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 1958770270  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958770270  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 1958770270  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 970
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

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 1958770270 1336 LQSQTKVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPpqkqavlfSPAHSPGAEEAKPPP-ASITTKVKSPAEE 1414
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP--------SPSPRDNGTESKAPDmTSPTSAVTTPTPN 519

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1415 PLFPAPLLLREKPKAEGPEEQKTvhSPIRSQPVALPEARSPTSPTSSLQPESLLAPptpptppstqlpiCSQPQPSSDAS 1494
Cdd:pfam05109  520 ATSPTPAVTTPTPNATSPTLGKT--SPTSAVTTPTPNATSPTPAVTTPTPNATIPT-------------LGKTSPTSAVT 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1495 IPSP-TKSPIRFQPVP----------AKTSTPLTPLPvksqgdPKDRLSGPLAVEEALKRSDlVEEFWMKSAEIRRSLGL 1563
Cdd:pfam05109  585 TPTPnATSPTVGETSPqanttnhtlgGTSSTPVVTSP------PKNATSAVTTGQHNITSSS-TSSMSLRPSSISETLSP 657

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1564 TPVDRNKGSEPSLPSP---------ALKPISLKSYSVDKSPQDEglcllKPPSVPKRLGLPKSAGDQPP-------LLTP 1627
Cdd:pfam05109  658 STSDNSTSHMPLLTSAhptggenitQVTPASTSTHHVSTSSPAP-----RPGTTSQASGPGNSSTSTKPgevnvtkGTPP 732

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1628 KSPSDKELRSNQEERRDLSSSSGLGLHGSSSNMKTLGSQSFNTSDSTMLTPPSSPPPPPPPNEE----PATLRR-KPRQT 1702
Cdd:pfam05109  733 KNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATtylpPSTSSKlRPRWT 812

                          410       420
                   ....*....|....*....|....*..
gi 1958770270 1703 FERreasviPPPTPASFMRPPREAAQP 1729
Cdd:pfam05109  813 FTS------PPVTTAQATVPVPPTSQP 833

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 1958770270  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958770270  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 1958770270  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 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 1958770270  503 LVNSRTTPKLTRNESVARSSKLLGWCQRQTDGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQ--NVEQNN 579
Cdd:COG5069    109 LISRLTIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNN 188

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958770270  580 QLAFDIAEKELGISPIMTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:COG5069    189 FQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRF 232

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 1958770270   85 TNTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRNN-VLHLWPFTIHDLRGLGAK-------------KFYGKFC 150
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGrGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270  151 AGAIDHISI-------------RQLQLILLKVALILGIEIHVNVEFQGLVQPPEdqeneriGWRALVHPKThpvsEYEFE 217
Cdd:COG0654     82 GRVLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVTGLEQDAD-------GVTVTLADGR----TLRAD 150

                   ....*....
gi 1958770270  218 VIIGGDGRR 226
Cdd:COG0654    151 LVVGADGAR 159

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958770270  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHYC 971
Cdd:pfam00412    1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDYY 54

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1369 PSQVSSPSQPPQKQAVlfSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLLLREKPKAEGPEEQKTVHSPIRSQPVA 1448
Cdd:PHA03247  2673 AAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1449 LPEARSPTSPTSSLQPESLLAPPTPP----------TPPSTQLPICSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPLTP 1518
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 1519 lPVKSQGDPKDRLSGPLAVEEALkrsdlveEFWMKSAeirrslglTPVDRNKGSEPSLPSPALKP----ISLKSYSVDKS 1594
Cdd:PHA03247  2831 -PTSAQPTAPPPPPGPPPPSLPL-------GGSVAPG--------GDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRS 2894

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958770270 1595 PQDEGLcllkPPSVPKRLGLPKSAgdQPPLLTPKSP 1630
Cdd:PHA03247  2895 TESFAL----PPDQPERPPQPQAP--PPPQPQPQPP 2924

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF---SRNNVLHlwPFTIHDLRGLG---------------AKKFYGK 148
Cdd:pfam01494    2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlPRAHGLN--QRTMELLRQAGledrilaegvphegmGLAFYNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270  149 FCAGAIDHIS-------IRQLQL--ILLKVALILGIEIHVNVEFQGLVQppeDQENERIgwRALVHpKTHPVSEYEFEVI 219
Cdd:pfam01494   80 RRRADLDFLTspprvtvYPQTELepILVEHAEARGAQVRFGTEVLSLEQ---DGDGVTA--VVRDR-RDGEEYTVRAKYL 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958770270  220 IGGDGRRNTLE---GFRRKEFRGKLAIAITANFINRNTTaeAKVEEISGVAFIFNQKF 274
Cdd:pfam01494  154 VGCDGGRSPVRktlGIEFEGFEGVPFGSLDVLFDAPDLS--DPVERAFVHYLIYAPHS 209

