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 1207192085  528 ESIVRSSKLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPI 607
Cdd:cd21251      2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1207192085  608 MTGKEMSVVVEPDKLSMVMYLSQFYEMFKD 637
Cdd:cd21251     82 MTGKEMASVGEPDKLSMVMYLTQFYEMFKD 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 1207192085 1086 CFFCRKRVYVMERLSAEGKFFHRSCFKCDYCGTTLRLSSYAFDVEDGKFYCKPHY 1140
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2221 AKERGRVTEKGKERSRERENEKRVKEK----MVKMKDVER-EKGKEEESVYVPHALAFKRSYATKKTYTEEELNAKLTRR 2295
Cdd:pfam17380  343 AMERERELERIRQEERKRELERIRQEEiameISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2296 VQ-KAARRQAKQEELKRLH--RAQMIQRQLEQVEEKQRQLEErgvavekaLRGEAGLYKGSSVSpKQRKRRSDYWGESNY 2372
Cdd:pfam17380  423 EQiRAEQEEARQREVRRLEeeRAREMERVRLEEQERQQQVER--------LRQQEEERKRKKLE-LEKEKRDRKRAEEQR 493

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2373 SEILDLHLgvepyvgTPRRRALylcpccapegmgkkddpklmqewfklVQEKNalvryESELMifarELELEDRQSRLQQ 2452
Cdd:pfam17380  494 RKILEKEL-------EERKQAM--------------------------IEEER-----KRKLL----EKEMEERQKAIYE 531

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1207192085 2453 ELRERMAiDDHLKTEEELAEEKQILNEMLEVVEQRDSLVALLEEQRL 2499
Cdd:pfam17380  532 EERRREA-EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577

104 kDa microneme/rhoptry antigen; Provisional

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192085 1840 EEPKSETMPIKPRTPVSPPQPKQK-----PVTAPVPTPRTNPPVVMRVKEPNKPRREEVRKS 1896
Cdd:PTZ00449   592 EEPKKPKRPRSAQRPTRPKSPKLPelldiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

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 1207192085  528 ESIVRSSKLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPI 607
Cdd:cd21251      2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1207192085  608 MTGKEMSVVVEPDKLSMVMYLSQFYEMFKD 637
Cdd:cd21251     82 MTGKEMASVGEPDKLSMVMYLTQFYEMFKD 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 1207192085 1086 CFFCRKRVYVMERLSAEGKFFHRSCFKCDYCGTTLRLSSYAFDVEDGKFYCKPHY 1140
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

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 1207192085   536 LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDF----ESLDEKDVEKNNQLAFDVAEREFGISPIMTGK 611
Cdd:smart00033    3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFEPE 82

                            90       100
                    ....*....|....*....|
gi 1207192085   612 EMsVVVEPDKLSMVMYLSQF 631
Cdd:smart00033   83 DL-VEGPKLILGVIWTLISL 101

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 1207192085  1085 VCFFCRKRVYVMER-LSAEGKFFHRSCFKCDYCGTTlrLSSYAFDVEDGKFYCKPH 1139
Cdd:smart00132    1 KCAGCGKPIYGTERvLRALGKVWHPECFKCATCGKP--LSGDTFFEKDGKLYCKDC 54

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 1488 VVTLPVDNDKTESQGQVFNTAEKTSANPRELIVDVVLSPIQKPALPiEEVHEVSPVVLVKSPGarffpepylpdkvkqni 1567
Cdd:pfam05109  404 IITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLP-SSTHVPTNLTAPASTG----------------- 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 1568 PPPQSPDVKTPhSPVAQIIALSPICSQPVPQ--------PGTASPKSPV--------QPQPCACSPTGNPLSPICTQSQP 1631
Cdd:pfam05109  466 PTVSTADVTSP-TPAGTTSGASPVTPSPSPRdngteskaPDMTSPTSAVttptpnatSPTPAVTTPTPNATSPTLGKTSP 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 1632 CNEPPSPLSTSspvrTQPVPAVTS-TPLAKPASENRTNEHLKDSTPELKKTD-LIEEFWLKSAEIRKSLG---LTPLERS 1706
Cdd:pfam05109  545 TSAVTTPTPNA----TSPTPAVTTpTPNATIPTLGKTSPTSAVTTPTPNATSpTVGETSPQANTTNHTLGgtsSTPVVTS 620

