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Conserved domains on  [gi|19920930|ref|NP_609210|]
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uncharacterized protein Dmel_CG7781, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 22-119 2.72e-12

Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for homoeostatic regulation of sleep under normal conditions and following sleep deprivation. It is a novel potassium channel subunit that modulates the Shaker potassium channel which regulates the sleep.


:

Pssm-ID: 435716  Cd Length: 85  Bit Score: 58.77  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930    22 IKCFVCNSHKDANCALDIPPD---NLLKDCDeqyssrgkgipTYCRKITQIIEFSvnslppDSRVIRTCAYQNQT-STNY 97
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNsssIKLVDCD-----------GGCVKIKTKGSGG------STRVTRGCGPELTEdIKDG 63

                          90       100
                  ....*....|....*....|..
gi 19920930    98 CYQRAGFGGRQVVCSCDTDNCN 119
Cdd:pfam17064  64 CSSSSSGGGGTITCFCNTDLCN 85
 
Name Accession Description Interval E-value
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 22-119 2.72e-12

Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for homoeostatic regulation of sleep under normal conditions and following sleep deprivation. It is a novel potassium channel subunit that modulates the Shaker potassium channel which regulates the sleep.


Pssm-ID: 435716  Cd Length: 85  Bit Score: 58.77  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930    22 IKCFVCNSHKDANCALDIPPD---NLLKDCDeqyssrgkgipTYCRKITQIIEFSvnslppDSRVIRTCAYQNQT-STNY 97
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNsssIKLVDCD-----------GGCVKIKTKGSGG------STRVTRGCGPELTEdIKDG 63

                          90       100
                  ....*....|....*....|..
gi 19920930    98 CYQRAGFGGRQVVCSCDTDNCN 119
Cdd:pfam17064  64 CSSSSSGGGGTITCFCNTDLCN 85
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 21-121 5.70e-11

extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in Drosophila melanogaster protein crooked and similar proteins; Crooked (Crok) is a glycosylphosphatidylinositol (GPI)-anchored protein that plays an essential role in septa formation, the membrane accumulation of SJ components and paracellular barrier functions. It required for septate junction (SJ) formation and function in a tissue-autonomous manner. Crooked is specifically required for correct membrane trafficking of Neurexin IV, a central SJ component. Crooked is a member of the Drosophila Ly6 superfamily. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467121  Cd Length: 104  Bit Score: 55.58  E-value: 5.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  21 AIKCFVCNSHKDANCAldIPPDNL---LKDC--DEQYSSRGKGIPTYCRKITQIIEfsvnslpPDSRVIRTCAYQNQ--- 92
Cdd:cd23592   2 AIKCWVCRSDYDPRCG--DPFDNLtlpITDCnqEKKPHHLPGVKATMCRKMRQKVN-------GEWRYIRSCAFLGEpgi 72

                        90       100       110
                ....*....|....*....|....*....|..
gi 19920930  93 -TSTNYCYQRAG-FGGRQVVCSCDT-DNCNGA 121
Cdd:cd23592  73 gGDERWCLERSGtYNIHIEDCTCNSkDGCNAA 104
 
Name Accession Description Interval E-value
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 22-119 2.72e-12

Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for homoeostatic regulation of sleep under normal conditions and following sleep deprivation. It is a novel potassium channel subunit that modulates the Shaker potassium channel which regulates the sleep.


Pssm-ID: 435716  Cd Length: 85  Bit Score: 58.77  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930    22 IKCFVCNSHKDANCALDIPPD---NLLKDCDeqyssrgkgipTYCRKITQIIEFSvnslppDSRVIRTCAYQNQT-STNY 97
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNsssIKLVDCD-----------GGCVKIKTKGSGG------STRVTRGCGPELTEdIKDG 63

                          90       100
                  ....*....|....*....|..
gi 19920930    98 CYQRAGFGGRQVVCSCDTDNCN 119
Cdd:pfam17064  64 CSSSSSGGGGTITCFCNTDLCN 85
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 21-121 5.70e-11

extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in Drosophila melanogaster protein crooked and similar proteins; Crooked (Crok) is a glycosylphosphatidylinositol (GPI)-anchored protein that plays an essential role in septa formation, the membrane accumulation of SJ components and paracellular barrier functions. It required for septate junction (SJ) formation and function in a tissue-autonomous manner. Crooked is specifically required for correct membrane trafficking of Neurexin IV, a central SJ component. Crooked is a member of the Drosophila Ly6 superfamily. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467121  Cd Length: 104  Bit Score: 55.58  E-value: 5.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  21 AIKCFVCNSHKDANCAldIPPDNL---LKDC--DEQYSSRGKGIPTYCRKITQIIEfsvnslpPDSRVIRTCAYQNQ--- 92
Cdd:cd23592   2 AIKCWVCRSDYDPRCG--DPFDNLtlpITDCnqEKKPHHLPGVKATMCRKMRQKVN-------GEWRYIRSCAFLGEpgi 72

