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Conserved domains on  [gi|2296749787|ref|XP_050455811|]
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uncharacterized protein LOC126853786 isoform X2 [Cataglyphis hispanica]

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 ...
 29-123 2.91e-11

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: 56.07  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  29 IQCYQCNSLTNSLCSELIPPDT---MKIDCldlrggkkYTMCRKITQTIEISayelqpNTRIIRGCGWDESSY-KNMCYK 104
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNSssiKLVDC--------DGGCVKIKTKGSGG------STRVTRGCGPELTEDiKDGCSS 66

                          90
                  ....*....|....*....
gi 2296749787 105 RNGFGAKQEVCSCSNDYCN 123
Cdd:pfam17064  67 SSSGGGGTITCFCNTDLCN 85
 
Name Accession Description Interval E-value
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 29-123 2.91e-11

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: 56.07  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  29 IQCYQCNSLTNSLCSELIPPDT---MKIDCldlrggkkYTMCRKITQTIEISayelqpNTRIIRGCGWDESSY-KNMCYK 104
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNSssiKLVDC--------DGGCVKIKTKGSGG------STRVTRGCGPELTEDiKDGCSS 66

                          90
                  ....*....|....*....
gi 2296749787 105 RNGFGAKQEVCSCSNDYCN 123
Cdd:pfam17064  67 SSSGGGGTITCFCNTDLCN 85
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 28-125 6.09e-08

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: 47.87  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  28 AIQCYQCNSLTNSLCSELIPPDTMKI-DC-----LDLRGGKKYTMCRKITQTIeisayelQPNTRIIRGCGW----DESS 97
Cdd:cd23592     2 AIKCWVCRSDYDPRCGDPFDNLTLPItDCnqekkPHHLPGVKATMCRKMRQKV-------NGEWRYIRSCAFlgepGIGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 2296749787  98 YKNMCYKRNG-FGAKQEVCSCSN-DYCNAA 125
Cdd:cd23592    75 DERWCLERSGtYNIHIEDCTCNSkDGCNAA 104
 
Name Accession Description Interval E-value
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
 29-123 2.91e-11

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: 56.07  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  29 IQCYQCNSLTNSLCSELIPPDT---MKIDCldlrggkkYTMCRKITQTIEISayelqpNTRIIRGCGWDESSY-KNMCYK 104
Cdd:pfam17064   1 IKCYSCNSSDDPGCGDPFPFNSssiKLVDC--------DGGCVKIKTKGSGG------STRVTRGCGPELTEDiKDGCSS 66

                          90
                  ....*....|....*....
gi 2296749787 105 RNGFGAKQEVCSCSNDYCN 123
Cdd:pfam17064  67 SSSGGGGTITCFCNTDLCN 85
TFP_LU_ECD_Crok cd23592
extracellular domain (ECD), Ly6/uPAR superfamily, three finger domain (TFD) fold, found in ...
 28-125 6.09e-08

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: 47.87  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  28 AIQCYQCNSLTNSLCSELIPPDTMKI-DC-----LDLRGGKKYTMCRKITQTIeisayelQPNTRIIRGCGW----DESS 97
Cdd:cd23592     2 AIKCWVCRSDYDPRCGDPFDNLTLPItDCnqekkPHHLPGVKATMCRKMRQKV-------NGEWRYIRSCAFlgepGIGG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 2296749787  98 YKNMCYKRNG-FGAKQEVCSCSN-DYCNAA 125
Cdd:cd23592    75 DERWCLERSGtYNIHIEDCTCNSkDGCNAA 104
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
 29-123 5.16e-06

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: 42.47  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  29 IQCYQCNSLTNSLCSELIPPdtmKIDCLDlrggkKYTMCRKITQTIEisayelQPNTRIIRGCGWDESSYKNMCYKRNGF 108
Cdd:cd00117     1 LKCYQCNSSNDPNCCNSSPT---LVTCSS-----PETFCRKIVGKVG------GGETLVIRGCATECECGCTECCSGTGT 66

                          90
                  ....*....|....*
gi 2296749787 109 GAKQEVCSCSNDYCN 123
Cdd:cd00117    67 SGTTCTSCCDTDLCN 81
TFP_LU_ECD_Twit cd23593
extracellular domain (ECD) found in Drosophila melanogaster Target of wit (Twit) and similar ...
 28-125 1.75e-05

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: 41.24  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  28 AIQCYQCNSLTNSLCSELIPPDTMKI---DCLDLRGGKKYT----MCRKITQTIeisayelQPNTRIIRGCGW-DESSYK 99
Cdd:cd23593     1 ALRCWSCSSDTDPFCGDPFNTTENHFhltDCDRTASPSYYLnerpVCRKIVQRV-------NGELVVIRSCAWeNEDDVD 73

                          90       100
                  ....*....|....*....|....*...
gi 2296749787 100 NMC-YKRNGFGAKQEVCS-CSNDYCNAA 125
Cdd:cd23593    74 GPCsNTSTGSYIKIESCEtCSTDGCNSA 101
TFP_LU_ECD_Bou cd23590
extracellular domain (ECD) found in Drosophila melanogaster protein boudin and similar ...
 29-125 4.79e-04

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: 37.03  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2296749787  29 IQCYQCNSLTNSLCSELIPPDTMKIDCLDlrGGKKYtmCRKITQTIEISayelqpNTRIIRGCgwDESSYKNMC-YKRNG 107
Cdd:cd23590     1 LKCYQCDSEKDPDCEENPPPDLEPTECPG--DDAKY--CIKTTGYYGGG------LIGTRRFC--SSRDMGNYCtYVTRP 68

                          90       100
                  ....*....|....*....|
gi 2296749787 108 FGAKQEVC--SCSNDYCNAA 125
Cdd:cd23590    69 DGRTYRACiyTCSTDGCNSA 88
 
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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