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Conserved domains on  [gi|38683799|ref|NP_149112|]
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ankyrin repeat domain-containing protein 13A [Homo sapiens]

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 ...
 156-469 2.53e-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: 375.82  E-value: 2.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   156 RVDITLLGFENMSWIRGRRSFIFKGED-NWAELMEVNHDDKVVTTERfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEEFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSashiTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ...
gi 38683799   467 ESY 469
Cdd:pfam11904 295 SGY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-119 5.30e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38683799  85 GDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666 164 GNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 156-469 2.53e-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: 375.82  E-value: 2.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   156 RVDITLLGFENMSWIRGRRSFIFKGED-NWAELMEVNHDDKVVTTERfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEEFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSashiTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ...
gi 38683799   467 ESY 469
Cdd:pfam11904 295 SGY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-119 5.30e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38683799  85 GDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666 164 GNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-96 6.49e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 6.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799    13 LHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77


                  ....*.
gi 38683799    91 YTVLQH 96
Cdd:pfam12796  78 KLLLEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-122 4.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184

                         90       100
                 ....*....|....*....|.
gi 38683799  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 38683799     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 ...
 156-469 2.53e-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: 375.82  E-value: 2.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   156 RVDITLLGFENMSWIRGRRSFIFKGED-NWAELMEVNHDDKVVTTERfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGdSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   235 SLDTKNIAFERTKSGfWGwRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKAD-------RNPLESLLGTV 307
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   308 EHQFGAQG-DLTTECATANNPTAITPDEYFNEefdlkdrdigrPKELTIRTQKFKAMLWMCEEFPLSLvEQVIPIIDLMA 386
Cdd:pfam11904 151 EEEKGWFGkTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   387 RTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSashiTNFEVDQSVFEIP 466
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSP----SSCEIDDDPFEIP 294


                  ...
gi 38683799   467 ESY 469
Cdd:pfam11904 295 SGY 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-119 5.30e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLeAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 38683799  85 GDPEMVYTVLQH------RDYHNTS----MALEGVPELLQKILEA 119
Cdd:COG0666 164 GNLEIVKLLLEAgadvnaRDNDGETplhlAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 3.69e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   4 ACDAGDHYPLHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIV-KLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193


                ....*....
gi 38683799  82 VSTGDPEMV 90
Cdd:COG0666 194 AENGHLEIV 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-97 7.73e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 7.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   4 ACDAGDHYPLHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIV-KLLleAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                        90
                ....*....|....*.
gi 38683799  82 VSTGDPEMVYTVLQHR 97
Cdd:COG0666 227 AENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-96 6.49e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 6.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799    13 LHLLVWKNDYRQLeKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77


                  ....*.
gi 38683799    91 YTVLQH 96
Cdd:pfam12796  78 KLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-90 1.11e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.11e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 38683799    41 GRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMV 90
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-96 1.29e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   6 DAGDHYPLHLLVWKNDYRQLEKEL-QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVST 84
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLaAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90
                ....*....|..
gi 38683799  85 GDPEMVYTVLQH 96
Cdd:COG0666 131 GNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-118 1.31e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799    45 LHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM---ALEGVPELLQKI 116
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaARSGHLEIVKLL 80


                  ..
gi 38683799   117 LE 118
Cdd:pfam12796  81 LE 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-122 4.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA----- 105
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpd 184

                         90       100
                 ....*....|....*....|.
gi 38683799  106 -LEGVPELLQK---ILEAPDF 122
Cdd:PTZ00322 185 sFTGKPPSLEDspiSSHHPDF 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 5.84e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 5.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   4 ACDAGDHYPLHLLVWKNDYrQLEKEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:COG0666 181 ARDNDGETPLHLAAENGHL-EIVKLLleAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259


                ....*....
gi 38683799  82 VSTGDPEMV 90
Cdd:COG0666 260 AAAGAALIV 268
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 12-97 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   12 PLHLLVWKNDYRQLEkELQGQNVEAVD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPE 88
Cdd:PHA02875  71 ELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149


                 ....*....
gi 38683799   89 MVYTVLQHR 97
Cdd:PHA02875 150 GIELLIDHK 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
33-81 5.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 5.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 38683799    33 NVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEA 81
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-96 5.91e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 5.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38683799   38 DPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEmVYTVLQH 96
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-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 38683799    40 RGRTLLHLAV-SLGHLESARVLLRHKADVTKENR 72
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
29-71 1.96e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 1.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 38683799    29 LQGQNVEAVDpRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 71
Cdd:pfam12796  50 LEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 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 38683799    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 38683799     40 RGRTLLHLAVSLGHLESARVLLRHKADVTK 69
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-119 1.66e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   6 DAGDHYPLHLLVWKNDYRQLEKELQGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTG 85
Cdd:COG0666  19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 38683799  86 DPEMVYTVLQH------RDYHNTSM----ALEGVPELLQKILEA 119
Cdd:COG0666  99 DLEIVKLLLEAgadvnaRDKDGETPlhlaAYNGNLEIVKLLLEA 142
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 31-101 4.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 4.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38683799   31 GQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHN 101
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 27-110 6.68e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 6.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799   27 KEL--QGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENrqgwtvLHEAVStgdPEMVYTVLQHRDYHNTSM 104
Cdd:PLN03192 639 KELlkQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN------TDDDFS---PTELRELLQKRELGHSIT 709


                 ....*.
gi 38683799  105 ALEGVP 110
Cdd:PLN03192 710 IVDSVP 715
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 6-96 8.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38683799    6 DAGDHYPLHLLVWKNDYRQLEKELQ-GQNVEAVDPRGRTLLHLAVS-LGHLESARVLLRHKADVT-KENRQGWTVLHEAV 82
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLEnGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNaKSYILGLTALHSSI 277

                         90
                 ....*....|....
gi 38683799   83 StgDPEMVYTVLQH 96
Cdd:PHA02878 278 K--SERKLKLLLEY 289
 
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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