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Conserved domains on  [gi|971421337|ref|XP_415193|]
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ankyrin repeat domain-containing protein 13A isoform X1 [Gallus gallus]

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 ...
 157-470 2.69e-126

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: 373.12  E-value: 2.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  157 RVDITLLGFENMSWERGRRSLIFKGEDAEGwAELIEINHDDKFVTTE--RFEISQHMerltlgsmtpKRREVERRLTTPI 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSP-GSLLELDHDEKEVQLEgaGAEASEEE----------VEEEVAARLQTPI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  235 INTCLDTKSIAFERTTSGFWvwRTEKAEGVNGYEAKVYMANNVNVVTKIRTEHLTEEEKKRYKAD-------RSPLESFL 307
Cdd:pfam11904  70 VRPGIDVTKISFERNKSGWR--RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  308 GTVEHEYGVQSAVKTTEYATSNNPTAITPEEYFDPefdlkgrdigrPKEVTIRTQKFKATLWMSEEFPLSLvEQVTPIID 387
Cdd:pfam11904 148 GIAEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILD 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  388 LMARTSAHFARLRDFITLEFPPGFPVKIEIPLFHVLNARITFENVNSCRTAERTSQTVGSAQGDSGANFEVDQSVFEIPK 467
Cdd:pfam11904 216 LLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 971421337  468 SYH 470
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-97 3.62e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  13 PLHVLVWNNEYRRLDEELQDQ-DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMV 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169


                 ....*.
gi 971421337  92 HMILQH 97
Cdd:COG0666  170 KLLLEA 175
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 157-470 2.69e-126

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: 373.12  E-value: 2.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  157 RVDITLLGFENMSWERGRRSLIFKGEDAEGwAELIEINHDDKFVTTE--RFEISQHMerltlgsmtpKRREVERRLTTPI 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSP-GSLLELDHDEKEVQLEgaGAEASEEE----------VEEEVAARLQTPI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  235 INTCLDTKSIAFERTTSGFWvwRTEKAEGVNGYEAKVYMANNVNVVTKIRTEHLTEEEKKRYKAD-------RSPLESFL 307
Cdd:pfam11904  70 VRPGIDVTKISFERNKSGWR--RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  308 GTVEHEYGVQSAVKTTEYATSNNPTAITPEEYFDPefdlkgrdigrPKEVTIRTQKFKATLWMSEEFPLSLvEQVTPIID 387
Cdd:pfam11904 148 GIAEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILD 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  388 LMARTSAHFARLRDFITLEFPPGFPVKIEIPLFHVLNARITFENVNSCRTAERTSQTVGSAQGDSGANFEVDQSVFEIPK 467
Cdd:pfam11904 216 LLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 971421337  468 SYH 470
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-97 3.62e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  13 PLHVLVWNNEYRRLDEELQDQ-DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMV 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169


                 ....*.
gi 971421337  92 HMILQH 97
Cdd:COG0666  170 KLLLEA 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 4.00e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 4.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971421337   42 GRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMIL 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-97 2.33e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 2.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971421337  26 LDEELQ-DQDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHmILQH 97
Cdd:PLN03192 541 LEELLKaKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYH 612
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.08e-03

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: 36.80  E-value: 1.08e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 971421337    41 RGRTLLHLAVSLGYIESAKVLLQHKADVTK 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-108 3.55e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKAD-----VTKENAQGWTVLHEAISTGDPEMVHMILQHRDYQQTSRTLG 108
Cdd:cd22192   43 DLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATG 122
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 157-470 2.69e-126

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: 373.12  E-value: 2.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  157 RVDITLLGFENMSWERGRRSLIFKGEDAEGwAELIEINHDDKFVTTE--RFEISQHMerltlgsmtpKRREVERRLTTPI 234
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSP-GSLLELDHDEKEVQLEgaGAEASEEE----------VEEEVAARLQTPI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  235 INTCLDTKSIAFERTTSGFWvwRTEKAEGVNGYEAKVYMANNVNVVTKIRTEHLTEEEKKRYKAD-------RSPLESFL 307
Cdd:pfam11904  70 VRPGIDVTKISFERNKSGWR--RQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSAleppegsRTPLQSFL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  308 GTVEHEYGVQSAVKTTEYATSNNPTAITPEEYFDPefdlkgrdigrPKEVTIRTQKFKATLWMSEEFPLSLvEQVTPIID 387
Cdd:pfam11904 148 GIAEEEKGWFGKTREESEAPPTNPTALTPEEYFDP-----------PKEESEKKKGFKATLWLSEDFPLSL-EQLLPILD 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  388 LMARTSAHFARLRDFITLEFPPGFPVKIEIPLFHVLNARITFENVNSCRTAERTSQTVGSAQGDSGANFEVDQSVFEIPK 467
Cdd:pfam11904 216 LLANKVKHFRRLREFITLKLPPGFPVKIEIPVFPTVNARITFTKFEELDPVEEFSTPIKSPERGSPSSCEIDDDPFEIPS 295


                  ...
gi 971421337  468 SYH 470
Cdd:pfam11904 296 GYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-97 3.62e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  13 PLHVLVWNNEYRRLDEELQDQ-DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMV 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169


                 ....*.
gi 971421337  92 HMILQH 97
Cdd:COG0666  170 KLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-97 1.64e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 1.64e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMILQH 97
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-98 1.04e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 1.04e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMILQHR 98
Cdd:COG0666  178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-97 3.69e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  10 DAFPLHVLVWNNEYRRLDEELQDQDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPE 89
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134


                 ....*...
gi 971421337  90 MVHMILQH 97
Cdd:COG0666  135 IVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 4.00e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 4.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971421337   42 GRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMIL 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-97 4.14e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971421337   34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKAdvTKENAQGWTVLHEAISTGDPEMVHMILQH 97
Cdd:pfam12796  22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-103 2.88e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 2.88e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971421337   46 LHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMV-----HMILQHRDYQQT 103
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkllleHADVNLKDNGRT 63
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-97 2.33e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 2.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971421337  26 LDEELQ-DQDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHmILQH 97
Cdd:PLN03192 541 LEELLKaKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYH 612
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-97 8.31e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 8.31e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMILQH 97
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-95 2.08e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  13 PLHVLVWNNeyrRLD--EELQDQ--DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDP 88
Cdd:COG0666  189 PLHLAAENG---HLEivKLLLEAgaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265


                 ....*..
gi 971421337  89 EMVHMIL 95
Cdd:COG0666  266 LIVKLLL 272
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-98 4.77e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  13 PLHVLVWNNEYRRLDEELQD----QDVDQRDprGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDP 88
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90
                 ....*....|
gi 971421337  89 EMVHMILQHR 98
Cdd:PHA02875 149 KGIELLIDHK 158
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-97 8.53e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337   8 ASDAFPLHVLVWNNEYRRLDEELQDQDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGD 87
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90
                 ....*....|
gi 971421337  88 PEMVHMILQH 97
Cdd:COG0666  100 LEIVKLLLEA 109
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-82 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971421337   29 ELQDQDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEA 82
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-111 1.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 1.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMILQHRDYQQTSRTLGGVP 111
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-72 1.55e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 971421337   30 LQDQDVDQRDpRGRTLLHLAVSLGYIESAKVLLQHKADVTKEN 72
Cdd:pfam12796  50 LEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 34-99 3.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 3.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMILQHRD 99
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 32-95 4.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 4.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971421337  32 DQDVDQRDPRgrTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTGDPEMVHMIL 95
Cdd:PHA02875 127 DPDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-72 5.62e-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: 37.65  E-value: 5.62e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 971421337   41 RGRTLLHLAV-SLGYIESAKVLLQHKADVTKEN 72
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.08e-03

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: 36.80  E-value: 1.08e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 971421337    41 RGRTLLHLAVSLGYIESAKVLLQHKADVTK 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-97 1.84e-03

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: 36.03  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|....
gi 971421337    74 QGWTVLHEAISTGDPEMVHMILQH 97
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-68 1.96e-03

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: 36.08  E-value: 1.96e-03
                          10        20
                  ....*....|....*....|....*...
gi 971421337   41 RGRTLLHLAVSLGYIESAKVLLQHKADV 68
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02795 PHA02795
ankyrin-like protein; Provisional
 33-86 2.63e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.36  E-value: 2.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 971421337  33 QDVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKADVTKENAQGWTVLHEAISTG 86
Cdd:PHA02795 212 EDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-108 3.55e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971421337  34 DVDQRDPRGRTLLHLAVSLGYIESAKVLLQHKAD-----VTKENAQGWTVLHEAISTGDPEMVHMILQHRDYQQTSRTLG 108
Cdd:cd22192   43 DLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATG 122
 
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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