NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157817264|ref|NP_001101681|]
View 

ankyrin repeat domain-containing protein 23 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-285 4.60e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 4.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHL 191
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 192 DILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170
                 ....*....|....
gi 157817264 272 MKNGASLTPVQLAR 285
Cdd:COG0666  214 AKDNDGKTALDLAA 227
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-285 4.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 4.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHL 191
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 192 DILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170
                 ....*....|....
gi 157817264 272 MKNGASLTPVQLAR 285
Cdd:COG0666  214 AKDNDGKTALDLAA 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-241 2.57e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264  149 LHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQgAQINAQDKIWsTPLHVAVRMGHSDCLE 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 157817264  229 HLIECGAHINAQD 241
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-295 2.69e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.63  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 158 RQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHI 237
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817264 238 NAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARDWQRGIREAL 295
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELL 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 117-284 1.41e-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: 55.79  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLL-AAGAAIE---TRDL-LDRTPVFWACRGGH 190
Cdd:cd22192   22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNepmTSDLyQGETALHIAVVNQN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQI------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGH 256
Cdd:cd22192  102 LNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPN 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157817264 257 HKATK----LLLLYGAKLG------MKNGASLTPVQLA 284
Cdd:cd22192  182 KTFACqmydLILSYDKEDDlqpldlVPNNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-239 6.83e-05

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: 39.11  E-value: 6.83e-05
                           10        20
                   ....*....|....*....|....*..
gi 157817264   213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-285 4.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 4.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHL 191
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 192 DILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170
                 ....*....|....
gi 157817264 272 MKNGASLTPVQLAR 285
Cdd:COG0666  214 AKDNDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-284 5.88e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 5.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHL 191
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 192 DILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                        170
                 ....*....|...
gi 157817264 272 MKNGASLTPVQLA 284
Cdd:COG0666  247 AKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-279 1.45e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLL 198
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 199 NQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASL 278
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                 .
gi 157817264 279 T 279
Cdd:COG0666  287 T 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-284 4.32e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 4.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 113 LEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLD 192
Cdd:COG0666   22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 193 ILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGM 272
Cdd:COG0666  102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                        170
                 ....*....|..
gi 157817264 273 KNGASLTPVQLA 284
Cdd:COG0666  182 RDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-241 2.57e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264  149 LHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQgAQINAQDKIWsTPLHVAVRMGHSDCLE 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 157817264  229 HLIECGAHINAQD 241
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-274 2.00e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264  183 FWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDkEGDTALHEAVRYGHHKATKL 262
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 157817264  263 LLLYGAKLGMKN 274
Cdd:pfam12796  80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-284 3.77e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 125 EALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQI 204
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 205 NAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-248 6.24e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 6.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLL 198
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157817264 199 NQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTAL 248
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-295 2.69e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.63  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 158 RQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHI 237
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817264 238 NAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARDWQRGIREAL 295
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELL 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-284 2.99e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.55  E-value: 2.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 125 EALIDKYL-ADGGDPNAHDK-LHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGA 202
Cdd:PHA02878 146 EAEITKLLlSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 203 QINAQDKIWSTPLHVAV-RMGHSDCLEHLIECGAHINAQDK-EGDTALHEAVRygHHKATKLLLLYGAKLGMKNGASLTP 280
Cdd:PHA02878 226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTP 303


                 ....
gi 157817264 281 VQLA 284
Cdd:PHA02878 304 LSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
119-208 3.18e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264  119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVnKLLAAGAAIETRDlLDRTPVFWACRGGHLDILKQLL 198
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 157817264  199 NQGAQINAQD 208
Cdd:pfam12796  82 EKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 127-284 1.78e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 127 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINA 206
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817264 207 QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-253 1.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWAC-RGGHLDIL 194
Cdd:PHA02878 172 LHYATENKDQRLTELLlSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDIL 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 195 KQLLNQGAQINAQDKIWS-TPLHVAVRmgHSDCLEHLIECGAHINAQDKEGDTALHEAVR 253
Cdd:PHA02878 252 KLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-284 4.24e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 4.24e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264  215 LHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGasLTPVQLA 284
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG--RTALHYA 68
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-288 4.97e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 4.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 122 ENQEALIDKyladGGDPNAHDKLHRTALHWA-CLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQ 200
Cdd:PHA02876 322 ENIRTLIML----GADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 201 GAQINAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAHINAQDKEGDTALHEAVRYG-HHKATKLLLLYGAKLGMKNGASL 278
Cdd:PHA02876 398 GADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQ 477

