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Conserved domains on  [gi|442619946|ref|NP_001262736|]
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subdued, isoform E [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, ...
258-834 3.48e-125

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: 383.47  E-value: 3.48e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  258 IKEYFGVKIGLYFAWLGYYTYMLLLASIVGVICFLYSWFSLknyvpvkdicqsgntnitmcplcdwcnfwdlketcnyak 337
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATL--------------------------------------- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  338 vtyliDNPSTVFFAVFMSFWATLFLELWKRYSAEITHRWDLTGFDvHEEHPRPQYLARLEHIPPtrvdyVTNIKEPTVPF 417
Cdd:pfam04547  42 -----FDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFE-EEEEPRPEFKGEKERINP-----VTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  418 WRMKLPATVFSFSVVLLLIALAFVAllaVVVYrmsmlaalkvgaspmttssaivlatasaafvnlcllyiLNYMYNHLAE 497
Cdd:pfam04547 111 WKRRLRRYLLSIPLVLLLIALLVLG---VIIY--------------------------------------LNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  498 YLTELEMWRTQTQFDDSLTLKIYLlqfvnyyasifyiaffkgkfvghpgeynklfdyrqeecssggclTELCIQLAIIMV 577
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVFL--------------------------------------------DRLRIQLAIIMV 185
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  578 GKQAFNTILEVYLPMFWRKVLAIQVGLSRLFNNTPNPDKAKDE-----RWMRDFKLLDWGArglFPEYLEMVLQYGFVTI 652
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKRKKKKKKEEPSVSIKDEPEEsefleRVEKEYELEPYDG---LDDYLEMVIQFGYVTL 262
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  653 FVAAFPLAPFFALLNNILEMRLDAKKLLTHHKRPVSQRVRDIGVWYRILDCIGKLSVITNGFII-AFTSDmiprlvyrhy 731
Cdd:pfam04547 263 FSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFTSD---------- 332
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  732 vnkqgtldgylnftlsefkvidsptlyslagdlsnittcrytdfrlppsspekytlssMFYIILACRLGFVVVFENFVAL 811
Cdd:pfam04547 333 ----------------------------------------------------------QYWSLLALLLAFVIVFEHVVLL 354
                         570       580
                  ....*....|....*....|...
gi 442619946  812 VMILVRWCIPDMSVELRDQIRRE 834
Cdd:pfam04547 355 LKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
37-255 3.11e-93

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: 293.70  E-value: 3.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946   37 FFEDCVRSIDFVLAYRINAHEPTELENT--EKRRVFEANLISQGLEVE--SSQKDQ-IWFVKIHAPLEVLRRYAEILKLR 111
Cdd:pfam16178   1 YFRDGKRKIDYVLVYEEEKEESKREEEKkrEKRETFEENLIEEGLELEreKEESDQgTHFVKIHAPWEVLCRYAEILKIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  112 MPMKEipgmsVVNRSTKSVFSSLKHVFQFFLRN-IYVDEEIFPKRAHRFTAIYSRDKEYLFDI-RQDCFFTTAVRSRIVE 189
Cdd:pfam16178  81 MPIKK-----KIEKEESSIPGRLDNLSRKLLSKpFIPDVETFPKEPDYFTAPFSRDKMYLFLIeDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619946  190 FILDRQRFPAKNQHDMafGIERLIAEGVYSAAYPLHDG-----EITETGTMRALLYKHWASVPKWYRYQPL 255
Cdd:pfam16178 156 EILSRTRYGGRKKKEV--GIKRLLNEGVYLAAYPLHDGpyklpKDPSELNERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
258-834 3.48e-125

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: 383.47  E-value: 3.48e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  258 IKEYFGVKIGLYFAWLGYYTYMLLLASIVGVICFLYSWFSLknyvpvkdicqsgntnitmcplcdwcnfwdlketcnyak 337
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATL--------------------------------------- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  338 vtyliDNPSTVFFAVFMSFWATLFLELWKRYSAEITHRWDLTGFDvHEEHPRPQYLARLEHIPPtrvdyVTNIKEPTVPF 417
Cdd:pfam04547  42 -----FDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFE-EEEEPRPEFKGEKERINP-----VTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  418 WRMKLPATVFSFSVVLLLIALAFVAllaVVVYrmsmlaalkvgaspmttssaivlatasaafvnlcllyiLNYMYNHLAE 497
Cdd:pfam04547 111 WKRRLRRYLLSIPLVLLLIALLVLG---VIIY--------------------------------------LNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  498 YLTELEMWRTQTQFDDSLTLKIYLlqfvnyyasifyiaffkgkfvghpgeynklfdyrqeecssggclTELCIQLAIIMV 577
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVFL--------------------------------------------DRLRIQLAIIMV 185
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  578 GKQAFNTILEVYLPMFWRKVLAIQVGLSRLFNNTPNPDKAKDE-----RWMRDFKLLDWGArglFPEYLEMVLQYGFVTI 652
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKRKKKKKKEEPSVSIKDEPEEsefleRVEKEYELEPYDG---LDDYLEMVIQFGYVTL 262
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  653 FVAAFPLAPFFALLNNILEMRLDAKKLLTHHKRPVSQRVRDIGVWYRILDCIGKLSVITNGFII-AFTSDmiprlvyrhy 731
Cdd:pfam04547 263 FSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFTSD---------- 332
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  732 vnkqgtldgylnftlsefkvidsptlyslagdlsnittcrytdfrlppsspekytlssMFYIILACRLGFVVVFENFVAL 811
Cdd:pfam04547 333 ----------------------------------------------------------QYWSLLALLLAFVIVFEHVVLL 354
                         570       580
                  ....*....|....*....|...
gi 442619946  812 VMILVRWCIPDMSVELRDQIRRE 834
Cdd:pfam04547 355 LKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
37-255 3.11e-93

