second calponin homology (CH) domain found in calmin and similar proteins; 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. Calmin 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 1953409455 186 QRKAIRTLLAWVQRKTRKYGVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 1953409455 266 PEDIMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

second calponin homology (CH) domain found in calmin and similar proteins; 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. Calmin 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 1953409455 186 QRKAIRTLLAWVQRKTRKYGVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 1953409455 266 PEDIMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

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 1953409455 191 RTLLAWVQRKTRKYG--VAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQ--ALEDSMRENLEKAFSIAHEALHIPR-LLE 265
Cdd:pfam00307   5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84

                          90       100
                  ....*....|....*....|....*.
gi 1953409455 266 PEDImVDtPDEQSIVTYVAQFLEHFP 291
Cdd:pfam00307  85 PEDL-VE-GDNKSVLTYLASLFRRFQ 108

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 1953409455   36 RTFTRWVNLHLEKcNPPLEVKDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033   1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                           90       100
                   ....*....|....*....|...
gi 1953409455  115 DAAEIADGNPsLVLGLIWNIILF 137
Cdd:smart00033  80 EPEDLVEGPK-LILGVIWTLISL 101

second calponin homology (CH) domain found in calmin and similar proteins; 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. Calmin 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 1953409455 186 QRKAIRTLLAWVQRKTRKYGVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 1953409455 266 PEDIMVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  29 ERENVQKRTFTRWVNLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953409455 109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  29 ERENVQKRTFTRWVNLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953409455 109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113

first 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 links 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  32 NVQKRTFTRWVNLHLEKCNPPLeVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1953409455 112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILHWQVK 107

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455 189 AIRTLLAWVQRKTRKYG-VAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLEPE 267
Cdd:cd21244     6 ARKALLLWAQEQCAKVGsISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85

                          90       100
                  ....*....|....*....|...
gi 1953409455 268 DIMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21244    86 DVDVVNPDEKSIMTYVAQFLQYS 108

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  33 VQKRTFTRWVNLHLEKCNPPleVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRE--RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*..
gi 1953409455 113 SIDAAEIADGNPSLVLGLIWNIILFFQ 139
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105

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 1953409455 187 RKAIRTLLAWVQRKTRKY-GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLE 265
Cdd:cd21194     1 KSAKDALLLWCQRKTAGYpGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                          90       100
                  ....*....|....*....|....*
gi 1953409455 266 PEDIMVDTPDEQSIVTYVAQFLEHF 290
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  29 ERENVQKRTFTRWVNLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21236    13 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHRLQNVQIALDYLKRRQ 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1953409455 109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21236    89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123

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 1953409455 193 LLAWVQRKTRKY-GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLEPEDIMV 271
Cdd:cd21189     6 LLLWARRTTEGYpGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPEDVDV 85

                          90       100
                  ....*....|....*....|
gi 1953409455 272 DTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21189    86 PEPDEKSIITYVSSLYDVFP 105

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  26 LQVERENVQKRTFTRWVNLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE 105
Cdd:COG5069     2 EAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455 106 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEltgnlsrnspssslspgsggtdsdssfpptpTAErsmavsvKD 185
Cdd:COG5069    81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT-------------------------------INE-------EG 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455 186 QRKAIRTLLAWVQRKTRKY--GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDM----KQALEDsmRENLEKAFSIAHEALH 259
Cdd:COG5069   123 ELTKHINLLLWCDEDTGGYkpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPnvldLQKKNK--ALNNFQAFENANKVIG 200

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953409455 260 IPRLLEPEDIM-VDTPDEQSIVTYVAQFLEHFPELEAED 297
Cdd:COG5069   201 IARLIGVEDIVnVSIPDERSIMTYVSWYIIRFGLLEKID 239

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  33 VQKRTFTRWVNLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE-DSNVKL 111
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKHIA--DLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEeDEGIKI 92

                          90       100
                  ....*....|....*....|....*....
gi 1953409455 112 VSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21311    93 VNIDSSDIVDGKLKLILGLIWTLILHYSI 121

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  31 ENVQKRTFTRWVNLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 1953409455 111 LVSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107

first 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 first CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  32 NVQKRTFTRWVNLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVEL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1953409455 112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  33 VQKRTFTRWVNLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVN--KRIYNLETDLSDGLRLIALLEVLSQKRMYKKYnKRPTFRQMKLENVSVALEFLERESIKL 81

                          90       100
                  ....*....|....*....|....*..
gi 1953409455 112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21228    82 VSIDSSAIVDGNLKLILGLIWTLILHY 108

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 1953409455 191 RTLLAWVQRKTRKY-GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPRLLEPEDI 269
Cdd:cd21187     3 KTLLAWCRQSTRGYeQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82

                          90       100
                  ....*....|....*....|..
gi 1953409455 270 MVDTPDEQSIVTYVAQFLEHFP 291
Cdd:cd21187    83 NVEQPDKKSILMYVTSLFQVLP 104

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455 184 KDQRKAIRTLLAWVQRKTRKY-GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPR 262
Cdd:cd21319     1 RETRSAKDALLLWCQMKTAGYpNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1953409455 263 LLEPEDIMVDTPDEQSIVTYVAQFLEHFPELE 294
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455 184 KDQRKAIRTLLAWVQRKTRKY-GVAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQALEDSMRENLEKAFSIAHEALHIPR 262
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYpNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953409455 263 LLEPEDIMVDTPDEQSIVTYVAQFLEHFPELEA 295
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  22 RVQNLQVERENVQKRTFTRWVNLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21316    42 RIKALADEREAVQKKTFTKWVNSHLARVS--CRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRM-RIHCLENVDKAL 118

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1953409455 102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21316   119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  31 ENVQKRTFTRWVNLHLeKCNPPlEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSH-RIFRLNNIAKALKFLEDSNV 109
Cdd:cd21310    14 KKIQQNTFTRWCNEHL-KCVQK-RLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNfRQMKLENVSVALEFLDREHI 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1953409455 110 KLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21310    92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953409455  16 GQISDIRVQNLQVERENVQKRTFTRWVNLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLlheyKSSSHRIFR-- 93
Cdd:cd21247     3 TEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL----PRPSRGKMRvh 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953409455  94 -LNNIAKALKFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21247    79 fLENNSKAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125

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 1953409455 191 RTLLAWVQRKTRKYG--VAVQDFAGSWRSGMAFLAVIKAIDPSLVDMKQ--ALEDSMRENLEKAFSIAHEALHIPR-LLE 265
Cdd:pfam00307   5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84