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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*.
gi 89885727   82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYFH 106

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89885727  188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHH 241
Cdd:cd09444    1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    215 CKQCSSTLHSGAYRATGEPGVFVCTHHSSEVTSVSPKSSNLASRKP--GGVTADTRPFGVSWTVQEANGEGTPlrvrtaa 292
Cdd:pfam17823  150 CRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPttAASSAPATLTPARGISTAATATGHP------- 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    293 wehAGGNTTAKgfVQTELKPPSTSQVHVGSSAGPKLPTITVTTTSVTSKALTHVTNSSPIGWSSPAQSSPANFNSRPVVS 372
Cdd:pfam17823  223 ---AAGTALAA--VGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAA 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    373 PSARNTHLPGSQGQTASKGVKTQLNLNSESSNTAVTPAWTSSASKTQQArekffqtppsapapaSAPAPAPTSKVPTVVT 452
Cdd:pfam17823  298 PMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLA---------------VVTTTKAQAKEPSASP 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    453 VP---TSKVPNV-VTAPTSKVPTVVTVPTSKVPTVVSAPTSKVPTVVSAPTSKVPTVVNSTNSRVTTVVNA-PTSKVPTV 527
Cdd:pfam17823  363 VPvlhTSMIPEVeATSPTTQPSPLLPTQGAAGPGILLAPEQVATEATAGTASAGPTPRSSGDPKTLAMASCqLSTQGQYL 442

                          330
                   ....*....|..
gi 89885727    528 VSATNGRVPTVV 539
Cdd:pfam17823  443 VVTTDPLTPALV 454

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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*.
gi 89885727   82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYFH 106

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89885727  188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHH 241
Cdd:cd09444    1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727   10 WCRQQCEGYR-DVSITNMTTSFRDGLAFCAILHRHRPDLI--NFSALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVA 86
Cdd:COG5069  133 WCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLdpNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVN 212

                         90       100
                 ....*....|....*....|
gi 89885727   87 LKVPDRLSILTYVSQYYNYF 106
Cdd:COG5069  213 VSIPDERSIMTYVSWYIIRF 232

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 89885727     187 ICGVCGKHVHLVQRHL-ADGRLYHRSCFRCKQCSSTLHSGAYRATGepGVFVCTHH 241
Cdd:smart00132    1 KCAGCGKPIYGTERVLrALGKVWHPECFKCATCGKPLSGDTFFEKD--GKLYCKDC 54

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727  843 QEELQRQLQDIESQLDALELRGVELEKRLRAAEGDASE-----DSLMVDWFRLIHEKQLLLRLESEL--MYKSKDQR--- 912
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEElqeelEELQKERQDLEQQRKQLEAQIAELqsEIAEREEElke 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89885727  913 LEEQQLDLQGELRRLMDKPEGLKSPQDRQREQELLSQYVNTVNDRSDIVDFLDEDRLREQEEDQMLENMIQNLGLQ 988
Cdd:COG4372  155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230

BDLF3; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727   455 TSKVPNVVTAPTSKVPTVVTVPTskvPTVVSAPTSKVPTVVSAPTSKVPTVVNSTNsrvTTVVNAPTSKVPTVVSATNGR 534
Cdd:PHA03255   25 TSSGSSTASAGNVTGTTAVTTPS---PSASGPSTNQSTTLTTTSAPITTTAILSTN---TTTVTSTGTTVTPVPTTSNAS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727   535 VPTVVTAHTGRVPAVMNTSASKVSPVVDAPAQESSREQAlsvlrkALPALTGSGTQAPNRSFPATSSVLVTLPknEVPqK 614
Cdd:PHA03255   99 TINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTS------ATTRITNATTLAPTLSSKGTSNATKTTA--ELP-T 169

                         170
                  ....*....|....*...
gi 89885727   615 VPSDKLSALTTQTPNFTI 632
Cdd:PHA03255  170 VPDERQPSLSYGLPLWTL 187

LIM domain; This family represents two copies of the LIM structural domain.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 89885727    188 CGVCGKHV---HLVQrhlADGRLYHRSCFRCKQCSSTLHSGAYRAT-GEPgvfVCTHH 241
Cdd:pfam00412    1 CAGCNRPIydrELVR---ALGKVWHPECFRCAVCGKPLTTGDFYEKdGKL---YCKHD 52

