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Conserved domains on  [gi|1958669178|ref|XP_006249523|]
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ankyrin repeat domain-containing protein 13A isoform X1 [Rattus norvegicus]

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 ...
267-581 3.70e-128

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: 381.60  E-value: 3.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 267 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 345
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 346 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 418
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 419 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 498
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 499 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 578
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295

                  ...
gi 1958669178 579 SYH 581
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-201 1.70e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLLEAGAdvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                  ....*....
gi 1958669178 193 VSTGDPEMV 201
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 ...
267-581 3.70e-128

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: 381.60  E-value: 3.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 267 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 345
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 346 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 418
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 419 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 498
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 499 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 578
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295

                  ...
gi 1958669178 579 SYH 581
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-201 1.70e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLLEAGAdvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                  ....*....
gi 1958669178 193 VSTGDPEMV 201
Cdd:COG0666   194 AENGHLEIV 202
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-207 1.88e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 124 LHLLVWNNDYRQLeKELRDQNAEA--LDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADAnlQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                  ....*.
gi 1958669178 202 YTVLQH 207
Cdd:pfam12796  78 KLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
121-208 2.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 121 RFPLHLLVWNNDYRQLEkELRDQNAEALD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGD 197
Cdd:PHA02875   69 ESELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                          90
                  ....*....|.
gi 1958669178 198 PEMVYTVLQHR 208
Cdd:PHA02875  148 IKGIELLIDHK 158
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-180 9.02e-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: 9.02e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958669178  151 RGRTLLHLAVSLGHLESARVLLRHKADVTK 180
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 ...
267-581 3.70e-128

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: 381.60  E-value: 3.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 267 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 345
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 346 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 418
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 419 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 498
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 499 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 578
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295

                  ...
gi 1958669178 579 SYH 581
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-201 1.70e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIV-KLLLEAGAdvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                  ....*....
gi 1958669178 193 VSTGDPEMV 201
Cdd:COG0666   194 AENGHLEIV 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-207 1.28e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYrQLEKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDL-EIVKLLLEAGAdvNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          90
                  ....*....|....*
gi 1958669178 193 VSTGDPEMVYTVLQH 207
Cdd:COG0666   161 AANGNLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-238 2.01e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 115 ARDTSSRFPLHLLVWNNDYRQLeKELRDQNA--EALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIV-KLLLEAGAdvNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958669178 193 VSTGDPEMVYTVLQHRDYHNTSMALEGVPELLHKILEAPDFYVQMK 238
Cdd:COG0666   227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-207 1.88e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 124 LHLLVWNNDYRQLeKELRDQNAEA--LDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADAnlQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                  ....*.
gi 1958669178 202 YTVLQH 207
Cdd:pfam12796  78 KLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
152-201 1.30e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.30e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958669178 152 GRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 201
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
109-207 4.76e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 109 LLAMSSARDTSSRFPLHLLVWNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTV 188
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
                          90
                  ....*....|....*....
gi 1958669178 189 LHEAVSTGDPEMVYTVLQH 207
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-226 2.04e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 156 LHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM-------ALEGVPEL 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaarsgHLEIVKLL 80

                  ...
gi 1958669178 224 LHK 226
Cdd:pfam12796  81 LEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
121-208 2.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 121 RFPLHLLVWNNDYRQLEkELRDQNAEALD---PRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGD 197
Cdd:PHA02875   69 ESELHDAVEEGDVKAVE-ELLDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
                          90
                  ....*....|.
gi 1958669178 198 PEMVYTVLQHR 208
Cdd:PHA02875  148 IKGIELLIDHK 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
149-233 4.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 149 DPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMA------LEGVPE 222
Cdd:PTZ00322  112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAnakpdsFTGKPP 191
                          90
                  ....*....|....
gi 1958669178 223 LLHK---ILEAPDF 233
Cdd:PTZ00322  192 SLEDspiSSHHPDF 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
107-207 1.59e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 107 GDLLAMSSARDTSSRFPLHLL--VWNNDYRQLEKELR-DQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENG 183
Cdd:PLN03192  510 GDLLGDNGGEHDDPNMASNLLtvASTGNAALLEELLKaKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA 589
                          90       100
                  ....*....|....*....|....
gi 1958669178 184 QGWTVLHEAVSTGDPEmVYTVLQH 207
Cdd:PLN03192  590 NGNTALWNAISAKHHK-IFRILYH 612
Ank_5 pfam13857
Ankyrin repeats (many copies);
139-192 2.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958669178 139 ELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 192
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-182 8.46e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 8.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669178 116 RDTSSRFPLHLLVwNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 182
Cdd:pfam12796  26 QDKNGRTALHLAA-KNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
151-182 2.24e-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: 38.81  E-value: 2.24e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958669178 151 RGRTLLHLAV-SLGHLESARVLLRHKADVTKEN 182
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
151-178 3.59e-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: 3.59e-04
                          10        20
                  ....*....|....*....|....*...
gi 1958669178 151 RGRTLLHLAVSLGHLESARVLLRHKADV 178
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-180 9.02e-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: 9.02e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958669178  151 RGRTLLHLAVSLGHLESARVLLRHKADVTK 180
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-207 2.46e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669178 108 DLLAMSSARDTSSRFPLHLLVWNNDYRQLEKELRDQNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWT 187
Cdd:COG0666    10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89
                          90       100
                  ....*....|....*....|
gi 1958669178 188 VLHEAVSTGDPEMVYTVLQH 207
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA 109
PHA02875 PHA02875
ankyrin repeat protein; Provisional
154-205 5.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 5.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958669178 154 TLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVL 205
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
 
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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