K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259    27 SQGIAEEvAEGTVGTSDKEGpsdwaEHLCKAASKSGESGGS----PGEASILDELKT--DLQGEARGKDEAQGDLAEEKV 100
Cdd:TIGR00927  631 SKGDVAE-AEHTGERTGEEG-----ERPTEAEGENGEESGGeaeqEGETETKGENESegEIPAERKGEQEGEGEIEAKEA 704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259   101 GKEDTTAASQEDTGkkEETKPEPNEvREKEEAMLASEKQKVDEKETNLESKEKSDV---NDKAKPEPKEDAGAEVTVNEA 177
Cdd:TIGR00927  705 DHKGETEAEEVEHE--GETEAEGTE-DEGEIETGEEGEEVEDEGEGEAEGKHEVETegdRKETEHEGETEAEGKEDEDEG 781

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568918259   178 ETESQEEADVKDQAKPELPEVDGKETGSDTKELVEPESPTEEQEQGKENESEERAA 233
Cdd:TIGR00927  782 EIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQEL 837

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 568918259  345 VKNMLLEWCRAMTRNY-EHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAEL--DPAKRRHNFTLAFSTAEKLADCAQ-L 420
Cdd:pfam00307   3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKvL 82

                          90       100
                  ....*....|....*....|....*.
gi 568918259  421 LEVDDMVRlavPDSKCVYTYIQELYR 446
Cdd:pfam00307  83 IEPEDLVE---GDNKSVLTYLASLFR 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259 346 KNMLLEWCRAMTRNYE-HVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRH--NFTLAFSTAEKLADCAQLLE 422
Cdd:COG5069  127 HINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIG 206

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568918259 423 VDDMVRLAVPDSKCVYTYIQELY--RSLVQK 451
Cdd:COG5069  207 VEDIVNVSIPDERSIMTYVSWYIirFGLLEK 237

MAEBL; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259   31 AEEV--AEGTVGTSDKEGPSDWAEHLCKAASKSGESGGSPGEASILDELKTDLQgEARGKDEAQGDLAEEKVGKEDTTAA 108
Cdd:PTZ00121 1427 AEEKkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKA 1505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259  109 SQE----DTGKKEETKPEPNEVREKEEAMLASEKQKVDEKETNLESKEKSDVNDKAKPEPKEDA-GAEVTVNEAETESQE 183
Cdd:PTZ00121 1506 AEAkkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAkKAEEDKNMALRKAEE 1585

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568918259  184 EADVKDQAKPELPEVDGKETGSDTKELVEPESPTEEQEQGKENESEERAAVIPSSPEE 241
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259  98 EKVGKEDTTAASQEDTGKKEETKPePNEVREKEEAMLASEKQKVDEKETNLESKEKSDVNDKAKPEPKEDAGA-EVTVNE 176
Cdd:NF040676 162 QKSVKAKEEAKTQKVAKAKETTKA-QEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVKPKEEEKVqEIVKPK 240

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568918259 177 AETESQEEADVKDQAKPElpEVDGKETGSDTKELVEPESPTEEQEQGKENEsEERAAVIPSSPEE 241
Cdd:NF040676 241 EEAKVQEEVKVKEEAKVQ--EIAKAKEEAKAQEIAKAKEEAKAQEIAKAKE-EAKAQEIAKAKEE 302

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 568918259 344 GVKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEV 423
Cdd:cd21200    1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80

                         90       100
                 ....*....|....*....|....*..
gi 568918259 424 DDMVRLA-VPDSKCVYTYIQELYRSLV 449
Cdd:cd21200   81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107

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 568918259 345 VKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVD 424
Cdd:cd21258    2 IKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVE 81

                         90       100
                 ....*....|....*....|....*
gi 568918259 425 DMVRLA-VPDSKCVYTYIQELYRSL 448
Cdd:cd21258   82 DMMIMGkKPDSKCVFTYVQSLYNHL 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 568918259 343 GGVK-NMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKlADCAQLL 421
Cdd:cd21199    6 GGSKrNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTL 84

                         90       100
                 ....*....|....*....|....*
gi 568918259 422 EVDDMVRLAVPDSKCVYTYIQELYR 446
Cdd:cd21199   85 TIDEMVSMERPDWQSVMSYVTAIYK 109

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 568918259 349 LLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLAdCAQLLEVDDMVR 428
Cdd:cd21198    6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLG-IPRLLDPADMVL 84

                         90
                 ....*....|....*..
gi 568918259 429 LAVPDSKCVYTYIQELY 445
Cdd:cd21198   85 LSVPDKLSVMTYLHQIR 101

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21291   12 KEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVED 91

                         90       100
                 ....*....|....*....|
gi 568918259 426 MVRLAVPDSKCVYTYIQELY 445
Cdd:cd21291   92 VCDVAKPDERSIMTYVAYYF 111