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 1707 KTAVEKSIVKTP----TPESSSPKSYTPEDLSEEQKPTFTGRSIIRRINIT----LEGQVISPVEPKSNGSEKkdLSSSS 1778
Cdd:pfam05109  621 PPKNATSAVTTGqhniTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTsahpTGGENITQVTPASTSTHH--VSTSS 698

                          330       340
                   ....*....|....*....|....*
gi 1207192085 1779 GLGLNGsvTTSQtaASDSYNNSDST 1803
Cdd:pfam05109  699 PAPRPG--TTSQ--ASGPGNSSTST 719

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085   90 NTKCLIIGAGPCGLRTAIELGFLGAKVVLLEKRDAFSRNN-VLHLWPFTIQDLRGLGAK-------------KFYGKFCA 155
Cdd:COG0654      3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGrGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSDG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085  156 GAIDHISI-------------RQLQLMLLKVALLLGIEIHVNVEFKGLIEPPEdqeneriGWRAEVHPRThpvnELEFDV 222
Cdd:COG0654     83 RVLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVTGLEQDAD-------GVTVTLADGR----TLRADL 151

                   ....*...
gi 1207192085  223 IIGADGRR 230
Cdd:COG0654    152 VVGADGAR 159

DNA double-strand break repair ATPase Rad50;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2220 RAKERGRVTEKGKE-RSRERENEKRVKEKMVKMKDVEREKGKEEESVYVphaLAFKRSYATKKTYTEEELnAKLTRRVQK 2298
Cdd:PRK03918   250 LEGSKRKLEEKIRElEERIEELKKEIEELEEKVKELKELKEKAEEYIKL---SEFYEEYLDELREIEKRL-SRLEEEING 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2299 AARRQAKQEELKRlhRAQMIQRQLEQVEEKQRQLEERGVAVEKALRGEAGLykgssvsPKQRKRRSDYWGESNYSEILDL 2378
Cdd:PRK03918   326 IEERIKELEEKEE--RLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL-------ERLKKRLTGLTPEKLEKELEEL 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2379 H---LGVEPYVGTPRRR--------------------ALYLCPCCAPEgmgkkddpkLMQEwfklvQEKNALVRYESELM 2435
Cdd:PRK03918   397 EkakEEIEEEISKITARigelkkeikelkkaieelkkAKGKCPVCGRE---------LTEE-----HRKELLEEYTAELK 462

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192085 2436 IFAREL-ELEDRQSRLQQELRErmaIDDHLKTEEELAEEKQILNEMLEVVEQrdslvalLEEQRLREKEEDK 2506
Cdd:PRK03918   463 RIEKELkEIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKELEEK-------LKKYNLEELEKKA 524

hypothetical protein; Provisional

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1207192085   88 CANTKCLIIGAGPCGLRTAIELGFLGAKVVLLEKRDAFSRN 128
Cdd:PRK06126     5 TSETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFN 45

104 kDa microneme/rhoptry antigen; Provisional

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192085 1840 EEPKSETMPIKPRTPVSPPQPKQK-----PVTAPVPTPRTNPPVVMRVKEPNKPRREEVRKS 1896
Cdd:PTZ00449   592 EEPKKPKRPRSAQRPTRPKSPKLPelldiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

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 1207192085  528 ESIVRSSKLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPI 607
Cdd:cd21251      2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1207192085  608 MTGKEMSVVVEPDKLSMVMYLSQFYEMFKD 637
Cdd:cd21251     82 MTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (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. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085  528 ESIVRSSKLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPI 607
Cdd:cd21195      1 SGDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPV 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1207192085  608 MTGKEMSVVVEPDKLSMVMYLSQFYEMFKD 637
Cdd:cd21195     81 TTGKEMASAQEPDKLSMVMYLSKFYELFRG 110

