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Conserved domains on  [gi|1622888206|ref|XP_028693716|]
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ankyrin repeat domain-containing protein 29 isoform X2 [Macaca mulatta]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 7.39e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLK 232
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 211-272 1.61e-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: 46.03  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888206 211 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGADPSLR 272
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 7.39e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLK 232
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-171 5.66e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 5.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 8.95e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 8.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1622888206 130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-257 5.80e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 5.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  66 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 138
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 139 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAER 204
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 205 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 257
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 211-272 1.61e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888206 211 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGADPSLR 272
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 2.52e-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: 37.57  E-value: 2.52e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888206   45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-274 2.77e-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: 2.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622888206 242 NGTSALHAAVLS-GNIKTVALLLEAGADPSLRNK 274
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-166 3.47e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  41 CRDSHGTTLLMVAAYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFGASte 106
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 107 frtkdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLD 159
Cdd:TIGR00870 201 ---------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIV 271


                  ....*..
gi 1622888206 160 VIRLLLA 166
Cdd:TIGR00870 272 LFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 242-271 1.63e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.63e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888206  242 NGTSALHAAVLSGNIKTVALLLEAGADPSL 271
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-232 7.39e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLK 232
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-274 7.42e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 7.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 172 NQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKF-SPTLGILKNGTSALHAA 250
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgADLNAKDKDGLTALLLA 259

                         250       260
                  ....*....|....*....|....
gi 1622888206 251 VLSGNIKTVALLLEAGADPSLRNK 274
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-215 4.34e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 4.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  15 AAFWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDV 94
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQP 174
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622888206 175 RQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTAL 215
Cdd:COG0666   249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-287 1.31e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALL 117
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVM 197
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 198 LLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNKRE 276
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         250
                  ....*....|.
gi 1622888206 277 SCYIARAENLH 287
Cdd:COG0666   253 LTALLLAAAAG 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-171 5.66e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 5.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 8.95e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 8.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1622888206 130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-173 5.10e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  83 LFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1622888206 163 LLLASGAKVNQ 173
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-273 4.08e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 182 LWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFsPTLGILKNGTSALHAAVLSGNIKTVAL 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1622888206 262 LLEAGADPSLRN 273
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-203 3.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 3.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 116 LLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPrqDGTAPLWIASQMGHSEVVR 195
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1622888206 196 VMLLRGAE 203
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-288 2.45e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 125 MQVVETLLKHGANIHDQLYDGATALFLAAQGGY-----LDVIRLLLASGAKVNQPRQDGTAPLWIASQ--MGHSEVVRVM 197
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 198 LLRGAERDAARNDGTTAL----------LKAA----NKGYN----DVIEELLKF-SPTLGILKNGTSALHAAVLSGNIKT 258
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLhlylesnkidLKILklliDKGVDinakNRVNYLLSYgVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622888206 259 VALLLEAGADPSLRNKR-ESC--YIARAENLHF 288
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYgDTPlhIAILNNNKEI 240
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 90-275 1.68e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  90 GHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGA 169
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 170 KVNQP-RQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGILKN-GTSAL 247
Cdd:PHA02875   93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCcGCTPL 172

                         170       180
                  ....*....|....*....|....*...
gi 1622888206 248 HAAVLSGNIKTVALLLEAGADPSLRNKR 275
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKN 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-104 2.14e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  17 FWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGHNDVVR 96
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1622888206  97 FLFGFGAS 104
Cdd:pfam12796  79 LLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-272 3.49e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 3.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDC---VRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGG 113
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 114 TALLA--ASQYGHMQVVETLLKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMG 189
Cdd:PHA03095  119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 190 HS--EVVRVMLLRGAERDAARNDGTTALLKAANKGY--NDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLE 264
Cdd:PHA03095  199 KPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIA 278


