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Conserved domains on  [gi|1039755809|ref|XP_017173359|]
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ankyrin repeat domain-containing protein 29 isoform X4 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-299 1.70e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.44  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 159 NDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755809 239 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLK 299
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 278-339 6.57e-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).


The actual alignment was detected with superfamily member cd21882:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 6.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809 278 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 339
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-299 1.70e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.44  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 159 NDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755809 239 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLK 299
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-208 3.27e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 117 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039755809 197 TLLKHGANIHDQ 208
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 105-238 5.28e-20

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 91.08  E-value: 5.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALL 184
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 185 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-282 9.33e-10

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: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 133 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 206
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 207 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 272
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1039755809 273 AARNDGTTAL 282
Cdd:cd22192   164 AQDSLGNTVL 173
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 278-339 6.57e-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: 6.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809 278 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 339
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 211-239 1.05e-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: 1.05e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039755809  211 DGATALFLAAQGGYLDVIRLLLSSGAKVN 239
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 309-341 1.27e-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: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039755809 309 NGTSALHAAVLS-GNVKTVALLLEAGADPALRNK 341
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 138-287 2.36e-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: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 138 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 206
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 207 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 269
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1039755809 270 DRDAARNDGTTaLLKAAN 287
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 309-336 8.35e-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: 8.35e-04
                           10        20
                   ....*....|....*....|....*...
gi 1039755809  309 NGTSALHAAVLSGNVKTVALLLEAGADP 336
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-299 1.70e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.44  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 159 NDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755809 239 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLK 299
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-342 4.82e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 4.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 158
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 159 NDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 239 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAA 317
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLA 259

                         250       260
                  ....*....|....*....|....*
gi 1039755809 318 VLSGNVKTVALLLEAGADPALRNKN 342
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
105-342 2.62e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.26  E-value: 2.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALL 184
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 185 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 264
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755809 265 LLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGADPALRNKN 342
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-282 1.19e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 1.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  82 AAFWAAKRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDV 161
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 162 VRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQP 241
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039755809 242 RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTAL 282
Cdd:COG0666   249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-208 3.27e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 117 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEcrTKDGGTALLAASQYGHMPVVE 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1039755809 197 TLLKHGANIHDQ 208
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
150-240 3.22e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 150 LFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 229
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039755809 230 LLLSSGAKVNQ 240
Cdd:pfam12796  79 LLLEKGADINV 89
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 105-238 5.28e-20

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 91.08  E-value: 5.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTkdGGTALL 184
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 185 AASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKV 238
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
249-340 4.14e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 249 LWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNVKTVAL 328
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1039755809 329 LLEAGADPALRN 340
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-270 6.28e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 6.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 183 LLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPrqDGTAPLWIASQMGHSEVVR 262
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1039755809 263 VMLLRGAD 270
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 105-335 7.30e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTECRTKDG 179
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 180 GTALLAASQY--GHMPVVETLLKHGANIHDQLYDGATALFLAAQGGY--LDVIRLLLSSGAKVNQprqdgtaplwiasqm 255
Cdd:PHA03100  107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA--------------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 256 ghSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLEAGA 334
Cdd:PHA03100  172 --KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 1039755809 335 D 335
Cdd:PHA03100  250 S 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-339 1.39e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTTLL-MVASYAGH--IDCVRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTECRTKDGG 180
Cdd:PHA03095   39 DVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 181 TALLA--ASQYGHMPVVETLLKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 256
Cdd:PHA03095  119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 257 HS--EVVRVMLLRGADRDAARNDGTTALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLLE 331
Cdd:PHA03095  199 KPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIA 278


                  ....*...
gi 1039755809 332 AGADPALR 339
Cdd:PHA03095  279 LGADINAV 286
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 194-342 1.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 194 VVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLSSGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVMLL 266
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 267 RGADRDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNVKTVA 327
Cdd:PHA03100  130 NGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEFVK 209

                         170
                  ....*....|....*
gi 1039755809 328 LLLEAGADPALRNKN 342
Cdd:PHA03100  210 YLLDLGANPNLVNKY 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-171 1.69e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  84 FWAAKRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVASYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGHNDVVR 163
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1039755809 164 FLFGFGAS 171
Cdd:pfam12796  79 LLLEKGAD 86
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 57-273 8.22e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 8.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  57 ERGpagggtADMCRMSFKKETPLanaaFWAAKRGNLALLKLLLNSGRVDVDCRDS-HGTTLLMVASYAGHIDCVRELVLQ 135
Cdd:PHA02876  295 ERG------ADVNAKNIKGETPL----YLMAKNGYDTENIRTLIMLGADVNAADRlYITPLHQASTLDRNKDIVITLLEL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 136 GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAAsQYGHMPV--VETLLKHGANIHDQLYDGA 213
Cdd:PHA02876  365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLS 443

