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Conserved domains on  [gi|1953346015|ref|XP_038292886|]
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ankyrin repeat domain-containing protein 13A isoform X2 [Canis lupus familiaris]

Protein Classification

GPCR_chapero_1 domain-containing protein( domain architecture ID 12790908)

GPCR_chapero_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 156-470 5.01e-127

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


:

Pssm-ID: 463391  Cd Length: 298  Bit Score: 375.05  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 156 RVDITLLGFENMSWIRGRRSFIFKGED-NRAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpkgrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVSVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEDFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEETGSQNLEGTQPDSashvTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ....
gi 1953346015 467 ESYH 470
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 1.16e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193


                  ....*....
gi 1953346015  82 VSTGDPEMV 90
Cdd:COG0666   194 AENGHLEIV 202
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 156-470 5.01e-127

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 375.05  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 156 RVDITLLGFENMSWIRGRRSFIFKGED-NRAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpkgrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVSVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEDFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEETGSQNLEGTQPDSashvTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ....
gi 1953346015 467 ESYH 470
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 1.16e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193


                  ....*....
gi 1953346015  82 VSTGDPEMV 90
Cdd:COG0666   194 AENGHLEIV 202
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-96 1.83e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  13 LHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENREGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77


                  ....*.
gi 1953346015  91 YTVLQH 96
Cdd:pfam12796  78 KLLLEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-122 5.24e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  31 GQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322  105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184

                          90       100
                  ....*....|....*....|.
gi 1953346015 106 -LEGVPELLQK---ILEAPDF 122
Cdd:PTZ00322  185 sFTGKPPSLEDspiSSHHPDF 205
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 40-69 7.61e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953346015   40 RGRTLLHLAVSLGHLESARVLLRHKADVTK 69
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 156-470 5.01e-127

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 375.05  E-value: 5.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 156 RVDITLLGFENMSWIRGRRSFIFKGED-NRAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpkgrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVSVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEDFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015 387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEETGSQNLEGTQPDSashvTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ....
gi 1953346015 467 ESYH 470
Cdd:pfam11904 295 SGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 1.16e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193


                  ....*....
gi 1953346015  82 VSTGDPEMV 90
Cdd:COG0666   194 AENGHLEIV 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-119 1.43e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLEKEL-RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAV 82
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953346015  83 STGDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666   162 ANGNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-97 6.25e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 6.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIV-KLLleAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                          90
                  ....*....|....*.
gi 1953346015  82 VSTGDPEMVYTVLQHR 97
Cdd:COG0666   227 AENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-96 1.83e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  13 LHLLVWNNDYRQLeKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENREGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77


                  ....*.
gi 1953346015  91 YTVLQH 96
Cdd:pfam12796  78 KLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-90 1.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953346015  41 GRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMV 90
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-96 1.60e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  13 LHLLVWNNDYRQLEKELRGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYT 92
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138


                  ....
gi 1953346015  93 VLQH 96
Cdd:COG0666   139 LLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-118 5.38e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 5.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  45 LHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM---ALEGVPELLQKI 116
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaARSGHLEIVKLL 80


                  ..
gi 1953346015 117 LE 118
Cdd:pfam12796  81 LE 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-122 5.24e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  31 GQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322  105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184

                          90       100
                  ....*....|....*....|.
gi 1953346015 106 -LEGVPELLQK---ILEAPDF 122
Cdd:PTZ00322  185 sFTGKPPSLEDspiSSHHPDF 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 6.96e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 6.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYrQLEKEL--RGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:COG0666   181 ARDNDGETPLHLAAENGHL-EIVKLLleAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259


                  ....*....
gi 1953346015  82 VSTGDPEMV 90
Cdd:COG0666   260 AAAGAALIV 268
Ank_5 pfam13857
Ankyrin repeats (many copies);
28-81 5.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 5.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953346015  28 ELRGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEA 81
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 12-97 1.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  12 PLHLLVWNNDYRQLEkELRGQNVEALD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPE 88
Cdd:PHA02875   71 ELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149


                  ....*....
gi 1953346015  89 MVYTVLQHR 97
Cdd:PHA02875  150 GIELLIDHK 158
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-96 9.07e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 9.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953346015  25 LEKELR-GQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEmVYTVLQH 96
Cdd:PLN03192  541 LEELLKaKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYH 612
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 40-72 1.34e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953346015  40 RGRTLLHLAV-SLGHLESARVLLRHKADVTKENR 72
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-71 2.25e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1953346015  37 LDPRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 71
Cdd:pfam12796  57 LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 40-67 3.03e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 3.03e-04
                          10        20
                  ....*....|....*....|....*...
gi 1953346015  40 RGRTLLHLAVSLGHLESARVLLRHKADV 67
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 40-69 7.61e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953346015   40 RGRTLLHLAVSLGHLESARVLLRHKADVTK 69
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-119 9.40e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.48  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015  13 LHLLVWNNDYRQLEKELRGQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYT 92
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1953346015  93 VLQH------RDYHNTSM----ALEGVPELLQKILEA 119
Cdd:COG0666   106 LLEAgadvnaRDKDGETPlhlaAYNGNLEIVKLLLEA 142
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 31-101 4.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 4.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953346015  31 GQNVEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENREGWTVLHEAVSTGDPEMVYTVLQHRDYHN 101
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-79 6.56e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953346015   4 ARDSSSHFPLHLLVWNNDYRQLEKEL--RGQNVEALDPRGRTLLH--LAVSLGHLESARVLLRHKADVTKENREGWTVLH 79
Cdd:PHA03095   78 APERCGFTPLHLYLYNATTLDVIKLLikAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
 
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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