146 RRDKCQKCNLPVFLAERVLVGKRAYHRTCLKCARCSSLLTPGSFYETEvNNIYCCETCPDEE 207
Cdd:cd09400    1 RREPCASCGLPVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSFYETE-YGSYCCETCPDEE 61

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 15292293      19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKAD----DIYENNDLAFTTAEKYLGIPALLDAADMV 94
Cdd:smart00033    6 WVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLGGKVVLFEPEDLV 85

                            90
                    ....*....|....*..
gi 15292293      95 SyEVPDRLSILTYLSQF 111
Cdd:smart00033   86 E-GPKLILGVIWTLISL 101

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 15292293     149 KCQKCNLPVFLAERVLVGK-RAYHRTCLKCARCSSLLTPGSFYETEvNNIYcCETC 203
Cdd:smart00132    1 KCAGCGKPIYGTERVLRALgKVWHPECFKCATCGKPLSGDTFFEKD-GKLY-CKDC 54

104 kDa microneme/rhoptry antigen; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   411 PEDHISPRKENKIFSNTESCSKQEGVLPKQMDL----------ESPKDKVIETKASETDYPEDLNPFKDDDSSKGAN-PF 479
Cdd:PTZ00449  588 PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIpkspkrpespKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKpPF 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   480 DSSDDEV---ELLKAIPAQQSKGKVVPPRPPPPKIGLSSISNPSEKPHSSPtlshgKKMPMPTPRISISKTQTPAKPMTH 556
Cdd:PTZ00449  668 DPKFKEKfydDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP-----RPLPPKLPRDEEFPFEPIGDPDAE 742

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   557 QGQKSSISSSSSEhlNSIRTFDRGADDRGSSISL-----PSANGPRKPLRASVGSPLRSEESSPTTSLSSITSPMRKKRQ 631
Cdd:PTZ00449  743 QPDDIEFFTPPEE--ERTFFHETPADTPLPDILAeefkeEDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRHRL 820

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   632 APLPPIQTDFDSDPG--------------FSKLSDEqkalLHTQLKAPNLGDSTRRLIpldqslLSDEATESSnyDESLS 697
Cdd:PTZ00449  821 DGLALSTTDLESDAGriakdasgkivklkRSKSFDD----LTTVEEAEEMGAEARKIV------VDDDGTEAD--DEDTH 888

                         330       340       350
                  ....*....|....*....|....*....|
gi 15292293   698 TSNADEEVNVVYRRILVPPTQPENTVERSK 727
Cdd:PTZ00449  889 PPEEKHKSEVRRRRPPKKPSKPKKPSKPKK 918

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*
gi 15292293   91 ADMVSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYF 105

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 15292293   14 KALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADM 93
Cdd:cd21197    3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDM 82

                         90
                 ....*....|....*....
gi 15292293   94 VSYEVPDRLSILTYLSQFY 112
Cdd:cd21197   83 VTMHVPDRLSIITYVSQYY 101

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKyLGIPALLDAADMVSYEV 98
Cdd:cd21198    9 WCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDPADMVLLSV 87

                         90
                 ....*....|....*..
gi 15292293   99 PDRLSILTYLSQFYKVL 115
Cdd:cd21198   88 PDKLSVMTYLHQIRAHF 104

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 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKyLGIPALLDA 90
Cdd:cd21254    1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79

                         90       100
                 ....*....|....*....|
gi 15292293   91 ADMVSYEVPDRLSILTYLSQ 110
Cdd:cd21254   80 SDMVLLAVPDKLTVMTYLYQ 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 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADMVSYEV 98
Cdd:cd21195   12 WCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMASAQE 91

                         90
                 ....*....|....*..
gi 15292293   99 PDRLSILTYLSQFYKVL 115
Cdd:cd21195   92 PDKLSMVMYLSKFYELF 108

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 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADMVSYEV 98
Cdd:cd21250   12 WCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMASAEE 91

                         90
                 ....*....|....*.
gi 15292293   99 PDRLSILTYLSQFYKV 114
Cdd:cd21250   92 PDKLSMVMYLSKFYEL 107

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 15292293   15 ALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADmV 94
Cdd:cd21248    6 ALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPED-V 84

                         90
                 ....*....|....*...
gi 15292293   95 SYEVPDRLSILTYLSQFY 112
Cdd:cd21248   85 NVEQPDEKSIITYVVTYY 102

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 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADMVSYEV 98
Cdd:cd21251   13 WCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMASVGE 92

