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 7510924    77 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 156
Cdd:cd21188    1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80

                         90       100
                 ....*....|....*....|....*
gi 7510924   157 RPEDIVEGNGKLTLGLIWTIILNFQ 181
Cdd:cd21188   81 RAEDIVDGNPKLTLGLIWTIILHFQ 105

SH3 domain; This entry represents an SH3 domain.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7510924     826 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 890
Cdd:pfam17902    1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924  1006 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL--PNPTPTQRVNH- 1082
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQEr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924  1083 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINmvlkvsk 1158
Cdd:cd00176   81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELE------- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7510924  1159 lgaqnEHFSQQQTVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1232
Cdd:cd00176  153 -----EELEAHEPRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213

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 7510924    77 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 156
Cdd:cd21188    1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80

                         90       100
                 ....*....|....*....|....*
gi 7510924   157 RPEDIVEGNGKLTLGLIWTIILNFQ 181
Cdd:cd21188   81 RAEDIVDGNPKLTLGLIWTIILHFQ 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    79 VQKKTFTKWVNKHLSKTD-HKIDDLFVDLRDGYALIALLEALTGERIQK--ENGYTRFHRIQNVQYCLDFLKKKNIKLVN 155
Cdd:COG5069    9 VQKKTFTKWTNEKLISGGqKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924   156 IRPEDIVEGNGKLTLGLIWTIILNFQVSVIrqrlllesSQHEQMSAKHTTT--NSQVTAGY-PRVNVNNFSSSWRDGLAF 232
Cdd:COG5069   89 IGPQDIVDGNPKLILGLIWSLISRLTIATI--------NEEGELTKHINLLlwCDEDTGGYkPEVDTFDFFRSWRDGLAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924   233 NAILHRYRSSAIDWNKIssDSVSNTERLNN--AFAAADREFGVERLLDAEDV-DTNNPDEKSIITYVSSLYNAL----PH 305
Cdd:COG5069  161 SALIHDSRPDTLDPNVL--DLQKKNKALNNfqAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFglleKI 238

                        250
                 ....*....|...
gi 7510924   306 EPEMSRLQKVQEE 318
Cdd:COG5069  239 DIALHRVYRLLEA 251

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 7510924       82 KTFTKWVNKHLSKTDH-KIDDLFVDLRDGYALIALLEALTGERIQKEN---GYTRFHRIQNVQYCLDFLKKKNIKLVNIR 157
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|.
gi 7510924      158 PEDIVEGNgKLTLGLIWTIIL 178
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLIS 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 7510924     207 NSQVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVER-LLDAEDVdtN 285
Cdd:pfam00307   12 NSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPKvLIEPEDL--V 89

                           90
                   ....*....|....*....
gi 7510924     286 NPDEKSIITYVSSLYNALP 304
Cdd:pfam00307   90 EGDNKSVLTYLASLFRRFQ 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 7510924      210 VTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS--DSVSNTERLNNAFAAADREFGVERLLDAEDVDTNNP 287
Cdd:smart00033   10 LLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKVVLFEPEDLVEGPK 89

                            90
                    ....*....|..
gi 7510924      288 DEKSIITYVSSL 299
Cdd:smart00033   90 LILGVIWTLISL 101

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924  1006 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQL--PNPTPTQRVNH- 1082
Cdd:cd00176    4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQEr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924  1083 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINmvlkvsk 1158
Cdd:cd00176   81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELE------- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7510924  1159 lgaqnEHFSQQQTVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1232
Cdd:cd00176  153 -----EELEAHEPRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213

Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 7510924   840 VTALCDYSDEN---VTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 884
Cdd:cd11908    3 VIALYDYQTNDpqeLALRYNEEYHLLDSSEIHWWRVQDKNGHEGYVPS 50

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    1006 QYDQKMAEL---LKKLEEAWRELNDAVGKPISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQLPNPTPTQRVNH 1082
Cdd:TIGR02168  674 ERRREIEELeekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    1083 DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADIVRQHEITLNSFDdlpAALDKLRGHHSQLleinmvlkvsklgaq 1162
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLL--------------- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    1163 NEHFSQQQTVIDQLNRNVALLRQHVSRT-----RINEghhpDVDAIEDEVQKLNVRWENVNSQIASRLLAVESALQIQMV 1237
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLeeqieELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 7510924    1238 YRSEYETEMSWLDTVEETINRLR-KPEELRP--EQYQQQLDMLIAEYTNLQE 1286
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRrELEELREklAQLELRLEGLEVRIDNLQE 943

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 7510924    77 DNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKLVNI 156
Cdd:cd21188    1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80

                         90       100
                 ....*....|....*....|....*
gi 7510924   157 RPEDIVEGNGKLTLGLIWTIILNFQ 181
Cdd:cd21188   81 RAEDIVDGNPKLTLGLIWTIILHFQ 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 7510924    74 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKL 153
Cdd:cd21236   12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 91

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7510924   154 VNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 185
Cdd:cd21236   92 VNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    74 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLKKKNIK 152
Cdd:cd21246   11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTkGKMRIHCLENVDKALQFLKEQRVH 90

                         90       100
                 ....*....|....*....|....*.
gi 7510924   153 LVNIRPEDIVEGNGKLTLGLIWTIIL 178
Cdd:cd21246   91 LENMGSHDIVDGNHRLTLGLIWTIIL 116

