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 459184576  395 VTRVLYFTDRDMTPCMTSISKRVGDITLGEFKTVIKKEGNYRFIFKALDPELGTVKEEVFHDDDVIPGWEGKIVAWV 471
Cdd:pfam00778   1 ETKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 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 459184576  395 VTRVLYFTDRDMTPCMTSISKRVGDITLGEFKTVIKKEGNYRFIFKALDPELGTVKEEVFHDDDVIPGWEGKIVAWV 471
Cdd:pfam00778   1 ETKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 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 459184576    4 QEQVQAYTAWVNSQLKKRGKNIV--NLGEDLKDGVALVAVVEIVSGHTLGGIKPTC-ENEKRENVLKVLQFMRNA-GIKL 79
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKsEFDKLENINLALDVAEKKlGVPK 80

                          90       100
                  ....*....|....*....|....*...
gi 459184576   80 HHVSVDEITSGNVKTIMQLILALAAHFK 107
Cdd:pfam00307  81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576 151 MQADVEKELAAIRDITQCLQKVLLEEIPGQpLEGHDADEQSVIIQARLDQAIVDKVNLEEENHIARQENRKLTSEKSALE 230
Cdd:COG1196  279 LELELEEAQAEEYELLAELARLEQDIARLE-ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576 231 QRFLQQEEELLSIRQQLLQSNLSRDKLQSEKAELIAELTETRRNQDELRTKCRDHERTLERMENEAIQNKINHSREIRKL 310
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                        170
                 ....*....|
gi 459184576 311 DKEIHLARQE 320
Cdd:COG1196  438 EEEEEALEEA 447

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 459184576   153 ADVEKELAAIRDITQCLQKV---LLEEIPGQPLEGHDADEQSVIIQARLDQAIVDKVNLEEENHIARQENRKLTSEKSAL 229
Cdd:TIGR02168  694 AELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576   230 EQRFLQQEEELLSIRQQLLQSNLSRDKLQSEKAELIAELTETRRNQDELRTKCRDHERTLERMEneaiqnkinhsREIRK 309
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE-----------RRLED 842

                          170       180
                   ....*....|....*....|.
gi 459184576   310 LDKEIH--LARQESYNGQIND 328
Cdd:TIGR02168  843 LEEQIEelSEDIESLAAEIEE 863

exonuclease subunit SbcC; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576  170 QKVLLEeiPGQP-----------LEGHDADEQSVIiQARLDQaivdkvnLEEENHIARQENRKLTSEKSALEQRFLQQEE 238
Cdd:PRK10246  496 QRAQLQ--AGQPcplcgstshpaVEAYQALEPGVN-QSRLDA-------LEKEVKKLGEEGAALRGQLDALTKQLQRDES 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576  239 ELLSIRQQllqsnlsRDKLQSEKAELIAELTETRRNQDELR---TKCRDHERTLERM-ENEAIQNKIN-HSREIRKLDKE 313
Cdd:PRK10246  566 EAQSLRQE-------EQALTQQWQAVCASLNITLQPQDDIQpwlDAQEEHERQLRLLsQRHELQGQIAaHNQQIIQYQQQ 638

                  ....*.
gi 459184576  314 IHLARQ 319
Cdd:PRK10246  639 IEQRQQ 644

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 459184576  395 VTRVLYFTDRDMTPCMTSISKRVGDITLGEFKTVIKKEGNYRFIFKALDPELGTVKEEVFHDDDVIPGWEGKIVAWV 471
Cdd:pfam00778   1 ETKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77

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 459184576   3 IQEQVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGGI--KPTCENEKRENVLKVLQFMRNAGIKLH 80
Cdd:cd21227    2 VEIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVikKPLNQHQKLENVTLALKAMAEDGIKLV 81

                         90       100
                 ....*....|....*....|....*.
gi 459184576  81 HVSVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21227   82 NIGNEDIVNGNLKLILGLIWHLILRY 107

