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 1720417384  515 NESVARSSKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720417384  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111

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 1720417384  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCEYCATTLRLSAYAYDIEDGKFYCKPHY 970
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

transcriptional regulator ICP4; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1280 PAETEGEAAEDGDPGDTGAELDDQHWSDDIPSDAeaehrlqsqakvkAELELRVSENEEEKPSDAPKQEERGTSQVSSPS 1359
Cdd:PHA03307    24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVA-------------GAAACDRFEPPTGPPPGPGTEAPANESRSTPTW 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1360 QPPEKQVGVFSPARSPGTEEAKSPLAT-KVKSPEEPLFPTPLLLREKPKAEVPEEQKAVLSPIrsqPVALPEARSPTSPT 1438
Cdd:PHA03307    91 SLSTLAPASPAREGSPTPPGPSSPDPPpPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP---AAGASPAAVASDAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1439 SLQPESLLApptpptppptQLPICSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPL-------TPLPVKSQGDPKDRLSG 1511
Cdd:PHA03307   168 SSRQAALPL----------SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPIsasasspAPAPGRSAADDAGASSS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1512 PLAVEEVLKRSDLVEEFWMKSAEIRRSLgLTPVDRSKG--SEPSLPSPASKPISLKSYSVDKSPQDEGlcllKPPSVPKR 1589
Cdd:PHA03307   238 DSSSSESSGCGWGPENECPLPRPAPITL-PTRIWEASGwnGPSSRPGPASSSSSPRERSPSPSPSSPG----SGPAPSSP 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1590 LGLPKSAGDQPplltpkSPSDKELRSSqEERRDLSSSSGLGLHDSSSNmktlgsqsfnTSDSTMLTPPSSPPPPPPPNEE 1669
Cdd:PHA03307   313 RASSSSSSSRE------SSSSSTSSSS-ESSRGAAVSPGPSPSRSPSP----------SRPPPPADPSSPRKRPRPSRAP 375

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1720417384 1670 PATLRRKPHQTFERREASIIPPPTPASfmRPPREPAQPPR 1709
Cdd:PHA03307   376 SSPAASAGRPTRRRARAAVAGRARRRD--ATGRFPAGRPR 413

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 1720417384  515 NESVARSSKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720417384  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111

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 1720417384  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCEYCATTLRLSAYAYDIEDGKFYCKPHY 970
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384  508 TTPKLTRNESVARSSKLLGWCQRQTEGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEK--NNQLAFD 584
Cdd:COG5069    114 TIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFE 193

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720417384  585 IAEKELGISPIMTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:COG5069    194 NANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRF 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 1720417384   916 CYFCQKRVYVMER-LSAEGKFFHRSCFKCEYCATTLRLSAYAydIEDGKFYCKPH 969
Cdd:smart00132    2 CAGCGKPIYGTERvLRALGKVWHPECFKCATCGKPLSGDTFF--EKDGKLYCKDC 54

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720417384  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCEYCATTLRLSAYAydIEDGKFYCKPHYC 971
Cdd:pfam00412    1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDYY 54

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF---SRNNVLHlwPFTIHDLRGLG---------------AKKFYGK 148
Cdd:pfam01494    2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlPRAHGLN--QRTMELLRQAGledrilaegvphegmGLAFYNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384  149 FCAGAIDHIS-------IRQLQL--ILLKVALILGIEIHVNVEFQGLVQppeDQENERIgwRALVHpKTHPVSEYEFEVI 219
Cdd:pfam01494   80 RRRADLDFLTspprvtvYPQTELepILVEHAEARGAQVRFGTEVLSLEQ---DGDGVTA--VVRDR-RDGEEYTVRAKYL 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417384  220 IGGDGRRNTLE---GFRRKEFRGKLAIAITANFINRNTTaeAKVEEISGVAFIFNQKF 274
Cdd:pfam01494  154 VGCDGGRSPVRktlGIEFEGFEGVPFGSLDVLFDAPDLS--DPVERAFVHYLIYAPHS 209

monooxygenase;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720417384   86 NTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDA---FSRNNVLHLWPFTIHDLRGLGAK 143
Cdd:PRK08244     2 KYEVIIIGGGPVGLMLASELALAGVKTCVIERLKEtvpYSKALTLHPRTLEILDMRGLLER 62

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1324 KVKAELELRVSENEEEKPSDAPKQEERGTSQVSSPSQPPEKQVG---VFSPARSPGTEEAKSPLATKVKSPEEPLFPTPL 1400
Cdd:NF033839   274 KFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPkpeVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 1401 LLR--EKPKAEV---PEEQKAVLSPIRSQPVALPEARSPTSPTSLQPESLLAPPTPPTPPPTQLP-ICSQPQPSSDASIP 1474
Cdd:NF033839   354 VKPqpEKPKPEVkpqPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPeVKPQPEKPKPEVKP 433

