Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720434525 460 TKCSICRQCPIKGFRYRSLKQFNVDICQTCFLTGRASKGNKLHYPIMEY 508
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.

                          10        20
                  ....*....|....*....|....*....
gi 1720434525 209 PWERAISPNKVPYYINHQAQTTCWDHPKM 237
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 238 TELYQTLADLNNIKFSAYRTAMKLRRVQKALRLDLVTLTTALEIFNEHDLQASE--HVMDVVEVIHCLTALYERLEEER- 314
Cdd:pfam09068   1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLEndLLLSVSELEALLSSIYFALNKRKp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720434525 315 -GILVNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGIACLC 356
Cdd:pfam09068  81 tTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720434525  456 VKHQTKCSICRQcPIKGFRYRSLKQFNVDICQTCFLTGRASKGNK 500
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.

                          10        20
                  ....*....|....*....|....*....
gi 1720434525 209 PWERAISPNKVPYYINHQAQTTCWDHPKM 237
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525  83 EHLLEIQGAMEELSSTLTQAEGVrATWEPIGDLfIDSLPEHIQAIKLFKEEFSPVKDGVKLVNDLAHQLAISDVHLSMEN 162
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEAL-LSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78

                          90       100
                  ....*....|....*....|....*..
gi 1720434525 163 SRALEQINIRWKQLQVSVAERLKQLQD 189
Cdd:pfam00435  79 QERLEELNERWEQLLELAAERKQKLEE 105

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.

                           10        20
                   ....*....|....*....|....*....
gi 1720434525  209 PWERAISPNKVPYYINHQAQTTCWDHPKM 237
Cdd:smart00456   5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 274 TLTTALEIFNEHDLQA-SEHVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGI 352
Cdd:cd16242     1 SLSTAIEAFDQHGLRAqNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 353 ACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSNVEPSVRSCFRFSTGKPVIEASQFLE 432
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                  ...
gi 1720434525 433 WVN 435
Cdd:cd16242   161 WLK 163

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has 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, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 275 LTTALEIFNEHDLQASEHVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGIAC 354
Cdd:cd16247     2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 355 LCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSNVEPSVRSCFRFSTGKPVIEASQFLEWV 434
Cdd:cd16247    82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 274 TLTTALEIFNEHDL-QASEHVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGI 352
Cdd:cd15901     1 DLSTVLSVFDRHGLsGSQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 353 ACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSNVEPSVRSCFRFSTGKPVIEASQFLE 432
Cdd:cd15901    81 ITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLS 160

                  ...
gi 1720434525 433 WVN 435
Cdd:cd15901   161 WLL 163

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720434525 460 TKCSICRQCPIKGFRYRSLKQFNVDICQTCFLTGRASKGNKLHYPIMEY 508
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins 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, dystrobrevins contain one or two syntrophin binding sites (SBSs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 279 LEIFNEHDLQASEH--VMDVVEVIHCLTALY----ERLEEERGIlvNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGI 352
Cdd:cd16244     6 IEAFRENGLNTLDPttELSVSRLETLLSSIYyqlnKRLPTTHQI--DVDQSISLLLNWLLAAYDPEATGRLTVFSVKVAL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720434525 353 ACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSnvEPSVRSCF 416
Cdd:cd16244    84 STLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCF 145

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has 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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 318 VNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGIACLCGTEVKEKLQYLFSQVANSG-----SQCDQrhlgaLLHEAIQ 392
Cdd:cd16249    49 INVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNgvmvyGRYDQ-----FLREVLK 123

                          90       100
                  ....*....|....*....|....
gi 1720434525 393 VPRQLGEVAAFGGSnvEPSVRSCF 416
Cdd:cd16249   124 LPTAVFEGPSFGYT--EQSARSCF 145

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has 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, beta-dystrobrevin contain two syntrophin binding sites (SBSs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525 279 LEIFNEHDLQASEHVMDV----VEVIhcLTALYERLEEERGIL--VNVPLCVDMSLNWLLNVFDSGRSGKMRALSFKTGI 352
Cdd:cd16250     6 IEAFRDNGLNTLDHSTEIsvsrLETI--ISSIYYQLNKRLPSThqISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAML 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720434525 353 ACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQVPRQLGEVAAFGGSnvEPSVRSCF 416
Cdd:cd16250    84 ATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYT--EHSVRTCF 145

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525   1 MEEVKSKGPYISSVLESAQAFLSQHPFEEleesqseskdTSPRQRIQNLSrfvwkqatvasELWEKLTARCVDQHRHIEH 80
Cdd:cd00176    46 EAELAAHEERVEALNELGEQLIEEGHPDA----------EEIQERLEELN-----------QRWEELRELAEERRQRLEE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525  81 TLEHLLEIQgAMEELSSTLTQAEGVRATWEPIGDLfiDSLPEHIQAIKLFKEEFSPVKDGVKLVNDLAHQLaISDVHLSM 160
Cdd:cd00176   105 ALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEEL-LEEGHPDA 180

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720434525 161 ENSRA--LEQINIRWKQLQVSVAERLKQLQDAH 191
Cdd:cd00176   181 DEEIEekLEELNERWEELLELAEERQKKLEEAL 213

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720434525 457 KHQTKCSICRQCPIKGFRYRSLKQFNVDICQTCFLT 492
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT 37

Spectrin repeats;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720434525   91 AMEELSSTLTQAEGVRATWEPIGDLfiDSLPEHIQAIKLFKEEFSPVKDGVKLVNDLAHQLAISDVHLSMENSRALEQIN 170
Cdd:smart00150   6 DADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEELN 83

                           90
                   ....*....|....*...
gi 1720434525  171 IRWKQLQVSVAERLKQLQ 188
Cdd:smart00150  84 ERWEELKELAEERRQKLE 101

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.

                          10        20
                  ....*....|....*....|....*..
gi 1720434525 209 PWERAISPNKVPYYINHQAQTTCWDHP 235
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720434525 462 CSICRQCPIKGFRYRSLKQFNVDICQTCFLTGRASKGNKLHY 503
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44