                  ....*...
gi 1622888206 265 AGADPSLR 272
Cdd:PHA03095  279 LGADINAV 286
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-268 3.69e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 113 GTALLAASQY--GHMQVVETLLKHGANIHDQLYDGATALFLAAQGGY--LDVIRLLLASGAKVNQprqdgtaplwiasqm 188
Cdd:PHA03100  107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA--------------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 189 ghSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLLEAGA 267
Cdd:PHA03100  172 --KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  .
gi 1622888206 268 D 268
Cdd:PHA03100  250 S 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-275 7.44e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  47 TTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF------------------- 107
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgi 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 108 ----RTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLW 183
Cdd:PHA02874  116 dvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 184 IASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANkgYNDVIEELLKFSPTLGILK-NGTSALHAAV-LSGNIKTVAL 261
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDiDGSTPLHHAInPPCDIDIIDI 273

                         250
                  ....*....|....
gi 1622888206 262 LLEAGADPSLRNKR 275
Cdd:PHA02874  274 LLYHKADISIKDNK 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-231 1.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 117 LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQggYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHS-EVVR 195
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIID 272

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622888206 196 VMLLRGAERDAARNDGTTAL---LKAANKgyNDVIEELL 231
Cdd:PHA02874  273 ILLYHKADISIKDNKGENPIdtaFKYINK--DPVIKDII 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-275 1.92e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  59 IDCVRELVLQGADINLQRESGTTALffaAQQGHN------DVVRFLFGFGASTEFRTKDGGTALLAASQYGH-MQVVETL 131
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 132 LKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPL--WIASQMGHSEVVRVMLLRGAERDAA 207
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAV 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622888206 208 RNDGTTALLKAAN--KGYNDVIEELLKFS-PTLGILKNGTSALHAAVLSGNIKT--VALLLEAGADPSLRNKR 275
Cdd:PHA03095  184 DDRFRSLLHHHLQsfKPRARIVRELIRAGcDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRY 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-206 3.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206   5 SFKKETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDS-HGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTAL 83
Cdd:PHA02876  304 NIKGETPL----YLMAKNGYDTENIRTLIMLGADVNAADRlYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPI 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  84 FFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL-LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGG-YLDVI 161
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVI 459

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622888206 162 RLLLASGAKVNQPRQDGTAPLWIAsqMGHSEVVRVMLLRGAE-RDA 206
Cdd:PHA02876  460 EMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAElRDS 503
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-283 3.84e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  62 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 141 QlydgATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGH-SEVVRVMLLRGAERDAARNDGTTALLKAA 219
Cdd:PHA02876  240 N----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 220 NKGYNdviEELLKFSPTLGILKNGTSALH------AAVLSGNIKTVALLLEAGADPSLRNKRESCYIARA 283
Cdd:PHA02876  316 KNGYD---TENIRTLIMLGADVNAADRLYitplhqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 55-263 5.01e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  55 YAGHIDCVRELV-LQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLK 133
Cdd:PHA02874   10 YSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 134 HG-------------------------ANIHDQlyDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQM 188
Cdd:PHA02874   90 NGvdtsilpipciekdmiktildcgidVNIKDA--ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622888206 189 GHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGI-LKNGTSALHAAVLSgNIKTVALLL 263
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNkCKNGFTPLHNAIIH-NRSAIELLI 242
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-257 5.80e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 5.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  66 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 138
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 139 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTA--------------PLWIASQMGHSEVVRVMLLRGAER 204
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 205 DAARNDGTTAL----LKAANKGYNDVIEELLKF-----SPTLGILKN--GTSALHAAVLSGNIK 257
Cdd:cd22192   163 RAQDSLGNTVLhilvLQPNKTFACQMYDLILSYdkeddLQPLDLVPNnqGLTPFKLAAKEGNIV 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 126-273 1.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 126 QVVETLLKHGA--NIHDQlYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAE 203
Cdd:PHA02878  148 EITKLLLSYGAdiNMKDR-HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622888206 204 RDAARNDGTTALLKAANKGYN-DVIEELLKFSPTLGILKN--GTSALHAAVLSGniKTVALLLEAGADPSLRN 273
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKSE--RKLKLLLEYGADINSLN 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 48-242 3.65e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  48 TLLMVAAYAGH-IDCVRE----LVLQGADINLQRESGTTALFFAAQQ--GHNDVVRFLFGFGASTEFRTKDGGTALLAAS 120
Cdd:PHA03100   70 TPLHYLSNIKYnLTDVKEivklLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 121 QYGH--MQVVETLLKHGANIH-----DQLYD-----------GATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPL 182
Cdd:PHA03100  150 ESNKidLKILKLLIDKGVDINaknrvNYLLSygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 183 WIASQMGHSEVVRVMLLRGAERDAARNdgtTALLKAANKGYNDVIEELLKFSPTLGILKN 242
Cdd:PHA03100  230 HIAILNNNKEIFKLLLNNGPSIKTIIE---TLLYFKDKDLNTITKIKMLKKSIMYMFLLD 286
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-98 4.59e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 4.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622888206  46 GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 151-234 5.86e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 151 LAAQGGYLDvIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEEL 230
Cdd:PTZ00322   89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....
gi 1622888206 231 LKFS 234
Cdd:PTZ00322  168 SRHS 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 35-274 6.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  35 GRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR------------------ 96
Cdd:PHA02876  167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllk 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  97 -----------FLFGFGASTEFRTKDGGTALLAASQYGHM-QVVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRL 163
Cdd:PHA02876  247 airnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 164 LLASGAKVNQPRQDGTAPLWIASQMG-HSEVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELLKFSPTLGIL-- 240
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsq 406

