NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1953086860|ref|XP_038399576|]
View 

ankyrin repeat domain-containing protein 29 isoform X3 [Canis lupus familiaris]

Protein Classification

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

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-249 8.64e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHM 94
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  95 QVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRD 174
Cdd:COG0666   134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953086860 175 AARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPA 249
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-249 8.64e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHM 94
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  95 QVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRD 174
Cdd:COG0666   134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953086860 175 AARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPA 249
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-110 2.80e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  19 LMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEfrTKDGGTALLAASQYGHMQVVE 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1953086860  99 TLLKHGANIHDQ 110
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 13-140 9.66e-19

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 9.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTkdGGTALLAASQYG 92
Cdd:PLN03192  556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRN 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953086860  93 HMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 140
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 35-226 1.84e-11

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: 63.88  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  35 VLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHGAN-----I 107
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAAPElvnepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 108 HDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADR 173
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953086860 174 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 226
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-189 4.60e-05

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: 44.30  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  40 DINLQRESGPTALFFAAQQGHNDVVRFLFEFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 108
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 109 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 171
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1953086860 172 DRDAARNDGTTaLLKAAN 189
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-141 3.14e-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: 37.18  E-value: 3.14e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953086860  113 DGATALFLAAQGGYLDVIRLLLSSGAKVN 141
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-249 8.64e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHM 94
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  95 QVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRD 174
Cdd:COG0666   134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953086860 175 AARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPA 249
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-201 1.56e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYG 92
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  93 HMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 172
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                         170       180
                  ....*....|....*....|....*....
gi 1953086860 173 RDAARNDGTTALLKAANKGYNDVIEELLK 201
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-262 2.55e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 2.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  16 TTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQ 95
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  96 VVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDA 175
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 176 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPAELTKN 254
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261


                  ....*...
gi 1953086860 255 ERILRLLR 262
Cdd:COG0666   262 AGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-184 6.71e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 6.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYG 92
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  93 HMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 172
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277

                         170
                  ....*....|..
gi 1953086860 173 RDAARNDGTTAL 184
Cdd:COG0666   278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-264 9.62e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 9.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  31 VRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQ 110
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 111 LYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANK 190
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953086860 191 GYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELP---AELTKNERILRLLRSK 264
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAldlAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-110 2.80e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  19 LMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEfrTKDGGTALLAASQYGHMQVVE 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1953086860  99 TLLKHGANIHDQ 110
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-142 4.17e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 4.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  52 LFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1953086860 132 LLLSSGAKVNQ 142
Cdd:pfam12796  79 LLLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 13-140 9.66e-19

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 9.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTkdGGTALLAASQYG 92
Cdd:PLN03192  556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRN 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953086860  93 HMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 140
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-242 1.66e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 151 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNIKTVAL 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1953086860 231 LLEAGADPALRN 242
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-172 3.89e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  85 LLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1953086860 165 VMLLRGAD 172
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-261 5.53e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 5.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  94 MQVVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVM 166
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 167 LLRGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKT 227
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1953086860 228 VALLLEAGADPALRNKANELPAE---LTKNERILRLL 261
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-179 3.96e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  18 LLMVASyAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVV 97
Cdd:PLN03192  529 LLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  98 EtLLKHGANIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAAR 177
Cdd:PLN03192  608 R-ILYHFASISDP-HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685


                  ..
gi 1953086860 178 ND 179
Cdd:PLN03192  686 TD 687
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-248 1.88e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  16 TTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEF------------------- 76
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgi 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  77 ----RTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLW 152
Cdd:PHA02874  116 dvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 153 IASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANkgYNDVIEELLKFSPTLGILK-NGTSALHAAV-LSGNIKTVAL 230
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDiDGSTPLHHAInPPCDIDIIDI 273

                         250
                  ....*....|....*...
gi 1953086860 231 LLEAGADPALRNKANELP 248
Cdd:PHA02874  274 LLYHKADISIKDNKGENP 291
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-259 2.30e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  29 DCVRELVLQGADINLQRESGPTALFFAAQQGHN-DVVRFLFEFGASTEFRTKDGGTALLA--ASQYGHMQVVETLLKHGA 105
Cdd:PHA03095   64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 106 NIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHS--EVVRVMLLRGADRDAARNDGT 181
Cdd:PHA03095  144 DVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 182 TALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPAELT---KNE 255
Cdd:PHA03095  224 TPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNG 303


