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 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21241    81 -------IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

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 119120859   737 QDLEDLEKRVPVMDAQYKmiAKKAHLFAKESPQEEANEMLTTM-----------SKLKEQLSKVKECCSPLLYEAQQLTV 805
Cdd:TIGR02168  677 REIEELEEKIEELEEKIA--ELEKALAELRKELEELEEELEQLrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   806 PLEELETQITSFYDSLGKINEILSVLEQEAqsstlfkqkhQELLASQENCKKSLTLIEKGSQSVQKLVTS---SQARKPW 882
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEI----------EELEAQIEQLKEELKALREALDELRAELTLlneEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   883 DHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAqegLEEKGDPEELLRRHTEFFSQLDQ 962
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901

                          250       260       270
                   ....*....|....*....|....*....|....
gi 119120859   963 RV------LNAFLKACDELTDILpEQEQQGLQEA 990
Cdd:TIGR02168  902 ELreleskRSELRRELEELREKL-AQLELRLEGL 934

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 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21241    81 -------IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKEF-GDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEeltsnlpqlqslsssassvdsmvstetasppskrKVAAKI 183
Cdd:COG5069    84 -------VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA----------------------------------TINEEG 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  184 QGNAKKTLLKWVQH-TAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKV-KTRSNRE-NLEDAFTIAETQLGIP 260
Cdd:COG5069   123 ELTKHINLLLWCDEdTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIA 202

                         250       260
                  ....*....|....*....|....
gi 119120859  261 RLLDPEDV-DVDKPDEKSIMTYVA 283
Cdd:COG5069   203 RLIGVEDIvNVSIPDERSIMTYVS 226

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 119120859    28 VQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPcEQGHRVKRIHAVANIGTALKFLEgrKSMyr 107
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-KKKLNKSEFDKLENINLALDVAE--KKL-- 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 119120859   108 gsPIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:pfam00307   77 --GVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109

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 119120859     31 RTFTKWINSHLAKRKPPmVVDDLFEDMKDGIKLLALLEVLSGQKLPceqGHRVK----RIHAVANIGTALKFLEGRKsmy 106
Cdd:smart00033    1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVD---KKKVAaslsRFKKIENINLALSFAEKLG--- 73

                            90       100       110
                    ....*....|....*....|....*....|...
gi 119120859    107 rgspIKLVNINATDIADGRPSIvLGLMWTIILY 139
Cdd:smart00033   74 ----GKVVLFEPEDLVEGPKLI-LGVIWTLISL 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 119120859  842 KQKHQELLASQENCKKSLTLIEkgsQSVQKLVTSSQARKPwdhtKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKK 921
Cdd:cd00176    39 LKKHEALEAELAAHEERVEALN---ELGEQLIEEGHPDAE----EIQERLEELNQRWEELRELAEERRQRLEEALDLQQF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  922 FEESR------AELEKVLRvAQEGLEEKGDPEELLRRHTEFFSQLDQR--VLNAFLKACDELTDILPEQEQQGLQEAVRK 993
Cdd:cd00176   112 FRDADdleqwlEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHepRLKSLNELAEELLEEGHPDADEEIEEKLEE 190

                         170
                  ....*....|...
gi 119120859  994 LHKQWKDLQGEAP 1006
Cdd:cd00176   191 LNERWEELLELAE 203

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 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
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 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21190    81 -------IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113

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 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkrIHAVANIGTALKFLEGRK 103
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV--FQCRSNIETALSFLKNKS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21242    79 -------IKLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111

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 119120859  184 QGNAKKTLLKWVQHTAGKqMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21245     1 QRKAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLL 79

                          90       100
                  ....*....|....*....|....*..
gi 119120859  264 DPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21245    80 EPEDVMVDSPDEQSIMTYVAQFLEHFP 106

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 119120859   28 VQKRTFTKWINSHLAKRKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGRKsmyr 107
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRK---- 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 119120859  108 gspIKLVNINATDIADGRPSIVLGLMWTIILYFQ 141
Cdd:cd21188    75 ---IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEE 144
Cdd:cd21191    81 -------VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114

