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Conserved domains on  [gi|45551089|ref|NP_725172|]
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dystrobrevin, isoform C [Drosophila melanogaster]

Protein Classification

EFh_DTN and ZZ_dystrophin domain-containing protein( domain architecture ID 11610980)

EFh_DTN and ZZ_dystrophin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 3.66e-100

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).


:

Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 301.85  E-value: 3.66e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATL 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 45551089 214 M 214
Cdd:cd16244 161 M 161
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 2.91e-27

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: 103.97  E-value: 2.91e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 45551089 241 TVCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDHEVKEY 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 439-523 9.58e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0542:

Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 439 DNSRAQRELIAQLESKNKEIMREIARLRRQQETEQmapenpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMR 518
Cdd:COG0542 433 EQDEASFERLAELRDELAELEEELEALKARWEAEK------ELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506


                ....*
gi 45551089 519 MLKNQ 523
Cdd:COG0542 507 LLREE 511
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 3.66e-100

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).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 301.85  E-value: 3.66e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATL 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 45551089 214 M 214
Cdd:cd16244 161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 16-140 4.54e-61

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: 198.92  E-value: 4.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089    16 VAILQDLrlQTFDSIRFASYRTASKLRYIQKSTNLHLVDIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 45551089    96 LPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIKVALATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 2.91e-27

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: 103.97  E-value: 2.91e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 45551089 241 TVCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDHEVKEY 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 3.17e-12

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: 61.30  E-value: 3.17e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45551089    237 IVHPTVCSVCHKEnFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQ 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 243-281 2.25e-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: 44.78  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 45551089   243 CSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSlNHQ 281
Cdd:pfam00569   7 CNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG-NHQ 44
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 439-523 9.58e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 439 DNSRAQRELIAQLESKNKEIMREIARLRRQQETEQmapenpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMR 518
Cdd:COG0542 433 EQDEASFERLAELRDELAELEEELEALKARWEAEK------ELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506


                ....*
gi 45551089 519 MLKNQ 523
Cdd:COG0542 507 LLREE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-522 1.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089    412 IARYAARLAQENRAPSNLPDNATPIGTDNSRAQR-ELIAQLESKNKEIMREIARLRRQQETEQMAPENPALINElrALRQ 490
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQ--ALDA 479

                           90       100       110
                   ....*....|....*....|....*....|..
gi 45551089    491 RKGELEgHLGALQDSRRQLMEQLEGLMRMLKN 522
Cdd:TIGR02168  480 AERELA-QLQARLDSLERLQENLEGFSEGVKA 510
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 446-522 2.67e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551089   446 ELIAQLESKNKEIMREIARLrrQQETEQMAPENPALINELRALRQrkgELEghlgALQDSRRQLMEQLEGLMRMLKN 522
Cdd:pfam06005   4 ELLEQLETKIQAAVDTIALL--QMENEELKEENEELKEEANELEE---ENQ----QLKQERNQWQERIRGLLGKLDE 71
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
442-521 3.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  442 RAQRELIAQLESKNKEIMREIARLRRQQE-TEQMAPENPALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRML 520
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEkLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275


                 .
gi 45551089  521 K 521
Cdd:PRK03918 276 E 276
 
Name Accession Description Interval E-value
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
 54-214 3.66e-100

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).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 301.85  E-value: 3.66e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd16244   1 DIWNVIEAFRENGLNTLDPTTELSVSRLETLLSSIYYQLNKRLPTTHQIDVDQSISLLLNWLLAAYDPEATGRLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATL 213
Cdd:cd16244  81 VALSTLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYNESAARSCFPGQSKVTVNDFLDVM 160


                .
gi 45551089 214 M 214
Cdd:cd16244 161 M 161
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
 54-214 4.14e-64

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).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 208.21  E-value: 4.14e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd16249   1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATL 213
Cdd:cd16249  81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTL 160


                .
gi 45551089 214 M 214
Cdd:cd16249 161 M 161
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 16-140 4.54e-61

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: 198.92  E-value: 4.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089    16 VAILQDLrlQTFDSIRFASYRTASKLRYIQKSTNLHLVDIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKR 95
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 45551089    96 LPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIKVALATMC 140
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
 54-214 1.03e-60

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).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 199.48  E-value: 1.03e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd16250   1 DIWNMIEAFRDNGLNTLDHSTEISVSRLETIISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATL 213
Cdd:cd16250  81 AMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCFPQQKKIMLNMFLDTM 160


                .
gi 45551089 214 M 214
Cdd:cd16250 161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 54-214 4.44e-37

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: 135.48  E-value: 4.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQsEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSkaGLLLNWLLAAYTSDNSGKIRVFSIK 133
Cdd:cd15901   1 DLSTVLSVFDRHGLSGSQDS-VLDCEELETILTELYIKLNKRRPDLIDVPRAS--DLLLNWLLNLYDRNRTGCIRLLSVK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 134 VALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF--HYKEGLEEEIFPAENKVTV---ND 208
Cdd:cd15901  78 IALITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFggHNVEAAVESCFQLARSRVGvseDT 157