DNA double-strand break repair ATPase Rad50;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 2021 ILERSSQKSKREPRTYTEEELSAKLTR---RVQKAARRQAKQEELKRLhRAQIIQRQLEQVEEKQRQLEERGVAVEKAL- 2096
Cdd:PRK03918   330 IKELEEKEERLEELKKKLKELEKRLEEleeRHELYEEAKAKKEELERL-KKRLTGLTPEKLEKELEELEKAKEEIEEEIs 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 2097 -----RGEADYWGESYYSGLIDLhlgvEPSGGTprrrplsfCPCCVQEgmgkkddpkLMQEwfklvQEKNAMVRYESELM 2171
Cdd:PRK03918   409 kitarIGELKKEIKELKKAIEEL----KKAKGK--------CPVCGRE---------LTEE-----HRKELLEEYTAELK 462

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958770270 2172 IFAREL-ELEDRQSRLQQELRErmaVEDHLKTEEELSEEKKILNEMLEVVEQrdslvalLEEQRLREKEEDK 2242
Cdd:PRK03918   463 RIEKELkEIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKELEEK-------LKKYNLEELEKKA 524

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 1958770270  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958770270  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 1958770270  520 RSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGK 599
Cdd:cd22198      1 RPEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80

                           90       100
                   ....*....|....*....|....*
gi 1958770270  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 1958770270 2074 QLEQVEEKQRQLEERGVAVEKALRGEADywgesyysglidlhlgvepsggtprrrplsfcpccvqegmGKKDDPKLMQEW 2153
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS----------------------------------------GDEEEEQLLQEW 40

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270 2154 FKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQ 2233
Cdd:pfam12130   41 FKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEED 120

                          170
                   ....*....|.
gi 1958770270 2234 RLREKEEDKDL 2244
Cdd:pfam12130  121 RLREEEEDEEL 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 1958770270  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84

                           90       100
                   ....*....|....*....|.
gi 1958770270  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 1958770270  916 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 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 1958770270  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21216     15 LLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIVN 94

                           90       100
                   ....*....|....*....|
gi 1958770270  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 1958770270  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21194      1 KSAKdaLLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                           90       100
                   ....*....|....*....|....*.
gi 1958770270  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 1958770270  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21248      1 RSAKdaLLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80

                           90       100
                   ....*....|....*....|....*.
gi 1958770270  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 1958770270  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21319      4 RSAKdaLLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83

                           90       100
                   ....*....|....*....|....*.
gi 1958770270  598 GKEMASvGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21319     84 PEDVFT-ENPDEKSIITYVVAFYHYF 108

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770270  521 SSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEkELGISPIMTGKE 600
Cdd:cd21255      3 SQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEPAD 81

                           90       100
                   ....*....|....*....|...
gi 1958770270  601 MASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21255     82 MVLLPIPDKLIVMTYLCQLRAHF 104

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 1958770270  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21321      2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKL 81

                           90       100
                   ....*....|....*....|....*...
gi 1958770270  596 MTgKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21321     82 LD-PEDVNVDQPDEKSIITYVATYYHYF 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 1958770270  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMaS 603
Cdd:cd21192      8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDV-L 86

                           90       100
                   ....*....|....*....|.
gi 1958770270  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 1958770270  513 TRNESVARSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKEL 590
Cdd:cd21322      9 TEDNRETRSAKdaLLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHL 88

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958770270  591 GISPIMTgKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21322     89 GLTKLLD-PEDVNMEAPDEKSIITYVVSFYHYF 120

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 1958770270  522 SKLLGWCQRQTDGYsgvNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKE 600
Cdd:cd21184      4 SLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80

                           90
                   ....*....|....*....
gi 1958770270  601 MASvGEPDKLSMVMYLTQF 619
Cdd:cd21184     81 MVS-PNVDELSVMTYLSYF 98

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 1958770270  522 SKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21200      4 QMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVEDM 83

                           90       100
                   ....*....|....*....|....
gi 1958770270  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 1958770270  512 LTRNESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEkELG 591
Cdd:cd21257      1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVG 79