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 119120859   15 TNVMQRLQDEQEIVQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGT 94
Cdd:cd21193     3 KGRIRALQEERINIQKKTFTKWINSFL--EKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRL-RVQKIENVNK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119120859   95 ALKFLEgrksmyrgSPIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21193    80 ALAFLK--------TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115

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 119120859   21 LQDEQEIVQKRTFTKWINSHLAKRkpPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALKFLE 100
Cdd:cd21246     9 LADEREAVQKKTFTKWVNSHLARV--GCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKM-RIHCLENVDKALQFLK 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119120859  101 GRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21246    86 EQR-------VHLENMGSHDIVDGNHRLTLGLIWTIIL 116

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 119120859  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAEtQLGIPRLLDP 265
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDP 79

                          90       100
                  ....*....|....*....|....*
gi 119120859  266 EDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21239    80 EDVDVSSPDEKSVITYVSSLYDVFP 104

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   24 EQEIVQKRTFTKWINSHLAKRKPPMVvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKEF-GDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEeltsnlpqlqslsssassvdsmvstetasppskrKVAAKI 183
Cdd:COG5069    84 -------VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA----------------------------------TINEEG 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  184 QGNAKKTLLKWVQH-TAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKV-KTRSNRE-NLEDAFTIAETQLGIP 260
Cdd:COG5069   123 ELTKHINLLLWCDEdTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIA 202

                         250       260
                  ....*....|....*....|....
gi 119120859  261 RLLDPEDV-DVDKPDEKSIMTYVA 283
Cdd:COG5069   203 RLIGVEDIvNVSIPDERSIMTYVS 226

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 119120859  189 KTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPEDV 268
Cdd:cd21187     3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82

                          90       100
                  ....*....|....*....|..
gi 119120859  269 DVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21187    83 NVEQPDKKSILMYVTSLFQVLP 104

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 119120859  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119120859  262 LLDPEDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDGQ 300
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGK 119

first 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. This model corresponds to the first CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859   23 DEQEIVQKRTFTKWINSHLAK-RKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEG 101
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGS--TRVHALNNVNKALQVLQK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119120859  102 RKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21231    77 NN-------VDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111

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 119120859  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21216    10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDA 89

                          90       100
                  ....*....|....*....|.
gi 119120859  266 ED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21216    90 EDiVNTPRPDERSVMTYVSCY 110

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 119120859   18 MQRLQDEQEIVQKRTFTKWINSHLAkrKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALK 97
Cdd:cd21318    28 IKALADEREAVQKKTFTKWVNSHLA--RVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRM-RIHSLENVDKALQ 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 119120859   98 FLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21318   105 FLKEQR-------VHLENVGSHDIVDGNHRLTLGLIWTIIL 138

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120859  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21291    11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90

                          90       100
                  ....*....|....*....|
gi 119120859  267 DV-DVDKPDEKSIMTYVAQF 285
Cdd:cd21291    91 DVcDVAKPDERSIMTYVAYY 110

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 119120859   23 DEQEIVQKRTFTKWINSHLAKRKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRvkRIHAVANIGTALKFLEGR 102
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKVRKH--INDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119120859  103 KsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEEL 145
Cdd:cd21237    77 Q-------VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112

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 119120859   28 VQKRTFTKWINSHLAKR-KPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21232     2 VQKKTFTKWINARFSKSgKPP--IKDMFTDLRDGRKLLDLLEGLTGKSLPKERGS--TRVHALNNVNRVLQVLHQNN--- 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119120859  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21232    75 ----VELVNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107

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 119120859   26 EIVQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKSm 105
Cdd:cd21311    13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEDEG- 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119120859  106 yrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21311    90 -----IKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121

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 119120859  187 AKKTLLKW-VQHTAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21253     2 GIKALQQWcRQQTEGYR-DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80