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622888206 241 KNGTsALHAAVLSGN-IKTVALLLEAGADPSLRNK 274
Cdd:PHA02876  407 KIGT-ALHFALCGTNpYMSVKTLIDRGANVNSKNK 440
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-223 1.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  62 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 141 QLYDGATALFLAAqgGYL---DVIRLLLASGAKVN-QPRQDGTAPLWIASqmgHSE-VVRVMLLRGAERDAARNDGTTAL 215
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNaKSYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304


                  ....*...
gi 1622888206 216 LKAANKGY 223
Cdd:PHA02878  305 SSAVKQYL 312
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-185 2.36e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSH-GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206 117 -LAASQYGHMQVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLASGAKVNQPRQDGTAPLWIA 185
Cdd:PHA02878  239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-172 2.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  19 AARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622888206  99 FGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 3.92e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 3.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 112 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 112-249 7.51e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 7.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 112 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASgAKVNQPRQDGTApLWIASQMGHS 191
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622888206 192 EVVRVMLLRGAERDAARNDGTTALLKAANKGYNDVIEELlkfsptlgiLKNGTSALHA 249
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL---------IMNGADVDKA 684
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-193 1.65e-08

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: 55.40  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206   9 ETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGH-------IDCVRELVLQGADINLQResGTT 81
Cdd:cd22192    18 ESPL----LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ--GET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  82 ALFFAAQQGHNDVVRFLFGFGAS--------TEFRTkdGGTALL---------AASQyGHMQVVETLLKHGANIHDQLYD 144
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADvvspratgTFFRP--GPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQDSL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888206 145 GATAL-FLAAQGGYL---DVIRLLLASGAKVNQ------PRQDGTAPLWIASQMGHSEV 193
Cdd:cd22192   169 GNTVLhILVLQPNKTfacQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVM 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-232 2.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 110 KDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMG 189
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622888206 190 HSEVVRVMLLRGAERD-AARNDGTTALLKAANKGYNDVIEELLK 232
Cdd:PHA02875  180 DIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIK 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-100 1.02e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888206  34 SGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 100
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-151 1.47e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  62 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKH------- 134
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 1622888206 135 GANIHDQLYDGATALFL 151
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-86 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622888206  35 GRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFA 86
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-132 3.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 3.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888206  79 GTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLL 132
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-198 4.44e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 117 LAASqyGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRV 196
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1622888206 197 ML 198
Cdd:PTZ00322  167 LS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-172 4.94e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  37 VDVDCRDSHGTTLLMVAAYA--GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLF------------- 99
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIdkgvdinaknrvn 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622888206 100 ---GFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA03100  177 yllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-165 1.94e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-75 4.46e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 4.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622888206  14 NAAFWAARRGNLALLKLLLNSGRVDVDCrdsHGTTLLMVAAYAGHIDCVRELVLQGADINLQ 75
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-218 4.85e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  38 DVDCRDSHGTT-LLMVAAYAGHIDCVRELVLQGADINLQRESGTTAL--FFAAQQGHNDVVRFLFGFGASTEFRTKDGGT 114
Cdd:PHA03095   75 DVNAPERCGFTpLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 115 AL--LAASQYGHMQVVETLLKHGANIHD-----------------------------------QLYDGATALFLAAQGGY 157