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755809 214 TALFLAAQGG-YLDVIRLLLSSGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAD-RDA 273
Cdd:PHA02876  444 TPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA03095 PHA03095
ankyrin-like protein; Provisional
 126-342 1.50e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 126 IDCVRELVLQGADINLQRESGTTALffaAQQGHN------DVVRFLFGFGASTECRTKDGGTALLAASQYGH-MPVVETL 198
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 199 LKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPL--WIASQMGHSEVVRVMLLRGADRDAA 274
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAV 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755809 275 RNDGTTALLKAAN--KGYNDVIEELLKFS-PTLGILKNGTSALHAAVLSGNVKT--VALLLEAGADPALRNKN 342
Cdd:PHA03095  184 DDRFRSLLHHHLQsfKPRARIVRELIRAGcDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRY 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-330 2.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 114 TTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTE-----CRTKDggtallaasq 188
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipCIEKD---------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 189 yghmpVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRG 268
Cdd:PHA02874  106 -----MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755809 269 ADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNVKTVALLL 330
Cdd:PHA02874  181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 157-342 7.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 157 GHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGA 236
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 237 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 314
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|....*...
gi 1039755809 315 HAAVLSGNVKTVALLLEAGADPALRNKN 342
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKN 200
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 104-298 1.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 104 VDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 183
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 184 LAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYlDVIRLLLSSgAKVNQPRQDGTAPLWIASQMGHS-EVVR 262
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINPPCDiDIID 272

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1039755809 263 VMLLRGADRDAARNDGTTAL---LKAANKgyNDVIEELL 298
Cdd:PHA02874  273 ILLYHKADISIKDNKGENPIdtaFKYINK--DPVIKDII 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 129-335 1.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 129 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 207
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 208 Q------------------LYDGA-----------TALFLAAQGGYLD-VIRLLLSSGAKVNQPRQDGTAPLWIASQMGH 257
Cdd:PHA02876  240 NdlsllkairnedletsllLYDAGfsvnsiddcknTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 258 -SEVVRVMLLRGADRDAARNDGTTALLKAAN-KGYNDVIEELLKfsptLGILKNG-----TSALHAAVLSGNVKTVALLL 330
Cdd:PHA02876  320 dTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLE----LGANVNArdycdKTPIHYAAVRNNVVIINTLL 395


                  ....*
gi 1039755809 331 EAGAD 335
Cdd:PHA02876  396 DYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 218-301 7.15e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 7.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 218 LAAQGGYLDvIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEEL 297
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1039755809 298 LKFS 301
Cdd:PTZ00322  168 SRHS 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 129-290 8.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 8.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 129 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHD 207
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 208 QLYDGATALFLAAqgGYL---DVIRLLLSSGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGADRDAARNDGTTAL 282
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1039755809 283 LKAANKGY 290
Cdd:PHA02878  305 SSAVKQYL 312
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 194-336 1.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 194 VVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADR 271
Cdd:PHA02878  149 ITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755809 272 DAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGNVktVALLLEAGADP 336
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSERK--LKLLLEYGADI 293
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 124-270 2.68e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 124 GHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHG 202
Cdd:PHA02875   79 GDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755809 203 A--NIHDQLydGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDG-TAPLWIASQMGHSEVVRVMLLRGAD 270
Cdd:PHA02875  159 AclDIEDCC--GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-165 3.67e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 3.67e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755809 113 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-232 5.83e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 5.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 179 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 232
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-282 9.33e-10

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: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 133 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC-RTKDGGTALLAASQYGHMPVVETLLKHG---AN--IH 206
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAApelVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 207 DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGADRD 272
Cdd:cd22192    84 SDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                         170
                  ....*....|
gi 1039755809 273 AARNDGTTAL 282
Cdd:cd22192   164 AQDSLGNTVL 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 85-341 9.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  85 WAAKRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINlqreSGTTALFFAAQQGHNDVVRF 164
Cdd:PHA02876  184 YAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 165 LFGFGASTECRTKDGGTALLAASQYGHMP-VVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRLLLSSGAKVNQPR 242
Cdd:PHA02876  259 LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 243 QDGTAPLWIASQMG-HSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL--KNGTsALHAAVL 319
Cdd:PHA02876  339 RLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqKIGT-ALHFALC 417

