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Conserved domains on  [gi|442616058|ref|NP_001259472|]
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uncharacterized protein Dmel_CG10353, isoform I [Drosophila melanogaster]

Protein Classification

anoctamin( domain architecture ID 11241320)

anoctamin (anion channel with 8 transmembrane domains) is a calcium-activated protein and may mediate the calcium-dependent exposure of phospholipids to the extracellular surface, a process called phospholipid scrambling

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
350-931 1.19e-96

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


:

Pssm-ID: 461349  Cd Length: 377  Bit Score: 309.90  E-value: 1.19e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  350 IKDYFGAKVALYFAWLGFYTQMLIPISVFGVLCFLYGFITwnsdpisrdicddngtimcpqcdrscdywrlnetctsskf 429
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLAT---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  430 nylIDNNMTVVFAFSMAIWAVVYLEFWKRYSAGLVHRWGLTGFtHHVEHPRPQYLARISRTKKLAGKAYeqdhtgkrtil 509
Cdd:pfam04547  41 ---LFDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGF-EEEEEPRPEFKGEKERINPVTGEKE----------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  510 dPDVPFWSFKFLPNFTSYSIMVLFICISVIaiaGIIIYrmaqrashsilgsensmtfkvmilpmtagiidlivislLDMV 589
Cdd:pfam04547 106 -PYYPPWKRRLRRYLLSIPLVLLLIALLVL---GVIIY--------------------------------------LNFV 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  590 YSNLAVKLTNYEYCRTQTEYDESLTIKNYvfqfvnyysslfyiaflkgkfvgypakynrvlgfrqeecnpggcLMELCMQ 669
Cdd:pfam04547 144 YTKLAKKLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQ 179
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  670 LVIIMAGKQAVNAIVEMLIPYLMR------TFKELSYRHGWYKSHQDQRLVPYNQFTEDYNLLPaeNNSLYvEYLEMVVQ 743
Cdd:pfam04547 180 LAIIMVTKQIINNITEVVLPYLKRkrrkkrKKKKKKEEPSVSIKDEPEESEFLERVEKEYELEP--YDGLD-DYLEMVIQ 256
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  744 FGFITLFSLAFPLAPLLALLNNVIEVRLDAIKMLRFLRRPVGMRARDIGVWHSIMTVVTRIAVASSAMIIAFSTnlipki 823
Cdd:pfam04547 257 FGYVTLFSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIYAFT------ 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  824 vyaasmgdpelnnylnftlavfntkdfqvqpllggsqhvnetvcrytefrnspedphpykrPMIYWKILTGRLAFIVIYQ 903
Cdd:pfam04547 331 -------------------------------------------------------------SDQYWSLLALLLAFVIVFE 349
                         570       580
                  ....*....|....*....|....*...
gi 442616058  904 NIITMLQGILRWAVPDVSGRLLKRIKRE 931
Cdd:pfam04547 350 HVVLLLKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
138-347 1.45e-72

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


:

Pssm-ID: 465044  Cd Length: 224  Bit Score: 239.00  E-value: 1.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  138 FDDGKRSVDFVLAYNGE-----TQLEEHRRKCEIFEANLQREGLQLEH---NKVQRVHFIKIHAPAEVLYRYAEILKIKV 209
Cdd:pfam16178   2 FRDGKRKIDYVLVYEEEkeeskREEEKKREKRETFEENLIEEGLELERekeESDQGTHFVKIHAPWEVLCRYAEILKIKM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  210 PLK-PIPGQDQIFAESaheFKTCFSRMCKSLFssvQLNTALFPEREPRIHLEFSRNYLELYD-TEHPNFLDASTRYSIIN 287
Cdd:pfam16178  82 PIKkKIEKEESSIPGR---LDNLSRKLLSKPF---IPDVETFPKEPDYFTAPFSRDKMYLFLiEDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442616058  288 FILQRQRFveGEETADNLGIEKLVQDGVYTCAYTLHDKD-----------DRDRLLKEWANISKWKNLQPL 347
Cdd:pfam16178 156 EILSRTRY--GGRKKKEVGIKRLLNEGVYLAAYPLHDGPyklpkdpselnERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
350-931 1.19e-96

