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Conserved domains on  [gi|1830868797|ref|XP_001355193|]
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dystrotelin [Drosophila pseudoobscura]

Protein Classification

EFh_DMD_DYTN_DTN and ZZ_dah domain-containing protein( domain architecture ID 11655114)

EFh_DMD_DYTN_DTN and ZZ_dah domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_DMD_DYTN_DTN super family cl07621
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 84-257 5.87e-63

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.


The actual alignment was detected with superfamily member cd16245:

Pssm-ID: 352774 [Multi-domain]  Cd Length: 164  Bit Score: 205.99  E-value: 5.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  84 PYKLVLAILERHGMpasSGSNLNLMVPPFQLTSLLHDIYFACEKLGHFTktssYTLETATALLANFFWNIYDPQRRHSIS 163
Cdd:cd16245     1 PLKLIMGVFDRHQL---SNSENNLCLPPDELEAVLHDIYFAAEKLGNFN----IDVDLATELLANLFLNVFDPERKKSIS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797 164 LLEIRVTFLLLCKlYSSEHMVGDFFGLLAEsRSQSVSRFAFEQLLNTLSKLLSYLGEAKAYGVHNLPLMMEQCFARCPHn 243
Cdd:cd16245    74 VLELKVFLTLLCG-SSLQEKYLYLFQLLAD-HNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPG- 150

                         170
                  ....*....|....
gi 1830868797 244 ASGLGEQQFHGLWT 257
Cdd:cd16245   151 LVGLTEYQFIGWWT 164
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 286-334 5.09e-19

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.


:

Pssm-ID: 239085  Cd Length: 49  Bit Score: 80.71  E-value: 5.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1830868797 286 NPCAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASHRMCEV 334
Cdd:cd02345     1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49
 
Name Accession Description Interval E-value
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 84-257 5.87e-63

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 205.99  E-value: 5.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  84 PYKLVLAILERHGMpasSGSNLNLMVPPFQLTSLLHDIYFACEKLGHFTktssYTLETATALLANFFWNIYDPQRRHSIS 163
Cdd:cd16245     1 PLKLIMGVFDRHQL---SNSENNLCLPPDELEAVLHDIYFAAEKLGNFN----IDVDLATELLANLFLNVFDPERKKSIS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797 164 LLEIRVTFLLLCKlYSSEHMVGDFFGLLAEsRSQSVSRFAFEQLLNTLSKLLSYLGEAKAYGVHNLPLMMEQCFARCPHn 243
Cdd:cd16245    74 VLELKVFLTLLCG-SSLQEKYLYLFQLLAD-HNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPG- 150

                         170
                  ....*....|....
gi 1830868797 244 ASGLGEQQFHGLWT 257
Cdd:cd16245   151 LVGLTEYQFIGWWT 164
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 49-175 1.08e-38

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.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 138.82  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  49 IMEKLQvDYGKYKYTVYRCASKFVALQKIFHTSKIPYKLVLAILERHGMpasSGSNLNLMVPPFQLTSLLHDIYFACEKl 128
Cdd:pfam09068   3 LMQELQ-DFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGL---NSLENDLLLSVSELEALLSSIYFALNK- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1830868797 129 gHFTKTSSYTLETATALLANFFWNIYDPQRRHSISLLEIRVTFLLLC 175
Cdd:pfam09068  78 -RKPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 286-334 5.09e-19

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.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 80.71  E-value: 5.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1830868797 286 NPCAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASHRMCEV 334
Cdd:cd02345     1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 284-326 6.21e-13

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.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 63.23  E-value: 6.21e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1830868797  284 HSNPCAGCRlEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHE 326
Cdd:smart00291   3 HSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 288-331 4.74e-06

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.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 44.01  E-value: 4.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGrheasHRM 331
Cdd:pfam00569   7 CNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
288-329 1.09e-03

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.98  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASH 329
Cdd:COG5114     8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49
 
Name Accession Description Interval E-value
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 84-257 5.87e-63

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 205.99  E-value: 5.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  84 PYKLVLAILERHGMpasSGSNLNLMVPPFQLTSLLHDIYFACEKLGHFTktssYTLETATALLANFFWNIYDPQRRHSIS 163
Cdd:cd16245     1 PLKLIMGVFDRHQL---SNSENNLCLPPDELEAVLHDIYFAAEKLGNFN----IDVDLATELLANLFLNVFDPERKKSIS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797 164 LLEIRVTFLLLCKlYSSEHMVGDFFGLLAEsRSQSVSRFAFEQLLNTLSKLLSYLGEAKAYGVHNLPLMMEQCFARCPHn 243
Cdd:cd16245    74 VLELKVFLTLLCG-SSLQEKYLYLFQLLAD-HNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPG- 150