                  ....
gi 1953086860 256 RILR 259
Cdd:PHA03095  304 RAVR 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 59-238 4.28e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  59 GHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGA 138
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 139 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 216
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|..
gi 1953086860 217 HAAVLSGNIKTVALLLEAGADP 238
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANI 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-205 7.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  28 IDCVRELVLQGADINLQRESGPTALFFAAQQGHN-----DVVRFLFEFGASTEFRTKDGGTALLAASQY--GHMQVVETL 100
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 101 LKHGANIHDQLYDGATALFLAAQGGY--LDVIRLL----------------LSSGAKVNQPRQDGTAPLWIASQMGHSEV 162
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953086860 163 VRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPT 205
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 31-248 3.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  31 VRELVLQ-GADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 109
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 110 QlydgATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGADRDAARNDGTTALLKAA 188
Cdd:PHA02876  240 N----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953086860 189 NKGYNdviEELLKFSPTLGILKNGTSALH------AAVLSGNIKTVALLLEAGADPALRNKANELP 248
Cdd:PHA02876  316 KNGYD---TENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTP 378
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 35-226 1.84e-11

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: 63.88  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  35 VLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHGAN-----I 107
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAAPElvnepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 108 HDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADR 173
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953086860 174 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 226
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-248 2.18e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  95 QVVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAD 172
Cdd:PHA02878  148 EITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953086860 173 RDAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGniKTVALLLEAGADPALRNKANELP 248
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTP 303
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-203 3.01e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 120 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 199
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1953086860 200 LKFS 203
Cdd:PTZ00322  168 SRHS 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 26-172 7.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 7.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  26 GHIDCVRELVLQGADIN-LQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHG 104
Cdd:PHA02875   79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953086860 105 A--NIHDQLydGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 172
Cdd:PHA02875  159 AclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-232 1.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  24 YAGHIDCVRELV-LQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLK 102
Cdd:PHA02874   10 YSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 103 HG-------------------------ANIHDQlyDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQM 157
Cdd:PHA02874   90 NGvdtsilpipciekdmiktildcgidVNIKDA--ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953086860 158 GHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNIKTVALLL 232
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-73 2.02e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 2.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953086860  15 GTTLLMVASYAGHIDCVRELvLQGADINLQrESGPTALFFAAQQGHNDVVRFLFEFGAS 73
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 31-192 2.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  31 VRELVLQGADINLQ-RESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 109
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 110 QLYDGATALFLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTAL 184
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1953086860 185 LKAANKGY 192
Cdd:PHA02878  305 SSAVKQYL 312
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 16-262 3.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 3.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  16 TTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHN-DVVRFLFEFGASTEFRTKDGGTALLAASQYGHM 94
Cdd:PHA02876  309 TPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  95 QVVETLLKHGANIHDQLYDGATALFLAAQGG--YLDViRLLLSSGAKVNQPRQDGTAPLWIASQMG-HSEVVRVMLLRGA 171
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGTnpYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 172 DRDAARNDGTTALLKAAnkGYNDVIEELLKFSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPAEL 251
Cdd:PHA02876  468 DVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNEVNPLKRVP 545

                         250
                  ....*....|.
gi 1953086860 252 TKNERILRLLR 262
Cdd:PHA02876  546 TRFTSLRESFK 556
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 52-218 9.83e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  52 LFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIR 131
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 132 LLLSSgAKVNQPRQDGTApLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKN 211
Cdd:PLN03192  609 ILYHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMN 677


                  ....*..
gi 1953086860 212 GTSALHA 218
Cdd:PLN03192  678 GADVDKA 684
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-141 1.15e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  11 IHSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQ 90
Cdd:PHA02875   98 FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953086860  91 YGHMQVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLSSGAKVN 141
Cdd:PHA02875  178 KGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 15-154 2.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTAL-LAASQYGH 93
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKD 247

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953086860  94 MQVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLSSGAKVNQPRQDGTAPLWIA 154
Cdd:PHA02878  248 YDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-134 2.29e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 2.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953086860  81 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 134
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-239 3.35e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  94 MQVVETLLKHGANIHdqlYDGA---TAL--FLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSE-VVRVM 166
Cdd:PHA03095   27 VEEVRRLLAAGADVN---FRGEygkTPLhlYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLL 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953086860 167 LLRGADRDAARNDGTTAL-LKAANKGYN-DVIEELLKFSPTLGILKN-GTSALHAAVLSGN--IKTVALLLEAGADPA 239
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSGFNINpKVIRLLLRKGADVNALDLyGMTPLAVLLKSRNanVELLRLLIDAGADVY 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
15-67 4.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 4.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFL 67
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 79-201 9.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 9.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  79 KDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 158
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1953086860 159 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIEELLK 201
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 31-120 1.23e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  31 VRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKH------- 103
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1953086860 104 GANIHDQLYDGATALFL 120
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-261 8.57e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.26  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 127 LDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFS-PT 205
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGaDI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953086860 206 LGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELP---AELTKNERILRLL 261
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPlhlAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
50-101 1.61e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.61e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953086860  50 TALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLL 101
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-248 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  17 TLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVR-----------------------------FL 67
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  68 FEFGASTEFRTKDGGTALLAASQYGHM-QVVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSGAKVNQPRQ 145
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 146 DGTAPLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsALHAAVLS 222
Cdd:PHA02876  340 LYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALCG 418