                        170
                 ....*....|
gi 157817264 279 TPVQLARDWQ 288
Cdd:PHA02876 478 YPLLIALEYH 487
PHA03095 PHA03095
ankyrin-like protein; Provisional
 130-270 5.17e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 5.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 130 KYLADGGDPNAHDKLHRTALHwACLKGHRQL----VNKLLAAGAAIETRDLLDRTPVF-WACRGGHLDILKQLLNQGAQI 204
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLH-LYLHYSSEKvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817264 205 NAQDKIWSTPLHVAVRmG---HSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKAT----KLLLLYGAKL 270
Cdd:PHA03095 111 NAKDKVGRTPLHVYLS-GfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNANvellRLLIDAGADV 180
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 117-304 2.70e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 117 LKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKq 196
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR- 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 197 LLNQGAQInAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLygaklgmkNGA 276
Cdd:PLN03192 609 ILYHFASI-SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM--------NGA 679

                        170       180       190
                 ....*....|....*....|....*....|
gi 157817264 277 SLTPVQLARDWQ-RGIREALQA-HVGHPRT 304
Cdd:PLN03192 680 DVDKANTDDDFSpTELRELLQKrELGHSIT 709
PHA03095 PHA03095
ankyrin-like protein; Provisional
 161-281 2.83e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 161 VNKLLAAGAAIETRDLLDRTP--VFWACRGG-HLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAH 236
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPlhLYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157817264 237 INAQDKEGDTALH-----EAVRYghhKATKLLLLYGAKLGMKNGASLTPV 281
Cdd:PHA03095 110 VNAKDKVGRTPLHvylsgFNINP---KVIRLLLRKGADVNALDLYGMTPL 156
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-270 4.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 4.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 114 EMFLKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWAC-LKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGH- 190
Cdd:PHA02876 241 DLSLLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYd 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQINAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAK 269
Cdd:PHA02876 321 TENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400


                 .
gi 157817264 270 L 270
Cdd:PHA02876 401 I 401
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-268 1.09e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 132 LADGGDPNAHDKLHRTALHWACLK--GHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGH--LDILKQLLNQGAQINAQ 207
Cdd:PHA03100  93 LEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAK 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817264 208 DKI----------------WSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGA 268
Cdd:PHA03100 173 NRVnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-284 1.27e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 125 EALIDKyladGGDPNAHDKLHRTALHwACLKGHR---QLVNKLLAAGAAIETRDLLDRTPVFWacrggHLD-------IL 194
Cdd:PHA03095 136 RLLLRK----GADVNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADVYAVDDRFRSLLHH-----HLQsfkprarIV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 195 KQLLNQGAQINAQDKIWSTPLHVAVRmgHSDC----LEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKL 270
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMAT--GSSCkrslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283

                        170
                 ....*....|....
gi 157817264 271 GMKNGASLTPVQLA 284
Cdd:PHA03095 284 NAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-274 1.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 132 LADGGDPNahDKLHRTALHWAclKGHRQ--LVNKLLAAGAAIETRDLLDRTPVFWACRGGH-----LDILKQLLNQGAQI 204
Cdd:PHA03100  24 EDDLNDYS--YKKPVLPLYLA--KEARNidVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817264 205 NAQDKIWSTPLHVAV--RMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHH--KATKLLLLYGAKLGMKN 274
Cdd:PHA03100 100 NAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-264 2.93e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 2.93e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157817264  211 WSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 264
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 113-249 4.33e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 4.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 113 LEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALH-WACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFwACRGG-- 189
Cdd:PHA03095  51 LHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfn 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817264 190 -HLDILKQLLNQGAQINAQDKIWSTPLHVAVRmgHSDC----LEHLIECGAHINAQDKEGDTALH 249
Cdd:PHA03095 130 iNPKVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNAnvelLRLLIDAGADVYAVDDRFRSLLH 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 113-264 8.35e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 113 LEMFLKAAAENQEALidKYLADGG-DPNAHDKLHRTALHWAC--LKGHRQLVNKLLAAGAAIETRDLLDRTPV-----FW 184
Cdd:PHA03095 156 LAVLLKSRNANVELL--RLLIDAGaDVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhsmatGS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 185 ACRGGHLDilkQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 264
Cdd:PHA03095 234 SCKRSLVL---PLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 117-289 1.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 117 LKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILK 195
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGaDVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 196 QLLNQ-----------------------------GAQINAQDKIWSTPLHVAVRMGH-SDCLEHLIECGAHINAQDKEGD 245
Cdd:PHA02876 229 AIIDNrsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGE 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157817264 246 TALHEAVRYGHH-KATKLLLLYGAKLGMKNGASLTPVQLARDWQR 289
Cdd:PHA02876 309 TPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-231 2.07e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 2.07e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157817264  179 RTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLI 231
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 191-282 3.07e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHeavRYGHHKAT----KLL 263
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLH---LYLYNATTldviKLL 103

