DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77

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 1370460505  23 QAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgNQQEMKNNVEKVLQFvASKKIRMHQTS 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-SEFDKLENINLALDV-AEKKLGVPKVL 82

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 103 --AKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:pfam00307  83 iePEDLVEGDNKSVLTYLASLFRRFQ 108

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  19 SQQLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRM 98
Cdd:COG5069     8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKL 86

                          90       100
                  ....*....|....*....|....*..
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:COG5069    87 FNIGPQDIVDGNPKLILGLIWSLISRL 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 1370460505  245 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 322
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                          170       180
                   ....*....|....*....|....*
gi 1370460505  403 KLEEALRKLSDVSYHQVDLERELEH 427
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLER 411

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77

Domain present in Dishevelled and axin; Domain of unknown function.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370460505  564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 640
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three 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 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21227     5 QKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVN 82

                          90       100
                  ....*....|....*....|....*
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21227    83 IGNEDIVNGNLKLILGLIWHLILRY 107

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 1370460505  20 QQLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKK 95
Cdd:cd21214     5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVISGE-----RLPKPERGKMRfhkiANVNKALDFIASKG 77

                          90       100
                  ....*....|....*....|...
gi 1370460505  96 IRMHQTSAKDIVDGNLKSIMRLV 118
Cdd:cd21214    78 VKLVSIGAEEIVDGNLKMTLGMI 100

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  17 EPSQQLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKI 96
Cdd:cd21285     7 ENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGI 86

                          90       100
                  ....*....|....*....|....*.
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALA 122
Cdd:cd21285    87 NIQGLSAEEIRNGNLKAILGLFFSLS 112

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 1370460505  21 QLQAYVAWVNAQLKK--RPavkPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASK 94
Cdd:cd21186     3 QKKTFTKWINSQLSKanKP---PIKDLFEDLRDGTRLLALLEVLTGKKL------KPEKGRMRvhhlNNVNRALQVLEQN 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370460505  95 KIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21186    74 NVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105

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 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQlspGNQqeMK-----NNVEKVLQFVASKK 95
Cdd:cd21241     6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEK---GRR--LKrvhflSNINTALKFLESKK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370460505  96 IRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLS-GVQLSPGNQQEMKNNVEKVLQFVASK-KIRM 98
Cdd:cd21225     5 QIKAFTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIEEDlKIRV 83

                          90       100
                  ....*....|....*....|...
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLAL 121
Cdd:cd21225    84 QGIGAEDFVDNNKKLILGLLWTL 106

first calponin homology (CH) domain found in the filamin family; 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. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other 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 1370460505  21 QLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGV-QLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21183     5 QANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKRSyNRRPAFQQHYLENVSTALKFIEADHIKLV 82

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108

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 1370460505  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21246    17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEVLSGERLP-----KPTKGKMRihclENVDKALQFLKEQRV 89

                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21246    90 HLENMGSHDIVDGN----HRLTLGL 110

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 1370460505  21 QLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKlsgvqLSPGNQQEMK----NNVEKVLQFVASkKI 96
Cdd:cd21193    17 QKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEK-----LGKPNRGRLRvqkiENVNKALAFLKT-KV 88

                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21193    89 RLENIGAEDIVDGN----PRLILGL 109

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four 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 1370460505  28 WVNAQLKKR-PAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLS-PGNQQEMKNNVEKVLQFVASKKIRMHqTSAKD 105
Cdd:cd21218    18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLeVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED 96

                          90
                  ....*....|....*.
gi 1370460505 106 IVDGNLKSIMRLVLAL 121
Cdd:cd21218    97 IVSGNPRLNLAFVATL 112

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 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVAS-KKIRMH 99
Cdd:cd21311    16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIV 93

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHY 119

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 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMH 99
Cdd:cd21310    17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKlENVSVALEFLDREHIKLV 94

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHY 120

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 1370460505  21 QLQAYVAWVNAQLKKrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21231     7 QKKTFTKWINAQFAK-FGKPPIEDLFTDLQDGRRLLELLEGLTGQKL--VKEKGSTRVHALNNVNKALQVLQKNNVDLVN 83

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21231    84 IGSADIVDGNHKLTLGLIWSIILHWQ 109

first calponin homology (CH) domain found in plectin and similar proteins; 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 can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin 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 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21235     7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFKPGSSRTVNQGR 137
Cdd:cd21235    79 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  19 SQQLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRM 98
Cdd:COG5069     8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKL 86

                          90       100
                  ....*....|....*....|....*..
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:COG5069    87 FNIGPQDIVDGNPKLILGLIWSLISRL 113

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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 1370460505  27 AWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLsgvQLSPGNQQEM--KNNVEKVLQFVaSKKIRMHQTSAK 104
Cdd:cd21221     8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLEKLANEKL---EVPEVAQSEEgqKQKLAVVLACV-NFLLGLEEDEAR 81

                          90       100
                  ....*....|....*....|....*
gi 1370460505 105 DIVDG----NLKSIMRLVLALAAHF 125
Cdd:cd21221    82 WTVDGiynkDLVSILHLLVALAHHY 106

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  23 QAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGE--KLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21307    19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFfiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFP 96

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21307    97 VNPEDIVNGDSKATIRVLYCLFSKYK 122

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 1370460505  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvQLSPGNQQ-EMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21316    54 QKKTFTKWVNSHLARVSC--RITDLYMDLRDGRMLIKLLEVLSGERLP--KPTKGRMRiHCLENVDKALQFLKEQRVHLE 129

                          90
                  ....*....|....*....
gi 1370460505 100 QTSAKDIVDGNLKSIMRLV 118
Cdd:cd21316   130 NMGSHDIVDGNHRLTLGLI 148

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (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 anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A 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 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21308    21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98

                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21308    99 SIDSKAIVDGNLKLILGLIWTLILHY 124

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 244 EEQLLEQQEYLEKEMEEAKKMISGLQALLLngslpEDEQERplalcepgvnpeeqlIIIQSRLDQSMEENQDLKKELLKC 323
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 324 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAK 403
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478