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Conserved domains on  [gi|1907070727|ref|XP_036010314|]
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ankyrin repeat domain-containing protein 23 isoform X1 [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];
1-171 4.06e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 4.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   1 MFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDIL 80
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  81 KRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKN 160
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170
                  ....*....|.
gi 1907070727 161 VASQTPVQLAR 171
Cdd:COG0666   217 NDGKTALDLAA 227
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-171 4.06e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 4.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   1 MFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDIL 80
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  81 KRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKN 160
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170
                  ....*....|.
gi 1907070727 161 VASQTPVQLAR 171
Cdd:COG0666   217 NDGKTALDLAA 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-127 3.95e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  35 LHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQgAQVNAQDKIWsTPLHVAVRMGHSDCLE 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907070727 115 HLIECGAHINAQD 127
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-170 1.05e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  13 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNA 92
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070727  93 QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-135 1.48e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAgaaieVRDLLD----------RTPVFWA 71
Cdd:cd22192    22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070727  72 CRGGHLDILKRLLNQGAQV------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALH 135
Cdd:cd22192    97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-125 4.11e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 4.11e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907070727   99 TPLHVAVRMGHSDCLEHLIECGAHINA 125
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-171 4.06e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 4.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   1 MFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDIL 80
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  81 KRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKN 160
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170
                  ....*....|.
gi 1907070727 161 VASQTPVQLAR 171
Cdd:COG0666   217 NDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-170 4.92e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 4.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   2 FLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILK 81
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  82 RLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNV 161
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*....
gi 1907070727 162 ASQTPVQLA 170
Cdd:COG0666   251 DGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-165 5.02e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 5.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   5 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 84
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  85 NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQ 164
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                  .
gi 1907070727 165 T 165
Cdd:COG0666   287 T 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-170 1.96e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 1.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   1 MFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDIL 80
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  81 KRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKN 160
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170
                  ....*....|
gi 1907070727 161 VASQTPVQLA 170
Cdd:COG0666   184 NDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-127 3.95e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  35 LHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQgAQVNAQDKIWsTPLHVAVRMGHSDCLE 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907070727 115 HLIECGAHINAQD 127
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-160 5.18e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 5.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  69 FWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDkEGDTALHEAVRYGHHKATKL 148
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1907070727 149 LLLYGAKLGVKN 160
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-170 1.05e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  13 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNA 92
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070727  93 QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-170 3.30e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  11 EALIDKYL-ADGGDPNAHDK-LHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGA 88
Cdd:PHA02878  146 EAEITKLLlSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  89 QVNAQDKIWSTPLHVAV-RMGHSDCLEHLIECGAHINAQDK-EGDTALHEAVRygHHKATKLLLLYGAKLGVKNVASQTP 166
Cdd:PHA02878  226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTP 303


                  ....
gi 1907070727 167 VQLA 170
Cdd:PHA02878  304 LSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-170 1.24e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.32  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  44 RQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHI 123
Cdd:PHA02874  104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070727 124 NAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-170 1.27e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  11 EALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQV 90
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  91 NAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-134 2.53e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   5 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 84
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907070727  85 NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTAL 134
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
5-94 6.48e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 6.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   5 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVnKLLAAGAAIEVRDlLDRTPVFWACRGGHLDILKRLL 84
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1907070727  85 NQGAQVNAQD 94
Cdd:pfam12796  82 EKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 8-174 8.87e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 8.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   8 ENQEALIDKyladGGDPNAHDKLHRTALHWA-CLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQ 86
Cdd:PHA02876  322 ENIRTLIML----GADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  87 GAQVNAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAHINAQDKEGDTALHEAVRYG-HHKATKLLLLYGAKLGVKNVASQ 164
Cdd:PHA02876  398 GADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQ 477

                         170
                  ....*....|
gi 1907070727 165 TPVQLARDWQ 174
Cdd:PHA02876  478 YPLLIALEYH 487
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-139 6.42e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 6.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWAC-RGGHLDIL 80
Cdd:PHA02878  172 LHYATENKDQRLTELLlSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDIL 251

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  81 KRLLNQGAQVNAQDKIWS-TPLHVAVRmgHSDCLEHLIECGAHINAQDKEGDTALHEAVR 139
Cdd:PHA02878  252 KLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 11-170 8.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 8.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  11 EALIDKyladGGDPNAHDKLHRTALHWACLKGHRQLVNK-----LLAAGAAIEVRDLLDRTPVFWA--CRGGHLDILKRL 83
Cdd:PHA03100   52 KILLDN----GADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  84 LNQGAQVNAQDKIWSTPLHVAVRMGHSDC------------------LEHLIECGAHINAQDKEGDTALHEAVRYGHHKA 145
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                         170       180
                  ....*....|....*....|....*
gi 1907070727 146 TKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHIA 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-154 1.59e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILkR 82
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-R 608

