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 83816971   601 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 676
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 83816971   601 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 676
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 83816971    24 QAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgNQQEMKNNVEKVLQFvASKKIRMHQTS 103
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-SEFDKLENINLALDV-AEKKLGVPKVL 82

                          90       100
                  ....*....|....*....|....*.
gi 83816971   104 --AKDIVDGNLKSIMRLVLALAAHFK 127
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 83816971  22 QLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 101
Cdd:COG5069  10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                        90       100
                ....*....|....*....|....*
gi 83816971 102 TSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:COG5069  89 IGPQDIVDGNPKLILGLIWSLISRL 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 83816971    282 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 359
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83816971    360 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 439
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                          170       180
                   ....*....|....*....|....*
gi 83816971    440 KLEEALRKLSDVSYHQVDLERELEH 464
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 83816971   601 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 676
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83816971    601 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 677
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 83816971  20 EQQLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRM 99
Cdd:cd21227   3 EIQKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                        90       100
                ....*....|....*....|....*..
gi 83816971 100 HQTSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21227  81 VNIGNEDIVNGNLKLILGLIWHLILRY 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 83816971  21 QQLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKK 96
Cdd:cd21214   5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVISGE-----RLPKPERGKMRfhkiANVNKALDFIASKG 77

                        90       100
                ....*....|....*....|...
gi 83816971  97 IRMHQTSAKDIVDGNLKSIMRLV 119
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 83816971  19 NEQQLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIR 98
Cdd:cd21285   8 NGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGIN 87

                        90       100
                ....*....|....*....|....*
gi 83816971  99 MHQTSAKDIVDGNLKSIMRLVLALA 123
Cdd:cd21285  88 IQGLSAEEIRNGNLKAILGLFFSLS 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 83816971  22 QLQAYVAWVNAQLKK--RPavkPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASK 95
Cdd:cd21186   3 QKKTFTKWINSQLSKanKP---PIKDLFEDLRDGTRLLALLEVLTGKKL------KPEKGRMRvhhlNNVNRALQVLEQN 73

                        90       100       110
                ....*....|....*....|....*....|..
gi 83816971  96 KIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 127
Cdd:cd21186  74 NVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105

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 83816971  22 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSpgNQQEMKNNVEKVLQFVASKKIRMHQ 101
Cdd:cd21242   6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGH--NVFQCRSNIETALSFLKNKSIKLIN 83

                        90       100
                ....*....|....*....|....*
gi 83816971 102 TSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21242  84 IHVPDIIEGKPSIILGLIWTIILHF 108

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 83816971  22 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 101
Cdd:cd21190   6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85

                        90       100
                ....*....|....*....|....*.
gi 83816971 102 TSAKDIVDGNLKSIMRLVLALAAHFK 127
Cdd:cd21190  86 INSTDIVDGKPSIVLGLIWTIILYFQ 111

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 83816971  22 QLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGV-QLSPGNQQEMKNNVEKVLQFVASKKIRMH 100
Cdd:cd21183   5 QANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKRSyNRRPAFQQHYLENVSTALKFIEADHIKLV 82

                        90       100
                ....*....|....*....|....*.
gi 83816971 101 QTSAKDIVDGNLKSIMRLVLALAAHF 126
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 83816971  22 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvqlsPGNQQEMK----NNVEKVLQFVASKKI 97
Cdd:cd21246  17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEVLSGERLP-----KPTKGKMRihclENVDKALQFLKEQRV 89

                        90       100
                ....*....|....*....|....*
gi 83816971  98 RMHQTSAKDIVDGNlksiMRLVLAL 122
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 83816971  14 LQEGFNEQQLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKlsgvqLSPGNQQEMK----NNVEKVL 89
Cdd:cd21193   9 LQEERINIQKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEK-----LGKPNRGRLRvqkiENVNKAL 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 83816971  90 QFVASkKIRMHQTSAKDIVDGNlksiMRLVLAL 122
Cdd:cd21193  82 AFLKT-KVRLENIGAEDIVDGN----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 83816971  29 WVNAQLKKR-PAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLS-PGNQQEMKNNVEKVLQFVASKKIRMHqTSAKD 106
Cdd:cd21218  18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLeVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED 96