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576   396 TRVLYFTDRDMTPCMTSISKRVGDITLGEFKTVIKKeGNYRFIFKALDPEL-GTVKEEVFHDDDVIPGWEGKIVAWVEEV 474
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLVSV 82

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 459184576   2 EIQeQVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLggIKPTCEN---EKRENVLKVLQFMRNAGIK 78
Cdd:cd21214    3 EKQ-QRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL--PKPERGKmrfHKIANVNKALDFIASKGVK 79

                         90       100
                 ....*....|....*....|.
gi 459184576  79 LHHVSVDEITSGNVKTIMQLI 99
Cdd:cd21214   80 LVSIGAEEIVDGNLKMTLGMI 100

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGGI--KPTCENEKRENVLKVLQFMRN-AGIKLHHV 82
Cdd:cd21311   16 QQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFnkRPTFRSQKLENVSVALKFLEEdEGIKIVNI 95

                         90       100
                 ....*....|....*....|....
gi 459184576  83 SVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21311   96 DSSDIVDGKLKLILGLIWTLILHY 119

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVS---GHTLGGIKPTCENEKRENVLKVLQFMRNAGIKLHHV 82
Cdd:cd21228    5 QQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSqkrMYKKYNKRPTFRQMKLENVSVALEFLERESIKLVSI 84

                         90       100
                 ....*....|....*....|....
gi 459184576  83 SVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21228   85 DSSAIVDGNLKLILGLIWTLILHY 108

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576   7 VQAYTAWVNSQLKKRGK-NIVNLGEDLKDGVALVAVVEIVSGHTLGGI--KPTCENEKRENVLKVLQFMRNAGI-KLHHV 82
Cdd:cd00014    1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                         90       100
                 ....*....|....*....|..
gi 459184576  83 SVDEITS-GNVKTIMQLILALA 103
Cdd:cd00014   81 EPEDLYEkGNLKKVLGTLWALA 102

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 459184576   4 QEQVQ--AYTAWVNSQLKKRG--KNIVNLGEDLKDGVALVAVVEIVSGHTLGGIKPTCENEKRENVLKVLQFMRNAGIKL 79
Cdd:cd21242    2 QEQTQkrTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIKL 81

                         90       100
                 ....*....|....*....|....*..
gi 459184576  80 HHVSVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21242   82 INIHVPDIIEGKPSIILGLIWTIILHF 108

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGGIKPTCENEKRENVLKVLQFMRNAGIKLHHVSVD 85
Cdd:cd21235    7 QKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIRND 86

                         90       100
                 ....*....|....*....|....*.
gi 459184576  86 EITSGNVKTIMQLILALAAHFKPASI 111
Cdd:cd21235   87 DIADGNPKLTLGLIWTIILHFQISDI 112

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576   3 IQEQVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGgiKPT---CENEKRENVLKVLQFMRnAGIKL 79
Cdd:cd21193   14 INIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLG--KPNrgrLRVQKIENVNKALAFLK-TKVRL 90

                         90       100
                 ....*....|....*....|
gi 459184576  80 HHVSVDEITSGNVKTIMQLI 99
Cdd:cd21193   91 ENIGAEDIVDGNPRLILGLI 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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGGIKPTCENEKRENVLKVLQFMRNAGIKLHHVSVD 85
Cdd:cd21237    7 QKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRND 86

                         90       100
                 ....*....|....*....|....*.
gi 459184576  86 EITSGNVKTIMQLILALAAHFKPASI 111
Cdd:cd21237   87 DITDGNPKLTLGLIWTIILHFQISDI 112

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTL---GGIKPTCENEKRENVLKVLQFMRNAGIKLHHV 82
Cdd:cd21310   17 QQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyrkYHPRPNFRQMKLENVSVALEFLDREHIKLVSI 96

                         90       100
                 ....*....|....*....|....
gi 459184576  83 SVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21310   97 DSKAIVDGNLKLILGLIWTLILHY 120

