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 529250185   358 GSSPNNASELS----LASLTEKIQKMEENqhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAE 433
Cdd:TIGR02168  664 GSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185   434 QLSQENEKLINLLQERvkNEEPSAQGGKVLELEQKctdiLEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKE 513
Cdd:TIGR02168  737 RLEAEVEQLEERIAQL--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185   514 ENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLE------ADKQKAIEASST--VGQTAENFEVQEMLK 585
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESelEALLNERASLEEALA 890

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185   586 VARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLS-RTSLKLQ---EKASESDAEIKDM 661
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEA 970

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529250185   662 KETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWR-RFQA 726
Cdd:TIGR02168  971 RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036

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 529250185   955 RNALLKWCQKKTEGY-ANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKR--NLLLAFEAAQ-SVGINPSLE 1030
Cdd:pfam00307    4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83

                           90       100
                   ....*....|....*....|....*...
gi 529250185  1031 LSEMLYTdrPDWQSVMQYVAQIYKYFET 1058
Cdd:pfam00307   84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  940 RDPLAALAREYGGSKRNALLKWCQKKTEGYAN-IDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQ--EKKRNLLLA 1016
Cdd:COG5069   112 RLTIATINEEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQA 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 529250185 1017 FEAAQ-SVGINPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET 1058
Cdd:COG5069   192 FENANkVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234

DNA double-strand break repair ATPase Rad50;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  375 KIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlinlLQERVKNEE 454
Cdd:PRK03918  311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  455 PSAQGGKVLELEQKCTDI-------------LEKSRFEREKLL-----------------------NIQQQLTCSLRKVE 498
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIeeeiskitarigeLKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIE 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  499 EENQGAIDMIKHLKEENEKLNGFLEHER--CNNSVMAKTLEECRVTLEGLKMENGSLKA-LLEADKQKAIEASSTVGQTA 575
Cdd:PRK03918  466 KELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLK 545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  576 ENFEVQEMLKVARAE----KDQLQLSCTELRQELLKANGE-IKHVSSLLAKMEKDYSYLKEVCD--HQAEQLSRTSLKLQ 648
Cdd:PRK03918  546 KELEKLEELKKKLAElekkLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDaeKELEREEKELKKLE 625

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529250185  649 EKASESDAEIKDMKETIFELEDQVEQHRavKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKE 716
Cdd:PRK03918  626 EELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  553 LKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEv 632
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  633 cdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTK 712
Cdd:COG1196   310 ---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 529250185  713 QIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKEL 767
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALL-ERLERLEEELEELEEALAELEEEEEEE 440

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  946 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGI 1025
Cdd:cd21199     1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 529250185 1026 NPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 1057
Cdd:cd21199    81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEL 1031
Cdd:cd21216    10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21216    90 EDIVNTPRPDERSVMTYVSCYYHAF 114

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  956 NALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLELSEM 1034
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDvAEQELGIPPVMTGQEM 82

                          90       100
                  ....*....|....*....|..
gi 529250185 1035 LYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd22198    83 ASLAVPDKLSMVSYLSQFYEAF 104

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGInPSLEL 1031
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDvAEQELGI-AKLLD 80

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 1031
Cdd:cd21248     2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAeQKLGLTKLLD- 80

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21248    81 PEDVNVEQPDEKSIITYVVTYYHYF 105

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 1031
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAeRQLGITKLLD- 83

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21319    84 PEDVFTENPDEKSIITYVVAFYHYF 108

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 1031
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80

                          90       100
                  ....*....|....*....|....*.
gi 529250185 1032 SEMLYT-DRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21258    81 EDMMIMgKKPDSKCVFTYVQSLYNHL 106

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  957 ALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLELSEML 1035
Cdd:cd21253     5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84

                          90       100
                  ....*....|....*....|..
gi 529250185 1036 YTDRPDWQSVMQYVAQIYKYFE 1057
Cdd:cd21253    85 ALKVPDKLSILTYVSQYYNYFH 106

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLELS 1032
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80

                          90       100
                  ....*....|....*....|....*
gi 529250185 1033 EMLYTDRPDWQSVMQYVAQIYKYFE 1057
Cdd:cd21255    81 DMVLLPIPDKLIVMTYLCQLRAHFT 105

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSV-GINPSLEL 1031
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80

                          90       100
                  ....*....|....*....|....*.
gi 529250185 1032 SEMLYTDR-PDWQSVMQYVAQIYKYF 1056
Cdd:cd21261    81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEL 1031
Cdd:cd21251     5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84

                          90       100
                  ....*....|....*....|....*.
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYFE 1057
Cdd:cd21251    85 KEMASVGEPDKLSMVMYLTQFYEMFK 110

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEl 1031
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSLYDVF 104

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  952 GSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLE 1030
Cdd:cd21192     2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRiAEQHLNIPRLLE 81

                          90       100
                  ....*....|....*....|....*..
gi 529250185 1031 LSEMLyTDRPDWQSVMQYVAQIYKYFE 1057
Cdd:cd21192    82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  958 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLElSEMLY 1036
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEhLGIEKLLD-PEDVN 83

                          90
                  ....*....|....*...
gi 529250185 1037 TDRPDWQSVMQYVAQIYK 1054
Cdd:cd21187    84 VEQPDKKSILMYVTSLFQ 101

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLElS 1032
Cdd:cd21240     4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82

                          90       100
                  ....*....|....*....|....
gi 529250185 1033 EMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21240    83 EDVDVPSPDEKSVITYVSSIYDAF 106

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. 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 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 1031
Cdd:cd21287    10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21287    90 EDIVGTARPDEKAIMTYVSSFYHAF 114

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185  953 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLEl 1031
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNlAEQHLGLTKLLD- 80

                          90       100
                  ....*....|....*....|....*
gi 529250185 1032 SEMLYTDRPDWQSVMQYVAQIYKYF 1056
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYHYF 105

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529250185    956 NALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPY----QELNSQEKKRNLLLAFEAAQSVGINPSLEL 1031
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80