                         250       260
                  ....*....|....*....|...
gi 1039755809 320 SGN-VKTVALLLEAGADPALRNK 341
Cdd:PHA02876  418 GTNpYMSVKTLIDRGANVNSKNK 440
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-239 3.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  86 AAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 165
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039755809 166 FGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLSSGAKVN 239
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 179-316 3.70e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 179 GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSgAKVNQPRQDGTApLWIASQMGHS 258
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755809 259 EVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 316
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 105-252 5.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 5.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSH-GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 183
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039755809 184 -LAASQYGHMPVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLSSGAKVNQPRQDGTAPLWIA 252
Cdd:PHA02878  239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-199 1.47e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 146 GTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLL 199
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 177-299 3.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 177 KDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMG 256
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039755809 257 HSEVVRVMLLRGADRD-AARNDGTTALLKAANKGYNDVIEELLK 299
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-187 6.17e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 6.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 101 SGRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL-------FGFGASTE 173
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqchFELGANAK 182

                          90
                  ....*....|....
gi 1039755809 174 CRTKDGGTALLAAS 187
Cdd:PTZ00322  183 PDSFTGKPPSLEDS 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-153 1.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755809 102 GRVDVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFA 153
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-337 1.75e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 105 DVDCRDSHGTT-LLMVASYAGHIDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTECRTKDGGT 181
Cdd:PHA03095   75 DVNAPERCGFTpLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 182 AL--LAASQYGHMPVVETLLKHGANIH----------DQLYD-------------------------GATALFLAAQGGY 224
Cdd:PHA03095  155 PLavLLKSRNANVELLRLLIDAGADVYavddrfrsllHHHLQsfkprarivreliragcdpaatdmlGNTPLHSMATGSS 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 225 LD--VIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELLKFSP 302
Cdd:PHA03095  235 CKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNP 314

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039755809 303 TL----GILKNGTSALHAAVLSGN---VKTVALLLEAGADPA 337
Cdd:PHA03095  315 SAetvaATLNTASVAGGDIPSDATrlcVAKVVLRGAFSLLPE 356
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 162-233 2.50e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755809 162 VRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLS 233
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 184-265 5.31e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 184 LAASqyGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRV 263
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1039755809 264 ML 265
Cdd:PTZ00322  167 LS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-218 5.96e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 129 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTALLAASQYGHMPVVETLLKH------- 201
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1039755809 202 GANIHDQLYDGATALFL 218
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 76-260 6.48e-07

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: 50.78  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809  76 ETPLanaaFWAAKRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVASYAGH-------IDCVRELVLQGADINLQResGTT 148
Cdd:cd22192    18 ESPL----LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ--GET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 149 ALFFAAQQGHNDVVRFLFGFGAS------TECRTKDGGTALL---------AASQyGHMPVVETLLKHGANIHDQLYDGA 213
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADvvspraTGTFFRPGPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQDSLGN 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809 214 TAL-FLAAQGGYL---DVIRLLLSSGAKVNQ------PRQDGTAPLWIASQMGHSEV 260
Cdd:cd22192   171 TVLhILVLQPNKTfacQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVM 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-239 1.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 104 VDVDCRDSHGTTLLMVASYA--GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLFGFGA--STECR-- 175
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVdiNAKNRvn 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755809 176 ----------TKD--GGTALLAASQYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN 239
Cdd:PHA03100  177 yllsygvpinIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-142 2.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 2.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809  66 ADMCRMSFKKETPLanaaFWAAKRGNLALLKLLLNSGRVDVDCrdsHGTTLLMVASYAGHIDCVRELVLQGADINLQ 142
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-265 2.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 2.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755809 214 TALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 265
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 224-342 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 224 YLDVIRLLLSSGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGADRDAARNDGTTALLKAAnkgYNDVIEEL 297
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039755809 298 LKFSPTLG--IL---KNGTSALHA--AVLSGNVKTVALLLEAGADPALRNKN 342
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLY 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-183 1.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039755809 137 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDGGTAL 183
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 181-336 2.22e-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: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 181 TALLAASQYGHMPVVETLLK-HGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAK-VNQPRQ----DGTAPLWIASQ 254
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 255 MGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDviEELLKFsptlgilkngtsalhaAVLSGNVKTVALLLEAGA 334
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNLIYYG--EHPLSF----------------AACVGNEEIVRLLIEHGA 160