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: 293.70  E-value: 3.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946   37 FFEDCVRSIDFVLAYRINAHEPTELENT--EKRRVFEANLISQGLEVE--SSQKDQ-IWFVKIHAPLEVLRRYAEILKLR 111
Cdd:pfam16178   1 YFRDGKRKIDYVLVYEEEKEESKREEEKkrEKRETFEENLIEEGLELEreKEESDQgTHFVKIHAPWEVLCRYAEILKIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  112 MPMKEipgmsVVNRSTKSVFSSLKHVFQFFLRN-IYVDEEIFPKRAHRFTAIYSRDKEYLFDI-RQDCFFTTAVRSRIVE 189
Cdd:pfam16178  81 MPIKK-----KIEKEESSIPGRLDNLSRKLLSKpFIPDVETFPKEPDYFTAPFSRDKMYLFLIeDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619946  190 FILDRQRFPAKNQHDMafGIERLIAEGVYSAAYPLHDG-----EITETGTMRALLYKHWASVPKWYRYQPL 255
Cdd:pfam16178 156 EILSRTRYGGRKKKEV--GIKRLLNEGVYLAAYPLHDGpyklpKDPSELNERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
258-834 3.48e-125

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: 383.47  E-value: 3.48e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  258 IKEYFGVKIGLYFAWLGYYTYMLLLASIVGVICFLYSWFSLknyvpvkdicqsgntnitmcplcdwcnfwdlketcnyak 337
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATL--------------------------------------- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  338 vtyliDNPSTVFFAVFMSFWATLFLELWKRYSAEITHRWDLTGFDvHEEHPRPQYLARLEHIPPtrvdyVTNIKEPTVPF 417
Cdd:pfam04547  42 -----FDPYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFE-EEEEPRPEFKGEKERINP-----VTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  418 WRMKLPATVFSFSVVLLLIALAFVAllaVVVYrmsmlaalkvgaspmttssaivlatasaafvnlcllyiLNYMYNHLAE 497
Cdd:pfam04547 111 WKRRLRRYLLSIPLVLLLIALLVLG---VIIY--------------------------------------LNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  498 YLTELEMWRTQTQFDDSLTLKIYLlqfvnyyasifyiaffkgkfvghpgeynklfdyrqeecssggclTELCIQLAIIMV 577
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVFL--------------------------------------------DRLRIQLAIIMV 185
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  578 GKQAFNTILEVYLPMFWRKVLAIQVGLSRLFNNTPNPDKAKDE-----RWMRDFKLLDWGArglFPEYLEMVLQYGFVTI 652
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKRKKKKKKEEPSVSIKDEPEEsefleRVEKEYELEPYDG---LDDYLEMVIQFGYVTL 262
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  653 FVAAFPLAPFFALLNNILEMRLDAKKLLTHHKRPVSQRVRDIGVWYRILDCIGKLSVITNGFII-AFTSDmiprlvyrhy 731
Cdd:pfam04547 263 FSAAFPLAPLFALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFTSD---------- 332
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  732 vnkqgtldgylnftlsefkvidsptlyslagdlsnittcrytdfrlppsspekytlssMFYIILACRLGFVVVFENFVAL 811
Cdd:pfam04547 333 ----------------------------------------------------------QYWSLLALLLAFVIVFEHVVLL 354
                         570       580
                  ....*....|....*....|...
gi 442619946  812 VMILVRWCIPDMSVELRDQIRRE 834
Cdd:pfam04547 355 LKFLIAWLIPDVPEWVRKERKRE 377
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
37-255 3.11e-93

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: 293.70  E-value: 3.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946   37 FFEDCVRSIDFVLAYRINAHEPTELENT--EKRRVFEANLISQGLEVE--SSQKDQ-IWFVKIHAPLEVLRRYAEILKLR 111
Cdd:pfam16178   1 YFRDGKRKIDYVLVYEEEKEESKREEEKkrEKRETFEENLIEEGLELEreKEESDQgTHFVKIHAPWEVLCRYAEILKIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619946  112 MPMKEipgmsVVNRSTKSVFSSLKHVFQFFLRN-IYVDEEIFPKRAHRFTAIYSRDKEYLFDI-RQDCFFTTAVRSRIVE 189
Cdd:pfam16178  81 MPIKK-----KIEKEESSIPGRLDNLSRKLLSKpFIPDVETFPKEPDYFTAPFSRDKMYLFLIeDKDTFFTNATRSRIVY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442619946  190 FILDRQRFPAKNQHDMafGIERLIAEGVYSAAYPLHDG-----EITETGTMRALLYKHWASVPKWYRYQPL 255
Cdd:pfam16178 156 EILSRTRYGGRKKKEV--GIKRLLNEGVYLAAYPLHDGpyklpKDPSELNERQLLYEEWARWGKWYKYQPL 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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