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Conserved domains on  [gi|665400242|ref|NP_001286318|]
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quiver, isoform C [Drosophila melanogaster]

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 ...
 34-124 3.84e-38

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: 125.16  E-value: 3.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242  34 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 112
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 665400242 113 GHMCFCEEDMCN 124
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 ...
 34-124 3.84e-38

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: 125.16  E-value: 3.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242  34 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 112
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 665400242 113 GHMCFCEEDMCN 124
Cdd:cd23595   79 GHLCFCEEDLCN 90
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 36-124 1.27e-14

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: 64.93  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242   36 IYCYECDSWTDARCKDPFNYTAlprDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQinlFMVDHVCMMESSGNGHM 115
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNS---SSIKLVDCDGGCVKIKTKGSGGSTRVTRGCGPELT---EDIKDGCSSSSSGGGGT 74

                          90
                  ....*....|.
gi 665400242  116 --CFCEEDMCN 124
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 ...
 34-124 3.84e-38

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: 125.16  E-value: 3.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242  34 RSIYCYECDSWTDARCKDPFNYTALPRdqPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESS-GN 112
Cdd:cd23595    1 DTILCYDCDSRQDPRCGDPFNESHLHE--PPLIKCKGCCVKWVHRKGNGRVRVRRTCSEQLKINYMMIDHVCMTESRsGN 78

                         90
                 ....*....|..
gi 665400242 113 GHMCFCEEDMCN 124
Cdd:cd23595   79 GHLCFCEEDLCN 90
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 36-124 1.27e-14

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: 64.93  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242   36 IYCYECDSWTDARCKDPFNYTAlprDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQinlFMVDHVCMMESSGNGHM 115
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNS---SSIKLVDCDGGCVKIKTKGSGGSTRVTRGCGPELT---EDIKDGCSSSSSGGGGT 74

                          90
                  ....*....|.
gi 665400242  116 --CFCEEDMCN 124
Cdd:pfam17064  75 itCFCNTDLCN 85
TFP_LU_ECD_Rtv cd23589
extracellular domain (ECD) found in Drosophila melanogaster protein retroactive and similar ...
 38-126 2.31e-05

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: 40.89  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242  38 CYECDS-WTDARCKDPFNYTALPRDQPPlmTCNGCCVKMVRHQRSPYE----VVRRMCtSQLQINLFMVDHVCMMESSGN 112
Cdd:cd23589    4 CYVCRSrGELGDCKDPFNRNAGGVEAVP--CASGWCLKIIEGEGSRSDdgdlATERMC-LPRGPPDGKERCSEAGINKKK 80

                         90
                 ....*....|....
gi 665400242 113 GHMCFCEEDMCNSS 126
Cdd:cd23589   81 VFMCFCDGDLCNGA 94
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 35-126 4.76e-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: 34.77  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400242  35 SIYCYECDSWTDARCKDPFNYTALP----RDQPPLMTCNGC----CVKMVRHQRSPYEVVRRmCTSQLQINLFMVDHVCM 106
Cdd:cd23592    2 AIKCWVCRSDYDPRCGDPFDNLTLPitdcNQEKKPHHLPGVkatmCRKMRQKVNGEWRYIRS-CAFLGEPGIGGDERWCL 80

                         90       100
                 ....*....|....*....|....
gi 665400242 107 MES-SGNGHM--CFCE-EDMCNSS 126
Cdd:cd23592   81 ERSgTYNIHIedCTCNsKDGCNAA 104
 
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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