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Conserved domains on  [gi|27883850|ref|NP_705722|]
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ankyrin repeat domain-containing protein 23 isoform 1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-284 3.60e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.60e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHL 191
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 192 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170
                ....*....|...
gi 27883850 272 VKNVASQTPVQLA 284
Cdd:COG0666 247 AKDKDGLTALLLA 259
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-284 3.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.60e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHL 191
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 192 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170
                ....*....|...
gi 27883850 272 VKNVASQTPVQLA 284
Cdd:COG0666 247 AKDKDGLTALLLA 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-241 8.04e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 8.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850   149 LHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQgAQVNAQDKIWsTPLHVAVRMGHSDCLE 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 27883850   229 HLIECGAHINAQD 241
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 127-284 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  127 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNA 206
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27883850  207 QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 117-249 6.69e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 6.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAgaaieVRDLLD----------RTPVFWA 185
Cdd:cd22192  22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27883850 186 CRGGHLDILKRLLNQGAQV------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALH 249
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-239 7.03e-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: 7.03e-05
                           10        20
                   ....*....|....*....|....*..
gi 27883850    213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-284 3.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.60e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHL 191
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 192 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170
                ....*....|...
gi 27883850 272 VKNVASQTPVQLA 284
Cdd:COG0666 247 AKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-285 3.60e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.60e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 112 GLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHL 191
Cdd:COG0666  54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 192 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:COG0666 134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                       170
                ....*....|....
gi 27883850 272 VKNVASQTPVQLAR 285
Cdd:COG0666 214 AKDNDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-279 5.97e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 5.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 198
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 199 NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQ 278
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                .
gi 27883850 279 T 279
Cdd:COG0666 287 T 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-284 2.67e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 2.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 113 LEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLD 192
Cdd:COG0666  22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 193 ILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGV 272
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                       170
                ....*....|..
gi 27883850 273 KNVASQTPVQLA 284
Cdd:COG0666 182 RDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-241 8.04e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 8.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850   149 LHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQgAQVNAQDKIWsTPLHVAVRMGHSDCLE 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 27883850   229 HLIECGAHINAQD 241
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-274 1.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850   183 FWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDkEGDTALHEAVRYGHHKATKL 262
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 27883850   263 LLLYGAKLGVKN 274
Cdd:pfam12796  80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-284 3.28e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 3.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 125 EALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQV 204
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 205 NAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-248 8.94e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 8.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 198
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27883850 199 NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTAL 248
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 127-284 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  127 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNA 206
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27883850  207 QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-284 4.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 4.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  125 EALIDKYL-ADGGDPNAHDK-LHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGA 202
Cdd:PHA02878 146 EAEITKLLlSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  203 QVNAQDKIWSTPLHVAV-RMGHSDCLEHLIECGAHINAQDK-EGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTP 280
Cdd:PHA02878 226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTP 303


                 ....
gi 27883850  281 VQLA 284
Cdd:PHA02878 304 LSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-284 1.40e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  158 RQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHI 237
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 27883850  238 NAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
119-208 2.51e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850   119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVnKLLAAGAAIEVRDlLDRTPVFWACRGGHLDILKRLL 198
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 27883850   199 NQGAQVNAQD 208
Cdd:pfam12796  82 EKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-288 9.19e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 9.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  122 ENQEALIDKyladGGDPNAHDKLHRTALHWA-CLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQ 200
Cdd:PHA02876 322 ENIRTLIML----GADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  201 GAQVNAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAHINAQDKEGDTALHEAVRYG-HHKATKLLLLYGAKLGVKNVASQ 278
Cdd:PHA02876 398 GADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQ 477