                ....*.
gi 45551089 209 FMATLM 214
Cdd:cd15901 158 FLSWLL 163
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
 144-232 9.00e-36

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: 462669  Cd Length: 90  Bit Score: 129.34  E-value: 9.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089   144 LVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPA---ENKVTVNDFMATLMSEpgPS 220
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGGIEPSVRSCFEQvggKPKITLNHFLDWLMSE--PQ 78

                          90
                  ....*....|..
gi 45551089   221 CLVWLPLVHRLA 232
Cdd:pfam09069  79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 241-289 2.91e-27

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: 103.97  E-value: 2.91e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 45551089 241 TVCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDHEVKEY 289
Cdd:cd02334   1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 54-187 9.72e-23

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.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 95.00  E-value: 9.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  54 DIWNVIEAFRENGLNTLEPQSeVSVARLETLVSSLYHNLNKRLPTAQQVP--VDskagLLLNWLLAAYTSDNSGKIRVFS 131
Cdd:cd16242   1 SLSTAIEAFDQHGLRAQNDKL-IDVPDMITCLTTIYEALEEEHPTLVNVPlcVD----LCLNWLLNVYDSGRSGKIRVLS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 45551089 132 IKVALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF 187
Cdd:cd16242  76 FKVGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAF 131
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
 58-198 2.26e-12

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: 65.39  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  58 VIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRlpTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIKVALA 137
Cdd:cd16245   5 IMGVFDRHQLSNSENNLCLPPDELEAVLHDIYFAAEKL--GNFNIDVDLATELLANLFLNVFDPERKKSISVLELKVFLT 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551089 138 TMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF--HYKEGLEEEIF 198
Cdd:cd16245  83 LLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFgsHLIELAVEQCF 145
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 237-281 3.17e-12

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: 61.30  E-value: 3.17e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45551089    237 IVHPTVCSVCHKEnFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQ 281
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
 60-187 5.33e-12

EF-hand-like motif found in dystrophin; 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. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 64.28  E-value: 5.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  60 EAFRENGLNtlEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVP--VDskagLLLNWLLAAYTSDNSGKIRVFSIKVALA 137
Cdd:cd16246   7 EALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPlcVD----MCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45551089 138 TMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF 187
Cdd:cd16246  81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASF 130
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
 60-187 1.03e-11

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue 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. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 63.28  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  60 EAFRENglnTLEPQSEV-SVARLETLVSSLYHNLNKRLPTAQQVP--VDskagLLLNWLLAAYTSDNSGKIRVFSIKVAL 136
Cdd:cd16248   7 EIFTEH---ELQMSERVmDVVEVIHCLTALYERLEEERGILVNVPlcVD----MCLNWLLNVYDSGRNGKIRVLSFKTGI 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 45551089 137 ATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF 187
Cdd:cd16248  80 VCLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAF 130
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
 60-187 1.47e-11

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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 62.99  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  60 EAFRENGLNtlEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVP--VDskagLLLNWLLAAYTSDNSGKIRVFSIKVALA 137
Cdd:cd16247   7 SVFKQHKLT--QNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPlcVD----MCLNWLLNVYDTGRTGKIRVLSLKIGLM 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45551089 138 TMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTF 187
Cdd:cd16247  81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAF 130
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 243-284 1.15e-10

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: 56.97  E-value: 1.15e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 45551089 243 CSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDH 284
Cdd:cd02338   3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDH 44
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 242-284 9.57e-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: 48.83  E-value: 9.57e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 45551089 242 VCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDH 284
Cdd:cd02335   2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 243-284 9.49e-07

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: 46.04  E-value: 9.49e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 45551089 243 CSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDH 284
Cdd:cd02345   3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 241-280 1.41e-06

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: 45.14  E-value: 1.41e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 45551089 241 TVCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNH 280
Cdd:cd02339   1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEH 40
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 242-289 1.69e-06

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: 45.12  E-value: 1.69e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 45551089 242 VCSVChKENFTGFRYRCQRCHAYQLCQECFwhGKTSLNHQNDHEVKEY 289
Cdd:cd02249   2 SCDGC-LKPIVGVRYHCLVCEDFDLCSSCY--AKGKKGHPPDHSFTEI 46
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 243-281 2.25e-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: 44.78  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 45551089   243 CSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSlNHQ 281
Cdd:pfam00569   7 CNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGG-NHQ 44
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 242-270 1.37e-04

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: 39.55  E-value: 1.37e-04
                        10        20
                ....*....|....*....|....*....
gi 45551089 242 VCSVCHKENfTGFRYRCQRCHAYQLCQEC 270
Cdd:cd02340   2 ICDGCQGPI-VGVRYKCLVCPDYDLCESC 29
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 255-286 3.48e-04