Cdd:PHA03095  155 PLavLLKSRNANVELLRLLIDAGADVYAvddrfrsllhhhlqsfkprarivreliragcdpaaTDMLGNTPLHSMATGSS 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622888206 158 LD--VIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLLRGAERDAARNDGTTALLKA 218
Cdd:PHA03095  235 CKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-198 9.86e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 9.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622888206 147 TALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVML 198
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 211-272 1.61e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888206 211 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGADPSLR 272
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAR 102
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-107 3.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 3.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622888206  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF 107
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-173 6.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  59 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGT---ALLAASQYGHMQVVET 130
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622888206 131 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLASGAKVNQ 173
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 157-274 1.08e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 157 YLDVIRLLLASGAKVNQPRQDGTAPLwiaSQMGHS------EVVRVMLLRGAERDAARNDGTTALLKAAnkgYNDVIEEL 230
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYL---YNATTLDV 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622888206 231 LKFSPTLG--IL---KNGTSALHAAVLSGNI--KTVALLLEAGADPSLRNK 274
Cdd:PHA03095  100 IKLLIKAGadVNakdKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDL 150
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 112-279 1.30e-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: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 112 GGTALLAASQYGHMQVVETL------------LKHGAN--IHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVnQPRQD 177
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAImllleaapdsgnPKELVNapCTDEFYQGQTALHIAIENRNLNLVRLLVENGADV-SARAT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 178 GTA--------------PLWIASQMGHSEVVRVMLLRGAE------RDAARNDGTTALLKAANKG----------YNDVI 227
Cdd:cd21882   105 GRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaleaQDSLGNTVLHALVLQADNTpensafvcqmYNLLL 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 228 EELLKFSPT--LGILKN--GTSALHAAVLSGNIKTVALLLE----AGADPSLRNKRESCY 279
Cdd:cd21882   185 SYGAHLDPTqqLEEIPNhqGLTPLKLAAVEGKIVMFQHILQrefsGPYQPLSRKFTEWTY 244
PHA02798 PHA02798
ankyrin-like protein; Provisional
 125-232 2.06e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 125 MQVVETLLKHGANIHDQLYDGATAL--FLAAQGGY---LDVIRLLLASGAKVNQPRQDGTAPLWIA---SQMGHSEVVRV 196
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLF 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622888206 197 MLLRGAERDAARNDGTTAL---LKAANKGYNDVIEELLK 232
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLqvyLQSNHHIDIEIIKLLLE 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 2.52e-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: 37.57  E-value: 2.52e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888206   45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-116 2.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 2.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622888206  70 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-274 2.77e-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: 2.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622888206 242 NGTSALHAAVLS-GNIKTVALLLEAGADPSLRNK 274
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-141 3.15e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 3.15e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622888206 111 DGGTAL-LAASQYGHMQVVETLLKHGANIHDQ 141
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-166 3.47e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  41 CRDSHGTTLLMVAAYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFGASte 106
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 107 frtkdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLD 159
Cdd:TIGR00870 201 ---------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIV 271


                  ....*..
gi 1622888206 160 VIRLLLA 166
Cdd:TIGR00870 272 LFRLKLA 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 211-274 3.71e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 3.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888206 211 GTTALLKAA---NKGYNDVIEELLKFSPTLGILK------------NGTSALHAAVLSGNIKTVALLLEAGADPSLRNK 274
Cdd:cd22193    29 GKTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKrfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAK 107
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-220 3.82e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  71 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 139
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 140 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN----------QPRQD----GTAPLWIASQMGHSEVVRVMLLRGA 202
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPA 199

