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Conserved domains on  [gi|224493323|sp|B4J8Z9|]
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RecName: Full=UPAR/Ly6 domain-containing protein qvr; AltName: Full=Protein quiver; AltName: Full=Protein sleepless; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFP_LU_ECD_Qvr cd23595
extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar ...
 37-127 8.35e-39

extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar proteins; Quiver (Qvr, also called protein SLEEPLESS) is a glycosylphosphatidylinositol (GPI)-anchored protein required for homeostatic regulation of sleep under normal conditions and after sleep deprivation in Drosophila. It is a bifunctional regulator of excitability and cholinergic synaptic transmission. It is critical for regulating the levels, localization, and activity of the sleep-modulating potassium channel Shaker. Quiver 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: 467124  Cd Length: 90  Bit Score: 127.09  E-value: 8.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  37 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 115
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 224493323 116 GHMCFCEEDMCN 127
Cdd:cd23595   79 GHLCFCEEDLCN 90
 
Name Accession Description Interval E-value
TFP_LU_ECD_Qvr cd23595
extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar ...
 37-127 8.35e-39

extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar proteins; Quiver (Qvr, also called protein SLEEPLESS) is a glycosylphosphatidylinositol (GPI)-anchored protein required for homeostatic regulation of sleep under normal conditions and after sleep deprivation in Drosophila. It is a bifunctional regulator of excitability and cholinergic synaptic transmission. It is critical for regulating the levels, localization, and activity of the sleep-modulating potassium channel Shaker. Quiver 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: 467124  Cd Length: 90  Bit Score: 127.09  E-value: 8.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  37 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 115
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 224493323 116 GHMCFCEEDMCN 127
Cdd:cd23595   79 GHLCFCEEDLCN 90
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 39-127 1.90e-15

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: 67.24  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323   39 IYCYECDSWTDARCKDPFNYTAlprDQPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQinlFMVDHVCMMESSGNGHM 118
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNS---SSIKLVDCDGGCVKIKTKGSGGSTRVTRGCGPELT---EDIKDGCSSSSSGGGGT 74

                          90
                  ....*....|.
gi 224493323  119 --CFCEEDMCN 127
Cdd:pfam17064  75 itCFCNTDLCN 85
 
Name Accession Description Interval E-value
TFP_LU_ECD_Qvr cd23595
extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar ...
 37-127 8.35e-39

extracellular domain (ECD) found in Drosophila melanogaster protein quiver and similar proteins; Quiver (Qvr, also called protein SLEEPLESS) is a glycosylphosphatidylinositol (GPI)-anchored protein required for homeostatic regulation of sleep under normal conditions and after sleep deprivation in Drosophila. It is a bifunctional regulator of excitability and cholinergic synaptic transmission. It is critical for regulating the levels, localization, and activity of the sleep-modulating potassium channel Shaker. Quiver 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: 467124  Cd Length: 90  Bit Score: 127.09  E-value: 8.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  37 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 115
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 224493323 116 GHMCFCEEDMCN 127
Cdd:cd23595   79 GHLCFCEEDLCN 90
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 39-127 1.90e-15

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: 67.24  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323   39 IYCYECDSWTDARCKDPFNYTAlprDQPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQinlFMVDHVCMMESSGNGHM 118
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNS---SSIKLVDCDGGCVKIKTKGSGGSTRVTRGCGPELT---EDIKDGCSSSSSGGGGT 74

                          90
                  ....*....|.
gi 224493323  119 --CFCEEDMCN 127
Cdd:pfam17064  75 itCFCNTDLCN 85
TFP_LU_ECD_Rtv cd23589
extracellular domain (ECD) found in Drosophila melanogaster protein retroactive and similar ...
 41-129 4.37e-06

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: 42.81  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  41 CYECDS-WTDARCKDPFNYTALPRDQPPlmTCNGCCVKMVRHQRSRYE----VVRRMCtSQLQINLFMVDHVCMMESSGN 115
Cdd:cd23589    4 CYVCRSrGELGDCKDPFNRNAGGVEAVP--CASGWCLKIIEGEGSRSDdgdlATERMC-LPRGPPDGKERCSEAGINKKK 80

                         90
                 ....*....|....
gi 224493323 116 GHMCFCEEDMCNSS 129
Cdd:cd23589   81 VFMCFCDGDLCNGA 94
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 38-129 1.28e-03

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: 36.32  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  38 SIYCYECDSWTDARCKDPFNYTALP----RDQPPLMTCNGC----CVKMVRHQRSRYEVVRRmCTSQLQINLFMVDHVCM 109
Cdd:cd23592    2 AIKCWVCRSDYDPRCGDPFDNLTLPitdcNQEKKPHHLPGVkatmCRKMRQKVNGEWRYIRS-CAFLGEPGIGGDERWCL 80

                         90       100
                 ....*....|....*....|....
gi 224493323 110 MES-SGNGHM--CFCE-EDMCNSS 129
Cdd:cd23592   81 ERSgTYNIHIedCTCNsKDGCNAA 104
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
 39-127 3.61e-03

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: 34.77  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224493323  39 IYCYECDSWTDARCkdpfnytalPRDQPPLMTCN---GCCVKMVRHQRSRYEVVRRMCTSQLQINlfMVDHVCMMESSGN 115
Cdd:cd00117    1 LKCYQCNSSNDPNC---------CNSSPTLVTCSspeTFCRKIVGKVGGGETLVIRGCATECECG--CTECCSGTGTSGT 69

                         90
                 ....*....|..
gi 224493323 116 GHMCFCEEDMCN 127
Cdd:cd00117   70 TCTSCCDTDLCN 81
 
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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