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070727  83 LLNQGAQVnAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGA 154
Cdd:PLN03192  609 ILYHFASI-SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-156 4.48e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWAC-LKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGH-LDI 79
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070727  80 LKRLLNQGAQVNAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKL 156
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-167 1.18e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  47 VNKLLAAGAAIEVRDLLDRTP--VFWACRGG-HLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHS-DCLEHLIECGAH 122
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPlhLYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907070727 123 INAQDKEGDTALH-----EAVRYghhKATKLLLLYGAKLGVKNVASQTPV 167
Cdd:PHA03095  110 VNAKDKVGRTPLHvylsgFNINP---KVIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-156 1.57e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  16 KYLADGGDPNAHDKLHRTALHwACLKGHRQL----VNKLLAAGAAIEVRDLLDRTPVF-WACRGGHLDILKRLLNQGAQV 90
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLH-LYLHYSSEKvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070727  91 NAQDKIWSTPLHV--AVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRygHHKAT----KLLLLYGAKL 156
Cdd:PHA03095  111 NAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNANvellRLLIDAGADV 180
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-175 5.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYLADGG-DPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILK 81
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGaDVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  82 RLLNQ-----------------------------GAQVNAQDKIWSTPLHVAVRMGH-SDCLEHLIECGAHINAQDKEGD 131
Cdd:PHA02876  229 AIIDNrsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGE 308

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907070727 132 TALHEAVRYGHH-KATKLLLLYGAKLGVKNVASQTPVQLARDWQR 175
Cdd:PHA02876  309 TPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-170 6.51e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   9 NQEALIDKYLADGGDPNAHDKLHRTALHwACLKG---HRQLVNKLLAAGAAIEVRDLLDRTP--VFWACRGGHLDILKRL 83
Cdd:PHA03095   95 TTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  84 LNQGAQVNAQDKIWSTPLHV--------------AVRMG-------------------HSDC----LEHLIECGAHINAQ 126
Cdd:PHA03095  174 IDAGADVYAVDDRFRSLLHHhlqsfkprarivreLIRAGcdpaatdmlgntplhsmatGSSCkrslVLPLLIAGISINAR 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907070727 127 DKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA03095  254 NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-150 1.66e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.66e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907070727 101 LHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-166 1.77e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   1 MFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALH-WACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGG--HL 77
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  78 DILKRLLNQGAQVNAQDKIWSTPLHVAVRmgHSDC----LEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKL--LLL 151
Cdd:PHA03095  133 KVIRLLLRKGADVNALDLYGMTPLAVLLK--SRNAnvelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIR 210

                         170
                  ....*....|....*
gi 1907070727 152 YGAKLGVKNVASQTP 166
Cdd:PHA03095  211 AGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-168 2.00e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  77 LDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHeavRYGHHKAT----KLL 149
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLH---LYLYNATTldviKLL 103

                          90
                  ....*....|....*....
gi 1907070727 150 LLYGAKLGVKNVASQTPVQ 168
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLH 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-128 6.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 6.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  47 VNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQ 126
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                  ..
gi 1907070727 127 DK 128
Cdd:PHA03100  255 IE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-170 1.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  66 TPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSD------------------CLEH-----LIECGAH 122
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILDCGID 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907070727 123 INAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-117 3.08e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907070727  65 RTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLI 117
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-150 3.46e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070727  97 WSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 150
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-170 3.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  44 RQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHS-----DCLEHLIE 118
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070727 119 CGAHINAQDKEGDTALHEAV--RYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-173 8.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 8.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  78 DILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLG 157
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90
                  ....*....|....*.
gi 1907070727 158 VKNVASQTPVQLARDW 173
Cdd:PHA02874  185 VKDNNGESPLHNAAEY 200
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 24-154 1.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  24 PNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEvrDLLDR---TPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTP 100
Cdd:PHA02875   61 PDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070727 101 LHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGA 154
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-150 1.56e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  16 KYLADGG-DPNAHDKLHRTALHWAC--LKGHRQLVNKLLAAGAAIEVRDLLDRTPV-----FWACRGGHLDilkRLLNQG 87
Cdd:PHA03095  171 RLLIDAGaDVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhsmatGSSCKRSLVL---PLLIAG 247

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070727  88 AQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLL 150
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-137 1.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907070727  83 LLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEA 137
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 50-119 5.56e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 5.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  50 LLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIEC 119
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 83-152 7.30e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 7.30e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  83 LLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLY 152
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
31-84 9.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 9.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070727  31 HRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 84
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-135 1.48e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   3 LKAAAENQEALIDKYL-ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAgaaieVRDLLD----------RTPVFWA 71
Cdd:cd22192    22 LLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070727  72 CRGGHLDILKRLLNQGAQV------------NAQDKIW--STPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALH 135
Cdd:cd22192    97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-165 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   5 AAAENQEALIDKYLADGGDPNAHDKLHRTALHWAclkghrqlvnkLLAAGAAIEVRDLLDRtpvfwacrgghldilkrll 84
Cdd:PHA02876  382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-----------LCGTNPYMSVKTLIDR------------------- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  85 nqGAQVNAQDKIWSTPLHVAVRMG-HSDCLEHLIECGAHINAQDKEGDTALHEAVRYghHKATKLLLLYGAKLGVKNVAS 163
Cdd:PHA02876  432 --GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGAELRDSRVLH 507


