calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as 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-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. 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 1720360560 321 GSAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVL 400
Cdd:cd21196     1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80

                          90       100
                  ....*....|....*....|....*.
gi 1720360560 401 SAQAVMAGSDPLGLIAYLSHFHSAFK 426
Cdd:cd21196    81 SAQAVVAGSDPLGLIAYLSHFHSAFK 106

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes 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. Eplin has also found to be tumor suppressor. 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 1720360560 498 CELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHpgDGHFYCLQH 551
Cdd:cd09358     1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASL--EGKLYCKPH 52

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as 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-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. 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 1720360560 321 GSAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVL 400
Cdd:cd21196     1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80

                          90       100
                  ....*....|....*....|....*.
gi 1720360560 401 SAQAVMAGSDPLGLIAYLSHFHSAFK 426
Cdd:cd21196    81 SAQAVVAGSDPLGLIAYLSHFHSAFK 106

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes 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. Eplin has also found to be tumor suppressor. 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 1720360560 498 CELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHpgDGHFYCLQH 551
Cdd:cd09358     1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASL--EGKLYCKPH 52

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 1720360560  326 EELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMG----ALEATTWALRVAEHELGITPVLS 401
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsrfkKIENINLALSFAEKLGGKVVLFE 80

                           90
                   ....*....|....*....
gi 1720360560  402 AQAVMAGS-DPLGLIAYLS 419
Cdd:smart00033  81 PEDLVEGPkLILGVIWTLI 99

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 1720360560  498 CELCGKHLYILERFC-VDGHFFHRSCFCCHTCEATLWPGGYgqHPGDGHFYCLQH 551
Cdd:smart00132   2 CAGCGKPIYGTERVLrALGKVWHPECFKCATCGKPLSGDTF--FEKDGKLYCKDC 54

DNA double-strand break repair ATPase Rad50;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360560 703 GAMTKYPTWRRTLMRRAKEEEMKRF-CKAQAIQRRLNEIEATMRELEAEGTKLELALRKESSSpEQQKKLwLDQLLRLIQ 781
Cdd:PRK03918  433 KAKGKCPVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKEL-AEQLKELEE 510

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360560 782 KKNSLVTEEAELMITVQELdLEEKQRQLDHELRGYmnrEETMKTEADLQSENQVLRKLLEVVNQRDALIqfqeERRLRE 860
Cdd:PRK03918  511 KLKKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSL---KKELEKLEELKKKLAELEKKLDELEEELAEL----LKELEE 581

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360560 731 QAIQRRLNEIEATMRELEAegtKLELALRKESSSPEQQKKLWLDQLL-RLIQKKNSLVTEEAELMITVQE-----LDLEE 804
Cdd:COG3206   222 SELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELLQSPVIqQLRAQLAELEAELAELSARYTPnhpdvIALRA 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360560 805 KQRQLDHELrgymnREETMKTEADLQSENQVLRKLLEVVNQRDAliqfQEERRLREMPA 863
Cdd:COG3206   299 QIAALRAQL-----QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPE 348

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as 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-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. 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 1720360560 321 GSAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVL 400
Cdd:cd21196     1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80

                          90       100
                  ....*....|....*....|....*.
gi 1720360560 401 SAQAVMAGSDPLGLIAYLSHFHSAFK 426
Cdd:cd21196    81 SAQAVVAGSDPLGLIAYLSHFHSAFK 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 1720360560 736 RLNEIEATMRELEAEGTKLELALRKESSSPEQQKKLwLDQLLRLIQKKNSLVTEEAELMITVQELDLEEKQRQLDHELRG 815
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRGEMSGDEEEEQL-LQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720360560 816 YMNREETMKTEADLQSENQVLRKLLEVVNQRDALIQFQEERRLREM 861
Cdd:pfam12130  80 LMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREE 125

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 1720360560 323 AGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSA 402
Cdd:cd21251     5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTG 84

                          90       100
                  ....*....|....*....|....*..
gi 1720360560 403 Q--AVMAGSDPLGLIAYLSHFHSAFKN 427
Cdd:cd21251    85 KemASVGEPDKLSMVMYLTQFYEMFKD 111

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [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-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 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 1720360560 327 ELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAVM 406
Cdd:cd21250     8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87

                          90       100
                  ....*....|....*....|..
gi 1720360560 407 AGSDP--LGLIAYLSHFHSAFK 426
Cdd:cd21250    88 SAEEPdkLSMVMYLSKFYELFR 109

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes 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. Eplin has also found to be tumor suppressor. 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 1720360560 498 CELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHpgDGHFYCLQH 551
Cdd:cd09358     1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASL--EGKLYCKPH 52

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. 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 1720360560 328 LLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAVMA 407
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84