                  ..
gi 1039755809 335 DP 336
Cdd:cd22192   161 DI 162
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 113-178 2.73e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755809 113 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKD 178
Cdd:PLN03192  622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 278-339 6.57e-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: 6.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809 278 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGADPALR 339
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
PHA02798 PHA02798
ankyrin-like protein; Provisional
 194-299 1.02e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 194 VVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLSSGAKVNQPRQDGTAPLWIA---SQMGHSEVVRVML 265
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMI 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039755809 266 LRGADRDAARNDGTTAL---LKAANKGYNDVIEELLK 299
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 211-239 1.05e-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: 1.05e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039755809  211 DGATALFLAAQGGYLDVIRLLLSSGAKVN 239
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 309-341 1.27e-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: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039755809 309 NGTSALHAAVLS-GNVKTVALLLEAGADPALRNK 341
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 179-331 1.54e-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: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 179 GGTALLAASQYGH-------MPVVETLLKHG-------ANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVnQPRQD 244
Cdd:cd21882    26 GKTCLHKAALNLNdgvneaiMLLLEAAPDSGnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 245 GTA--------------PLWIASQMGHSEVVRVMLLRGAD------RDAARNDGTTALLKAANKG----------YNDVI 294
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039755809 295 EELLKFSPT--LGILKN--GTSALHAAVLSGNVKTVALLLE 331
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQ 225
PHA02798 PHA02798
ankyrin-like protein; Provisional
 126-240 1.70e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 126 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTECRTKDGGT---ALLAASQYGHMPVVET 197
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039755809 198 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLSSGAKVNQ 240
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
278-330 2.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 278 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNVKTVALLL 330
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 112-141 2.35e-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: 2.35e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755809  112 HGTTLLMVASYAGHIDCVRELVLQGADINL 141
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 138-287 2.36e-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: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 138 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTECRTKDGGTALLAASQyGHMPVVETLLKHGANIH----------- 206
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 207 ---DQLYDGATALFLAAQGGYLDVIRLLLSSGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 269
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1039755809 270 DRDAARNDGTTaLLKAAN 287
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 178-208 2.92e-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: 2.92e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755809 178 DGGTAL-LAASQYGHMPVVETLLKHGANIHDQ 208
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 194-329 4.39e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 194 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLSSGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGADRDA 273
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039755809 274 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNVKTVALL 329
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
PHA03095 PHA03095
ankyrin-like protein; Provisional
 104-200 5.40e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 104 VDVDCRDSHGTTLLMVAsyAGHIDCVRELVLQ----GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKDG 179
Cdd:PHA03095  213 CDPAATDMLGNTPLHSM--ATGSSCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                          90       100
                  ....*....|....*....|.
gi 1039755809 180 GTALLAASQYGHMPVVETLLK 200
Cdd:PHA03095  291 NTPLSLMVRNNNGRAVRAALA 311
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 278-335 5.87e-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: 5.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039755809 278 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNVKTVALLLEAGAD 335
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 278-341 6.01e-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: 6.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755809 278 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNVKTVALLLEAGADPALRNK 341
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-298 6.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039755809 245 GTAPLWIASQMGHSEVVRVMLLRGADRDAARNDGTTALLKAANKGYNDVIEELL 298
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 309-336 8.35e-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: 8.35e-04
                           10        20
                   ....*....|....*....|....*...
gi 1039755809  309 NGTSALHAAVLSGNVKTVALLLEAGADP 336
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 188-340 1.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755809 188 QYGHMPVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLSSGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 267
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755809 268 gaDRDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNV-KTVALLLEAGADPALRN 340
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKN 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-142 2.04e-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: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755809 112 HGTTLLMVASY-AGHIDCVRELVLQGADINLQ 142
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 178-207 2.54e-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: 2.54e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755809  178 DGGTALLAASQYGHMPVVETLLKHGANIHD 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
310-342 3.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039755809 310 GTSALHAAVLSGNVKTVALLLEAGADPALRNKN 342
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN 33
PHA02795 PHA02795
ankyrin-like protein; Provisional
 105-157 6.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.44  E-value: 6.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755809 105 DVDCRDSHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQG 157
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 178-206 7.57e-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: 7.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 1039755809 178 DGGTALLAASQYGHMPVVETLLKHGANIH 206
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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