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Conserved domains on  [gi|1039755803|ref|XP_017173356|]
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ankyrin repeat domain-containing protein 29 isoform X1 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12356329)

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

Gene Ontology:  GO:0005515
PubMed:  17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-352 2.76e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 110 DSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALL 189
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 190 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 269
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 270 LLRGADRDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKAN 348
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 1039755803 349 ELPA 352
Cdd:COG0666   286 LTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-147 6.38e-06

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  66 ADMCRMSFKKETPLanaaFWAAKRGNlallklllnsgrvdVDC------RDSVRRDTHGTTLLMVASYAGHIDCVRELVL 139
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGH--------------LEIvkllleHADVNLKDNGRTALHYAARSGHLEIVKLLLE 82


                  ....*...
gi 1039755803 140 QGADINLQ 147
Cdd:pfam12796  83 KGADINVK 90
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-352 2.76e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 110 DSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALL 189
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 190 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 269
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 270 LLRGADRDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKAN 348
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 1039755803 349 ELPA 352
Cdd:COG0666   286 LTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-213 5.15e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 122 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039755803 202 TLLKHGANIHDQ 213
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 115-243 2.19e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 86.85  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 115 DTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALLAASQY 194
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKR 632

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039755803 195 GHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 243
Cdd:PLN03192  633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-287 1.25e-09

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: 59.64  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 138 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 211
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 212 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 277
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1039755803 278 AARNDGTTAL 287
Cdd:cd22192   164 AQDSLGNTVL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-147 6.38e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  66 ADMCRMSFKKETPLanaaFWAAKRGNlallklllnsgrvdVDC------RDSVRRDTHGTTLLMVASYAGHIDCVRELVL 139
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGH--------------LEIvkllleHADVNLKDNGRTALHYAARSGHLEIVKLLLE 82


                  ....*...
gi 1039755803 140 QGADINLQ 147
Cdd:pfam12796  83 KGADINVK 90
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-244 1.25e-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: 38.72  E-value: 1.25e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039755803  216 DGATALFLAAQGGYLDVIRLLLSSGAKVN 244
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-292 2.86e-04

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: 42.76  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 143 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 211
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 212 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 274
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1039755803 275 DRDAARNDGTTaLLKAAN 292
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-352 2.76e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 110 DSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALL 189
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 190 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 269
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 270 LLRGADRDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKAN 348
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 1039755803 349 ELPA 352
Cdd:COG0666   286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-304 1.47e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFA 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADIN-----AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 159 AQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 238
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755803 239 SGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLK 304
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-381 1.47e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 119 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMP 198
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 199 VVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDA 278
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 279 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPAELTKN 357
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         250       260
                  ....*....|....*....|....
gi 1039755803 358 ERILHLLRQKEGPGKNELGSILDR 381
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
134-367 3.11e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 3.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 134 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQ 213
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 214 LYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANK 293
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755803 294 GYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELP---AELTKNERILHLLRQK 367
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAldlAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-213 5.15e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 122 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039755803 202 TLLKHGANIHDQ 213
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-245 4.88e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 155 LFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039755803 235 LLLSSGAKVNQ 245
Cdd:pfam12796  79 LLLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 115-243 2.19e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 86.85  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 115 DTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALLAASQY 194
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKR 632

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1039755803 195 GHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 243
Cdd:PLN03192  633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-345 5.92e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 5.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 254 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNVKTVAL 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1039755803 334 LLEAGADPALRN 345
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
188-275 8.93e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 8.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 188 LLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 267
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1039755803 268 VMLLRGAD 275
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 199-364 5.48e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 5.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 199 VVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVMLL 271
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 272 RGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVA 332
Cdd:PHA03100  130 NGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFVK 209