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. 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. 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. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259 347 NMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDDM 426
Cdd:cd22198    3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                         90
                 ....*....|....*....
gi 568918259 427 VRLAVPDSKCVYTYIQELY 445
Cdd:cd22198   83 ASLAVPDKLSMVSYLSQFY 101

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21194    4 KDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAED 83

                         90       100
                 ....*....|....*....|
gi 568918259 426 mVRLAVPDSKCVYTYIQELY 445
Cdd:cd21194   84 -VDVARPDEKSIMTYVASYY 102

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 568918259 349 LLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLAdCAQLLEVDDMVR 428
Cdd:cd21255    6 LLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLG-VPRLLEPADMVL 84

                         90
                 ....*....|....*.
gi 568918259 429 LAVPDSKCVYTYIQEL 444
Cdd:cd21255   85 LPIPDKLIVMTYLCQL 100

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 568918259  345 VKNMLLEWCRAMTRNY-EHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAEL--DPAKRRHNFTLAFSTAEKLADCAQ-L 420
Cdd:pfam00307   3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKvL 82

                          90       100
                  ....*....|....*....|....*.
gi 568918259  421 LEVDDMVRlavPDSKCVYTYIQELYR 446
Cdd:pfam00307  83 IEPEDLVE---GDNKSVLTYLASLFR 105

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21249    6 KEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDPED 85

                         90       100
                 ....*....|....*....|
gi 568918259 426 mVRLAVPDSKCVYTYIQELY 445
Cdd:cd21249   86 -VAVPHPDERSIMTYVSLYY 104

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 568918259 345 VKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVD 424
Cdd:cd21189    2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81

                         90       100
                 ....*....|....*....|.
gi 568918259 425 DmVRLAVPDSKCVYTYIQELY 445
Cdd:cd21189   82 D-VDVPEPDEKSIITYVSSLY 101

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 568918259 349 LLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDDmVR 428
Cdd:cd21187    5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED-VN 83

                         90       100
                 ....*....|....*....|
gi 568918259 429 LAVPDSKCVYTYIQELYRSL 448
Cdd:cd21187   84 VEQPDKKSILMYVTSLFQVL 103

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 568918259 343 GGVKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLE 422
Cdd:cd21192    2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81

                         90
                 ....*....|....*....
gi 568918259 423 VDDMVrLAVPDSKCVYTYI 441
Cdd:cd21192   82 VEDVL-VDKPDERSIMTYV 99

second calponin homology (CH) domain found in dystrophin and similar proteins; 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. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by 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, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918259 348 MLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDY---AELDPAKRRHNFtlAFSTAEKLADCAQLLEVD 424
Cdd:cd21233    4 ILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnsvVSQQSATERLDH--AFNIARQHLGIEKLLDPE 81

                         90       100
                 ....*....|....*....|....*..
gi 568918259 425 DmVRLAVPDSKCVYTYIQELYRSLVQK 451
Cdd:cd21233   82 D-VATAHPDKKSILMYVTSLFQVLPQQ 107

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21289   12 KEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAED 91

                         90       100
                 ....*....|....*....|...
gi 568918259 426 MVRLAVPDSKCVYTYIQELYRSL 448
Cdd:cd21289   92 IVNTPKPDEKAIMTYVSCFYHAF 114

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21288   12 KEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAED 91

                         90       100
                 ....*....|....*....|...
gi 568918259 426 MVRLAVPDSKCVYTYIQELYRSL 448
Cdd:cd21288   92 IVNTPKPDERAIMTYVSCFYHAF 114

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 568918259 346 KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21320    4 KDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPED 83

                         90       100
                 ....*....|....*....|
gi 568918259 426 mVRLAVPDSKCVYTYIQELY 445
Cdd:cd21320   84 -ISVDHPDEKSIITYVVTYY 102

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 568918259 349 LLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAEL---DPAKRRHnftLAFSTAEKLADCAQLLEVDD 425
Cdd:cd21226    5 LLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIeqmDAEARLN---LAFDFAEKKLGIPKLLEAED 81

                         90       100
                 ....*....|....*....|..
gi 568918259 426 MVRlAVPDSKCVYTYIQELYRS 447
Cdd:cd21226   82 VMT-GNPDERSIVLYTSLFYHA 102

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 568918259 343 GGVKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLE 422
Cdd:cd21243    4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83

                         90
                 ....*....|....*....
gi 568918259 423 VDDmVRLAVPDSKCVYTYI 441
Cdd:cd21243   84 PED-VDVDKPDEKSIMTYV 101

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 568918259 347 NMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDDM 426
Cdd:cd21250    7 NKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86

                         90
                 ....*....|....*....
gi 568918259 427 VRLAVPDSKCVYTYIQELY 445
Cdd:cd21250   87 ASAEEPDKLSMVMYLSKFY 105