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Conserved domains on  [gi|564379684|ref|XP_006249524|]
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ankyrin repeat domain-containing protein 13A isoform X2 [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 ...
 143-457 2.32e-129

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: 380.44  E-value: 2.32e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  143 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 221
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  222 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 294
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  295 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 374
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  375 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 454
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 564379684  455 SYH 457
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-77 9.47e-13

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 9.47e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 77
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 143-457 2.32e-129

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: 380.44  E-value: 2.32e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  143 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 221
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  222 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 294
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  295 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 374
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  375 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 454
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 564379684  455 SYH 457
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-77 9.47e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 9.47e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 77
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
28-77 1.48e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564379684   28 GRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 77
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 9-109 1.41e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684   9 GCSVSV-ILHTSNAE--ALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRD 85
Cdd:PTZ00322  93 GDAVGArILLTGGADpnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564379684  86 YHNTSMA------LEGVPELLHK---ILEAPDF 109
Cdd:PTZ00322 173 CHFELGAnakpdsFTGKPPSLEDspiSSHHPDF 205
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 27-56 7.44e-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: 7.44e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 564379684    27 RGRTLLHLAVSLGHLESARVLLRHKADVTK 56
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 ...
 143-457 2.32e-129

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: 380.44  E-value: 2.32e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  143 RVDITLLGFENMSWIRGRRSLIFKG-GDNWAELMEVNHDDRVVTTEHfDLSQEMERLTLDlmkpksrEVERRLTSPVINT 221
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGdGDSPGSLLELDHDEKEVQLEG-AGAEASEEEVEE-------EVAARLQTPIVRP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  222 SLDTKNVAFERTKSGfWGwRTDKAEVVNGYEAKVYSVNNVSVITKIRTEHLTEEEKKRYK-------EDRNPLESLLGTV 294
Cdd:pfam11904  73 GIDVTKISFERNKSG-WR-RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKsaleppeGSRTPLQSFLGIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  295 EHQFGAQGQDLTTECATVNNPTAITPDEYFDEdfdlkdrdigrPKELTIRTQKFKATLWMCEEFPLSLvEQVIPIIDLMA 374
Cdd:pfam11904 151 EEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILDLLA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  375 RTSAHFARLRDFIKLDFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEErqsVEGTQAECAASDATNFEVDQSVFEIPE 454
Cdd:pfam11904 219 NKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEE---FSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 564379684  455 SYH 457
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-77 9.47e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 9.47e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 77
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-83 1.33e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 1.33e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH 83
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-114 3.55e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 3.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMALEGVPEL 99
Cdd:COG0666  178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         90
                 ....*....|....*
gi 564379684 100 LHKILEAPDFYVQMK 114
Cdd:COG0666  258 LAAAAGAALIVKLLL 272
Ank_4 pfam13637
Ankyrin repeats (many copies);
28-77 1.48e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564379684   28 GRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMV 77
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-83 3.49e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 3.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379684   19 SNAEALDPRGRTLLHLAVSLGHLESARVLLRHKAdvTKENGQGWTVLHEAVSTGDPEMVYTVLQH 83
Cdd:pfam12796  21 ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-83 6.34e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 6.34e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379684  20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH 83
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
32-102 1.66e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684   32 LHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH-----RDYHNTSM-------ALEGVPEL 99
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHadvnlKDNGRTALhyaarsgHLEIVKLL 80


                  ...
gi 564379684  100 LHK 102
Cdd:pfam12796  81 LEK 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 9-109 1.41e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684   9 GCSVSV-ILHTSNAE--ALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRD 85
Cdd:PTZ00322  93 GDAVGArILLTGGADpnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564379684  86 YHNTSMA------LEGVPELLHK---ILEAPDF 109
Cdd:PTZ00322 173 CHFELGAnakpdsFTGKPPSLEDspiSSHHPDF 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-83 4.42e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 4.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564379684  25 DPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEmVYTVLQH 83
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYH 612
Ank_5 pfam13857
Ankyrin repeats (many copies);
20-68 6.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 6.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564379684   20 NAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEA 68
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 27-84 1.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564379684  27 RGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHR 84
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 27-58 2.10e-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: 2.10e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564379684   27 RGRTLLHLAV-SLGHLESARVLLRHKADVTKEN 58
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-58 2.20e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 564379684   24 LDPRGRTLLHLAVSLGHLESARVLLRHKADVTKEN 58
Cdd:pfam12796  57 LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 27-54 2.96e-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: 2.96e-04
                          10        20
                  ....*....|....*....|....*...
gi 564379684   27 RGRTLLHLAVSLGHLESARVLLRHKADV 54
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 27-56 7.44e-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: 7.44e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 564379684    27 RGRTLLHLAVSLGHLESARVLLRHKADVTK 56
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-81 4.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 4.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564379684  30 TLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVL 81
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-83 5.32e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.17  E-value: 5.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564379684  15 ILHTSNAEALDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQH 83
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-88 7.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379684   8 LGCSVSVilHTSNAEAldprgRTLLHLAVSLGHLESARVLLRHKADVTKENGQGWTVLHEAVSTGDPEMVYTVLQHRDYH 87
Cdd:PHA02874 111 LDCGIDV--NIKDAEL-----KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183


                 .
gi 564379684  88 N 88
Cdd:PHA02874 184 N 184
 
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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