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039755803 333 LLLEAGADPALRNKANELPAE---LTKNERILHLL 364
Cdd:PHA03100  210 YLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
 114-361 2.58e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 114 RDTHGTTLL-MVASYAGH--IDCVRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGTALL 189
Cdd:PHA03095   43 RGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 190 A--ASQYGHMPVVETLLKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHS-- 263
Cdd:PHA03095  123 VylSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 264 EVVRVMLLRGADRDAARNDGTTALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGAD 340
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         250       260
                  ....*....|....*....|....
gi 1039755803 341 PALRNKANELPAELT---KNERIL 361
Cdd:PHA03095  283 INAVSSDGNTPLSLMvrnNNGRAV 306
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-278 2.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.55  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  57 ERGpagggtADMCRMSFKKETPLanaaFWAAKRGNLALLKLLLNSGRVDVDCRDSVrrdtHGTTLLMVASYAGHIDCVRE 136
Cdd:PHA02876  295 ERG------ADVNAKNIKGETPL----YLMAKNGYDTENIRTLIMLGADVNAADRL----YITPLHQASTLDRNKDIVIT 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 137 LVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAAsQYGHMPV--VETLLKHGANIHDQL 214
Cdd:PHA02876  361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKN 439

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755803 215 YDGATALFLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAD-RDA 278
Cdd:PHA02876  440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 131-308 3.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 131 IDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTECRTKDGGTALLAASQY--GHMPVVETL 203
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 204 LKHGANIHDQLYDGATALFLAAQGGY--LDVIRLL----------------LSSGAKVNQPRQDGTAPLWIASQMGHSEV 265
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039755803 266 VRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPT 308
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 119-335 3.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 119 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTE-----CRTKDggtallaasq 193
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipCIEKD---------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 194 yghmpVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 273
Cdd:PHA02874  106 -----MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755803 274 ADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNVKTVALLL 335
Cdd:PHA02874  181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 134-351 1.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 134 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 212
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 213 QlydgATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGADRDAARNDGTTALLKAA 291
Cdd:PHA02876  240 N----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755803 292 NKGYNdviEELLKFSPTLGILKNGTSALH------AAVLSGNVKTVALLLEAGADPALRNKANELP 351
Cdd:PHA02876  316 KNGYD---TENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTP 378
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 162-341 1.84e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 162 GHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGA 241
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 242 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 319
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|..
gi 1039755803 320 HAAVLSGNVKTVALLLEAGADP 341
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANI 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 199-351 4.09e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 199 VVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 276
Cdd:PHA02878  149 ITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755803 277 DAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGNVktVALLLEAGADPALRNKANELP 351
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTP 303
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 134-295 1.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 134 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 212
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 213 QLYDGATALFLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTAL 287
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1039755803 288 LKAANKGY 295
Cdd:PHA02878  305 SSAVKQYL 312
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 223-306 1.21e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 223 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 302
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1039755803 303 LKFS 306
Cdd:PTZ00322  168 SRHS 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 129-275 3.53e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 129 GHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHG 207
Cdd:PHA02875   79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755803 208 A--NIHDQLydGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 275
Cdd:PHA02875  159 AclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-170 3.79e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 3.79e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755803 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 170
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-237 5.95e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 5.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755803 184 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-287 1.25e-09

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: 59.64  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 138 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 211
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 212 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 277
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1039755803 278 AARNDGTTAL 287
Cdd:cd22192   164 AQDSLGNTVL 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 184-321 4.94e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 184 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSgAKVNQPRQDGTApLWIASQMGHS 263
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755803 264 EVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 321
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-244 7.93e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHM 197
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039755803 198 PVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLSSGAKVN 244
Cdd:PHA02875  182 AICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-204 1.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755803 151 GTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLL 204
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 85-351 3.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  85 WAAKRGNLALLKLLLNSGrVDVDCrdsVRRDthGTTLLMVASYAGHIDCVRELVLQGADINlqreSGTTALFFAAQQGHN 164
Cdd:PHA02876  184 YAAERGNAKMVNLLLSYG-ADVNI---IALD--DLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 165 DVVRFLFGFGASTECRTKDGGTALLAASQYGHMP-VVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSGAK 242
Cdd:PHA02876  254 ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGAD 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 243 VNQPRQDGTAPLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsAL 319
Cdd:PHA02876  334 VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-AL 412

