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 1207171713   90 ICKIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQG 169
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1207171713  170 LSAEEVCNGNLKSILGLFFILSRYK 194
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 1207171713 1187 AVGTPTSTKRRDTGKVGSGRSSPVTINQTDkekvAGSDQEGTGLPTSPKSSPTSTQSGLRQPGSKYPDIASPTfrrlfgs 1266
Cdd:pfam05109  409 ATNATTTTHKVIFSKAPESTTTSPTLNTTG----FAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT------- 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1267 kaSSKPSSPGTPDSgkcPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQsggssplygKTPDLGTDSP-ASSPASGLSL 1345
Cdd:pfam05109  478 --PAGTTSGASPVT---PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS---------PTPAVTTPTPnATSPTLGKTS 543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1346 PSNARPWP-PNLSSSSAgskdtlschsmtslhtsseSIDLPLPHHHGPKVTRTGSVKSTLSegmPLDRNTLPKKGLRYPP 1424
Cdd:pfam05109  544 PTSAVTTPtPNATSPTP-------------------AVTTPTPNATIPTLGKTSPTSAVTT---PTPNATSPTVGETSPQ 601

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1425 SSRQtsheegkewlrSHSTGGLQDTGSPLSPP--GTTCANAGKYHYSN------LLSPTSMSQYNIPSTSMSRSNSIPaq 1496
Cdd:pfam05109  602 ANTT-----------NHTLGGTSSTPVVTSPPknATSAVTTGQHNITSsstssmSLRPSSISETLSPSTSDNSTSHMP-- 668

                          330
                   ....*....|....
gi 1207171713 1497 dsfeLYGEGHPLGG 1510
Cdd:pfam05109  669 ----LLTSAHPTGG 678

Herpesvirus phosphoprotein 85 (HHV6-7 U14/HCMV UL25); This family includes UL25 proteins from HCMV, as well as U14 proteins from HHV 6 and HHV7. These 85 kD phosphoproteins appear to act as structural antigens, but their precise function is otherwise unknown.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713  938 DASSWAGAEDLkkvdEEMEPGMDPSckwktSSPSSSCQGEDISQKTGLPmSQTGSWRRGMSAQVGIT----PPRTKGTST 1013
Cdd:PHA03249    32 DPRPRAPTEDL----DRMEAGLSSY-----SSSSDNKSSFEVVSETDSG-SEAEAERGRRAGMGGRNkatkPSRRNKTTQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1014 SLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSG 1093
Cdd:PHA03249   102 CRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEEDEGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFC 181

                   ....
gi 1207171713 1094 SATL 1097
Cdd:PHA03249   182 DSDI 185

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 1207171713   90 ICKIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQG 169
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1207171713  170 LSAEEVCNGNLKSILGLFFILSRYK 194
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   87 ESKICKIYTDWANHYLAKSGCPRlIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVS 166
Cdd:COG5069      7 QKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVK 85

                           90       100
                   ....*....|....*....|....*
gi 1207171713  167 VQGLSAEEVCNGNLKSILGLFFILS 191
Cdd:COG5069     86 LFNIGPQDIVDGNPKLILGLIWSLI 110

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713  2061 HRRIILSGPSGTGKSYLATKLAYFILSKTGREV----TDTNLATFNVDQKSSKDLRQYLSSLAEQCN--TEECEIELPTV 2134
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRlaLALARKLKPDV 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171713  2135 VILDNLHHIGS---------LSDIFNGFLNCKYHKCPyVIGTMNQGVSSSPNLELH 2181
Cdd:smart00382   82 LILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1565 HSEgqTVQnttQIRKLRRELDASQEKVATLTSQL-AANAHLVAAfEKSLAnmtcrlqsltmtaEQK---ESELAELRETI 1640
Cdd:pfam07926   52 HAE--DIK---ALQALREELNELKAEIAELKAEAeSAKAELEES-EESWE-------------EQKkelEKELSELEKRI 112

                   ....*...
gi 1207171713 1641 EALKTQNT 1648
Cdd:pfam07926  113 EDLNEQNK 120

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 2064 IILSGPSGTGKSYLATKLAyfilSKTGREVTDTNLATFnVDQ---KSSKDLRQYLsslaeqcntEECEIELPTVVILDNL 2140
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVA----KELGAPFIEISGSEL-VSKyvgESEKRLRELF---------EAAKKLAPCVIFIDEI 66