                        90
                ....*....|....*.
gi 83816971 107 IVDGNLKSIMRLVLAL 122
Cdd:cd21218  97 IVSGNPRLNLAFVATL 112

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83816971  22 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKKI 97
Cdd:cd21317  32 QKKTFTKWVNSHLAR--VTCRIGDLYTDLRDGRMLIRLLEVLSGE-----QLPKPTKGRMRihclENVDKALQFLKEQKV 104

                        90       100
                ....*....|....*....|....*
gi 83816971  98 RMHQTSAKDIVDGNlksiMRLVLAL 122
Cdd:cd21317 105 HLENMGSHDIVDGN----HRLTLGL 125

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 83816971  22 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMH 100
Cdd:cd21310  17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKlENVSVALEFLDREHIKLV 94

                        90       100
                ....*....|....*....|....*.
gi 83816971 101 QTSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21310  95 SIDSKAIVDGNLKLILGLIWTLILHY 120

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. 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 83816971  43 VQDLRQDLRDGVILAYLIEIVAGEK--LSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQT----SAKDIVDGNLKSIM 116
Cdd:cd21223  26 VTNLAVDLRDGVRLCRLVELLTGDWslLSKLRVPAISRLQKLHNVEVALKALKEAGVLRGGDgggiTAKDIVDGHREKTL 105

                ....*..
gi 83816971 117 RLVLALA 123
Cdd:cd21223 106 ALLWRII 112

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 83816971  12 DVLQEGFNEQ---QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NN 84
Cdd:cd21236   5 NVLERYKDERdkvQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMRfhrlQN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 83816971  85 VEKVLQFVASKKIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 127
Cdd:cd21236  77 VQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83816971  22 QLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 101
Cdd:COG5069  10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                        90       100
                ....*....|....*....|....*
gi 83816971 102 TSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:COG5069  89 IGPQDIVDGNPKLILGLIWSLISRL 113

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83816971  27 VAWVNAQLkkRPAVKPVQDLRQDLRDGVILAYLIEIVAG--EKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSA 104
Cdd:cd21222  22 LQFVNKHL--AKLNIEVTDLATQFHDGVYLILLIGLLEGffVPLHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRP 99

                        90       100
                ....*....|....*....|..
gi 83816971 105 KDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21222 100 EDIVNGDLKSILRVLYSLFSKY 121

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 83816971  24 QAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGE--KLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 101
Cdd:cd21307  19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFfiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFP 96

                        90       100
                ....*....|....*....|....*.
gi 83816971 102 TSAKDIVDGNLKSIMRLVLALAAHFK 127
Cdd:cd21307  97 VNPEDIVNGDSKATIRVLYCLFSKYK 122

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (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. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B 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 83816971  22 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 100
Cdd:cd21309  18 QQNTFTRWCNEHLKC--VNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLV 95

                        90       100
                ....*....|....*....|....*.
gi 83816971 101 QTSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21309  96 SIDSKAIVDGNLKLILGLVWTLILHY 121

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 83816971  22 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 100
Cdd:cd21308  21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98

                        90       100
                ....*....|....*....|....*.
gi 83816971 101 QTSAKDIVDGNLKSIMRLVLALAAHF 126
Cdd:cd21308  99 SIDSKAIVDGNLKLILGLIWTLILHY 124

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83816971  29 WVNAQLKKRPavkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgnqQEMKNNVEKVLQfvASKKIRM-HQTSAKDI 107
Cdd:cd21185   9 WVRQLLPDVD----VNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDP---EESENNIQRGLE--AGKSLGVePVLTAEEM 79