                         170
                  ....*....|....
gi 1830868797 244 ASGLGEQQFHGLWT 257
Cdd:cd16245   151 LVGLTEYQFIGWWT 164
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 84-257 1.32e-41

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.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 148.57  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  84 PYKLVLAILERHGMPASSGSnlnlMVPPFQLTSLLHDIYFACEKLGHFTktssYTLETATALLANFFWNIYDPQRRHSIS 163
Cdd:cd15901     1 DLSTVLSVFDRHGLSGSQDS----VLDCEELETILTELYIKLNKRRPDL----IDVPRASDLLLNWLLNLYDRNRTGCIR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797 164 LLEIRVTFLLLCKlYSSEHMVGDFFGLLAESrSQSVSRFAFEQLLNTLSKLLSYLGEAKAYGVHNLPLMMEQCFARCPHn 243
Cdd:cd15901    73 LLSVKIALITLCA-ASLLDKYRYLFGQLADS-SGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARS- 149

                         170
                  ....*....|....
gi 1830868797 244 ASGLGEQQFHGLWT 257
Cdd:cd15901   150 RVGVSEDTFLSWLL 163
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 49-175 1.08e-38

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.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 138.82  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1830868797  49 IMEKLQvDYGKYKYTVYRCASKFVALQKIFHTSKIPYKLVLAILERHGMpasSGSNLNLMVPPFQLTSLLHDIYFACEKl 128
Cdd:pfam09068   3 LMQELQ-DFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGL---NSLENDLLLSVSELEALLSSIYFALNK- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1830868797 129 gHFTKTSSYTLETATALLANFFWNIYDPQRRHSISLLEIRVTFLLLC 175
Cdd:pfam09068  78 -RKPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 286-334 5.09e-19

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.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 80.71  E-value: 5.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1830868797 286 NPCAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASHRMCEV 334
Cdd:cd02345     1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 284-326 6.21e-13

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.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 63.23  E-value: 6.21e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1830868797  284 HSNPCAGCRlEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHE 326
Cdd:smart00291   3 HSYSCDTCG-KPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 288-333 5.87e-12

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 60.53  E-value: 5.87e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1830868797 288 CAGCrLEHIIGIRFKCQVCRDLSLCLPCFAAGFvgGRHEASHRMCE 333
Cdd:cd02249     3 CDGC-LKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTE 45
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 287-329 2.68e-08

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 50.37  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1830868797 287 PCAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASH 329
Cdd:cd02335     2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 288-330 2.45e-07

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 47.45  E-value: 2.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAagfvGGRHEASHR 330
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYH----GDKHDLEHR 41
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 287-331 3.30e-07

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 47.34  E-value: 3.30e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1830868797 287 PCAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASHRM 331
Cdd:cd02338     2 SCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 288-333 9.45e-07

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.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 45.81  E-value: 9.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASHRMCE 333
Cdd:cd02334     3 CNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKE 48
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 288-331 4.74e-06

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.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 44.01  E-value: 4.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGrheasHRM 331
Cdd:pfam00569   7 CNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN-----HQM 45
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 288-331 1.72e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 42.25  E-value: 1.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1830868797 288 CAGCrLEHIIGIRFKCQVCRDLSLCLPCFAagfvGGRHeASHRM 331
Cdd:cd02340     3 CDGC-QGPIVGVRYKCLVCPDYDLCESCEA----KGVH-PEHAM 40
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 288-325 2.32e-04

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 39.10  E-value: 2.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRH 325
Cdd:cd02344     3 CDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
288-329 1.09e-03

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 41.98  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1830868797 288 CAGCRLEHIIGIRFKCQVCRDLSLCLPCFAAGFVGGRHEASH 329
Cdd:COG5114     8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 288-331 6.88e-03

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 35.10  E-value: 6.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1830868797 288 CAGCRLEHIIGIRFKCQVC--RDLSLCLPCFAAgfvGGRHEASHRM 331
Cdd:cd02341     3 CDSCGIEPIPGTRYHCSECddGDFDLCQDCVVK---GESHQEDHWL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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