NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622888214|ref|XP_028693717|]
View 

ankyrin repeat domain-containing protein 29 isoform X6 [Macaca mulatta]

Protein Classification

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

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

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

Graphical summary

 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];
1-230 1.19e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVET 80
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  81 LLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARND 160
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888214 161 GTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPA 230
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-230 1.19e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVET 80
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  81 LLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARND 160
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888214 161 GTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPA 230
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-91 4.34e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVET 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1622888214  81 LLKHGANIHDQ 91
Cdd:pfam12796  80 LLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-121 1.16e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   2 VAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALLAASQYGHMQVVETL 81
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKEL 641

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622888214  82 LKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 121
Cdd:PLN03192  642 LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 16-207 3.34e-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: 62.72  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  16 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 88
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  89 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAER 154
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622888214 155 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 207
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 21-170 2.79e-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: 41.99  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  21 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 89
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  90 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 152
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1622888214 153 ERDAARNDGTTaLLKAAN 170
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-122 7.87e-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: 36.03  E-value: 7.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622888214   94 DGATALFLAAQGGYLDVIRLLLASGAKVN 122
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-230 1.19e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVET 80
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  81 LLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARND 160
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888214 161 GTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPA 230
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-243 1.43e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVET 80
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  81 LLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARND 160
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 161 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPAELTKNERIL 239
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265


                  ....
gi 1622888214 240 RLLR 243
Cdd:COG0666   266 LIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-245 2.09e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQ 91
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  92 LYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANK 171
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622888214 172 GYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELP---AELTKNERILRLLRSK 245
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAldlAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-91 4.34e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVET 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1622888214  81 LLKHGANIHDQ 91
Cdd:pfam12796  80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
33-123 3.57e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  33 LFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1622888214 113 LLLASGAKVNQ 123
Cdd:pfam12796  79 LLLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-121 1.16e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   2 VAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALLAASQYGHMQVVETL 81
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKEL 641

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622888214  82 LKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 121
Cdd:PLN03192  642 LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
132-223 3.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 132 LWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNIKTVAL 211
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1622888214 212 LLEAGADPSLRN 223
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-242 1.84e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  75 MQVVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLASGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVM 147
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 148 LLRGAERDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKT 208
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622888214 209 VALLLEAGADPSLRNKANELPAE---LTKNERILRLL 242
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-153 2.32e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  66 LLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPrqDGTAPLWIASQMGHSEVVR 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1622888214 146 VMLLRGAE 153
Cdd:pfam12796  79 LLLEKGAD 86
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-160 5.18e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 5.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVEt 80
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR- 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  81 LLKHGANIHDQlYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARND 160
Cdd:PLN03192  609 ILYHFASISDP-HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-245 3.01e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  40 GHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGA 119
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 120 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 197
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622888214 198 HAAVLSGNIKTVALLLEAGADPSL--RNKANELPAELTKNER--ILRLLRSK 245
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKidIVRLFIKR 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-240 5.01e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 5.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  10 DCVRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGTALLA--ASQYGHMQVVETLLKHGA 86
Cdd:PHA03095   64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  87 NIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHS--EVVRVMLLRGAERDAARNDGT 162
Cdd:PHA03095  144 DVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 163 TALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPAELT---KNE 236
Cdd:PHA03095  224 TPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNG 303


                  ....
gi 1622888214 237 RILR 240
Cdd:PHA03095  304 RAVR 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 3-229 1.92e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   3 AAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF-----------------------RT 59
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgidvniKD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  60 KDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMG 139
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 140 HSEVVRVMLLRGAERDAARNDGTTALLKAANkgYNDVIEELLKFSPTLGILK-NGTSALHAAV-LSGNIKTVALLLEAGA 217
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDiDGSTPLHHAInPPCDIDIIDILLYHKA 279