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039755803 320 HAAVLSGN-VKTVALLLEAGADPALRNKANELP 351
Cdd:PHA02876  413 HFALCGTNpYMSVKTLIDRGANVNSKNKDLSTP 445
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 110-257 4.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 110 DSVRRDTH-GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 188
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755803 189 -LAASQYGHMPVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLSSGAKVNQPRQDGTAPLWIA 257
Cdd:PHA02878  239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
230-367 4.56e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 230 LDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFS-PT 308
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGaDI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755803 309 LGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELP---AELTKNERILHLLRQK 367
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPlhlAAYNGNLEIVKLLLEA 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-304 4.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 4.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 182 KDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 261
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039755803 262 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIEELLK 304
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 167-238 3.64e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 3.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755803 167 VRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 238
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-270 7.67e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 7.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 189 LAASqyGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 268
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1039755803 269 ML 270
Cdd:PTZ00322  167 LS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
109-158 8.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 8.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039755803 109 RDSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFA 158
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-223 8.75e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 134 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKH------- 206
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1039755803 207 GANIHDQLYDGATALFL 223
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-270 3.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 3.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755803 219 TALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 270
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-147 6.38e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  66 ADMCRMSFKKETPLanaaFWAAKRGNlallklllnsgrvdVDC------RDSVRRDTHGTTLLMVASYAGHIDCVRELVL 139
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGH--------------LEIvkllleHADVNLKDNGRTALHYAARSGHLEIVKLLLE 82


                  ....*...
gi 1039755803 140 QGADINLQ 147
Cdd:pfam12796  83 KGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 119-342 7.17e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 119 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL--LAASQY 194
Cdd:PHA03095   85 TPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRN 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 195 GHMPVVETLLKHGANIH----------DQLYD-------------------------GATALFLAAQGGYLD--VIRLLL 237
Cdd:PHA03095  165 ANVELLRLLIDAGADVYavddrfrsllHHHLQsfkprarivreliragcdpaatdmlGNTPLHSMATGSSCKrsLVLPLL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 238 SSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTL----GILK 313
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvaATLN 324

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039755803 314 NGTSALHAAVLSGN---VKTVALLLEAGADPA 342
Cdd:PHA03095  325 TASVAGGDIPSDATrlcVAKVVLRGAFSLLPE 356
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 115-244 7.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 115 DTHGTTLLMVASYA--GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLFGFGA--STECR-------- 180
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVdiNAKNRvnyllsyg 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 181 ----TKD--GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN 244
Cdd:PHA03100  183 vpinIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-192 8.30e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 101 SGRVDVDCRDsvrrdTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL-------FGF 173
Cdd:PTZ00322  103 TGGADPNCRD-----YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqchFEL 177

                          90
                  ....*....|....*....
gi 1039755803 174 GASTECRTKDGGTALLAAS 192
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLEDS 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
142-188 1.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039755803 142 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 188
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 76-265 2.70e-05

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: 46.16  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803  76 ETPLanaaFWAAKRGNLALLKLLLNSGRVDVdcrdsVRRDTHGTTLLMVASYAGH-------IDCVRELVLQGADINLQR 148
Cdd:cd22192    18 ESPL----LLAAKENDVQAIKKLLKCPSCDL-----FQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 149 esGTTALFFAAQQGHNDVVRFLFGFGAS------TECRTKDGGTALL---------AASQyGHMPVVETLLKHGANIHDQ 213
Cdd:cd22192    89 --GETALHIAVVNQNLNLVRELIARGADvvspraTGTFFRPGPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQ 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755803 214 LYDGATAL-FLAAQGGYL---DVIRLLLSSGAKVNQ------PRQDGTAPLWIASQMGHSEV 265
Cdd:cd22192   166 DSLGNTVLhILVLQPNKTfacQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 186-341 2.73e-05

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: 46.16  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 186 TALLAASQYGHMPVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAK-VNQPRQ----DGTAPLWIASQ 259
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 260 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDviEELLKFsptlgilkngtsalhaAVLSGNVKTVALLLEAGA 339
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIYYG--EHPLSF----------------AACVGNEEIVRLLIEHGA 160


                  ..
gi 1039755803 340 DP 341
Cdd:cd22192   161 DI 162
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-183 3.37e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 3.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755803 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKD 183
Cdd:PLN03192  622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 283-344 8.02e-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: 44.49  E-value: 8.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755803 283 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 344
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
PHA02798 PHA02798
ankyrin-like protein; Provisional
 199-304 1.23e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 199 VVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRVML 270
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMI 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039755803 271 LRGADRDAARNDGTTAL---LKAANKGYNDVIEELLK 304
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-244 1.25e-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: 38.72  E-value: 1.25e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039755803  216 DGATALFLAAQGGYLDVIRLLLSSGAKVN 244
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 314-346 1.34e-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: 38.81  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039755803 314 NGTSALHAAVLS-GNVKTVALLLEAGADPALRNK 346
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 193-361 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 193 QYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 272
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 273 gaDRDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNV-KTVALLLEAGADPALRNK 346
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKNI 305