                         90
                 ....*....|....*....
gi 157817264 264 LLYGAKLGMKNGASLTPVQ 282
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLH 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-242 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 161 VNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQ 240
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ..
gi 157817264 241 DK 242
Cdd:PHA03100 255 IE 256
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-251 2.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 2.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157817264  197 LLNQG-AQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEA 251
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 180-284 5.18e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 5.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 180 TPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSD------------------CLEH-----LIECGAH 236
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILDCGID 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157817264 237 INAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-268 5.98e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 5.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 110 PVGLEMFLKaaaeNQEAlIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEtrDLLDR---TPVFWAC 186
Cdd:PHA02875  38 PIKLAMKFR----DSEA-IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLAT 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 187 RGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLY 266
Cdd:PHA02875 111 ILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190


                 ..
gi 157817264 267 GA 268
Cdd:PHA02875 191 GA 192
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 117-284 1.41e-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: 55.79  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLL-AAGAAIE---TRDL-LDRTPVFWACRGGH 190
Cdd:cd22192   22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNepmTSDLyQGETALHIAVVNQN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQI------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGH 256
Cdd:cd22192  102 LNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPN 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 157817264 257 HKATK----LLLLYGAKLG------MKNGASLTPVQLA 284
Cdd:cd22192  182 KTFACqmydLILSYDKEDDlqpldlVPNNQGLTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-284 1.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 158 RQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHS-----DCLEHLIE 232
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157817264 233 CGAHINAQDKEGDTALHEAV--RYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_4 pfam13637
Ankyrin repeats (many copies);
145-198 3.49e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 3.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157817264  145 HRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLL 198
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 164-233 2.58e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 164 LLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIEC 233
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-266 3.28e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 3.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 197 LLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLY 266
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-198 2.22e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 104 PQVPLEPVGLEMF----LKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDR 179
Cdd:PTZ00322  70 TEEVIDPVVAHMLtvelCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149

                         90
                 ....*....|....*....
gi 157817264 180 TPVFWACRGGHLDILKQLL 198
Cdd:PTZ00322 150 TPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-242 7.17e-06

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: 42.28  E-value: 7.17e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 157817264  213 TPLHVAV-RMGHSDCLEHLIECGAHINAQDK 242
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 119-270 1.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWAclkghrqlvnkLLAAGAAIETRDLLDRtpvfwacrgghldilkqll 198
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-----------LCGTNPYMSVKTLIDR------------------- 431

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817264 199 nqGAQINAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYghHKATKLLLLYGAKL 270
Cdd:PHA02876 432 --GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 163-284 1.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 163 KLLAAGAAIETRDLLD-RTPVFWACRGGHLDILKQLLNQGAQINaqDKIWS---TPLHVAVRMGHSDCLEHLIECGAHIN 238
Cdd:PHA02875  52 KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPD 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157817264 239 AQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 170-284 1.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 170 AIETRDLLDRTPVFWACRGGHL-DILKQLLNQGAQINAQ----DKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEG 244
Cdd:PHA02884  24 AIKKKNKICIANILYSSIKFHYtDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEA 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157817264 245 D-TALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA02884 104 KiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 227-286 2.11e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.26  E-value: 2.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817264 227 LEHLIECGAHINAQDK-EGDTALHEAV-RYGHHKATKLLLLYGAKLGMKNGASLTPVQLARD 286
Cdd:PHA02741  80 IDHLIELGADINAQEMlEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAID 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-284 2.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157817264  230 LIECG-AHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 127-200 5.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 5.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817264 127 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQ 200
Cdd:PHA03095 239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-239 6.83e-05

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: 39.11  E-value: 6.83e-05
                           10        20
                   ....*....|....*....|....*..
gi 157817264   213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-284 7.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 144 LHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGH 223
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817264 224 SDCLEHLIECGAHIN-AQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLA 284
Cdd:PHA02875  81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-239 8.16e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 8.16e-05
                          10        20
                  ....*....|....*....|....*..
gi 157817264  213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 178-206 8.39e-05

