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Conserved domains on  [gi|568998420|ref|XP_006523441|]
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ankyrin repeat domain-containing protein 66 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];
8-178 2.96e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 2.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   8 DMTKLHQAVAAGDCNSVKKILKKGLcDPNYKDadWNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGA-DVNAQD--NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFLEIAEPECRDHRQRGLLLDERDPDWDLKRRELELSLPAP 167
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276

                        170
                 ....*....|.
gi 568998420 168 DQNSNKKKKRI 178
Cdd:COG0666  277 LLAAALLDLLT 287
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-178 2.96e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 2.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   8 DMTKLHQAVAAGDCNSVKKILKKGLcDPNYKDadWNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGA-DVNAQD--NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFLEIAEPECRDHRQRGLLLDERDPDWDLKRRELELSLPAP 167
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276

                        170
                 ....*....|.
gi 568998420 168 DQNSNKKKKRI 178
Cdd:COG0666  277 LLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-96 1.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   12 LHQAVAAGDCNSVKKILKKGlCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGArpCLVTDVGWTAAHFAAESGHLN 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDK--NGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLE 75


                  ....*
gi 568998420   92 VLKAL 96
Cdd:pfam12796  76 IVKLL 80
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-121 1.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  10 TKLHQAVAAGDCNSVKKILKKG--LCDPNYKDADwndrTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM----TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYG 121
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 43-68 1.13e-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: 40.65  E-value: 1.13e-05
                           10        20
                   ....*....|....*....|....*.
gi 568998420    43 NDRTPLHWAAIRGQMEVIHLLIQYGA 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-96 8.13e-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: 36.53  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  12 LHQAVAAGDCNSVKKILKKGLCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQygARPCLVTDV-------GWTAAHFA 84
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHIA 96

                         90
                 ....*....|..
gi 568998420  85 AESGHLNVLKAL 96
Cdd:cd22192   97 VVNQNLNLVREL 108
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 44-119 8.16e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   44 DRTPLHWAAIRGQMEVIHLLIQYGAR--------PCLVTDVGWTAAH------FAAESGHLNVLKALHALPSAIDAADFF 109
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASvparacgdFFVKSQGVDSFYHgesplnAAACLGSPSIVALLSEDPADILTADSL 207

                          90
                  ....*....|
gi 568998420  110 GDTPKRIAQI 119
Cdd:TIGR00870 208 GNTLLHLLVM 217
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-178 2.96e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 2.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   8 DMTKLHQAVAAGDCNSVKKILKKGLcDPNYKDadWNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGA-DVNAQD--NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFLEIAEPECRDHRQRGLLLDERDPDWDLKRRELELSLPAP 167
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276

                        170
                 ....*....|.
gi 568998420 168 DQNSNKKKKRI 178
Cdd:COG0666  277 LLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-96 1.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   12 LHQAVAAGDCNSVKKILKKGlCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGArpCLVTDVGWTAAHFAAESGHLN 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDK--NGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLE 75


                  ....*
gi 568998420   92 VLKAL 96
Cdd:pfam12796  76 IVKLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-129 3.39e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   48 LHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKALhaLPSAIDAADFFGDTPKRIAQIYGQKDCVD 127
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDNGRTALHYAARSGHLEIVK 78


                  ..
gi 568998420  128 FL 129
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-129 3.95e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 3.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   4 SKIADMTKLHQAVAAGDCNSVKKILKKGLCDPNYKDADWNdrTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHF 83
Cdd:COG0666   49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568998420  84 AAESGHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFL 129
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
45-97 2.28e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568998420   45 RTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKALH 97
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-121 1.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  10 TKLHQAVAAGDCNSVKKILKKG--LCDPNYKDADwndrTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkfADDVFYKDGM----TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYG 121
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 21-96 4.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 4.89e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568998420  21 CNSVKKILKKGlCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKAL 96
Cdd:PHA03100 172 KNRVNYLLSYG-VPINIKDV--YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-96 3.13e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   6 IADM--TKLHQAVAAGDCNSVKKILKKGlCDPNYKDADwnDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHF 83
Cdd:PTZ00322  78 VAHMltVELCQLAASGDAVGARILLTGG-ADPNCRDYD--GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154

                         90
                 ....*....|...
gi 568998420  84 AAESGHLNVLKAL 96
Cdd:PTZ00322 155 AEENGFREVVQLL 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-129 1.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  22 NSVKKILKKGLcDPNYKDADwnDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKALHALPS 101
Cdd:PHA02874 105 DMIKTILDCGI-DVNIKDAE--LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100
                 ....*....|....*....|....*...
gi 568998420 102 AIDAADFFGDTPKRIAQIYGQKDCVDFL 129
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLL 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-70 4.20e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 4.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568998420    9 MTKLHQAVAAGDCNSVKKILKKglCDPNYKDadwNDRTPLHWAAIRGQMEVIHLLIQYGARP 70
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH--ADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-129 4.94e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.80  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   6 IADMTKLHQAVAAGDCNSVKKILKKGLCDPNYKDADWNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAA 85
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568998420  86 ESGHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFL 129
Cdd:COG0666   96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-108 2.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  24 VKKILKKGLCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKALHALPSAI 103
Cdd:PHA02876 160 IAEMLLEGGADVNAKDI--YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237


