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Conserved domains on  [gi|2217328500|ref|XP_047300570|]
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anoctamin-7 isoform X21 [Homo sapiens]

Protein Classification

anoctamin( domain architecture ID 11069330)

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, ...
318-660 6.81e-73

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: 242.10  E-value: 6.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 318 VRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDiptqelcgskdsfemcplcldcpfwllssacalaqv 397
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATLFDP------------------------------------ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 398 reeagrlfdhgGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDtEERPRPQFAASAPMTapNPITGEDEPYFPE 477
Cdd:pfam04547  45 -----------YTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEE-EEEPRPEFKGEKERI--NPVTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 478 RS-RARRMLAGSvvivvmvavvvmclvSIILyrAIMAIVVsrsgntllaawasriasltgsvvnLVFILILSKIYVSLAH 556
Cdd:pfam04547 111 WKrRLRRYLLSI---------------PLVL--LLIALLV------------------------LGVIIYLNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 557 VLTRWEMHRTQTKFEDAFTLKVFifqfvnfysspvyiaffkgrfvgypgnyhtlfgvrneecaaggcLIELAQELLVIMV 636
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQLAIIMV 185
                         330       340
                  ....*....|....*....|....
gi 2217328500 637 GKQVINNMQEVLIPAAVRLRHHLR 660
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKR 209
Anoct_dimer super family cl24682
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
67-315 2.00e-47

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.


The actual alignment was detected with superfamily member pfam16178:

Pssm-ID: 465044  Cd Length: 224  Bit Score: 167.74  E-value: 2.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500  67 KPRIaDFVLVWEEDlkldrqqDSAARDRTDMHRTWRETFLDNLRAAGLCVDQALTE------------PW---------- 124
Cdd:pfam16178   6 KRKI-DYVLVYEEE-------KEESKREEEKKREKRETFEENLIEEGLELEREKEEsdqgthfvkihaPWevlcryaeil 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 125 ---VPTAGRPGREHHSALRPPQRLLGCALLLRRRPAPEaalagvtqpglqlvgrpagmaghpqrpaggcarrtprvlllp 201
Cdd:pfam16178  78 kikMPIKKKIEKEESSIPGRLDNLSRKLLSKPFIPDVE------------------------------------------ 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 202 vqseqaaTLPPNLLHCSHA------HSFLGSDnQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFP 275
Cdd:pfam16178 116 -------TFPKEPDYFTAPfsrdkmYLFLIED-KDTFFTNATRSRIVYEILSRTRYGGRKKKEVGIKRLLNEGVYLAAYP 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217328500 276 LHDGPFKTPPEGPQaprLNQRQVLFQHWARWGKWNKYQPL 315
Cdd:pfam16178 188 LHDGPYKLPKDPSE---LNERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
318-660 6.81e-73

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: 242.10  E-value: 6.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 318 VRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDiptqelcgskdsfemcplcldcpfwllssacalaqv 397
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATLFDP------------------------------------ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 398 reeagrlfdhgGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDtEERPRPQFAASAPMTapNPITGEDEPYFPE 477
Cdd:pfam04547  45 -----------YTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEE-EEEPRPEFKGEKERI--NPVTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 478 RS-RARRMLAGSvvivvmvavvvmclvSIILyrAIMAIVVsrsgntllaawasriasltgsvvnLVFILILSKIYVSLAH 556
Cdd:pfam04547 111 WKrRLRRYLLSI---------------PLVL--LLIALLV------------------------LGVIIYLNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 557 VLTRWEMHRTQTKFEDAFTLKVFifqfvnfysspvyiaffkgrfvgypgnyhtlfgvrneecaaggcLIELAQELLVIMV 636
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQLAIIMV 185
                         330       340
                  ....*....|....*....|....
gi 2217328500 637 GKQVINNMQEVLIPAAVRLRHHLR 660
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKR 209
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
67-315 2.00e-47