                        90       100       110
                ....*....|....*....|....*....|..
gi 19920930  93 -TSTNYCYQRAG-FGGRQVVCSCDT-DNCNGA 121
Cdd:cd23592  73 gGDERWCLERSGtYNIHIEDCTCNSkDGCNAA 104
TFP_LU_ECD_Bou cd23590
extracellular domain (ECD) found in Drosophila melanogaster protein boudin and similar ...
 22-121 2.50e-09

extracellular domain (ECD) found in Drosophila melanogaster protein boudin and similar proteins; Boudin (Bou) is a glycosylphosphatidylinositol (GPI)-anchored membrane protein secreted extracellularly. It is a member of the Drosophila Ly6 superfamily. Boudin plays an essential role in the organization of septate junctions (SJs) and the maintenance of paracellular barriers in Drosophila epithelia and chordotonal organs. It is required for SJ formation in a non-cell-autonomous fashion. Boudin contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467119  Cd Length: 88  Bit Score: 50.90  E-value: 2.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  22 IKCFVCNSHKDANCALDIPPDNLLKDCDEQYSSrgkgiptYCRKITQIIEFSVnslppdSRVIRTCAYQNqtSTNYC-YQ 100
Cdd:cd23590   1 LKCYQCDSEKDPDCEENPPPDLEPTECPGDDAK-------YCIKTTGYYGGGL------IGTRRFCSSRD--MGNYCtYV 65

                        90       100
                ....*....|....*....|...
gi 19920930 101 RAGFGGRQVVC--SCDTDNCNGA 121
Cdd:cd23590  66 TRPDGRTYRACiyTCSTDGCNSA 88
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
 22-119 6.73e-09

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


Pssm-ID: 467060  Cd Length: 81  Bit Score: 49.79  E-value: 6.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  22 IKCFVCNSHKDANCALDIPPdnlLKDCDEQYssrgkgipTYCRKITQIIEfsvnslPPDSRVIRTCAYQNQTSTNYCYQR 101
Cdd:cd00117   1 LKCYQCNSSNDPNCCNSSPT---LVTCSSPE--------TFCRKIVGKVG------GGETLVIRGCATECECGCTECCSG 63

                        90
                ....*....|....*...
gi 19920930 102 AGFGGRQVVCSCDTDNCN 119
Cdd:cd00117  64 TGTSGTTCTSCCDTDLCN 81
TFP_LU_ECD_Twit cd23593
extracellular domain (ECD) found in Drosophila melanogaster Target of wit (Twit) and similar ...
 21-121 2.88e-08

extracellular domain (ECD) found in Drosophila melanogaster Target of wit (Twit) and similar proteins; Twit is a GPI-anchored membrane ligand of the Ly6 family that participates in retrograde signalling as a downstream target of the bone morphogenetic protein (BMP) pathway receptor encoded by Wishful thinking (Wit). It acts in neurons, regulating spontaneous neurotransmitter release during the maturation of larval neuromuscular junctions. Twit contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467122  Cd Length: 101  Bit Score: 48.56  E-value: 2.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  21 AIKCFVCNSHKDANCALDIPPDN---LLKDCDEQ----YSSRGKGIptyCRKITQIiefsVNSLPpdsRVIRTCAYQNQT 93
Cdd:cd23593   1 ALRCWSCSSDTDPFCGDPFNTTEnhfHLTDCDRTaspsYYLNERPV---CRKIVQR----VNGEL---VVIRSCAWENED 70

                        90       100       110
                ....*....|....*....|....*....|.
gi 19920930  94 ST-NYC-YQRAGFGGRQVVCS-CDTDNCNGA 121
Cdd:cd23593  71 DVdGPCsNTSTGSYIKIESCEtCSTDGCNSA 101
TFP_LU_ECD_Rtv cd23589
extracellular domain (ECD) found in Drosophila melanogaster protein retroactive and similar ...
 23-121 4.78e-03

extracellular domain (ECD) found in Drosophila melanogaster protein retroactive and similar proteins; Retroactive (Rtv) is a membrane-anchored extracellular protein required for cuticle organization in the larva of Drosophila melanogaster. It is a member of the Drosophila Ly6 superfamily. Retroactive contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467118  Cd Length: 94  Bit Score: 34.34  E-value: 4.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920930  23 KCFVCNSH-KDANCAldIPPDNLLKDCDEQYSSRGkgiptYCRKITQIIEFsvNSLPPDSRVIRTCAYQN-QTSTNYCYQ 100
Cdd:cd23589   3 RCYVCRSRgELGDCK--DPFNRNAGGVEAVPCASG-----WCLKIIEGEGS--RSDDGDLATERMCLPRGpPDGKERCSE 73

                        90       100
                ....*....|....*....|.
gi 19920930 101 RAGFGGRQVVCSCDTDNCNGA 121
Cdd:cd23589  74 AGINKKKVFMCFCDGDLCNGA 94
 
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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