                         170
                  ....*....|....*...
gi 1622888206 203 ERDAARNDGTTaLLKAAN 220
Cdd:TIGR00870 200 DILTADSLGNT-LLHLLV 216
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 211-268 4.06e-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: 4.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622888206 211 GTTALLKAA---NKGYNDVIEELLKFSPTLGILKN------------GTSALHAAVLSGNIKTVALLLEAGAD 268
Cdd:cd22196    47 GKTCLLKAMlnlHNGQNDTISLLLDIAEKTGNLKEfvnaaytdsyykGQTALHIAIERRNMHLVELLVQNGAD 119
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-75 1.03e-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: 36.11  E-value: 1.03e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622888206  45 HGTTLLMVAAY-AGHIDCVRELVLQGADINLQ 75
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-172 1.06e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622888206  144 DGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 158-274 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 158 LDVIRLLLASGAKVNQPRQDGTAPLWIA----SQMGHSEVVRVMLLRG---AER-------------------DAARNDG 211
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINKCSvfyTLVaikdafnnrnveifkiiltNRYKNIQ 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 212 TTALLKAANKGYNDVIEE-----LLKFSPTLGIL--KNGTSALHAAVLSGNIKTVALLLEAGADPSLRNK 274
Cdd:PHA02878  130 TIDLVYIDKKSKDDIIEAeitklLLSYGADINMKdrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-263 1.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622888206 211 GTTALLKAANKGYNDVIEELLKFSPTLGIL-KNGTSALHAAVLSGNIKTVALLL 263
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-96 1.60e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 1.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR 96
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 242-271 1.63e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.63e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888206  242 NGTSALHAAVLSGNIKTVALLLEAGADPSL 271
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 121-273 2.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 121 QYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlr 200
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-- 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622888206 201 gaERDAARNDGTTALLKAANKgyNDVIEELLKFSP-----TLGILKNgtSALHAAVLSGNI-KTVALLLEAGADPSLRN 273
Cdd:PHA02876  232 --DNRSNINKNDLSLLKAIRN--EDLETSLLLYDAgfsvnSIDDCKN--TPLHHASQAPSLsRLVPKLLERGADVNAKN 304
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 127-262 2.53e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 127 VVETLLKHGANIHDqlydgatalflaaqggyLDVIRLLLASGAKVNQPRQDgtAPLWIASQMGHSEVVRVMLLRGAERDA 206
Cdd:PLN03192  493 ILKNFLQHHKELHD-----------------LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDI 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622888206 207 ARNDGTTALLKAANKGYNDVIEELLKFSPTLGILK-NGTSALHAAVLSGNIKTVALL 262
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL 610
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-133 2.99e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  37 VDVDCRDSHGTTLLMVAAYagHIDCVRELVLQ----GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMAT--GSSCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                          90       100
                  ....*....|....*....|.
gi 1622888206 113 GTALLAASQYGHMQVVETLLK 133
Cdd:PHA03095  291 NTPLSLMVRNNNGRAVRAALA 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-140 3.24e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 3.24e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622888206  111 DGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02795 PHA02795
ankyrin-like protein; Provisional
 38-90 3.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.82  E-value: 3.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622888206  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQG 90
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 147-268 3.40e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.84  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 147 TALFLAAQGGYLDVI-RLLLASGAKVNQPRQDGTAPLWIASQMGHSEVVRVMLlrgaerDAARNdgttallkaankgynd 225
Cdd:cd22192    19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM------EAAPE---------------- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622888206 226 vieelLKFSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGAD 268
Cdd:cd22192    77 -----LVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-272 3.68e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 141 QLYDGATALFLAAQGGYLDVIRLLLASGAKVNQ--PRQDGTAPL-WIASQMGHSEVVRVMLLRgaERDAARNDgttALLK 217
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLNIncPDRLGRSALfVAAIENENLELTELLLNL--SCRGAVGD---TLLH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206 218 AANKGYNDVIEELLK---------------FSPTLGILKNGTSALHAAVLSGNIKTVALLLEAGADPSLR 272
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgplelaNDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-139 4.66e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622888206  47 TTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH---NDVVRFLFGFGASTEFRTKDGGTALLAASQYG 123
Cdd:PHA02798   77 TILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSN 156

                          90
                  ....*....|....*....
gi 1622888206 124 H---MQVVETLLKHGANIH 139
Cdd:PHA02798  157 HhidIEIIKLLLEKGVDIN 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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