                        170
                 ....*....|
gi 27883850  279 TPVQLARDWQ 288
Cdd:PHA02876 478 YPLLIALEYH 487
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-253 5.61e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWAC-RGGHLDIL 194
Cdd:PHA02878 172 LHYATENKDQRLTELLlSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDIL 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  195 KRLLNQGAQVNAQDKIWS-TPLHVAVRmgHSDCLEHLIECGAHINAQDKEGDTALHEAVR 253
Cdd:PHA02878 252 KLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 125-284 7.20e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 7.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  125 EALIDKyladGGDPNAHDKLHRTALHWACLKGHRQLVNK-----LLAAGAAIEVRDLLDRTPVFWA--CRGGHLDILKRL 197
Cdd:PHA03100  52 KILLDN----GADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  198 LNQGAQVNAQDKIWSTPLHVAVRMGHSDC------------------LEHLIECGAHINAQDKEGDTALHEAVRYGHHKA 259
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                        170       180
                 ....*....|....*....|....*
gi 27883850  260 TKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 130-270 6.63e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  130 KYLADGGDPNAHDKLHRTALHwACLKGHRQL----VNKLLAAGAAIEVRDLLDRTPVF-WACRGGHLDILKRLLNQGAQV 204
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLH-LYLHYSSEKvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27883850  205 NAQDKIWSTPLHVAVRmG---HSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKAT----KLLLLYGAKL 270
Cdd:PHA03095 111 NAKDKVGRTPLHVYLS-GfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNANvellRLLIDAGADV 180
PHA03095 PHA03095
ankyrin-like protein; Provisional
 161-281 6.63e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  161 VNKLLAAGAAIEVRDLLDRTP--VFWACRGG-HLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAH 236
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPlhLYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 27883850  237 INAQDKEGDTALH-----EAVRYghhKATKLLLLYGAKLGVKNVASQTPV 281
Cdd:PHA03095 110 VNAKDKVGRTPLHvylsgFNINP---KVIRLLLRKGADVNALDLYGMTPL 156
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 117-268 1.41e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  117 LKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILkR 196
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-R 608

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27883850  197 LLNQGAQVnAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGA 268
Cdd:PLN03192 609 ILYHFASI-SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-264 1.75e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 1.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 27883850   215 LHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 123-284 2.29e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  123 NQEALIDKYLADGGDPNAHDKLHRTALHwACLKG---HRQLVNKLLAAGAAIEVRDLLDRTP--VFWACRGGHLDILKRL 197
Cdd:PHA03095  95 TTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  198 LNQGAQVNAQDKIWSTPLHV--------------AVRMG-------------------HSDC----LEHLIECGAHINAQ 240
Cdd:PHA03095 174 IDAGADVYAVDDRFRSLLHHhlqsfkprarivreLIRAGcdpaatdmlgntplhsmatGSSCkrslVLPLLIAGISINAR 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 27883850  241 DKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA03095 254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-270 2.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  114 EMFLKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWAC-LKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGH- 190
Cdd:PHA02876 241 DLSLLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYd 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  191 LDILKRLLNQGAQVNAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAK 269
Cdd:PHA02876 321 TENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400


                 .
gi 27883850  270 L 270
Cdd:PHA02876 401 I 401
PHA03095 PHA03095
ankyrin-like protein; Provisional
 113-280 3.02e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  113 LEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALH-WACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFwACRGG-- 189
Cdd:PHA03095  51 LHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfn 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  190 -HLDILKRLLNQGAQVNAQDKIWSTPLHVAVRmgHSDC----LEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKL-- 262
Cdd:PHA03095 130 iNPKVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNAnvelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVre 207

                        170
                 ....*....|....*...
gi 27883850  263 LLLYGAKLGVKNVASQTP 280
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 191-282 1.49e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  191 LDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHeavRYGHHKAT----KLL 263
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLH---LYLYNATTldviKLL 103

                         90
                 ....*....|....*....
gi 27883850  264 LLYGAKLGVKNVASQTPVQ 282
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLH 122
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-231 2.24e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 2.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27883850   179 RTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLI 231
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-264 2.63e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 2.63e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 27883850   211 WSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 264
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 117-289 4.09e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 4.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  117 LKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILK 195
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGaDVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  196 RLLNQ-----------------------------GAQVNAQDKIWSTPLHVAVRMGH-SDCLEHLIECGAHINAQDKEGD 245
Cdd:PHA02876 229 AIIDNrsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGE 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 27883850  246 TALHEAVRYGHH-KATKLLLLYGAKLGVKNVASQTPVQLARDWQR 289
Cdd:PHA02876 309 TPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-242 3.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  161 VNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQ 240
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ..
gi 27883850  241 DK 242
Cdd:PHA03100 255 IE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 113-264 7.28e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  113 LEMFLKAAAENQEALidKYLADGG-DPNAHDKLHRTALHWAC--LKGHRQLVNKLLAAGAAIEVRDLLDRTPV-----FW 184
Cdd:PHA03095 156 LAVLLKSRNANVELL--RLLIDAGaDVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhsmatGS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  185 ACRGGHLDilkRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 264
Cdd:PHA03095 234 SCKRSLVL---PLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 180-284 9.06e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 9.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  180 TPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSD------------------CLEH-----LIECGAH 236
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILDCGID 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 27883850  237 INAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-284 2.10e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  158 RQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHS-----DCLEHLIE 232
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27883850  233 CGAHINAQDKEGDTALHEAV--RYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-251 2.10e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 2.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27883850   197 LLNQG-AQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEA 251
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 192-287 4.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  192 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 271
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90
                 ....*....|....*.
gi 27883850  272 VKNVASQTPVQLARDW 287
Cdd:PHA02874 185 VKDNNGESPLHNAAEY 200
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-268 5.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  110 PVGLEMFLKaaaeNQEAlIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEvrDLLDR---TPVFWAC 186
Cdd:PHA02875  38 PIKLAMKFR----DSEA-IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLAT 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  187 RGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLY 266
Cdd:PHA02875 111 ILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190