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


Pssm-ID: 461349  Cd Length: 377  Bit Score: 309.90  E-value: 1.19e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  350 IKDYFGAKVALYFAWLGFYTQMLIPISVFGVLCFLYGFITwnsdpisrdicddngtimcpqcdrscdywrlnetctsskf 429
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLAT---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  430 nylIDNNMTVVFAFSMAIWAVVYLEFWKRYSAGLVHRWGLTGFtHHVEHPRPQYLARISRTKKLAGKAYeqdhtgkrtil 509
Cdd:pfam04547  41 ---LFDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGF-EEEEEPRPEFKGEKERINPVTGEKE----------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  510 dPDVPFWSFKFLPNFTSYSIMVLFICISVIaiaGIIIYrmaqrashsilgsensmtfkvmilpmtagiidlivislLDMV 589
Cdd:pfam04547 106 -PYYPPWKRRLRRYLLSIPLVLLLIALLVL---GVIIY--------------------------------------LNFV 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  590 YSNLAVKLTNYEYCRTQTEYDESLTIKNYvfqfvnyysslfyiaflkgkfvgypakynrvlgfrqeecnpggcLMELCMQ 669
Cdd:pfam04547 144 YTKLAKKLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQ 179
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  670 LVIIMAGKQAVNAIVEMLIPYLMR------TFKELSYRHGWYKSHQDQRLVPYNQFTEDYNLLPaeNNSLYvEYLEMVVQ 743
Cdd:pfam04547 180 LAIIMVTKQIINNITEVVLPYLKRkrrkkrKKKKKKEEPSVSIKDEPEESEFLERVEKEYELEP--YDGLD-DYLEMVIQ 256
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  744 FGFITLFSLAFPLAPLLALLNNVIEVRLDAIKMLRFLRRPVGMRARDIGVWHSIMTVVTRIAVASSAMIIAFSTnlipki 823
Cdd:pfam04547 257 FGYVTLFSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIYAFT------ 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  824 vyaasmgdpelnnylnftlavfntkdfqvqpllggsqhvnetvcrytefrnspedphpykrPMIYWKILTGRLAFIVIYQ 903
Cdd:pfam04547 331 -------------------------------------------------------------SDQYWSLLALLLAFVIVFE 349
                         570       580
                  ....*....|....*....|....*...
gi 442616058  904 NIITMLQGILRWAVPDVSGRLLKRIKRE 931
Cdd:pfam04547 350 HVVLLLKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
138-347 1.45e-72

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


Pssm-ID: 465044  Cd Length: 224  Bit Score: 239.00  E-value: 1.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  138 FDDGKRSVDFVLAYNGE-----TQLEEHRRKCEIFEANLQREGLQLEH---NKVQRVHFIKIHAPAEVLYRYAEILKIKV 209
Cdd:pfam16178   2 FRDGKRKIDYVLVYEEEkeeskREEEKKREKRETFEENLIEEGLELERekeESDQGTHFVKIHAPWEVLCRYAEILKIKM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  210 PLK-PIPGQDQIFAESaheFKTCFSRMCKSLFssvQLNTALFPEREPRIHLEFSRNYLELYD-TEHPNFLDASTRYSIIN 287
Cdd:pfam16178  82 PIKkKIEKEESSIPGR---LDNLSRKLLSKPF---IPDVETFPKEPDYFTAPFSRDKMYLFLiEDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442616058  288 FILQRQRFveGEETADNLGIEKLVQDGVYTCAYTLHDKD-----------DRDRLLKEWANISKWKNLQPL 347
Cdd:pfam16178 156 EILSRTRY--GGRKKKEVGIKRLLNEGVYLAAYPLHDGPyklpkdpselnERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
350-931 1.19e-96

