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 1622863092 374 GVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDV 453
Cdd:cd21260     1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622863092 454 DDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK 489
Cdd:cd21260    81 EDMVRMSVPDSKCVYTYIQELYRSLVQKGLVKTKKK 116

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (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. SMTNL1 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 1622863092 374 GVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDV 453
Cdd:cd21260     1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622863092 454 DDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK 489
Cdd:cd21260    81 EDMVRMSVPDSKCVYTYIQELYRSLVQKGLVKTKKK 116

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 1622863092  377 NMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDY----AELDPTKRRHNFTLAFSTAEKLADCAQLLD 452
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 1622863092  453 VDDMVRLAvPDSKCVYTYIQEL 474
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092    5 EGKPSEDGTTVSPVADNPEMSGGGAPAEETKGTAGKAINEG--PPAEAGKQEKAPAEDGISVELQGEANGlDEVKVESQG 82
Cdd:TIGR00927  643 ERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGeiPAERKGEQEGEGEIEAKEADHKGETEA-EEVEHEGET 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092   83 EAGGKEDaEAELKEEDGEKEETTAASQEMTGRKEETKSEPKEAEEKEESMLASEKQKAEEKEAKPESGQKADANDRDKPE 162
Cdd:TIGR00927  722 EAEGTED-EGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGK 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092  163 PKATVEEEEAKTASQEETGQREKRSTEPKEKATDEEAKAESQkkavveDEAKAEPKESDGKEEAKHDTTKEADAKEEEPG 242
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQ------GEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEE 874

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1622863092  243 SPSEEQEQDVEKEPEGGAgvlPSSpEEWPES 273
Cdd:TIGR00927  875 EEEEEEEEEEEEEEENEE---PLS-LEWPET 901

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092 108 SQEMTGRKEETKSEPKEAEEKeesmLASEKQKAEEKEAKPE----SGQKADANDRDKPEPKATVEEEEAKTASQEETGQR 183
Cdd:pfam05262 208 SQEDAKRAQQLKEELDKKQID----ADKAQQKADFAQDNADkqrdEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREI 283

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622863092 184 EKRSTEPKEKATD----EEAKAESQKKAVVEDEAKAEPKESDGKEEAK 227
Cdd:pfam05262 284 EKAQIEIKKNDEEalkaKDHKAFDLKQESKASEKEAEDKELEAQKKRE 331

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (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. SMTNL1 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 1622863092 374 GVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDV 453
Cdd:cd21260     1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622863092 454 DDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK 489
Cdd:cd21260    81 EDMVRMSVPDSKCVYTYIQELYRSLVQKGLVKTKKK 116

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 1622863092 374 GVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDV 453
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622863092 454 DDMVRLAVPDSKCVYTYIQELYRSLVQKGLVK 485
Cdd:cd21259    81 EDMVRMREPDWKCVYTYIQEFYRCLVQKGLVK 112

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092 375 VKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVD 454
Cdd:cd21261     2 IKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVE 81

                          90       100
                  ....*....|....*....|....*
gi 1622863092 455 DMVRLA-VPDSKCVYTYIQELYRSL 478
Cdd:cd21261    82 DMMVMGrKPDPMCVFTYVQSLYNHL 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 1622863092 373 GGVK-NMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKlADCAQLL 451
Cdd:cd21199     6 GGSKrNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTL 84

                          90       100
                  ....*....|....*....|....*
gi 1622863092 452 DVDDMVRLAVPDSKCVYTYIQELYR 476
Cdd:cd21199    85 TIDEMVSMERPDWQSVMSYVTAIYK 109

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 1622863092 374 GVKNmLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDV 453
Cdd:cd21253     2 GIKA-LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                          90       100
                  ....*....|....*....|..
gi 1622863092 454 DDMVRLAVPDSKCVYTYIQELY 475
Cdd:cd21253    81 EDMVALKVPDKLSILTYVSQYY 102

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 1622863092 373 GGVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLAdCAQLLD 452
Cdd:cd21256    13 GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVG-IKSTLD 91

                          90       100
                  ....*....|....*....|....
gi 1622863092 453 VDDMVRLAVPDSKCVYTYIQELYR 476
Cdd:cd21256    92 INEMVRTERPDWQSVMTYVTAIYK 115

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 1622863092 376 KNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDD 455
Cdd:cd21194     4 KDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAED 83

                          90       100
                  ....*....|....*....|
gi 1622863092 456 mVRLAVPDSKCVYTYIQELY 475
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 1622863092 379 LLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLAdCAQLLDVDDMVR 458
Cdd:cd21255     6 LLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLG-VPRLLEPADMVL 84

