calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1958789390  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 1999 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 2066
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 2067 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 2117
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 2118 GTMNQGVSSspnlelhhnfrwvlcanhmepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSVLEt 2194
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789390 2195 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2264
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1958789390  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105

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 1958789390  204 THAAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRV-PAASSSNKAQgasnlnrrsqsfnsidks 282
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTgPTVSTADVTS------------------ 475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  283 kpPNYANGNEKDSSKGPQPSSGINGN-TQPPSTSGQPPASAIPSPNASKPWRSKSMNVKHSATSTMLTVKQPSPATSPTP 361
Cdd:pfam05109  476 --PTPAGTTSGASPVTPSPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTP 553

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  362 SSDRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQATSSGPNDSGKDDDAfsesgemegfNSGLNSGGSTNSSPK 441
Cdd:pfam05109  554 NATSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPV 617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  442 VSpklTPPK-AGSKNFSNKKSLLQPKEKEEKNRDKNKACAEKPGKEEKDQ-----MMDATPKKTSKIASLIPKGSKTAAA 515
Cdd:pfam05109  618 VT---SPPKnATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTshmplLTSAHPTGGENITQVTPASTSTHHV 694

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  516 kkdslipSSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFQKAITMEKTSTPSLSA 582
Cdd:pfam05109  695 -------STSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 1999 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 2066
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 2067 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 2117
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 2118 GTMNQGVSSspnlelhhnfrwvlcanhmepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSVLEt 2194
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789390 2195 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2264
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390 2016 IILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGvelpvVIILDNLHHV 2095
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96

                   .
gi 1958789390 2096 G 2096
Cdd:cd00009     97 S 97

EBNA-3B; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  226 TARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKSKPPNYANGNEKDSSKGP---QPS 302
Cdd:PHA03378   678 PTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPgraRPP 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390  303 SGINGNTQPPSTSG-----QPPASAIPSPNaSKPWRSKSMNVKHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSA 377
Cdd:PHA03378   758 AAAPGRARPPAAAPgaptpQPPPQAPPAPQ-QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRG 836

                          170
                   ....*....|..
gi 1958789390  378 -PSGQK-SMLEK 387
Cdd:PHA03378   837 rPSLKKpAALER 848

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1958789390  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21212      3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGIT 82

                           90       100
                   ....*....|....*....|...
gi 1958789390  161 AEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21212     83 AEDIVDGNLKAILGLFFSLSRYK 105

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21215      7 KTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTNIG 84

                           90
                   ....*....|....*....
gi 1958789390  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21215     85 AEDIVDGNLKLILGLLWTL 103

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21227      7 NTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIG 84

                           90
                   ....*....|....*....
gi 1958789390  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21227     85 NEDIVNGNLKLILGLIWHL 103

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNV-QGL 159
Cdd:cd00014      2 EELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPElDLF 80

                           90       100
                   ....*....|....*....|...
gi 1958789390  160 SAEEI-RNGNLKAILGLFFSLSR 181
Cdd:cd00014     81 EPEDLyEKGNLKKVLGTLWALAL 103

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   83 YTDWANHYLAKSGhkRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAA-RGVNVQGLSA 161
Cdd:cd21311     20 FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIVNIDS 97

                           90
                   ....*....|....*...
gi 1958789390  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21311     98 SDIVDGKLKLILGLIWTL 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQsqMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21188      6 KTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFH--RLQNVQTALDFLKYRKIKLVNIR 81

                           90
                   ....*....|....*....
gi 1958789390  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21188     82 AEDIVDGNPKLTLGLIWTI 100

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARGVNVQGL 159
Cdd:cd21183      7 NTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADHIKLVNI 84

                           90       100
                   ....*....|....*....|
gi 1958789390  160 SAEEIRNGNLKAILGLFFSL 179
Cdd:cd21183     85 GSGDIVNGNIKLILGLIWTL 104

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (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. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   83 YTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21310     21 FTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHIKLVSIDS 98

                           90
                   ....*....|....*...
gi 1958789390  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21310     99 KAIVDGNLKLILGLIWTL 116

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21190      8 KTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVNIN 87

                           90       100
                   ....*....|....*....|..
gi 1958789390  161 AEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21190     88 STDIVDGKPSIVLGLIWTIILY 109

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (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. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21309     22 FTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99

                           90
                   ....*....|....*...
gi 1958789390  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21309    100 KAIVDGNLKLILGLVWTL 117

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   63 EFGEKKALQGTAKDIEdSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGcpRSQSQMIEN 141
Cdd:cd21317     17 ERSRIKALADEREAVQ-KKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQLpKPTKG--RMRIHCLEN 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958789390  142 VDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21317     92 VDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTI 129

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKrLIKDLQQDIADGVLLADIIQIIANEKVEDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21186      5 KTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVNIS 81

                           90
                   ....*....|....*....
gi 1958789390  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21186     82 SNDIVDGNPKLTLGLVWSI 100

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21241      8 KTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKLVNIN 87

                           90       100
                   ....*....|....*....|..
gi 1958789390  161 AEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21241     88 PTDIVDGKPSIVLGLIWTIILY 109

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) 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. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also 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. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   60 STCEFGEKKALQGTAKDIE--DSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGcpRSQS 136
Cdd:cd21316     33 SSARLFERSRIKALADEREavQKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRI 108

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958789390  137 QMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21316    109 HCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTI 151

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:COG5069     12 KTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFNIG 90

                           90       100
                   ....*....|....*....|
gi 1958789390  161 AEEIRNGNLKAILGLFFSLS 180
Cdd:COG5069     91 PQDIVDGNPKLILGLIWSLI 110

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   81 KIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21231      9 KTFTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHA--LNNVNKALQVLQKNNVDLVNIG 85

                           90
                   ....*....|....*....
gi 1958789390  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21231     86 SADIVDGNHKLTLGLIWSI 104

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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 1958789390   87 ANHYLAKSGhkRLIKDLQQDIADGVLLADIIQIIANEKV--EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEI 164
Cdd:cd21222     25 VNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPEDI 102

                           90
                   ....*....|....*....
gi 1958789390  165 RNGNLKAILGLFFSL-SRY 182
Cdd:cd21222    103 VNGDLKSILRVLYSLfSKY 121

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789390   78 EDSKIYTDWANHYlaksGHKRLIKDLQQDIADGVLLadiIQIIanEKVEdiNGC----------PRSQSQMIENVDVCLS 147
Cdd:cd21219      4 REERAFRMWLNSL----GLDPLINNLYEDLRDGLVL---LQVL--DKIQ--PGCvnwkkvnkpkPLNKFKKVENCNYAVD 72