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 1207192085 2321 QLEQVEEKQRQLEERGVAVEKALRGEAGlykgssvspkqrkrrsdywgesnyseildlhlgvepyvgtprrralylcpcc 2400
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS---------------------------------------------------- 28

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192085 2401 apegmGKKDDPKLMQEWFKLVQEKNALVRYESELMIFARELELEDRQSRLQQELRERMAIDDHLKTEEELAEEKQILNEM 2480
Cdd:pfam12130   29 -----GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEEL 103

                          170       180
                   ....*....|....*....|....*...
gi 1207192085 2481 LEVVEQRDSLVALLEEQRLREKEEDKDL 2508
Cdd:pfam12130  104 VEIVEQRDALVDSLEEDRLREEEEDEEL 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 1207192085  536 LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMTGKEMSV 615
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84

                           90       100
                   ....*....|....*....|.
gi 1207192085  616 VVEPDKLSMVMYLSQFYEMFK 636
Cdd:cd21197     85 MHVPDRLSIITYVSQYYNHFR 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 1207192085  533 SSKLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAErEFGISPIMTGKE 612
Cdd:cd21198      3 GQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDPAD 81

                           90       100
                   ....*....|....*....|...
gi 1207192085  613 MSVVVEPDKLSMVMYLSQFYEMF 635
Cdd:cd21198     82 MVLLSVPDKLSVMTYLHQIRAHF 104

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 1207192085  536 LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMTGKEMSV 615
Cdd:cd21252      5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84

                           90       100
                   ....*....|....*....|..
gi 1207192085  616 VVEPDKLSMVMYLSQFYEMFKD 637
Cdd:cd21252     85 MKVPDCLSIMTYVSQYYNHFSN 106

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 1207192085  532 RSSK--LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMT 609
Cdd:cd21194      1 KSAKdaLLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                           90       100
                   ....*....|....*....|....*.
gi 1207192085  610 GKEMSvVVEPDKLSMVMYLSQFYEMF 635
Cdd:cd21194     81 AEDVD-VARPDEKSIMTYVASYYHYF 105

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 1207192085  535 KLLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMTGKEMS 614
Cdd:cd21189      5 ALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPEDVD 84

                           90       100
                   ....*....|....*....|.
gi 1207192085  615 vVVEPDKLSMVMYLSQFYEMF 635
Cdd:cd21189     85 -VPEPDEKSIITYVSSLYDVF 104

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 1207192085  532 RSSK--LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMT 609
Cdd:cd21248      1 RSAKdaLLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80

                           90       100
                   ....*....|....*....|....*..
gi 1207192085  610 GKEmsVVVE-PDKLSMVMYLSQFYEMF 635
Cdd:cd21248     81 PED--VNVEqPDEKSIITYVVTYYHYF 105

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 1207192085  531 VRSSK--LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIM 608
Cdd:cd21249      2 LRSAKeaLLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81

                           90       100
                   ....*....|....*....|....*..
gi 1207192085  609 TGKEMsVVVEPDKLSMVMYLSQFYEMF 635
Cdd:cd21249     82 DPEDV-AVPHPDERSIMTYVSLYYHYF 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 1207192085  536 LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAErEFGISPIMTGKEMSV 615
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEMVS 91

                           90       100
                   ....*....|....*....|.
gi 1207192085  616 VVEPDKLSMVMYLSQFYEMFK 636
Cdd:cd21199     92 MERPDWQSVMSYVTAIYKHFE 112

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 1207192085  536 LLNWCQRQTEGY-RGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESL--DEKDVEKNNQLAFDVAEREFGISPIMTGKE 612
Cdd:pfam00307    7 LLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKVLIEPE 86

                           90       100
                   ....*....|....*....|....
gi 1207192085  613 MsvVVEPDKLSMVMYLSQFYEMFK 636
Cdd:pfam00307   87 D--LVEGDNKSVLTYLASLFRRFQ 108

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 1207192085  536 LLNWCQRQTEGYRGVSVSDLTTSWKSGLALCALIHRYRPDLIDFESLDEKDVEKNNQLAFDVAEREFGISPIMTGKEMsV 615
Cdd:cd21192      8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDV-L 86