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720417384 1475 SPTKSPIRFQPVPAKTSTPLTPLPVKSQGDPKDRLSGP 1512
Cdd:NF033839   434 QPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP 471

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 2033 EELSAKLTRRVQKAARRQAKQEELKRLhraqiiQRQLEQVEEKQRQLEERGVAVEKALRGEAvepsggtprrrplsfcpc 2112
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEEL------EEELEELEAELEELREELEKLEKLLQLLP------------------ 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384 2113 cvqegmgkkddpkLMQEWFKLVQEKNAM-VRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEGELSEEKKiLN 2191
Cdd:COG4717    130 -------------LYQELEALEAELAELpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQ 195

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720417384 2192 EMLEVVEQRDSLVALLEEQRLREKEEDKDLEAAM 2225
Cdd:COG4717    196 DLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

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 1720417384  515 NESVARSSKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720417384  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111

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 1720417384  520 RSSKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGK 599
Cdd:cd22198      1 RPEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80

                           90       100
                   ....*....|....*....|....*
gi 1720417384  600 EMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd22198     81 EMASLAVPDKLSMVSYLSQFYEAFK 105

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 1720417384 2068 QLEQVEEKQRQLEERGVAVEKALRGEAVepsggtprrrplsfcpccvqegmGKKDDPKLMQEWFKLVQEKNAMVRYESEL 2147
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS-----------------------GDEEEEQLLQEWFKLVNEKNALVRRESEL 57

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720417384 2148 MIFARELELEDRQSRLQQELRERMAVEDHLKTEGELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEEDKDL 2221
Cdd:pfam12130   58 MYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. 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. 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 family 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 1720417384  524 LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84

                           90       100
                   ....*....|....*....|.
gi 1720417384  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21197     85 MHVPDRLSIITYVSQYYNHFR 105

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 1720417384  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCEYCATTLRLSAYAYDIEDGKFYCKPHY 970
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

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 1720417384  524 LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21216     15 LLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIVN 94

                           90       100
                   ....*....|....*....|
gi 1720417384  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21216     95 TPRPDERSVMTYVSCYYHAF 114

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 1720417384  520 RSSK--LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMT 597
Cdd:cd21194      1 KSAKdaLLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                           90       100
                   ....*....|....*....|....*.
gi 1720417384  598 GKEMAsVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21194     81 AEDVD-VARPDEKSIMTYVASYYHYF 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 1720417384  520 RSSK--LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMT 597
Cdd:cd21248      1 RSAKdaLLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80

                           90       100
                   ....*....|....*....|....*.
gi 1720417384  598 gKEMASVGEPDKLSMVMYLTQFYEMF 623
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 1720417384  520 RSSK--LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMT 597
Cdd:cd21319      4 RSAKdaLLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                           90       100
                   ....*....|....*....|....*.
gi 1720417384  598 GKEMASvGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21319     84 PEDVFT-ENPDEKSIITYVVAFYHYF 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 1720417384  520 RSSK--LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMT 597
Cdd:cd21249      3 RSAKeaLLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82

                           90       100
                   ....*....|....*....|....*.
gi 1720417384  598 GKEMAsVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21249     83 PEDVA-VPHPDERSIMTYVSLYYHYF 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 1720417384  524 LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKeLGISPIMTGKEMAS 603
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMVS 91

                           90       100
                   ....*....|....*....|.
gi 1720417384  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21199     92 MERPDWQSVMSYVTAIYKHFE 112

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 1720417384  524 LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGKEMaS 603
Cdd:cd21192      8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDV-L 86

                           90       100
                   ....*....|....*....|.
gi 1720417384  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21192     87 VDKPDERSIMTYVSQFLRMFP 107

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384  513 TRNESVARSSK--LLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKEL 590
Cdd:cd21322      9 TEDNRETRSAKdaLLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHL 88

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720417384  591 GISPIMTgKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21322     89 GLTKLLD-PEDVNMEAPDEKSIITYVVSFYHYF 120

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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417384  522 SKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21200      4 QMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVEDM 83

                           90       100
                   ....*....|....*....|....
gi 1720417384  602 ASVG-EPDKLSMVMYLTQFYEMFK 624
Cdd:cd21200     84 VRMGnRPDWKCVFTYVQSLYRHLR 107

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that 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 1720417384  512 LTRNESVARSSKLLGWCQRQTEGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEkELG 591
Cdd:cd21257      1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720417384  592 ISPIMTGKEMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21257     80 IKPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112