                 ..
gi 27883850  267 GA 268
Cdd:PHA02875 191 GA 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
145-198 9.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 27883850   145 HRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 198
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 164-233 2.63e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  164 LLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIEC 233
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-266 3.37e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 3.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  197 LLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLY 266
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 117-249 6.69e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 6.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 117 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAgaaieVRDLLD----------RTPVFWA 185
Cdd:cd22192  22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27883850 186 CRGGHLDILKRLLNQGAQV------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALH 249
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 119-279 1.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  119 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWAclkghrqlvnkLLAAGAAIEVRDLLDRtpvfwacrgghldilkrll 198
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-----------LCGTNPYMSVKTLIDR------------------- 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  199 nqGAQVNAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYghHKATKLLLLYGAKLGVKNVAS 277
Cdd:PHA02876 432 --GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGAELRDSRVLH 507


                 ..
gi 27883850  278 QT 279
Cdd:PHA02876 508 KS 509
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-198 1.78e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  104 PQVPLEPVGLEMF----LKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDR 179
Cdd:PTZ00322  70 TEEVIDPVVAHMLtvelCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149

                         90
                 ....*....|....*....
gi 27883850  180 TPVFWACRGGHLDILKRLL 198
Cdd:PTZ00322 150 TPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 127-200 4.90e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 4.90e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27883850  127 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQ 200
Cdd:PHA03095 239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-242 7.91e-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: 41.89  E-value: 7.91e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 27883850   213 TPLHVAV-RMGHSDCLEHLIECGAHINAQDK 242
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 215-286 1.16e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 1.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27883850  215 LHVAVRMGHSDCLEH---LIECGAHINAQD-KEGDTALHEAVRYGHHK-ATKLLLLYGAKLGVKNVASQTPVQLARD 286
Cdd:PHA02736  59 VHIVSNPDKADPQEKlklLMEWGADINGKErVFGNTPLHIAVYTQNYElATWLCNQPGVNMEILNYAFKTPYYVACE 135
PHA02741 PHA02741
hypothetical protein; Provisional
 185-286 1.60e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.65  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  185 ACRGGHLDILKRLL------NQGAQVNAQDKIWSTPLHVAVRMGHS----DCLEHLIECGAHINAQDK-EGDTALHEAV- 252
Cdd:PHA02741  28 AARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAh 107

                         90       100       110
                 ....*....|....*....|....*....|....
gi 27883850  253 RYGHHKATKLLLLYGAKLGVKNVASQTPVQLARD 286
Cdd:PHA02741 108 RRDHDLAEWLCCQPGIDLHFCNADNKSPFELAID 141
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-284 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 27883850  144 LHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGH 223
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27883850  224 SDCLEHLIECGAHIN-AQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02875  81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 147-268 2.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  147 TALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDC 226
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 27883850  227 LEHLIECGAHINAQDKEGD-TALHEAVRYGHHKATKLLLLYGA 268
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 170-284 4.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  170 AIEVRDLLDRTPVFWACRGGHL-DILKRLLNQGAQVNAQ----DKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEG 244
Cdd:PHA02884  24 AIKKKNKICIANILYSSIKFHYtDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEA 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 27883850  245 D-TALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02884 104 KiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-239 7.03e-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: 7.03e-05
                           10        20
                   ....*....|....*....|....*..
gi 27883850    213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 213-239 7.77e-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: 7.77e-05
                          10        20
                  ....*....|....*....|....*..
gi 27883850   213 TPLHVAVRMGHSDCLEHLIECGAHINA 239
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-284 9.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 9.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27883850   230 LIECG-AHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-165 2.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 27883850   118 KAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLL 165
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 178-206 2.62e-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: 2.62e-04
                           10        20
                   ....*....|....*....|....*....
gi 27883850    178 DRTPVFWACRGGHLDILKRLLNQGAQVNA 206
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 230-301 3.77e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 3.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27883850  230 LIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLARdwQRGIRDALQAHVGH 301
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRH 170
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 27883850 206 AQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDK--EGDTALHEAVRYGHHKATKLLL 264
Cdd:cd22192  12 QQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLM 71
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-182 4.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 27883850   133 ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPV 182
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 179-284 4.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  179 RTPVFWACRGGHLDILKRLLNQGAQVNaqDKIWS---TPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYG 255
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90       100
                 ....*....|....*....|....*....
gi 27883850  256 HHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIA 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
164-218 5.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27883850   164 LLAAG-AAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVA 218
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-209 6.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  123 NQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGA 202
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 ....*..
gi 27883850  203 QVNAQDK 209
Cdd:PHA03100 250 SIKTIIE 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
 191-274 7.78e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 7.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  191 LDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHEAVRYGHH---KATKLLL 264
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168

