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Conserved domains on  [gi|2462606981|ref|XP_054210689|]
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ankyrin repeat domain-containing protein 6 isoform X27 [Homo sapiens]

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];
98-188 8.35e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 8.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 177
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90
                  ....*....|.
gi 2462606981 178 NPEVALLLTKA 188
Cdd:COG0666   198 HLEIVKLLLEA 208
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-188 8.35e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 8.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 177
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90
                  ....*....|.
gi 2462606981 178 NPEVALLLTKA 188
Cdd:COG0666   198 HLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-185 3.21e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 104 LHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 2462606981 184 LL 185
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-190 1.40e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIV 162
Cdd:PTZ00322   65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                          90       100
                  ....*....|....*....|....*...
gi 2462606981 163 NNAGQTPLETARYHNNPEVALLLTKAPQ 190
Cdd:PTZ00322  145 DKDGKTPLELAEENGFREVVQLLSRHSQ 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-161 1.83e-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: 39.11  E-value: 1.83e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462606981  133 GDTALHVAAALNHKKVAKILLEAGADTTI 161
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-181 1.91e-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: 44.62  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 107 ATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAK-----IL-LEAGADT----TIVNNAGQTPLETARYH 176
Cdd:cd22192   143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLVPNNQGLTPFKLAAKE 222


                  ....*
gi 2462606981 177 NNPEV 181
Cdd:cd22192   223 GNIVM 227
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-188 8.35e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 8.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 177
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90
                  ....*....|.
gi 2462606981 178 NPEVALLLTKA 188
Cdd:COG0666   198 HLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-188 1.56e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE 180
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233


                  ....*...
gi 2462606981 181 VALLLTKA 188
Cdd:COG0666   234 IVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-185 3.00e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 3.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETAR 174
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          90
                  ....*....|.
gi 2462606981 175 YHNNPEVALLL 185
Cdd:COG0666   162 ANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-188 2.89e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYH 176
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90
                  ....*....|..
gi 2462606981 177 NNPEVALLLTKA 188
Cdd:COG0666   131 GNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-185 3.21e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 104 LHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 2462606981 184 LL 185
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-188 1.01e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNP 179
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265


                  ....*....
gi 2462606981 180 EVALLLTKA 188
Cdd:COG0666   266 LIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 5.35e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.35e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 101 QTALHRATVVGNTEIIAALIhEGCALDRQDKaGDTALHVAAALNHKKVAKILLEAGADTTIVN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-190 1.40e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIV 162
Cdd:PTZ00322   65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                          90       100
                  ....*....|....*....|....*...
gi 2462606981 163 NNAGQTPLETARYHNNPEVALLLTKAPQ 190
Cdd:PTZ00322  145 DKDGKTPLELAEENGFREVVQLLSRHSQ 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 101-188 9.14e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 101 QTALH------RAtvvgNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKI--LLEAGADTTIVNNAGQTPLET 172
Cdd:PHA03095  188 RSLLHhhlqsfKP----RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHY 263

                          90
                  ....*....|....*.
gi 2462606981 173 ARYHNNPEVALLLTKA 188
Cdd:PHA03095  264 AAVFNNPRACRRLIAL 279
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-185 9.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 9.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 133 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 185
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 2.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 121 HEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 4.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462606981 102 TALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILL 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 119-191 4.82e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 4.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606981 119 LIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 191
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
PHA03095 PHA03095
ankyrin-like protein; Provisional
 100-191 6.29e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 100 DQTALHRATVVGNTE--IIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 177
Cdd:PHA03095  222 GNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301

                          90
                  ....*....|....*
gi 2462606981 178 NPE-VALLLTKAPQV 191
Cdd:PHA03095  302 NGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-199 1.39e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 137 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-173 3.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462606981  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 173
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-188 3.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGK------VRKDPRRSER---------- 95
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKtflhyaIKKGDLESIKmlfeygadvn 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  96 -EKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETAR 174
Cdd:PHA02874  152 iEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231