                           90       100
                   ....*....|....*....|....
gi 1207171713 2141 HHIGS---------LSDIFNGFLN 2155
Cdd:pfam00004   67 DALAGsrgsggdseSRRVVNQLLT 90

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207171713 2037 IDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFI 2085
Cdd:PRK11331   170 LEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLL 218

DNA packaging tegument protein UL25; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713  938 DASSWAGAEDLkkvdEEMEPGMDPSckwktSSPSSSCQGEDISQKTGLPmSQTGSWRRGMSAQVGIT----PPRTKGTST 1013
Cdd:PHA03249    32 DPRPRAPTEDL----DRMEAGLSSY-----SSSSDNKSSFEVVSETDSG-SEAEAERGRRAGMGGRNkatkPSRRNKTTQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713 1014 SLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSG 1093
Cdd:PHA03249   102 CRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEEDEGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFC 181

                   ....
gi 1207171713 1094 SATL 1097
Cdd:PHA03249   182 DSDI 185

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 1207171713   90 ICKIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQG 169
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1207171713  170 LSAEEVCNGNLKSILGLFFILSRYK 194
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 1207171713   91 CKIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGL 170
Cdd:cd21212      2 IEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGI 81

                           90       100
                   ....*....|....*....|....
gi 1207171713  171 SAEEVCNGNLKSILGLFFILSRYK 194
Cdd:cd21212     82 TAEDIVDGNLKAILGLFFSLSRYK 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 1207171713   92 KIYTDWANHYLAKSGCPrlIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLS 171
Cdd:cd21215      7 KTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTNIG 84

                           90
                   ....*....|....*....
gi 1207171713  172 AEEVCNGNLKSILGLFFIL 190
Cdd:cd21215     85 AEDIVDGNLKLILGLLWTL 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 1207171713   92 KIYTDWANHYLAKSGcPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGV-SVQGL 170
Cdd:cd00014      2 EELLKWINEVLGEEL-PVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDLF 80

                           90       100
                   ....*....|....*....|...
gi 1207171713  171 SAEE-VCNGNLKSILGLFFILSR 192
Cdd:cd00014     81 EPEDlYEKGNLKKVLGTLWALAL 103

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   92 KIYTDWANHYLAKSGCPrlIKDLTQDIPDGVLLAEIIQIIANEKIEDINScPKSHSQMIENVECCLSFLGARgVSVQGLS 171
Cdd:cd21193     19 KTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNR-GRLRVQKIENVNKALAFLKTK-VRLENIG 94

                           90
                   ....*....|....*
gi 1207171713  172 AEEVCNGNLKSILGL 186
Cdd:cd21193     95 AEDIVDGNPRLILGL 109

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 1207171713   92 KIYTDWANHYLAKSGCPrlIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLS 171
Cdd:cd21227      7 NTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIG 84

                           90
                   ....*....|....*
gi 1207171713  172 AEEVCNGNLKSILGL 186
Cdd:cd21227     85 NEDIVNGNLKLILGL 99

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 1207171713   94 YTDWANHYLAKSGcpRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFL-GARGVSVQGLSA 172
Cdd:cd21311     20 FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLeEDEGIKIVNIDS 97

                           90
                   ....*....|....*...
gi 1207171713  173 EEVCNGNLKSILGLFFIL 190
Cdd:cd21311     98 SDIVDGKLKLILGLIWTL 115

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   92 KIYTDWANHYLAKSGCPrlIKDLTQDIPDGVLLAEIIQIIANEKIEDINScPKSHSQMIENVECCLSFLGARGVSVQGLS 171
Cdd:cd21246     19 KTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTK-GKMRIHCLENVDKALQFLKEQRVHLENMG 95

                           90
                   ....*....|....*....
gi 1207171713  172 AEEVCNGNLKSILGLFFIL 190
Cdd:cd21246     96 SHDIVDGNHRLTLGLIWTI 114

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 1207171713   92 KIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLS 171
Cdd:cd21190      8 KTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVNIN 87

                           90       100
                   ....*....|....*....|..
gi 1207171713  172 AEEVCNGNLKSILGLFFILSRY 193
Cdd:cd21190     88 STDIVDGKPSIVLGLIWTIILY 109

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 1207171713   92 KIYTDWANHYLAKSGcpRLIKDLTQDIPDGVLLAEIIQIIANEKIE-DINSCPKSHSQMIENVECCLSFLGARGVSVQGL 170
Cdd:cd21183      7 NTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADHIKLVNI 84