                         250       260
                  ....*....|....*....|....*..
gi 1953086860 223 GN-IKTVALLLEAGADPALRNKANELP 248
Cdd:PHA02876  419 TNpYMSVKTLIDRGANVNSKNKDLSTP 445
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 64-135 2.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953086860  64 VRFLFEFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 135
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 86-167 2.71e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  86 LAASqyGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 165
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1953086860 166 ML 167
Cdd:PTZ00322  167 LS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-141 4.26e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  26 GHIDCVRELVLQGADINLQRESGPTALFFAAQQGHND--VVRFLF----------------EFGASTEFRTKDGGTALLA 87
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIdkgvdinaknrvnyllSYGVPINIKDVYGFTPLHY 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953086860  88 ASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN 141
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-239 1.51e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  16 TTLLMVASYAGHIDCVRELVLQGADINLQRESGPTAL--FFAAQQGHNDVVRFLFEFGASTEFRTKDGGTAL--LAASQY 91
Cdd:PHA03095   85 TPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRN 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  92 GHMQVVETLLKHGANIHD-----------------------------------QLYDGATALFLAAQGGYLD--VIRLLL 134
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAvddrfrsllhhhlqsfkprarivreliragcdpaaTDMLGNTPLHSMATGSSCKrsLVLPLL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 135 SSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTL----GILK 210
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvaATLN 324

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1953086860 211 NGTSALHAAVLSGN---IKTVALLLEAGADPA 239
Cdd:PHA03095  325 TASVAGGDIPSDATrlcVAKVVLRGAFSLLPE 356
PHA03095 PHA03095
ankyrin-like protein; Provisional
 126-261 1.88e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 126 YLDVIRLLLSSGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGADRDAARNDGTTALLKAAnkgYNDVIEEL 199
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953086860 200 LKFSPTLG--IL---KNGTSALHAAVLSGNI--KTVALLLEAGADPALRNKANELP-AELTKNER----ILRLL 261
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPlAVLLKSRNanveLLRLL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-238 2.76e-06

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: 48.09  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  83 TALLAASQYGHMQVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAK-VNQPRQ----DGTAPLWIASQ 156
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 157 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDviEELLKFsptlgilkngtsalhaAVLSGNIKTVALLLEAGA 236
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIYYG--EHPLSF----------------AACVGNEEIVRLLIEHGA 160


                  ..
gi 1953086860 237 DP 238
Cdd:cd22192   161 DI 162
PHA02798 PHA02798
ankyrin-like protein; Provisional
 28-142 3.40e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  28 IDCVRELVLQGADIN-LQRE-SGPTALFFAAQQGHN---DVVRFLFEFGASTEFRTKDGGT---ALLAASQYGHMQVVET 99
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEySTPLCTILSNIKDYKhmlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953086860 100 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLSSGAKVNQ 142
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-167 7.65e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 7.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953086860 116 TALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 167
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-125 9.16e-06

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: 46.54  E-value: 9.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESG------PTALF--------FAAQQGHNDVVRFLFEFGASTEFRTKD 80
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIyygehplsFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953086860  81 GGTAL----LAASQYGHMQVVETLLKHGANIHDQL------YDGATALFLAAQGG 125
Cdd:cd22192   169 GNTVLhilvLQPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEG 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
10-52 9.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 9.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953086860  10 WIHSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTAL 52
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 180-261 1.52e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 180 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNIKTVALLLEAGADPALRNKA 244
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKelvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953086860 245 N-------------ELP---AELTKNERILRLL 261
Cdd:cd21882   106 RffrkspgnlfyfgELPlslAACTNQEEIVRLL 138
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 90-258 2.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  90 QYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 169
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 170 gaDRDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNI-KTVALLLEAGADPALRNK 243
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKNI 305