                         90
                 ....*....|....*..
gi 15292293   99 PDRLSILTYLSQFYKVL 115
Cdd:cd21251   93 PDKLSMVMYLTQFYEMF 109

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21189    1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80

                         90       100
                 ....*....|....*....|....*
gi 15292293   91 ADmVSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21189   81 ED-VDVPEPDEKSIITYVSSLYDVF 104

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADMVSYE- 97
Cdd:cd21200    9 WCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVEDMVRMGn 88

                         90
                 ....*....|....*...
gi 15292293   98 VPDRLSILTYLSQFYKVL 115
Cdd:cd21200   89 RPDWKCVFTYVQSLYRHL 106

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, 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-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15292293   12 GTK--ALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYlGIPALLD 89
Cdd:cd21199    7 GSKrnALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLT 85

                         90       100
                 ....*....|....*....|....
gi 15292293   90 AADMVSYEVPDRLSILTYLSQFYK 113
Cdd:cd21199   86 IDEMVSMERPDWQSVMSYVTAIYK 109

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 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADMVSYEV 98
Cdd:cd21259    9 WCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVEDMVRMRE 88

                         90
                 ....*....|....*..
gi 15292293   99 PDRLSILTYLSQFYKVL 115
Cdd:cd21259   89 PDWKCVYTYIQEFYRCL 105

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 15292293   14 KALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADM 93
Cdd:cd21192    6 KALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDV 85

                         90
                 ....*....|....*...
gi 15292293   94 VSyEVPDRLSILTYLSQF 111
Cdd:cd21192   86 LV-DKPDERSIMTYVSQF 102

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 15292293    3 DRRGTKvgTGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYL 82
Cdd:cd21322   11 DNRETR--SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHL 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15292293   83 GIPALLDAADmVSYEVPDRLSILTYLSQFYKVLGK 117
Cdd:cd21322   89 GLTKLLDPED-VNMEAPDEKSIITYVVSFYHYFSK 122

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 15292293     14 KALEYWCRVVTQGY-NGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRL--KADDIYENNDLAFTTAEKYLGIP-ALLD 89
Cdd:pfam00307    5 KELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPkVLIE 84

                           90       100
                   ....*....|....*....|....*
gi 15292293     90 AADMVSyevPDRLSILTYLSQFYKV 114
Cdd:pfam00307   85 PEDLVE---GDNKSVLTYLASLFRR 106

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 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. 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 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21290   13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDA 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 15292293   91 ADMVSYEVPDRLSILTYLSQFYKVLGKSLKHP 122
Cdd:cd21290   93 EDIVNTARPDEKAIMTYVSSFYHAFSGAQKAE 124

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 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDA 90
Cdd:cd21320    2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81

                         90       100
                 ....*....|....*....|....*..
gi 15292293   91 ADmVSYEVPDRLSILTYLSQFYKVLGK 117
Cdd:cd21320   82 ED-ISVDHPDEKSIITYVVTYYHYFSK 107

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 15292293   11 TGTKALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKyLGIPALLDA 90
Cdd:cd21239    1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79

                         90       100
                 ....*....|....*....|....*
gi 15292293   91 ADmVSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21239   80 ED-VDVSSPDEKSVITYVSSLYDVF 103

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 15292293   14 KALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADm 93
Cdd:cd21234    3 KILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED- 81

                         90       100
                 ....*....|....*....|..
gi 15292293   94 VSYEVPDRLSILTYLSQFYKVL 115
Cdd:cd21234   82 VAVQLPDKKSIIMYLTSLFEVL 103

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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 15292293   14 KALEYWCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAADM 93
Cdd:cd21226    3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82

                         90
                 ....*....|....*....
gi 15292293   94 VSYEvPDRLSILTYLSQFY 112
Cdd:cd21226   83 MTGN-PDERSIVLYTSLFY 100

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 15292293   19 WCRVVTQGYNGVKVENMTTSWRNGLAFCAIIHHFRPDLIDFDRLKADDIYENNDLAFTTAEKYLGIPALLDAAD-MVSYE 97
Cdd:cd21258    9 WCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVEDmMIMGK 88

                         90
                 ....*....|....*...
gi 15292293   98 VPDRLSILTYLSQFYKVL 115
Cdd:cd21258   89 KPDSKCVFTYVQSLYNHL 106