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: 39.11  E-value: 8.39e-05
                           10        20
                   ....*....|....*....|....*....
gi 157817264   178 DRTPVFWACRGGHLDILKQLLNQGAQINA 206
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 147-268 9.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 147 TALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDC 226
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157817264 227 LEHLIECGAHINAQDKEGD-TALHEAVRYGHHKATKLLLLYGA 268
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-209 1.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 123 NQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGA 202
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 ....*..
gi 157817264 203 QINAQDK 209
Cdd:PHA03100 250 SIKTIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-165 2.53e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 157817264  118 KAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLL 165
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 215-286 2.97e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817264 215 LHVAVRMGHSDCLEH---LIECGAHINAQD-KEGDTALHEAVRYGHHK-ATKLLLLYGAKLGMKNGASLTPVQLARD 286
Cdd:PHA02736  59 VHIVSNPDKADPQEKlklLMEWGADINGKErVFGNTPLHIAVYTQNYElATWLCNQPGVNMEILNYAFKTPYYVACE 135
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 206-264 4.10e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 4.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817264 206 AQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDK--EGDTALHEAVRYGHHKATKLLL 264
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLM 71
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 230-301 6.57e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 6.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817264 230 LIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARdwQRGIREALQAHVGH 301
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRH 170
PHA02798 PHA02798
ankyrin-like protein; Provisional
 191-274 7.25e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHEAVRYGHH---KATKLLL 264
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168

                         90
                 ....*....|
gi 157817264 265 LYGAKLGMKN 274
Cdd:PHA02798 169 EKGVDINTHN 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-182 7.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 7.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157817264  133 ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPV 182
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 146-219 1.07e-03

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: 40.63  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 146 RTALHWACLKGHRQLVNKLLAAGAAIETR---DLLDRTP-----------VFWACRgGHLDILKQLLNQGAQI---NAQD 208
Cdd:cd21882   74 QTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgelplSLAACT-NQEEIVRLLLENGAQPaalEAQD 152

                         90
                 ....*....|.
gi 157817264 209 KIWSTPLHVAV 219
Cdd:cd21882  153 SLGNTVLHALV 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-209 1.15e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157817264  179 RTPVFWAC-RGGHLDILKQLLNQGAQINAQDK 209
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-206 1.21e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 1.21e-03
                          10        20
                  ....*....|....*....|....*...
gi 157817264  179 RTPVFWACRGGHLDILKQLLNQGAQINA 206
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
164-218 1.44e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157817264  164 LLAAG-AAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVA 218
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 243-270 1.83e-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: 1.83e-03
                           10        20
                   ....*....|....*....|....*...
gi 157817264   243 EGDTALHEAVRYGHHKATKLLLLYGAKL 270
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 146-172 2.30e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 2.30e-03
                           10        20
                   ....*....|....*....|....*..
gi 157817264   146 RTALHWACLKGHRQLVNKLLAAGAAIE 172
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02917 PHA02917
ankyrin-like protein; Provisional
 226-304 3.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.21  E-value: 3.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817264 226 CLEHLIEcgahINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARDWQRGIrEALQAHVGHPRT 304
Cdd:PHA02917 438 CLPYLKD----INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNI-ELLKMLLCHKPT 511
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-270 3.84e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|....*...
gi 157817264  243 EGDTALHEAVRYGHHKATKLLLLYGAKL 270
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 191-248 4.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817264 191 LDILKQLLNQGAQINAQDKIWSTPLHVAV----RMGHS-DCLEHLIECGAHINAQDKEGDTAL 248
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILsnikDYKHMlDIVKILIENGADINKKNSDGETPL 113
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 191-296 4.87e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.59  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 191 LDILKQLLNQGAQINAQDK--------------IWSTPLHVAVRMGHSDCLEHLIE-CGAHINAQDKEGDTALHEAVRYG 255
Cdd:cd22194  154 GDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEkESTDITSQDSRGNTVLHALVTVA 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157817264 256 HHKAT----------KLLLLYGAK--LGMKNGASLTPVQLARdwQRGIREALQ 296
Cdd:cd22194  234 EDSKTqndfvkrmydMILLKSENKnlETIRNNEGLTPLQLAA--KMGKAEILK 284
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-274 5.20e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 5.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 157817264  243 EGDTALHEAV-RYGHHKATKLLLLYGAKLGMKN 274
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 189-267 5.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.02  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 189 GHLDILKQLL-NQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYG 267
Cdd:PHA02874  12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 132-238 8.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817264 132 LADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIW 211
Cdd:PHA02875 122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

                         90       100
                 ....*....|....*....|....*...
gi 157817264 212 S-TPLHVAVRMGHSDCLEHLIECGAHIN 238
Cdd:PHA02875 202 CvAALCYAIENNKIDIVRLFIKRGADCN 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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