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Conserved domains on  [gi|1907151174|ref|XP_036019044|]
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ankyrin repeat domain-containing protein 13C isoform X1 [Mus musculus]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-199 4.30e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1907151174 194 TALLRK 199
Cdd:COG0666   203 KLLLEA 208
GPCR_chapero_1 super family cl46312
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-302 7.29e-12

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.


The actual alignment was detected with superfamily member pfam11904:

Pssm-ID: 480652  Cd Length: 298  Bit Score: 64.96  E-value: 7.29e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907151174 259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ 302
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQ 44
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-199 4.30e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1907151174 194 TALLRK 199
Cdd:COG0666   203 KLLLEA 208
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-302 7.29e-12

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: 64.96  E-value: 7.29e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907151174 259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ 302
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQ 44
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-199 1.15e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 117 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 195
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1907151174 196 LLRK 199
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-198 8.35e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 8.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 190
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                  ....*...
gi 1907151174 191 QMITALLR 198
Cdd:PHA02875  149 KGIELLID 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-168 7.19e-05

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: 39.11  E-value: 7.19e-05
                           10        20
                   ....*....|....*....|....*.
gi 1907151174  143 HGNTPLHLAVMLGNKECAHLLLAHNA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 111-199 1.79e-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: 43.08  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 111 PSLYPVHECVFKGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLA 182
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALH 94

                          90
                  ....*....|....*..
gi 1907151174 183 EAISYGDRQMITALLRK 199
Cdd:cd22192    95 IAVVNQNLNLVRELIAR 111
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-199 4.30e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.22  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1907151174 194 TALLRK 199
Cdd:COG0666   203 KLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-199 1.12e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169


                  ....*.
gi 1907151174 194 TALLRK 199
Cdd:COG0666   170 KLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-229 5.71e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907151174 194 TALLRKLKQQSRESVGEKRPRLLKALKELGDFYLEL 229
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 259-302 7.29e-12

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: 64.96  E-value: 7.29e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907151174 259 RLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQ 302
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQ 44
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
131-199 5.58e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 5.58e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907151174 131 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-199 1.15e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 117 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 195
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 1907151174 196 LLRK 199
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-198 8.35e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 8.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 190
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                  ....*...
gi 1907151174 191 QMITALLR 198
Cdd:PHA02875  149 KGIELLID 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-207 2.33e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 2.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 148 LHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRKLKQQSRES 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
Ank_4 pfam13637
Ankyrin repeats (many copies);
144-197 2.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907151174 144 GNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 197
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-174 6.65e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 6.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRtHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKN 174
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 146-197 5.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 5.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907151174 146 TPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 197
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-201 9.44e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.49  E-value: 9.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 193
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268


                  ....*...
gi 1907151174 194 TALLRKLK 201
Cdd:COG0666   269 KLLLLALL 276
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 140-197 1.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 1.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151174 140 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYgDRQMITALL 197
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-174 1.74e-05

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: 41.12  E-value: 1.74e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907151174 143 HGNTPLHLAV-MLGNKECAHLLLAHNAPVKVKN 174
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-197 1.87e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 116 VHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMIT 194
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGaDVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207


                  ...
gi 1907151174 195 ALL 197
Cdd:PHA02874  208 LLI 210
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-197 3.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 115 PVHECVFKGDVRRLSSLI-RTHNIGQKDNHGNTPLHLAVmLGNKECAHLLLaHNAPVKVKNAQGWSPLAEAISYG-DRQM 192
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIdHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDI 270


                  ....*
gi 1907151174 193 ITALL 197
Cdd:PHA02874  271 IDILL 275
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-184 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 4.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907151174 136 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEA 184
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-168 7.19e-05

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: 39.11  E-value: 7.19e-05
                           10        20
                   ....*....|....*....|....*.
gi 1907151174  143 HGNTPLHLAVMLGNKECAHLLLAHNA 168
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 141-188 1.02e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907151174 141 DNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYG 188
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 111-199 1.79e-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: 43.08  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 111 PSLYPVHECVFKGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLA 182
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALH 94

                          90
                  ....*....|....*..
gi 1907151174 183 EAISYGDRQMITALLRK 199
Cdd:cd22192    95 IAVVNQNLNLVRELIAR 111
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-170 2.56e-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: 37.62  E-value: 2.56e-04
                          10        20
                  ....*....|....*....|....*...
gi 1907151174 143 HGNTPLHLAVMLGNKECAHLLLAHNAPV 170
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-198 5.12e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 5.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907151174 140 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 198
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-164 8.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 8.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907151174 115 PVHECVFKGDVRRLSSLI-RTHNIGQKDNHGNTPLHLAVMLGNKECAHLLL 164
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
131-199 1.50e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.94  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907151174 131 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-201 2.83e-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: 39.23  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 119 CVFKGDVRRLssLIRTH-NIGQKDNHGNTPLHLAVMLGNKECA----HLLLAHNAPVK------VKNAQGWSPLAEAISY 187
Cdd:cd22192   145 CVGNEEIVRL--LIEHGaDIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKE 222

                          90
                  ....*....|....
gi 1907151174 188 GDRQMITALLRKLK 201
Cdd:cd22192   223 GNIVMFQHLVQKRR 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 136-198 3.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 3.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907151174 136 NIGQKDNH-GNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 198
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
PHA03095 PHA03095
ankyrin-like protein; Provisional
 141-199 4.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 4.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 141 DNHGNTPLHLAVMLGNKE-CAHLLLAhNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 199
Cdd:PHA03095  254 NRYGQTPLHYAAVFNNPRaCRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-198 4.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907151174 136 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 198
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 136-258 6.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 136 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLrklkqQSRESVGEKRPRL 215
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSNINKNDLSL 244

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 216 LKALKELG-----------------DFYLELHWDFQSWVPLLSRILPsdacKIYKQGINI 258
Cdd:PHA02876  245 LKAIRNEDletslllydagfsvnsiDDCKNTPLHHASQAPSLSRLVP----KLLERGADV 300
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 131-228 7.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151174 131 LIRTHNIGQKDNHGNTPLHLAVMLG-NKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI------TALLRKLKQQ 203
Cdd:PHA02874  241 LINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikdiiaNAVLIKEADK 320

                          90       100
                  ....*....|....*....|....*
gi 1907151174 204 SRESVGEKRPRLLKAlKELGDFYLE 228
Cdd:PHA02874  321 LKDSDFLEHIEIKDN-KEFSDFIKE 344
 
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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