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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21253    1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                         90       100
                 ....*....|....*....|....*.
gi 89885727   82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253   81 EDMVALKVPDKLSILTYVSQYYNYFH 106

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    849 QLQDIESQLDALELRGVELEKRLR-AAEGDASEDSLMVDWFRLIHEKQLLLRLESELMYKSKDQRLEEQQLDLQGELRRL 927
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRgEMSGDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELREL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 89885727    928 MDKPEGLKSPQDRQREQELLSQYVNTVNDRSDIVDFLDEDRLREQEEDQML 978
Cdd:pfam12130   81 MSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131

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 89885727    3 AIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDAE 82
Cdd:cd22198    1 RPEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80

                         90       100
                 ....*....|....*....|....*
gi 89885727   83 DMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd22198   81 EMASLAVPDKLSMVSYLSQFYEAFK 105

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; 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. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also 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 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 89885727    7 LQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAeEQLGIPALLDAEDMVA 86
Cdd:cd21198    6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAA-AKLGIPRLLDPADMVL 84

                         90       100
                 ....*....|....*....|
gi 89885727   87 LKVPDRLSILTYVSQYYNYF 106
Cdd:cd21198   85 LSVPDKLSVMTYLHQIRAHF 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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21194    2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81

                         90       100
                 ....*....|....*....|....*
gi 89885727   82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21194   82 ED-VDVARPDEKSIMTYVASYYHYF 105

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; 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. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. 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 89885727    3 AIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEqLGIPALLDAE 82
Cdd:cd21254    2 ASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEPS 80

                         90       100
                 ....*....|....*....|....*..
gi 89885727   83 DMVALKVPDRLSILTYVSQYYNYFHGR 109
Cdd:cd21254   81 DMVLLAVPDKLTVMTYLYQIRAHFSGQ 107

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 89885727  188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHH 241
Cdd:cd09444    1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54

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 89885727    3 AIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDAE 82
Cdd:cd21189    2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81

                         90       100
                 ....*....|....*....|....
gi 89885727   83 DmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21189   82 D-VDVPEPDEKSIITYVSSLYDVF 104

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 89885727    1 MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLD 80
Cdd:cd21251    4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMT 83

                         90       100
                 ....*....|....*....|....*.
gi 89885727   81 AEDMVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21251   84 GKEMASVGEPDKLSMVMYLTQFYEMF 109

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21321    5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84

                         90       100
                 ....*....|....*....|....*
gi 89885727   82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21321   85 ED-VNVDQPDEKSIITYVATYYHYF 108

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) 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. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 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 89885727    1 MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLD 80
Cdd:cd21249    3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82

                         90       100
                 ....*....|....*....|....*.
gi 89885727   81 AEDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21249   83 PED-VAVPHPDERSIMTYVSLYYHYF 107

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 89885727    6 ALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQlGIPALLDAEDMV 85
Cdd:cd21199   12 ALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLTIDEMV 90

                         90       100
                 ....*....|....*....|.
gi 89885727   86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21199   91 SMERPDWQSVMSYVTAIYKHF 111

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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21287   10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDA 89

                         90       100
                 ....*....|....*....|....*..
gi 89885727   82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21287   90 EDIVGTARPDEKAIMTYVSSFYHAFSG 116

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 89885727    1 MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLD 80
Cdd:cd21192    2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81

                         90       100
                 ....*....|....*....|....*.
gi 89885727   81 AEDMVALKvPDRLSILTYVSQYYNYF 106
Cdd:cd21192   82 VEDVLVDK-PDERSIMTYVSQFLRMF 106

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 89885727      1 MAAIKALQEWCRQQCEGYRD-VSITNMTTSFRDGLAFCAILHRHRPDLINFSAL--RKENIYENNKLAFQVAEEQLGIP- 76
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPk 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 89885727     77 ALLDAEDMVAlkvPDRLSILTYVSQYYNYFHG 108
Cdd:pfam00307   81 VLIEPEDLVE---GDNKSVLTYLASLFRRFQA 109

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 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. 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 89885727    2 AAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDA 81
Cdd:cd21290   13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDA 92

                         90       100
                 ....*....|....*....|....*..
gi 89885727   82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21290   93 EDIVNTARPDEKAIMTYVSSFYHAFSG 119

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89885727    1 MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLD 80
Cdd:cd21243    4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83