                          90
                  ....*....|....*.
gi 1622863092 459 LAVPDSKCVYTYIQEL 474
Cdd:cd21255    85 LPIPDKLIVMTYLCQL 100

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 1622863092 376 KNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDD 455
Cdd:cd21248     4 KDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPED 83

                          90       100
                  ....*....|....*....|
gi 1622863092 456 mVRLAVPDSKCVYTYIQELY 475
Cdd:cd21248    84 -VNVEQPDEKSIITYVVTYY 102

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 1622863092 375 VKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVD 454
Cdd:cd21189     2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81

                          90       100
                  ....*....|....*....|.
gi 1622863092 455 DmVRLAVPDSKCVYTYIQELY 475
Cdd:cd21189    82 D-VDVPEPDEKSIITYVSSLY 101

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 1622863092 375 VKNMLLEWCRAMTKKY-EHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL--DPTKRRHNFTLAFSTAEKLADCAQ-L 450
Cdd:pfam00307   3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKvL 82

                          90       100
                  ....*....|....*....|....*.
gi 1622863092 451 LDVDDMVRlavPDSKCVYTYIQELYR 476
Cdd:pfam00307  83 IEPEDLVE---GDNKSVLTYLASLFR 105

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 1622863092 379 LLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL---DPTKR-RHNFTLAFstaEKLAdCAQLLDVD 454
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLvkdSPESRlEHAFTVAH---EHLG-IEKLLDPE 80

                          90       100
                  ....*....|....*....|....
gi 1622863092 455 DmVRLAVPDSKCVYTYIQELYRSL 478
Cdd:cd21187    81 D-VNVEQPDKKSILMYVTSLFQVL 103

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863092 379 LLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDDMVR 458
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84

                          90
                  ....*....|....*..
gi 1622863092 459 LAVPDSKCVYTYIQELY 475
Cdd:cd21252    85 MKVPDCLSIMTYVSQYY 101

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 1622863092 376 KNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDD 455
Cdd:cd21289    12 KEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAED 91

                          90       100
                  ....*....|....*....|...
gi 1622863092 456 MVRLAVPDSKCVYTYIQELYRSL 478
Cdd:cd21289    92 IVNTPKPDEKAIMTYVSCFYHAF 114

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 1622863092 373 GGVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLD 452
Cdd:cd21192     2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81

                          90
                  ....*....|....*....
gi 1622863092 453 VDDMVrLAVPDSKCVYTYI 471
Cdd:cd21192    82 VEDVL-VDKPDERSIMTYV 99

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 1622863092  377 NMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDY----AELDPTKRRHNFTLAFSTAEKLADCAQLLD 452
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 1622863092  453 VDDMVRLAvPDSKCVYTYIQEL 474
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101

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 1622863092 378 MLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL----DPTKRRHNftlAFSTAEKLADCAQLLDV 453
Cdd:cd21233     4 ILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvsqqSATERLDH---AFNIARQHLGIEKLLDP 80

                          90       100
                  ....*....|....*....|....*...
gi 1622863092 454 DDmVRLAVPDSKCVYTYIQELYRSLVQK 481
Cdd:cd21233    81 ED-VATAHPDKKSILMYVTSLFQVLPQQ 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 1622863092 376 KNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLAdCAQLLDVDD 455
Cdd:cd21239     3 KERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLG-VTRLLDPED 81

                          90       100
                  ....*....|....*....|
gi 1622863092 456 mVRLAVPDSKCVYTYIQELY 475
Cdd:cd21239    82 -VDVSSPDEKSVITYVSSLY 100

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 1622863092 379 LLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDDMVR 458
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAS 88

                          90
                  ....*....|....*..
gi 1622863092 459 LAVPDSKCVYTYIQELY 475
Cdd:cd21195    89 AQEPDKLSMVMYLSKFY 105

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 1622863092 379 LLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL---DPTKRRHnftLAFSTAEKLADCAQLLDVDD 455
Cdd:cd21226     5 LLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIeqmDAEARLN---LAFDFAEKKLGIPKLLEAED 81

                          90       100
                  ....*....|....*....|..
gi 1622863092 456 MVRlAVPDSKCVYTYIQELYRS 477
Cdd:cd21226    82 VMT-GNPDERSIVLYTSLFYHA 102

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 1622863092 378 MLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDY---AELDPTKRRHNftlAFSTAEKLADCAQLLDVD 454
Cdd:cd21234     4 ILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWdkvVKMSPVERLEH---AFSKAKNHLGIEKLLDPE 80

                          90       100
                  ....*....|....*....|....
gi 1622863092 455 DmVRLAVPDSKCVYTYIQELYRSL 478
Cdd:cd21234    81 D-VAVQLPDKKSIIMYLTSLFEVL 103

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 1622863092 377 NMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPTKRRHNFTLAFSTAEKLADCAQLLDVDDM 456
Cdd:cd21250     7 NKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86