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: 167.74  E-value: 2.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500  67 KPRIaDFVLVWEEDlkldrqqDSAARDRTDMHRTWRETFLDNLRAAGLCVDQALTE------------PW---------- 124
Cdd:pfam16178   6 KRKI-DYVLVYEEE-------KEESKREEEKKREKRETFEENLIEEGLELEREKEEsdqgthfvkihaPWevlcryaeil 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 125 ---VPTAGRPGREHHSALRPPQRLLGCALLLRRRPAPEaalagvtqpglqlvgrpagmaghpqrpaggcarrtprvlllp 201
Cdd:pfam16178  78 kikMPIKKKIEKEESSIPGRLDNLSRKLLSKPFIPDVE------------------------------------------ 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 202 vqseqaaTLPPNLLHCSHA------HSFLGSDnQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFP 275
Cdd:pfam16178 116 -------TFPKEPDYFTAPfsrdkmYLFLIED-KDTFFTNATRSRIVYEILSRTRYGGRKKKEVGIKRLLNEGVYLAAYP 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217328500 276 LHDGPFKTPPEGPQaprLNQRQVLFQHWARWGKWNKYQPL 315
Cdd:pfam16178 188 LHDGPYKLPKDPSE---LNERQLLYEEWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
318-660 6.81e-73

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: 242.10  E-value: 6.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 318 VRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDiptqelcgskdsfemcplcldcpfwllssacalaqv 397
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLATLFDP------------------------------------ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 398 reeagrlfdhgGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDtEERPRPQFAASAPMTapNPITGEDEPYFPE 477
Cdd:pfam04547  45 -----------YTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEE-EEEPRPEFKGEKERI--NPVTGEKEPYYPP 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 478 RS-RARRMLAGSvvivvmvavvvmclvSIILyrAIMAIVVsrsgntllaawasriasltgsvvnLVFILILSKIYVSLAH 556
Cdd:pfam04547 111 WKrRLRRYLLSI---------------PLVL--LLIALLV------------------------LGVIIYLNFVYTKLAK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 557 VLTRWEMHRTQTKFEDAFTLKVFifqfvnfysspvyiaffkgrfvgypgnyhtlfgvrneecaaggcLIELAQELLVIMV 636
Cdd:pfam04547 150 KLTDWENHRTQSEYENSLILKVF--------------------------------------------LDRLRIQLAIIMV 185
                         330       340
                  ....*....|....*....|....
gi 2217328500 637 GKQVINNMQEVLIPAAVRLRHHLR 660
Cdd:pfam04547 186 TKQIINNITEVVLPYLKRKRRKKR 209
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
67-315 2.00e-47

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: 167.74  E-value: 2.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500  67 KPRIaDFVLVWEEDlkldrqqDSAARDRTDMHRTWRETFLDNLRAAGLCVDQALTE------------PW---------- 124
Cdd:pfam16178   6 KRKI-DYVLVYEEE-------KEESKREEEKKREKRETFEENLIEEGLELEREKEEsdqgthfvkihaPWevlcryaeil 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 125 ---VPTAGRPGREHHSALRPPQRLLGCALLLRRRPAPEaalagvtqpglqlvgrpagmaghpqrpaggcarrtprvlllp 201
Cdd:pfam16178  78 kikMPIKKKIEKEESSIPGRLDNLSRKLLSKPFIPDVE------------------------------------------ 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217328500 202 vqseqaaTLPPNLLHCSHA------HSFLGSDnQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFP 275
Cdd:pfam16178 116 -------TFPKEPDYFTAPfsrdkmYLFLIED-KDTFFTNATRSRIVYEILSRTRYGGRKKKEVGIKRLLNEGVYLAAYP 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217328500 276 LHDGPFKTPPEGPQaprLNQRQVLFQHWARWGKWNKYQPL 315
Cdd:pfam16178 188 LHDGPYKLPKDPSE---LNERQLLYEEWARWGKWYKYQPL 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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