                         170       180
                  ....*....|....*....|..
gi 1039755803 347 ANELPAEL-------TKNERIL 361
Cdd:PHA02876  306 KGETPLYLmakngydTENIRTL 327
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 283-368 1.73e-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: 43.63  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 283 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNVKTVALLLEAGADPALRNKA 347
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAKG 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039755803 348 N--------------ELPAEL---TKNERILHLLRQKE 368
Cdd:cd22193   109 RffqpkyqgegfyfgELPLSLaacTNQPDIVQYLLENE 146
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 184-336 1.87e-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: 43.33  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 184 GGTALLAASQYGH-------MPVVETLLKHG-------ANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVnQPRQD 249
Cdd:cd21882    26 GKTCLHKAALNLNdgvneaiMLLLEAAPDSGnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 250 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANKG----------YNDVI 299
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039755803 300 EELLKFSPT--LGILKN--GTSALHAAVLSGNVKTVALLLE 336
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
PHA02798 PHA02798
ankyrin-like protein; Provisional
 131-245 2.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 131 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGT---ALLAASQYGHMPVVET 202
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039755803 203 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLSSGAKVNQ 245
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-335 2.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755803 283 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLL 335
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 2.75e-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: 37.95  E-value: 2.75e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755803  117 HGTTLLMVASYAGHIDCVRELVLQGADINL 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-292 2.86e-04

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: 42.76  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 143 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 211
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 212 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 274
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1039755803 275 DRDAARNDGTTaLLKAAN 292
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-213 3.09e-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: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755803 183 DGGTAL-LAASQYGHMPVVETLLKHGANIHDQ 213
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 199-334 5.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 199 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLSSGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGADRDA 278
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755803 279 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNVKTVALL 334
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-205 6.22e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 110 DSVRRDTHGTTLLMVAsyAGHIDCVRELVLQ----GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGG 185
Cdd:PHA03095  214 DPAATDMLGNTPLHSM--ATGSSCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                          90       100
                  ....*....|....*....|
gi 1039755803 186 TALLAASQYGHMPVVETLLK 205
Cdd:PHA03095  292 TPLSLMVRNNNGRAVRAALA 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-303 6.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755803 250 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELL 303
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 283-340 7.08e-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: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755803 283 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGAD 340
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-178 8.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 104 VDVDCRDSVR-----------RDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 172
Cdd:PHA03100  167 VDINAKNRVNyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....*.
gi 1039755803 173 FGASTE 178
Cdd:PHA03100  247 NGPSIK 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
315-364 8.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 8.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755803 315 GTSALHAAVLSGNVKTVALLLEAGADPALRNKANELP---AELTKNERILHLL 364
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAlhfAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 314-341 9.56e-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: 9.56e-04
                           10        20
                   ....*....|....*....|....*...
gi 1039755803  314 NGTSALHAAVLSGNVKTVALLLEAGADP 341
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 117-147 2.21e-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: 35.34  E-value: 2.21e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755803 117 HGTTLLMVASY-AGHIDCVRELVLQGADINLQ 147
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 183-212 2.93e-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: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755803  183 DGGTALLAASQYGHMPVVETLLKHGANIHD 212
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 314-354 3.88e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 3.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039755803 314 NGTSALHAAVLSGNVKTVALLLEAGADPALRNKANELPAEL 354
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 213-349 7.07e-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: 38.52  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755803 213 QLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQ--PRQDGTAPL-WIASQMGHSEVVRVMLLRGadRDAARNDgttALLK 289
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLNIncPDRLGRSALfVAAIENENLELTELLLNLS--CRGAVGD---TLLH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755803 290 AANKGYNDVIEELLK---------------FSPTLGILKNGTSALHAAVLSGNVKTVALLLEAGADPALRNKANE 349
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgplelaNDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-211 8.75e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 8.75e-03
                          10        20
                  ....*....|....*....|....*....
gi 1039755803 183 DGGTALLAASQYGHMPVVETLLKHGANIH 211
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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