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTL---GGIKPTCENEKRENVLKVLQFMRNAGIKLHHV 82
Cdd:cd21308   21 QQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMhrkHNQRPTFRQMQLENVSVALEFLDRESIKLVSI 100

                         90       100
                 ....*....|....*....|....
gi 459184576  83 SVDEITSGNVKTIMQLILALAAHF 106
Cdd:cd21308  101 DSKAIVDGNLKLILGLIWTLILHY 124

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGgiKPT---CENEKRENVLKVLQFMRNAGIKLHHV 82
Cdd:cd21318   39 QKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLP--KPTrgrMRIHSLENVDKALQFLKEQRVHLENV 116

                         90
                 ....*....|....*..
gi 459184576  83 SVDEITSGNVKTIMQLI 99
Cdd:cd21318  117 GSHDIVDGNHRLTLGLI 133

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGgiKPTcENEKR----ENVLKVLQFMRNAGIKLHH 81
Cdd:cd21317   32 QKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLP--KPT-KGRMRihclENVDKALQFLKEQKVHLEN 108

                         90
                 ....*....|....*...
gi 459184576  82 VSVDEITSGNVKTIMQLI 99
Cdd:cd21317  109 MGSHDIVDGNHRLTLGLI 126

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 459184576  14 VNSQLKKRGKNIVNLGEDLKDGVALVavveIVSGhTLGG---------IKPTCENEKRENVLKVLQFMRNAGIKLHHVSV 84
Cdd:cd21222   25 VNKHLAKLNIEVTDLATQFHDGVYLI----LLIG-LLEGffvplheyhLTPSTDDEKLHNVKLALELMEDAGISTPKIRP 99

                         90       100
                 ....*....|....*....|..
gi 459184576  85 DEITSGNVKTIMQLILALAAHF 106
Cdd:cd21222  100 EDIVNGDLKSILRVLYSLFSKY 121

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 459184576   6 QVQAYTAWVNSQLKKRGKN-IVNLGEDLKDGVALVAVVEIVSGHTLGGIKPTCENEKRENVLKVLQFMRNAGIKLHHVSV 84
Cdd:cd21231    7 QKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVDLVNIGS 86

                         90       100
                 ....*....|....*....|...
gi 459184576  85 DEITSGNVKTIMQLILALAAHFK 107
Cdd:cd21231   87 ADIVDGNHKLTLGLIWSIILHWQ 109

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 459184576   6 QVQAYTAWVNSQLKKRGK-NIVNLGEDLKDGVALVAVVEIVSGHTLGGIKPTCENEKRENVLKVLQFMRNAGIKLHHVSV 84
Cdd:cd21232    3 QKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGG 82

                         90       100
                 ....*....|....*....|...
gi 459184576  85 DEITSGNVKTIMQLILALAAHFK 107
Cdd:cd21232   83 TDIVDGNHKLTLGLLWSIILHWQ 105

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 459184576   6 QVQAYTAWVNSQLKKRGKNIVNLGEDLKDGVALVAVVEIVSGHTLGgiKPTCENEK---RENVLKVLQFMRNAGIKLHHV 82
Cdd:cd21316   54 QKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLP--KPTKGRMRihcLENVDKALQFLKEQRVHLENM 131

                         90
                 ....*....|....*..
gi 459184576  83 SVDEITSGNVKTIMQLI 99
Cdd:cd21316  132 GSHDIVDGNHRLTLGLI 148

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576 182 LEGHDADEQSVIIQARLDQAIVDKVNLEEENHIARQENRKLTSEKSALEQRFLQQEEELLSIRQQLLQSNLSRDKLQSEK 261
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 459184576 262 AELIAELTETRRNQDELRTKCRDHERTLERMENEAIQNKinhSREIRKLDKEIHLARQES 321
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL---RAAAELAAQLEELEEAEE 410