                         90
                 ....*....|
gi 27883850  265 LYGAKLGVKN 274
Cdd:PHA02798 169 EKGVDINTHN 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-209 8.50e-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: 36.11  E-value: 8.50e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 27883850   179 RTPVFWAC-RGGHLDILKRLLNQGAQVNAQDK 209
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 146-173 1.61e-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: 1.61e-03
                           10        20
                   ....*....|....*....|....*...
gi 27883850    146 RTALHWACLKGHRQLVNKLLAAGAAIEV 173
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 243-270 1.87e-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: 1.87e-03
                           10        20
                   ....*....|....*....|....*...
gi 27883850    243 EGDTALHEAVRYGHHKATKLLLLYGAKL 270
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-206 1.91e-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: 35.31  E-value: 1.91e-03
                          10        20
                  ....*....|....*....|....*...
gi 27883850   179 RTPVFWACRGGHLDILKRLLNQGAQVNA 206
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 146-219 2.07e-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: 39.48  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 146 RTALHWACLKGHRQLVNKLLAAGAAIEVR---DLLDRTP-----------VFWACRgGHLDILKRLLNQGAQ---VNAQD 208
Cdd:cd21882  74 QTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgelplSLAACT-NQEEIVRLLLENGAQpaaLEAQD 152

                        90
                ....*....|.
gi 27883850 209 KIWSTPLHVAV 219
Cdd:cd21882 153 SLGNTVLHALV 163
PHA02798 PHA02798
ankyrin-like protein; Provisional
 191-248 2.78e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 2.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27883850  191 LDILKRLLNQGAQVNAQDKIWSTPLHVAV----RMGHS-DCLEHLIECGAHINAQDKEGDTAL 248
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILsnikDYKHMlDIVKILIENGADINKKNSDGETPL 113
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-270 3.62e-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: 34.54  E-value: 3.62e-03
                          10        20
                  ....*....|....*....|....*...
gi 27883850   243 EGDTALHEAVRYGHHKATKLLLLYGAKL 270
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-274 3.87e-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: 34.57  E-value: 3.87e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 27883850   243 EGDTALHEAV-RYGHHKATKLLLLYGAKLGVKN 274
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 180-268 4.80e-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: 38.46  E-value: 4.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850 180 TPVFWACRGGHLDILKRLL-NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAH-----INAQDKEGDTALHEAVR 253
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98

                        90
                ....*....|....*
gi 27883850 254 YGHHKATKLLLLYGA 268
Cdd:cd22192  99 NQNLNLVRELIARGA 113
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 146-175 4.90e-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: 4.90e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 27883850   146 RTALHWACLK-GHRQLVNKLLAAGAAIEVRD 175
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02917 PHA02917
ankyrin-like protein; Provisional
 226-291 5.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.44  E-value: 5.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27883850  226 CLEHLIEcgahINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLARDWQRGI 291
Cdd:PHA02917 438 CLPYLKD----INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNI 499
Ank_2 pfam12796
Ankyrin repeats (3 copies);
248-284 5.54e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.48  E-value: 5.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 27883850   248 LHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 284
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA 37
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 114-178 7.73e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 37.19  E-value: 7.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27883850 114 EMFLKAAAENQEALIDKYLaDGGDPnAHDKLHRtALHWACLKGHrqLVNKLLAAGAA-IEVRDLLD 178
Cdd:cd04170 199 EELLEAVAETDEELMEKYL-EEGEL-TEEELRA-GLRRALRAGL--IVPVFFGSALTgIGVRRLLD 259
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 193-257 8.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.41  E-value: 8.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27883850  193 ILKRLlnqgaQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHH 257
Cdd:PHA02989 243 ILKYI-----KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNI 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 132-238 8.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  132 LADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIW 211
Cdd:PHA02875 122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

                         90       100
                 ....*....|....*....|....*...
gi 27883850  212 S-TPLHVAVRMGHSDCLEHLIECGAHIN 238
Cdd:PHA02875 202 CvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 189-272 9.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883850  189 GHLDILKRLL-NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYG 267
Cdd:PHA02874  12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91


                 ....*
gi 27883850  268 AKLGV 272
Cdd:PHA02874  92 VDTSI 96
 
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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