                           90       100
                   ....*....|....*....|
gi 1207171713  171 SAEEVCNGNLKSILGLFFIL 190
Cdd:cd21183     85 GSGDIVNGNIKLILGLIWTL 104

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 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-2 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 1207171713   92 KIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEDinscPKSHS--QMIENVECCLSFLGARGVSVQG 169
Cdd:cd21242      8 RTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPR----EKGHNvfQCRSNIETALSFLKNKSIKLIN 83

                           90
                   ....*....|....*..
gi 1207171713  170 LSAEEVCNGNLKSILGL 186
Cdd:cd21242     84 IHVPDIIEGKPSIILGL 100

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 1207171713   89 KICKIYTDWANHYLAKSGcpRLIKDLTQDIPDGVLLAEIIQIIANEKI--EDINSCPKSHSQMIENVECCLSFLGARGVS 166
Cdd:cd21222     16 EVKELLLQFVNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGIS 93

                           90       100
                   ....*....|....*....|....*...
gi 1207171713  167 VQGLSAEEVCNGNLKSILG-LFFILSRY 193
Cdd:cd21222     94 TPKIRPEDIVNGDLKSILRvLYSLFSKY 121

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 1207171713   83 REAEESKIckiYTDWANHYLAKSGCPrlIKDLTQDIPDGVLLAEIIQIIANEKIEDINScPKSHSQMIENVECCLSFLGA 162
Cdd:cd21316     50 REAVQKKT---FTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLPKPTK-GRMRIHCLENVDKALQFLKE 123

                           90       100
                   ....*....|....*....|....*...
gi 1207171713  163 RGVSVQGLSAEEVCNGNLKSILGLFFIL 190
Cdd:cd21316    124 QRVHLENMGSHDIVDGNHRLTLGLIWTI 151

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   92 KIYTDWANHYLAKSGCPRLIKDLTQDIPDGVLLAEIIQIIANEKIEdinscPKSHSQM----IENVECCLSFLGARgVSV 167
Cdd:cd21247     23 KTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLP-----RPSRGKMrvhfLENNSKAITFLKTK-VPV 96

                           90       100
                   ....*....|....*....|...
gi 1207171713  168 QGLSAEEVCNGNLKSILGLFFIL 190
Cdd:cd21247     97 KLIGPENIVDGDRTLILGLIWII 119

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   92 KIYTDWANHYLAKSgcPRLIKDLTQDIPDGVLLAEIIQIIANEkiedinSCPKSHSQM----IENVECCLSFLGARGVSV 167
Cdd:cd21235      9 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 80

                           90       100
                   ....*....|....*....|...
gi 1207171713  168 QGLSAEEVCNGNLKSILGLFFIL 190
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTI 103

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 1207171713   94 YTDWANHYLAKSGcpRLIKDLTQDIPDGVLLAEIIQIIANEKI-EDINSCPKSHSQMIENVECCLSFLGARGVSVQGLSA 172
Cdd:cd21309     22 FTRWCNEHLKCVN--KRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99

                           90
                   ....*....|....*...
gi 1207171713  173 EEVCNGNLKSILGLFFIL 190
Cdd:cd21309    100 KAIVDGNLKLILGLVWTL 117

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171713   92 KIYTDWANHYLAKsgCPRLIKDLTQDIPDGVLLAEIIQIIANEKIedinscPKSHSQM----IENVECCLSFLGARGVSV 167
Cdd:cd21237      9 KTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEVLSGVKL------PREKGRMrfhrLQNVQIALDFLKQRQVKL 80

                           90       100
                   ....*....|....*....|...
gi 1207171713  168 QGLSAEEVCNGNLKSILGLFFIL 190
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTI 103

first calponin homology (CH) domain found in dystonin and similar proteins; 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. Dystonin 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 1207171713   92 KIYTDWANHYLAKsgCPRLIKDLTQDIPDGVLLAEIIQIIANEkiedinSCPKSHSQM----IENVECCLSFLGARGVSV 167
Cdd:cd21236     20 KTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEVLSGD------TLPREKGRMrfhrLQNVQIALDYLKRRQVKL 91

                           90       100
                   ....*....|....*....|...
gi 1207171713  168 QGLSAEEVCNGNLKSILGLFFIL 190
Cdd:cd21236     92 VNIRNDDITDGNPKLTLGLIWTI 114