                         170
                  ....*....|....
gi 2462606981 175 YHNNPEVALLLTKA 188
Cdd:PHA02874  232 IHNRSAIELLINNA 245
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-164 6.03e-06

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: 43.43  E-value: 6.03e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462606981 133 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 164
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-170 3.31e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462606981 102 TALHRATVVGNTE-IIAALIHEGCALDRQDKAGDTALHV-AAALN-HKKVAKILLEAGADTTIVNNAGQTPL 170
Cdd:PHA03095   85 TPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-172 1.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHK-KVAKILLEAGADTTIVNNAGQTPLET 172
Cdd:PHA03095   44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHV 123
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-161 1.83e-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: 39.11  E-value: 1.83e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462606981  133 GDTALHVAAALNHKKVAKILLEAGADTTI 161
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-181 1.91e-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: 44.62  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 107 ATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAK-----IL-LEAGADT----TIVNNAGQTPLETARYH 176
Cdd:cd22192   143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLVPNNQGLTPFKLAAKE 222


                  ....*
gi 2462606981 177 NNPEV 181
Cdd:cd22192   223 GNIVM 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-187 6.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981 102 TALHRA--TVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNH--KKVAKILLEAGAD----------------TTI 161
Cdd:PHA03100  108 TPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDinaknrvnyllsygvpINI 187

                          90       100
                  ....*....|....*....|....*..
gi 2462606981 162 VNNAGQTPLETARYHNNPE-VALLLTK 187
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEfVKYLLDL 214
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-173 9.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  99 GDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAA---------------------------------ALNH 145
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgyckdydilklllehgvdvnaksyilgltalhsSIKS 279

                          90       100
                  ....*....|....*....|....*...
gi 2462606981 146 KKVAKILLEAGADTTIVNNAGQTPLETA 173
Cdd:PHA02878  280 ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-164 1.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 102 TALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 164
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 22-189 1.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  22 DYATPGANSFLLPANRVNShwSANAISDWS--MSNHIAPASEIVQDAVATVKAMKEDKNKKnHRGKVRKDPRRSE-REKE 98
Cdd:cd22194    16 DMDSPQSPQDDTPSNPNSP--SAELAKEEQrdKKKRLKKVSEAAVEELGELLKELKDLSRR-RRKTDVPDFLMHKlTASD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  99 GDQTALHRA--TVVGNT-EIIAALI----HEGCaLDR--------QDKAGDTALHVAAALNHKKVAKILLEAGADTTI-- 161
Cdd:cd22194    93 TGKTCLMKAllNINENTkEIVRILLafaeENGI-LDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAha 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462606981 162 -------VNNA-----GQTPLETARYHNNPE-VALLLTKAP 189
Cdd:cd22194   172 kgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-196 1.80e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606981  97 KEGDqTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYH 176
Cdd:PHA02875  100 KDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          90       100
                  ....*....|....*....|.
gi 2462606981 177 NNPEVA-LLLTKAPQVLRFSR 196
Cdd:PHA02875  179 GDIAICkMLLDSGANIDYFGK 199
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-185 2.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 2.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462606981 113 TEIIAALIHEGCALDRQDK-AGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA-RYHNNPEVALLL 185
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAvKHYNKPIVHILL 221
PHA02946 PHA02946
ankyin-like protein; Provisional
 112-170 2.65e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 2.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462606981 112 NTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 170
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-191 3.92e-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: 3.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462606981 133 GDTALHVAAALNHKKVAKILLEagADTTIVNNA-------GQTPLETARYHNNPE-VALLLTKAPQV 191
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHIAVVNQNLNlVRELIARGADV 115
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 4.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 4.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462606981  86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGDTALHVA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 111-163 4.76e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 4.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462606981 111 GNTEIIAALIHEGCALDRQDKAGDTALHVAAALNHKKVAKILLEAGADTTIVN 163
Cdd:PLN03192  633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-158 4.99e-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: 34.93  E-value: 4.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462606981 133 GDTALHVAAALNHKKVAKILLEAGAD 158
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
 
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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