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 38.84  E-value: 3.48e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 45551089 255 RYRCQRCHAYQLCQECFWHGKTSLNHQNDHEV 286
Cdd:cd02343  14 RYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 439-523 9.58e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 439 DNSRAQRELIAQLESKNKEIMREIARLRRQQETEQmapenpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMR 518
Cdd:COG0542 433 EQDEASFERLAELRDELAELEEELEALKARWEAEK------ELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506


                ....*
gi 45551089 519 MLKNQ 523
Cdd:COG0542 507 LLREE 511
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 243-280 1.93e-03

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: 36.41  E-value: 1.93e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 45551089 243 CSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNH 280
Cdd:cd02344   3 CDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 412-522 1.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089    412 IARYAARLAQENRAPSNLPDNATPIGTDNSRAQR-ELIAQLESKNKEIMREIARLRRQQETEQMAPENPALINElrALRQ 490
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQ--ALDA 479

                           90       100       110
                   ....*....|....*....|....*....|..
gi 45551089    491 RKGELEgHLGALQDSRRQLMEQLEGLMRMLKN 522
Cdd:TIGR02168  480 AERELA-QLQARLDSLERLQENLEGFSEGVKA 510
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
442-524 2.08e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 442 RAQRELIAQLESKNKEIMREIARLRRQQETEQMAPENPA------LINELRALRQRKGELEGHLGALQDSRRQLMEQLEG 515
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                ....*....
gi 45551089 516 LMRMLKNQQ 524
Cdd:COG4717 232 LENELEAAA 240
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 442-546 2.54e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 442 RAQRELIAQLESKNKEIMREIARLRRQQETEQMAPEnpALINE----LRALRQRKGELEGHLGALQDSRRQLMEQLEGLM 517
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALE--ALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLE 233

                        90       100
                ....*....|....*....|....*....
gi 45551089 518 RMLKNQQTASPrSTPNSSPRSGKSPPMPG 546
Cdd:COG4942 234 AEAAAAAERTP-AAGFAALKGKLPWPVSG 261
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 446-522 2.67e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551089   446 ELIAQLESKNKEIMREIARLrrQQETEQMAPENPALINELRALRQrkgELEghlgALQDSRRQLMEQLEGLMRMLKN 522
Cdd:pfam06005   4 ELLEQLETKIQAAVDTIALL--QMENEELKEENEELKEEANELEE---ENQ----QLKQERNQWQERIRGLLGKLDE 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 446-511 3.39e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551089    446 ELIAQLESKNKEIMREIARLRRqqETEQMAPENPALINELRALRQRKGELEGHLGALQDSRRQLME 511
Cdd:TIGR02168  958 ALENKIEDDEEEARRRLKRLEN--KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
442-521 3.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089  442 RAQRELIAQLESKNKEIMREIARLRRQQE-TEQMAPENPALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRML 520
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEkLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275


                 .
gi 45551089  521 K 521
Cdd:PRK03918 276 E 276
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
442-516 4.73e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 442 RAQRELIAQLESKN---KEIMREIARLRRQQETEQMAPENP-ALINELRALRQRKGELE------GHLGALQDSRRQLME 511
Cdd:COG1340  95 DELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEkELVEKIKELEKELEKAKkaleknEKLKELRAELKELRK 174


                ....*
gi 45551089 512 QLEGL 516
Cdd:COG1340 175 EAEEI 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-524 4.73e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089    443 AQRELIAQLESKNKEIMREIARLRRQQETEQmapenpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRMLKN 522
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELE------ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940


                   ..
gi 45551089    523 QQ 524
Cdd:TIGR02168  941 LQ 942
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 442-536 6.51e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 442 RAQRELIAQLESKNKEIMREIARLRRQQEteqmapenpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRMLK 521
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIA---------ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107

                        90
                ....*....|....*
gi 45551089 522 NQQTASPRSTPNSSP 536
Cdd:COG4942 108 ELLRALYRLGRQPPL 122
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 385-526 7.06e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 385 LDSASGTAGTTMSRVAAASANDEEHRLIARYAARLAQENRAPSNLPD---NATPIGTDNSRAQreLIAQLESKNKEIMRE 461
Cdd:COG3883  60 LEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllGSESFSDFLDRLS--ALSKIADADADLLEE 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551089 462 IARLRRQQETEQMAPEnpALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRMLKNQQTA 526
Cdd:COG3883 138 LKADKAELEAKKAELE--AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
441-525 8.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 8.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551089 441 SRAQRELIA---QLESKNKEIMREIARLR-RQQETEQMAPENPALINELRALRQRKGELEGHL-------GALQDSRRQL 509
Cdd:COG4372  55 EQAREELEQleeELEQARSELEQLEEELEeLNEQLQAAQAELAQAQEELESLQEEAEELQEELeelqkerQDLEQQRKQL 134

                        90
                ....*....|....*.
gi 45551089 510 MEQLEGLMRMLKNQQT 525
Cdd:COG4372 135 EAQIAELQSEIAEREE 150
 
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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