                         250
                  ....*....|..
gi 1622888214 218 DPSLRNKANELP 229
Cdd:PHA02874  280 DISIKDNKGENP 291
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-229 5.68e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 90
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  91 QlydgATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGAERDAARNDGTTALLKAA 169
Cdd:PHA02876  240 N----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622888214 170 NKGYNdviEELLKFSPTLGILKNGTSALH------AAVLSGNIKTVALLLEAGADPSLRNKANELP 229
Cdd:PHA02876  316 KNGYD---TENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTP 378
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 76-229 2.50e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  76 QVVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAE 153
Cdd:PHA02878  148 EITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888214 154 RDAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGniKTVALLLEAGADPSLRNKANELP 229
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTP 303
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 5-213 2.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   5 YAGHIDCVRELV-LQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLK 83
Cdd:PHA02874   10 YSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  84 HG-------------------------ANIHDQlyDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQM 138
Cdd:PHA02874   90 NGvdtsilpipciekdmiktildcgidVNIKDA--ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622888214 139 GHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNIKTVALLL 213
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 16-207 3.34e-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: 62.72  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  16 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 88
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  89 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAER 154
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622888214 155 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 207
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-229 1.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  10 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIH 89
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  90 DQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAERDAARNDGTTALLKAA 169
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAI 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622888214 170 NKGYN-DVIEELLKFSPTLGILKN-GTSALHAAVlsGNIKTVALLLEAGADPSLRNKANELP 229
Cdd:PHA02874  263 NPPCDiDIIDILLYHKADISIKDNkGENPIDTAF--KYINKDPVIKDIIANAVLIKEADKLK 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 12-192 2.34e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQGADINLQRESGTTALFFAAQQ--GHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGH--MQVVETLLKHGAN 87
Cdd:PHA03100   89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  88 IH-----DQLYD-----------GATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 151
Cdd:PHA03100  169 INaknrvNYLLSygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622888214 152 AERDAARNdgtTALLKAANKGYNDVIEELLKFSPTLGILKN 192
Cdd:PHA03100  249 PSIKTIIE---TLLYFKDKDLNTITKIKMLKKSIMYMFLLD 286
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 3-153 2.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   3 AAYAGHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETL 81
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622888214  82 LKHGA--NIHDQLydGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAE 153
Cdd:PHA02875  155 IDHKAclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-184 3.49e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 101 LAAQGGYLDvIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEEL 180
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1622888214 181 LKFS 184
Cdd:PTZ00322  168 SRHS 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-156 4.76e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  10 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL-LAASQYGHMQVVETLLKHGANI 88
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANV 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  89 HDQLYDGATALFLAAQGG-YLDVIRLLLASGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAE-RDA 156
Cdd:PHA02876  436 NSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 12-173 1.04e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 90
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  91 QLYDGATALFLAAqgGYL---DVIRLLLASGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGAERDAARNDGTTAL 165
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1622888214 166 LKAANKGY 173
Cdd:PHA02878  305 SSAVKQYL 312
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-115 1.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888214  62 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 115
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-199 5.44e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 5.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  62 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASgAKVNQPRQDGTApLWIASQMGHS 141
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622888214 142 EVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 199
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-48 1.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.00e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622888214   2 VAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 48
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 10-135 2.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  10 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL-LAASQYGHMQVVETLLKHGANI 88
Cdd:PHA02878  182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDV 261

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622888214  89 HDQLY-DGATALFLAAQGGylDVIRLLLASGAKVNQPRQDGTAPLWIA 135
Cdd:PHA02878  262 NAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-243 2.67e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 90
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  91 QLYDGATALFLAAQGG--YLDViRLLLASGAKVNQPRQDGTAPLWIASQMG-HSEVVRVMLLRGAERDAARNDGTTALLK 167
Cdd:PHA02876  404 LSQKIGTALHFALCGTnpYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622888214 168 AAnkGYNDVIEELLKFSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPAELTKNERILRLLR 243
Cdd:PHA02876  483 AL--EYHGIVNILLHYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNEVNPLKRVPTRFTSLRESFK 556
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 7-181 2.73e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   7 GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGA 86
Cdd:PHA02874  135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  87 NIHDQLYDGATALFLAAQggYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHS-EVVRVMLLRGAERDAARNDGTTAL 165
Cdd:PHA02874  215 HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPI 292

                         170
                  ....*....|....*....
gi 1622888214 166 ---LKAANKgyNDVIEELL 181
Cdd:PHA02874  293 dtaFKYINK--DPVIKDII 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-220 3.47e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  75 MQVVETLLKHGANIHdqlYDGA---TAL--FLAAQGG-YLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSE-VVRVM 147
Cdd:PHA03095   27 VEEVRRLLAAGADVN---FRGEygkTPLhlYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLL 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622888214 148 LLRGAERDAARNDGTTAL-LKAANKGYN-DVIEELLKFSPTLGILKN-GTSALHAAVLSGN--IKTVALLLEAGADPS 220
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSGFNINpKVIRLLLRKGADVNALDLyGMTPLAVLLKSRNanVELLRLLIDAGADVY 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 2-122 9.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   2 VAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETL 81
Cdd:PHA02875  108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622888214  82 LKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLASGAKVN 122
Cdd:PHA02875  188 LDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-101 9.52e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 9.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  12 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKH------- 84
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1622888214  85 GANIHDQLYDGATALFL 101
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-229 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   3 AAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR-----------------------------FLFGFGA 53
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLLYDAGF 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  54 STEFRTKDGGTALLAASQYGHM-QVVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLASGAKVNQPRQDGTAP 131
Cdd:PHA02876  265 SVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITP 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 132 LWIASQMG-HSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsALHAAVLSGN-IK 207
Cdd:PHA02876  345 LHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALCGTNpYM 423