                 ....*
gi 568998420 104 DAADF 108
Cdd:PHA02876 238 NKNDL 242
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-64 4.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568998420    9 MTKLHQAVAAGDCNSVKKILKKGLcDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLI 64
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGA-DINAVDG--NGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-117 5.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 5.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568998420   63 LIQYGARPCLVTDVGW-TAAHFAAESGHLNVLKALHALPSAIDAADFFGDTPKRIA 117
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 10-129 1.00e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  10 TKLHQAVAAGDCNSVKKILKKGlCDPNYKDADWNdrTPLHWAAIRGQMEVIHLLIQYGA--RPCLVTDVgwtaAHFAAES 87
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGN--TALWNAISAKHHKIFRILYHFASisDPHAAGDL----LCTAAKR 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568998420  88 GHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFL 129
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-129 1.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568998420   77 GWTAAHFAAESGHLNVLKALHALPSAIDAADFFGDTPKRIAQIYGQKDCVDFL 129
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 43-68 1.13e-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: 40.65  E-value: 1.13e-05
                           10        20
                   ....*....|....*....|....*.
gi 568998420    43 NDRTPLHWAAIRGQMEVIHLLIQYGA 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-120 2.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  10 TKLHQAVAAGDCNSVKKILKKGlCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGH 89
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYG-ADVNIEDD--NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568998420  90 LNVLKALHALPSAIDAADFFGDTPKRIAQIY 120
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-96 3.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   9 MTKLHQAVAAGDCNSVKKILKKGlCDPNYKDAdwNDRTPLHWAA-----IRGQMEVIHLLIQYGARPCLVTDVGWTAAHF 83
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNG-ADINSSTK--NNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90
                 ....*....|....*
gi 568998420  84 AA--ESGHLNVLKAL 96
Cdd:PHA03100 113 AIskKSNSYSIVEYL 127
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 43-75 7.97e-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: 38.42  E-value: 7.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568998420   43 NDRTPLHWAAIR-GQMEVIHLLIQYGARPCLVTD 75
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-84 1.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568998420  10 TKLHQAVAAG-DCNSVKKILKKGlcdPNYKDADWNDRTPLHWAAIRGQMEVIHLLIQYGAR-PCLVTDVGwTAAHFA 84
Cdd:PHA02876 343 TPLHQASTLDrNKDIVITLLELG---ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIG-TALHFA 415
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 43-68 2.59e-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: 36.85  E-value: 2.59e-04
                          10        20
                  ....*....|....*....|....*.
gi 568998420   43 NDRTPLHWAAIRGQMEVIHLLIQYGA 68
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 24-117 2.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  24 VKKILKKGlCDPNYKDADwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAESGHLNVLKALHALPSAI 103
Cdd:PHA02878 150 TKLLLSYG-ADINMKDRH-KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90
                 ....*....|....
gi 568998420 104 DAADFFGDTPKRIA 117
Cdd:PHA02878 228 DARDKCGNTPLHIS 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 7-121 4.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.31  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   7 ADMTKLHqAVAAGDC---NSVKKILKKGLcDPNYKDADwnDRTPLHwAAIRGQ---MEVIHLLIQYGARPCLVTDVGWTA 80
Cdd:PHA03095 116 VGRTPLH-VYLSGFNinpKVIRLLLRKGA-DVNALDLY--GMTPLA-VLLKSRnanVELLRLLIDAGADVYAVDDRFRSL 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568998420  81 AHFAAESGHLN--VLKALHALPSAIDAADFFGDTPKRIAQIYG 121
Cdd:PHA03095 191 LHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGS 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
27-84 4.70e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568998420   27 ILKKGLCDPNYKDADWNdrTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFA 84
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGY--TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-96 8.13e-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: 36.53  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  12 LHQAVAAGDCNSVKKILKKGLCDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQygARPCLVTDV-------GWTAAHFA 84
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHIA 96

                         90
                 ....*....|..
gi 568998420  85 AESGHLNVLKAL 96
Cdd:cd22192   97 VVNQNLNLVREL 108
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 44-119 8.16e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420   44 DRTPLHWAAIRGQMEVIHLLIQYGAR--------PCLVTDVGWTAAH------FAAESGHLNVLKALHALPSAIDAADFF 109
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASvparacgdFFVKSQGVDSFYHgesplnAAACLGSPSIVALLSEDPADILTADSL 207

                          90
                  ....*....|
gi 568998420  110 GDTPKRIAQI 119
Cdd:TIGR00870 208 GNTLLHLLVM 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-106 9.34e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 36.16  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  10 TKLHQAVAAGDCNS--VKKILKKGLcDPNYKDAdwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGWTAAHFAAES 87
Cdd:PHA03095 224 TPLHSMATGSSCKRslVLPLLIAGI-SINARNR--YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300

                         90       100
                 ....*....|....*....|..
gi 568998420  88 GHLNVLKA-LHALPSA--IDAA 106
Cdd:PHA03095 301 NNGRAVRAaLAKNPSAetVAAT 322
PHA02791 PHA02791
ankyrin-like protein; Provisional
 12-106 9.62e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 35.79  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998420  12 LHQAVAAGDCNSVKKILKKGLCDPNYKDadwNDRTPLHWAAIRGQMEVIHLLIQYGARPCLVTDVGW-TAAHFAAESGHL 90
Cdd:PHA02791  65 LHQAATLEDTKIVKILLFSGMDDSQFDD---KGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDV 141

                         90
                 ....*....|....*..
gi 568998420  91 NVLKA-LHALPSAIDAA 106
Cdd:PHA02791 142 SIVSYfLSEIPSTFDLA 158
 
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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