                         170       180
                  ....*....|....*....|..
gi 1953086860 244 ANELPAEL-------TKNERIL 258
Cdd:PHA02876  306 KGETPLYLmakngydTENIRTL 327
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-189 4.60e-05

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: 44.30  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  40 DINLQRESGPTALFFAAQQGHNDVVRFLFEFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 108
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 109 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 171
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1953086860 172 DRDAARNDGTTaLLKAAN 189
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
PHA02798 PHA02798
ankyrin-like protein; Provisional
 94-201 6.15e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  94 MQVVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRV 165
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1953086860 166 MLLRGADRDAARNDGTTAL---LKAANKGYNDVIEELLK 201
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-85 1.53e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1953086860  39 ADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEFRTKDGGTAL 85
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 81-233 1.55e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  81 GGTALLAASQYGHMQVVETL------------LKHGAN--IHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVnQPRQD 146
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAImllleaapdsgnPKELVNapCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 147 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANKG----------YNDVI 196
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953086860 197 EELLKFSPT--LGILKN--GTSALHAAVLSGNIKTVALLLE 233
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-44 1.57e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINLQ 44
Cdd:pfam12796  59 DNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-89 1.83e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  14 HGTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFL-------FEFGASTEFRTKDGGTALL 86
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqchFELGANAKPDSFTGKPPSL 193


                  ...
gi 1953086860  87 AAS 89
Cdd:PTZ00322  194 EDS 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 80-110 2.40e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 2.40e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1953086860  80 DGGTAL-LAASQYGHMQVVETLLKHGANIHDQ 110
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 211-243 2.95e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 2.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953086860 211 NGTSALHAAVLS-GNIKTVALLLEAGADPALRNK 243
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-141 3.14e-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: 37.18  E-value: 3.14e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953086860  113 DGATALFLAAQGGYLDVIRLLLSSGAKVN 141
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 180-237 3.53e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.72  E-value: 3.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953086860 180 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGAD 237
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 96-231 3.85e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  96 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLSSGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGADRDA 175
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953086860 176 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNIKTVALL 231
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 116-261 4.18e-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: 41.54  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 116 TALFLAAQGGYLDVI-RLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlrgadrDAARNdgttallkaankgynd 194
Cdd:cd22192    19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPE---------------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 195 vieelLKFSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPA---------LRNKAN-----ELP---AELTKNERI 257
Cdd:cd22192    77 -----LVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPlsfAACVGNEEI 151


                  ....
gi 1953086860 258 LRLL 261
Cdd:cd22192   152 VRLL 155
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 180-243 5.71e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 5.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953086860 180 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNIKTVALLLEAGADPALRNK 243
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 14-43 6.82e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 6.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953086860   14 HGTTLLMVASYAGHIDCVRELVLQGADINL 43
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
180-232 8.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 8.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953086860 180 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLL 232
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 211-238 1.27e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.27e-03
                           10        20
                   ....*....|....*....|....*...
gi 1953086860  211 NGTSALHAAVLSGNIKTVALLLEAGADP 238
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-200 1.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953086860 147 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELL 200
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 13-134 1.52e-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: 39.68  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  13 SHGTTLLMVASYAGHIDCVRELVLQGADINL-------QRESGPTALF-------FAAQQGHNDVVRFLFEFGAStefrt 78
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD----- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860  79 kdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLDVIR 131
Cdd:TIGR00870 201 ------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIVLFR 274


                  ...
gi 1953086860 132 LLL 134
Cdd:TIGR00870 275 LKL 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-76 1.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953086860  15 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGPTALFFAAQQGHNDVVRFLFEFGASTEF 76
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-261 2.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953086860 212 GTSALHAAVLSGNIKTVALLLEAGADPALRNKANELP---AELTKNERILRLL 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAlhfAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-109 2.52e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 2.52e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953086860   80 DGGTALLAASQYGHMQVVETLLKHGANIHD 109
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 14-44 2.98e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1953086860  14 HGTTLLMVASY-AGHIDCVRELVLQGADINLQ 44
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-251 3.52e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 3.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1953086860 211 NGTSALHAAVLSGNIKTVALLLEAGADPALRNKANELPAEL 251
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 110-246 6.51e-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: 37.75  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953086860 110 QLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQ--PRQDGTAPL-WIASQMGHSEVVRVMLLRGadRDAARNDgttALLK 186
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLNIncPDRLGRSALfVAAIENENLELTELLLNLS--CRGAVGD---TLLH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953086860 187 AANKGYNDVIEELLK---------------FSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPALRNKANE 246
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgplelaNDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH