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Conserved domains on  [gi|407728607|ref|NP_001258398|]
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GA-binding protein subunit beta-1 isoform f [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 2.41e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                 ....
gi 407728607  89 VLLK 92
Cdd:COG0666  204 LLLE 207
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 2.41e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                 ....
gi 407728607  89 VLLK 92
Cdd:COG0666  204 LLLE 207
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-92 1.90e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607   10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                  ....
gi 407728607   89 VLLK 92
Cdd:pfam12796  79 LLLE 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
6-92 5.34e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                 ....*...
gi 407728607  85 NIVEVLLK 92
Cdd:PTZ00322 162 EVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
71-93 1.94e-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: 36.80  E-value: 1.94e-04
                           10        20
                   ....*....|....*....|...
gi 407728607    71 DRTPLHMAASEGHANIVEVLLKE 93
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
10-92 2.93e-04

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: 39.61  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95
                         90
                 ....*....|....*
gi 407728607  78 AASEGHANIVEVLLK 92
Cdd:cd22192   96 AVVNQNLNLVRELIA 110
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 2.41e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                 ....
gi 407728607  89 VLLK 92
Cdd:COG0666  204 LLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 1.42e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                 ....
gi 407728607  89 VLLK 92
Cdd:COG0666  171 LLLE 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-92 1.90e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607   10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                  ....
gi 407728607   89 VLLK 92
Cdd:pfam12796  79 LLLE 82
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-131 5.74e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 5.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 407728607  89 VLLKEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEA 131
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-93 2.74e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 2.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 407728607   42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKE 93
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 3.32e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 407728607   38 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
6-92 5.34e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                 ....*...
gi 407728607  85 NIVEVLLK 92
Cdd:PTZ00322 162 EVVQLLSR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-92 1.40e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                 ....
gi 407728607  89 VLLK 92
Cdd:COG0666  138 LLLE 141
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-106 3.65e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.64  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
                         90
                 ....*....|....*...
gi 407728607  89 VLLKEREALQKQLDEANR 106
Cdd:COG0666  270 LLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-92 1.31e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 92
Cdd:PHA03095  64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140
PHA02876 PHA02876
ankyrin repeat protein; Provisional
14-104 4.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  14 ARAGQDDE-VRILMANGAPFT-TDWLGTSPLHLAAQYGHFSTTEV-LLRAGVSRDARTKVDRTPLHMAASEGHANIVEVL 90
Cdd:PHA02876 315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
                         90
                 ....*....|....*..
gi 407728607  91 LK---EREALQKQLDEA 104
Cdd:PHA02876 395 LDygaDIEALSQKIGTA 411
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
34-92 7.08e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 7.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 407728607  34 TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLK 92
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK 579
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-79 1.94e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 1.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407728607  22 VRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEV--LLRAGVSRDARTKVDRTPLHMAA 79
Cdd:PHA03095 205 VRELIRAGCdPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-63 5.33e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 5.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 407728607   10 LLEAARAGQDDEVRILMANGAPFTTDwLGTSPLHLAAQYGHFSTTEVLLRAGVS 63
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
13-94 8.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 8.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  13 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHAnIVEVLL 91
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVkDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242

                 ...
gi 407728607  92 KER 94
Cdd:PHA02874 243 NNA 245
PHA02875 PHA02875
ankyrin repeat protein; Provisional
5-97 1.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607   5 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASE 81
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145
                         90
                 ....*....|....*.
gi 407728607  82 GHANIVEVLLKEREAL 97
Cdd:PHA02875 146 GDIKGIELLIDHKACL 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
71-93 1.94e-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: 36.80  E-value: 1.94e-04
                           10        20
                   ....*....|....*....|...
gi 407728607    71 DRTPLHMAASEGHANIVEVLLKE 93
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 2.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 407728607   10 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
10-92 2.93e-04

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: 39.61  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95
                         90
                 ....*....|....*
gi 407728607  78 AASEGHANIVEVLLK 92
Cdd:cd22192   96 AVVNQNLNLVRELIA 110
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 3.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 407728607   30 APFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
22-92 5.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 5.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407728607  22 VRILMANGAPFT--TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLK 92
Cdd:PHA02878 150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
20-92 7.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.11  E-value: 7.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407728607  20 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLK 92
Cdd:PHA03100 173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA02878 PHA02878
ankyrin repeat protein; Provisional
5-80 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728607   5 DLGKKLLEAARAGQD-DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAAS 80
Cdd:PHA02878 166 HKGNTALHYATENKDqRLTELLLSYGAnVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
38-69 1.43e-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. 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: 34.57  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 407728607   38 GTSPLHLAA-QYGHFSTTEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
13-98 4.21e-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: 36.14  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728607  13 AARAGQDDEVRILMANGA-PFTTDWLGTSPLH-LAAQYGHFSTTEV--LLRAGVSRDARTKVDR-------TPLHMAASE 81
Cdd:cd22192  143 AACVGNEEIVRLLIEHGAdIRAQDSLGNTVLHiLVLQPNKTFACQMydLILSYDKEDDLQPLDLvpnnqglTPFKLAAKE 222
                         90
                 ....*....|....*..
gi 407728607  82 GHANIVEVLLKEREALQ 98
Cdd:cd22192  223 GNIVMFQHLVQKRRHIQ 239
PHA02875 PHA02875
ankyrin repeat protein; Provisional
20-91 4.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 36.12  E-value: 4.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407728607  20 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 91
Cdd:PHA02875 116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-97 4.98e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.47  E-value: 4.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 407728607   57 LLRAG-VSRDARTKVDRTPLHMAASEGHANIVEVLLKEREAL 97
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDL 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
72-92 5.68e-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: 32.61  E-value: 5.68e-03
                          10        20
                  ....*....|....*....|.
gi 407728607   72 RTPLHMAASEGHANIVEVLLK 92
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLE 23
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-98 6.63e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 35.39  E-value: 6.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407728607  34 TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKEREALQ 98
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
24-90 9.88e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 35.23  E-value: 9.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407728607  24 ILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVL 90
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
 
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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