                          90       100
                  ....*....|....*....|..
gi 1720360560 408 GSDP--LGLIAYLSHFHSAFKN 427
Cdd:cd21252    85 MKVPdcLSIMTYVSQYYNHFSN 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 1720360560 326 EELLHWCQEQTAG-FPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSEL--QGMGALEATTWALRVAEHELGITPVLsA 402
Cdd:pfam00307   5 KELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKVL-I 83

                          90       100
                  ....*....|....*....|....*
gi 1720360560 403 QAV-MAGSDPLGLIAYLSHFHSAFK 426
Cdd:pfam00307  84 EPEdLVEGDNKSVLTYLASLFRRFQ 108

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360560 324 GTEELLHWCQEQtagFPGVHVTDFSSSWADGLALCALVHHLQPGLL-EPSELQGMGALEATTWALRVAEHELGITPVLSA 402
Cdd:cd21184     2 GKSLLLEWVNSK---IPEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITP 78

                          90       100
                  ....*....|....*....|...
gi 1720360560 403 QAVMAGS-DPLGLIAYLSHFHSA 424
Cdd:cd21184    79 EDMVSPNvDELSVMTYLSYFRNA 101

The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule interacting with CasL): MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semapho-rin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM domain and calporin homology domain are known for interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein monooxygenase (MO) is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL was characterized to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL was also named junctional Rab13-binding protein (JRAB). 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 1720360560 498 CELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHPGDGHFYCLQH 551
Cdd:cd09439     1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPH 54

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 1720360560 326 EELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAV 405
Cdd:cd21216    13 EGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDI 92

                          90       100
                  ....*....|....*....|..
gi 1720360560 406 --MAGSDPLGLIAYLSHFHSAF 425
Cdd:cd21216    93 vnTPRPDERSVMTYVSCYYHAF 114

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. 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 1720360560 321 GSAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVL 400
Cdd:cd21291     8 GLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLL 87

                          90       100
                  ....*....|....*....|....*..
gi 1720360560 401 SAQAV--MAGSDPLGLIAYLSHFHSAF 425
Cdd:cd21291    88 DVEDVcdVAKPDERSIMTYVAYYFHAF 114

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 1720360560 328 LLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEhELGITPVLSA----- 402
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIdemvs 91

                          90
                  ....*....|.
gi 1720360560 403 ------QAVMA 407
Cdd:cd21199    92 merpdwQSVMS 102

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360560 326 EELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAV 405
Cdd:cd21226     3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82

                          90       100
                  ....*....|....*....|.
gi 1720360560 406 MAGS-DPLGLIAYLSHFHSAF 425
Cdd:cd21226    83 MTGNpDERSIVLYTSLFYHAF 103

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 1720360560 322 SAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLS 401
Cdd:cd21321     4 KSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLD 83

                          90       100
                  ....*....|....*....|....*
gi 1720360560 402 AQAVMAGS-DPLGLIAYLSHFHSAF 425
Cdd:cd21321    84 PEDVNVDQpDEKSIITYVATYYHYF 108

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720360560 328 LLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVL 400
Cdd:cd21200     6 LLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLL 78

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 1720360560 323 AGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEhELGITPVLSA 402
Cdd:cd21240     4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAE-RLGVTRLLDA 82

                          90       100
                  ....*....|....*....|....
gi 1720360560 403 QAVMAGS-DPLGLIAYLSHFHSAF 425
Cdd:cd21240    83 EDVDVPSpDEKSVITYVSSIYDAF 106

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 1720360560 328 LLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAVMA 407
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84

                          90
                  ....*....|....*
gi 1720360560 408 GS-DPLGLIAYLSHF 421
Cdd:cd21187    85 EQpDKKSILMYVTSL 99

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. 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 1720360560 322 SAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLS 401
Cdd:cd21289     9 TSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLD 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720360560 402 AQAVMAGSDP--LGLIAYLSHFHSAFKNTSHS 431
Cdd:cd21289    89 AEDIVNTPKPdeKAIMTYVSCFYHAFAGAEQA 120

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 1720360560 322 SAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLS 401
Cdd:cd21287     9 TSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLD 88

                          90       100
                  ....*....|....*....|....*.
gi 1720360560 402 AQAVMAGSDP--LGLIAYLSHFHSAF 425
Cdd:cd21287    89 AEDIVGTARPdeKAIMTYVSSFYHAF 114

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 1720360560 498 CELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHPGDGHFYCLQH 551
Cdd:cd09444     1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54

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 1720360560 322 SAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLS 401
Cdd:cd21290    12 TSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLD 91

                          90       100
                  ....*....|....*....|....*.
gi 1720360560 402 AQAVM--AGSDPLGLIAYLSHFHSAF 425
Cdd:cd21290    92 AEDIVntARPDEKAIMTYVSSFYHAF 117

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360560 326 EELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAV 405
Cdd:cd21238     5 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 84

                          90       100
                  ....*....|....*....|
gi 1720360560 406 -MAGSDPLGLIAYLSHFHSA 424
Cdd:cd21238    85 dVPQPDEKSIITYVSSLYDA 104