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    74 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIKL 153
Cdd:cd21237    1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7510924   154 VNIRPEDIVEGNGKLTLGLIWTIILNFQVSVI 185
Cdd:cd21237   81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    74 DERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLDFLKKKnIK 152
Cdd:cd21193   11 EERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNrGRLRVQKIENVNKALAFLKTK-VR 89

                         90       100
                 ....*....|....*....|....*.
gi 7510924   153 LVNIRPEDIVEGNGKLTLGLIWTIIL 178
Cdd:cd21193   90 LENIGAEDIVDGNPRLILGLIWTIIL 115

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 7510924   211 TAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLLDAEDVDTNNPDEK 290
Cdd:cd21248   15 TAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKS--NALYNLQNAFNVAEQKLGLTKLLDPEDVNVEQPDEK 92

                         90
                 ....*....|
gi 7510924   291 SIITYVSSLY 300
Cdd:cd21248   93 SIITYVVTYY 102

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    80 QKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQK-ENGYTRFHRIQNVQYCLDFLKKKNIKLVNIRP 158
Cdd:cd21214    6 QRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVSIGA 85

                         90       100
                 ....*....|....*....|
gi 7510924   159 EDIVEGNGKLTLGLIWTIIL 178
Cdd:cd21214   86 EEIVDGNLKMTLGMIWTIIL 105

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    66 CLNFNLIPDERDNVQKKTFTKWVNKHLSKTDHKIDDLFVDLRDGYALIALLEALTGERIQKEN-GYTRFHRIQNVQYCLD 144
Cdd:cd21318   25 CSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTrGRMRIHSLENVDKALQ 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 7510924   145 FLKKKNIKLVNIRPEDIVEGNGKLTLGLIWTIIL 178
Cdd:cd21318  105 FLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138

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 7510924    75 ERDNVQKKTFTKWVNKHLSKTDHK--IDDLFVDLRDGYALIALLEALTGERIQKENGYT--RFHRIQNVQYCLDFLKKKN 150
Cdd:cd21190    1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 7510924   151 IKLVNIRPEDIVEGNGKLTLGLIWTIILNFQV 182
Cdd:cd21190   81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112

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 7510924   211 TAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSdsvSN-TERLNNAFAAADREFGVERLLDAEDVDTNNPDE 289
Cdd:cd21319   18 TAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKK---SNaRHNLEHAFNVAERQLGITKLLDPEDVFTENPDE 94

                         90
                 ....*....|..
gi 7510924   290 KSIITYVSSLYN 301
Cdd:cd21319   95 KSIITYVVAFYH 106

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924    75 ERDNVQKKTFTKWVNKHLSK--TDHKIDDLFVDLRDGYALIALLEALTGERIQKENGYTRFHRIQNVQYCLDFLKKKNIK 152
Cdd:cd21242    1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 7510924   153 LVNIRPEDIVEGNGKLTLGLIWTIILNFQV 182
Cdd:cd21242   81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110

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 7510924   209 QVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADReFGVERLLDAEDVDTNNPD 288
Cdd:cd21239   12 QMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQS--NLANLEHAFYVAEK-LGVTRLLDPEDVDVSSPD 88

                         90
                 ....*....|....*.
gi 7510924   289 EKSIITYVSSLYNALP 304
Cdd:cd21239   89 EKSVITYVSSLYDVFP 104

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924   199 MSAKHTTT--NSQVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADReFGVERL 276
Cdd:cd21240    3 MSAKEKLLlwTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQS--NRENLEQAFEVAER-LGVTRL 79

                         90       100
                 ....*....|....*....|....*...
gi 7510924   277 LDAEDVDTNNPDEKSIITYVSSLYNALP 304
Cdd:cd21240   80 LDAEDVDVPSPDEKSVITYVSSIYDAFP 107

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 7510924   211 TAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGVERLLDAEDVDTNNPDEK 290
Cdd:cd21321   18 TAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYN--LQNAFNVAEKELGLTKLLDPEDVNVDQPDEK 95

                         90
                 ....*....|.
gi 7510924   291 SIITYVSSLYN 301
Cdd:cd21321   96 SIITYVATYYH 106

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7510924   211 TAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLLDAED-VDTNNPDE 289
Cdd:cd21216   23 TAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKD--DPRENLNLAFDVAEKHLDIPKMLDAEDiVNTPRPDE 100

                         90
                 ....*....|...
gi 7510924   290 KSIITYVSSLYNA 302
Cdd:cd21216  101 RSVMTYVSCYYHA 113

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 7510924   211 TAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKI-SSDSVSNterLNNAFAAADREFGVERLLDAEDVDTNNPDE 289
Cdd:cd21249   17 TAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLrPDRPLYN---LANAFLVAEQELGISQLLDPEDVAVPHPDE 93

                         90
                 ....*....|..
gi 7510924   290 KSIITYVSSLYN 301
Cdd:cd21249   94 RSIMTYVSLYYH 105

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 7510924   209 QVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSdsVSNTERLNNAFAAADREFGVERLLDAEDVDTNNPD 288
Cdd:cd21234   11 QSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVK--MSPVERLEHAFSKAKNHLGIEKLLDPEDVAVQLPD 88