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


Pssm-ID: 461349  Cd Length: 377  Bit Score: 309.90  E-value: 1.19e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  350 IKDYFGAKVALYFAWLGFYTQMLIPISVFGVLCFLYGFITwnsdpisrdicddngtimcpqcdrscdywrlnetctsskf 429
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLAT---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  430 nylIDNNMTVVFAFSMAIWAVVYLEFWKRYSAGLVHRWGLTGFtHHVEHPRPQYLARISRTKKLAGKAYeqdhtgkrtil 509
Cdd:pfam04547  41 ---LFDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGF-EEEEEPRPEFKGEKERINPVTGEKE----------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  510 dPDVPFWSFKFLPNFTSYSIMVLFICISVIaiaGIIIYrmaqrashsilgsensmtfkvmilpmtagiidlivislLDMV 589
Cdd:pfam04547 106 -PYYPPWKRRLRRYLLSIPLVLLLIALLVL---GVIIY--------------------------------------LNFV 143
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  590 YSNLAVKLTNYEYCRTQTEYDESLTIKNYvfqfvnyysslfyiaflkgkfvgypakynrvlgfrqeecnpggcLMELCMQ 669
Cdd:pfam04547 144 YTKLAKKLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQ 179
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  670 LVIIMAGKQAVNAIVEMLIPYLMR------TFKELSYRHGWYKSHQDQRLVPYNQFTEDYNLLPaeNNSLYvEYLEMVVQ 743
Cdd:pfam04547 180 LAIIMVTKQIINNITEVVLPYLKRkrrkkrKKKKKKEEPSVSIKDEPEESEFLERVEKEYELEP--YDGLD-DYLEMVIQ 256
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  744 FGFITLFSLAFPLAPLLALLNNVIEVRLDAIKMLRFLRRPVGMRARDIGVWHSIMTVVTRIAVASSAMIIAFSTnlipki 823
Cdd:pfam04547 257 FGYVTLFSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIYAFT------ 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  824 vyaasmgdpelnnylnftlavfntkdfqvqpllggsqhvnetvcrytefrnspedphpykrPMIYWKILTGRLAFIVIYQ 903
Cdd:pfam04547 331 -------------------------------------------------------------SDQYWSLLALLLAFVIVFE 349
                         570       580
                  ....*....|....*....|....*...
gi 442616058  904 NIITMLQGILRWAVPDVSGRLLKRIKRE 931
Cdd:pfam04547 350 HVVLLLKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
138-347 1.45e-72

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


Pssm-ID: 465044  Cd Length: 224  Bit Score: 239.00  E-value: 1.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  138 FDDGKRSVDFVLAYNGE-----TQLEEHRRKCEIFEANLQREGLQLEH---NKVQRVHFIKIHAPAEVLYRYAEILKIKV 209
Cdd:pfam16178   2 FRDGKRKIDYVLVYEEEkeeskREEEKKREKRETFEENLIEEGLELERekeESDQGTHFVKIHAPWEVLCRYAEILKIKM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616058  210 PLK-PIPGQDQIFAESaheFKTCFSRMCKSLFssvQLNTALFPEREPRIHLEFSRNYLELYD-TEHPNFLDASTRYSIIN 287
Cdd:pfam16178  82 PIKkKIEKEESSIPGR---LDNLSRKLLSKPF---IPDVETFPKEPDYFTAPFSRDKMYLFLiEDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442616058  288 FILQRQRFveGEETADNLGIEKLVQDGVYTCAYTLHDKD-----------DRDRLLKEWANISKWKNLQPL 347
Cdd:pfam16178 156 EILSRTRY--GGRKKKEVGIKRLLNEGVYLAAYPLHDGPyklpkdpselnERQLLYEEWARWGKWYKYQPL 224
 
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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