                         250       260
                  ....*....|....*....|..
gi 1622888214 208 TVALLLEAGADPSLRNKANELP 229
Cdd:PHA02876  424 SVKTLIDRGANVNSKNKDLSTP 445
Ank_4 pfam13637
Ankyrin repeats (many copies);
29-82 1.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888214  29 GTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLL 82
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-148 2.93e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  67 LAASqyGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRV 146
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1622888214 147 ML 148
Cdd:PTZ00322  167 LS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-229 3.99e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  64 TALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLL-----------------------LASGAK 120
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 121 VNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHA 199
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGESPLHN 196

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622888214 200 AVLSGNIKTVALLLEAGADPSLRNKANELP 229
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-242 6.25e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 108 LDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFS-PT 186
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGaDI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888214 187 LGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELP---AELTKNERILRLL 242
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPlhlAAYNGNLEIVKLL 139
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-115 1.31e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888214  45 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 115
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 73-229 2.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  73 GHMQVVETLLKHGAN-IHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 151
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 152 A----------ERDAARN-------------DGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNIK 207
Cdd:PHA02874   92 VdtsilpipciEKDMIKTildcgidvnikdaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFD 171

                         170       180
                  ....*....|....*....|..
gi 1622888214 208 TVALLLEAGADPSLRNKANELP 229
Cdd:PHA02874  172 IIKLLLEKGAYANVKDNNGESP 193
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 161-242 3.32e-06

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: 47.57  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 161 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGADPSLRNKA 225
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622888214 226 N-------------ELP---AELTKNERILRLL 242
Cdd:cd21882   106 RffrkspgnlfyfgELPlslAACTNQEEIVRLL 138
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 7-122 5.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   7 GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLF----------------GFGASTEFRTKDGGTALLA 68
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIdkgvdinaknrvnyllSYGVPINIKDVYGFTPLHY 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888214  69 ASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 122
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-242 5.73e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 107 YLDVIRLLLASGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGAERDAARNDGTTALLKAAnkgYNDVIEEL 180
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622888214 181 LKFSPTLG--IL---KNGTSALHAAVLSGNI--KTVALLLEAGADPSLRNKANELP-AELTKNER----ILRLL 242
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPlAVLLKSRNanveLLRLL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-148 5.82e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622888214  97 TALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 148
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-242 1.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 108 LDVIRLLLASGAKVNQPRQDGTAPLWIA----SQMGHSEVVRVMLLRG---AER-------------------DAARNDG 161
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINKCSvfyTLVaikdafnnrnveifkiiltNRYKNIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 162 TTALLKAANKGYNDVIEE-----LLKFSPTLGIL--KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELP---AE 231
Cdd:PHA02878  130 TIDLVYIDKKSKDDIIEAeitklLLSYGADINMKdrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPlhhAV 209

                         170
                  ....*....|.
gi 1622888214 232 LTKNERILRLL 242
Cdd:PHA02878  210 KHYNKPIVHIL 220
PHA02798 PHA02798
ankyrin-like protein; Provisional
 9-123 4.61e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   9 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGT---ALLAASQYGHMQVVET 80
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622888214  81 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLASGAKVNQ 123
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-219 4.84e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   9 IDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL--LAASQYGHMQVVETLLKH 84
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  85 GANIHD-----------------------------------QLYDGATALFLAAQGGYLD--VIRLLLASGAKVNQPRQD 127
Cdd:PHA03095  177 GADVYAvddrfrsllhhhlqsfkprarivreliragcdpaaTDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 128 GTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTL----GILKNGTSALHAAVLS 203
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvaATLNTASVAGGDIPSD 336

                         250
                  ....*....|....*....
gi 1622888214 204 GN---IKTVALLLEAGADP 219
Cdd:PHA03095  337 ATrlcVAKVVLRGAFSLLP 355
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 62-214 1.05e-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: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  62 GGTALLAASQYGHMQVVETL------------LKHGAN--IHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVnQPRQD 127
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAImllleaapdsgnPKELVNapCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 128 GTA--------------PLWIASQMGHSEVVRVMLLRGAE------RDAARNDGTTALLKAANKG----------YNDVI 177
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622888214 178 EELLKFSPT--LGILKN--GTSALHAAVLSGNIKTVALLLE 214
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 71-239 1.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  71 QYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 150
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 151 gaERDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNI-KTVALLLEAGADPSLRNK 224
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKNI 305

                         170       180
                  ....*....|....*....|..
gi 1622888214 225 ANELPAEL-------TKNERIL 239
Cdd:PHA02876  306 KGETPLYLmakngydTENIRTL 327
PHA02798 PHA02798
ankyrin-like protein; Provisional
 75-182 1.51e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  75 MQVVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLASGAKVNQPRQDGTAPLWIA---SQMGHSEVVRV 146
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622888214 147 MLLRGAERDAARNDGTTAL---LKAANKGYNDVIEELLK 182
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 192-224 2.24e-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: 2.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622888214 192 NGTSALHAAVLS-GNIKTVALLLEAGADPSLRNK 224
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
20-66 2.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622888214  20 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 66
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 61-91 2.57e-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: 2.57e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622888214  61 DGGTAL-LAASQYGHMQVVETLLKHGANIHDQ 91
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 21-170 2.79e-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: 41.99  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  21 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 89
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  90 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 152
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1622888214 153 ERDAARNDGTTaLLKAAN 170
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 2-106 2.95e-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: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   2 VAAYAGHIDCVRELVLQGADINLQRESGT------TALF--------FAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL- 66
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIyygehplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLh 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622888214  67 ---LAASQYGHMQVVETLLKHGANIHDQL------YDGATALFLAAQGG 106
Cdd:cd22192   175 ilvLQPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEG 223
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 161-218 2.97e-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: 2.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622888214 161 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGAD 218
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 161-224 3.22e-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: 41.70  E-value: 3.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888214 161 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNIKTVALLLEAGADPSLRNK 224
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
Ank_4 pfam13637
Ankyrin repeats (many copies);
161-213 7.73e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 7.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888214 161 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLL 213
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-122 7.87e-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: 36.03  E-value: 7.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622888214   94 DGATALFLAAQGGYLDVIRLLLASGAKVN 122
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-227 1.05e-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: 40.06  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  91 QLYDGATALFLAAQGGYLDVIRLLLASGAKVNQ--PRQDGTAPL-WIASQMGHSEVVRVMLLRgaERDAARNDgttALLK 167
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLNIncPDRLGRSALfVAAIENENLELTELLLNL--SCRGAVGD---TLLH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622888214 168 AANKGYNDVIEELLK---------------FSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANE 227
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgplelaNDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 192-232 1.17e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622888214 192 NGTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELPAEL 232
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-36 1.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622888214   1 MVAAYAGHIDCVRELVLQGADINLQRESGTTALFFA 36
Cdd:pfam13857  21 HVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 192-221 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: 35.26  E-value: 1.27e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888214  192 NGTSALHAAVLSGNIKTVALLLEAGADPSL 221
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 97-242 1.53e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 39.61  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  97 TALFLAAQGGYLDVI-RLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlrgaerDAARNdgttallkaankgynd 175
Cdd:cd22192    19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPE---------------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214 176 vieelLKFSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPS---------LRNKAN-----ELP---AELTKNERI 238
Cdd:cd22192    77 -----LVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVspratgtffRPGPKNliyygEHPlsfAACVGNEEI 151


                  ....
gi 1622888214 239 LRLL 242
Cdd:cd22192   152 VRLL 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
193-242 1.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622888214 193 GTSALHAAVLSGNIKTVALLLEAGADPSLRNKANELP---AELTKNERILRLL 242
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAlhfAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-212 2.15e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214  77 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLASGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGAERDA 156
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888214 157 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNIKTVALL 212
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 61-90 2.46e-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: 34.49  E-value: 2.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888214   61 DGGTALLAASQYGHMQVVETLLKHGANIHD 90
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 5-89 6.19e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888214   5 YAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH---NDVVRFLFGFGASTEFRTKDGGTALLAASQYGH---MQVV 78
Cdd:PHA02798   85 YKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEII 164

                          90
                  ....*....|.
gi 1622888214  79 ETLLKHGANIH 89
Cdd:PHA02798  165 KLLLEKGVDIN 175
 
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