                  ..
gi 1907070727 164 QT 165
Cdd:PHA02876  508 KS 509
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 18-84 6.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 6.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070727  18 LADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLL 84
Cdd:PTZ00322  102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 13-86 4.33e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070727  13 LIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQ 86
Cdd:PHA03095  239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-170 4.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  30 LHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGH 109
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070727 110 SDCLEHLIECGAHIN-AQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 33-154 7.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  33 TALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDC 112
Cdd:PHA02875  104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907070727 113 LEHLIECGAHINAQDKEGD-TALHEAVRYGHHKATKLLLLYGA 154
Cdd:PHA02875  184 CKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 101-172 1.02e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 1.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070727 101 LHVAVRMGHSDCLEH---LIECGAHINAQD-KEGDTALHEAVRYGHHK-ATKLLLLYGAKLGVKNVASQTPVQLARD 172
Cdd:PHA02736   59 VHIVSNPDKADPQEKlklLMEWGADINGKErVFGNTPLHIAVYTQNYElATWLCNQPGVNMEILNYAFKTPYYVACE 135
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 56-170 1.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  56 AIEVRDLLDRTPVFWACRGGHL-DILKRLLNQGAQVNAQ----DKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEG 130
Cdd:PHA02884   24 AIKKKNKICIANILYSSIKFHYtDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEA 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907070727 131 D-TALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02884  104 KiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 71-172 2.59e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.72  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  71 ACRGGHLDILKRLL------NQGAQVNAQDKIWSTPLHVAVRMGHS----DCLEHLIECGAHINAQDK-EGDTALHEAV- 138
Cdd:PHA02741   28 AARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAh 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907070727 139 RYGHHKATKLLLLYGAKLGVKNVASQTPVQLARD 172
Cdd:PHA02741  108 RRDHDLAEWLCCQPGIDLHFCNADNKSPFELAID 141
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-128 7.28e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 7.28e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907070727  99 TPLHVAV-RMGHSDCLEHLIECGAHINAQDK 128
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 33-105 1.08e-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: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  33 TALHWACLKGHRQLVNKLLAAGAAIEvrdlldrTP----------------------VFWACRGgHLDILKRLLNQGAQV 90
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVV-------SPratgtffrpgpknliyygehplSFAACVG-NEEIVRLLIEHGADI 162

                          90
                  ....*....|....*
gi 1907070727  91 NAQDKIWSTPLHVAV 105
Cdd:cd22192   163 RAQDSLGNTVLHILV 177
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-187 1.16e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070727 116 LIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLARdwQRGIRDALQAHVGH 187
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-150 1.26e-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: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907070727  92 AQDKIWSTPLHVAVRMGHSDCLEHLIECgAHINAQDK--EGDTALHEAVRYGHHKATKLLL 150
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLM 71
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-170 1.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  65 RTPVFWACRGGHLDILKRLLNQGAQVNaqDKIWS---TPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYG 141
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100
                  ....*....|....*....|....*....
gi 1907070727 142 HHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-95 2.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727   9 NQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGA 88
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  ....*..
gi 1907070727  89 QVNAQDK 95
Cdd:PHA03100  250 SIKTIIE 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
 77-160 2.56e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  77 LDILKRLLNQGAQVNAQDKIWSTPLHVAVRMGHSDCLE---HLIECGAHINAQDKEGDTALHEAVRYGHH---KATKLLL 150
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168

                          90
                  ....*....|
gi 1907070727 151 LYGAKLGVKN 160
Cdd:PHA02798  169 EKGVDINTHN 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
116-170 4.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 4.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070727 116 LIECG-AHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLA 170
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-125 4.11e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 4.11e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907070727   99 TPLHVAVRMGHSDCLEHLIECGAHINA 125
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-125 4.69e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 4.69e-04
                          10        20
                  ....*....|....*....|....*..
gi 1907070727  99 TPLHVAVRMGHSDCLEHLIECGAHINA 125
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 32-105 6.99e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.48  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  32 RTALHWACLKGHRQLVNKLLAAGAAIEVR---DLLDRTP-----------VFWACRgGHLDILKRLLNQGAQ---VNAQD 94
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgelplSLAACT-NQEEIVRLLLENGAQpaaLEAQD 152

                          90
                  ....*....|.
gi 1907070727  95 KIWSTPLHVAV 105
Cdd:cd21882   153 SLGNTVLHALV 163
PHA02798 PHA02798
ankyrin-like protein; Provisional
 77-134 9.70e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 9.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070727  77 LDILKRLLNQGAQVNAQDKIWSTPLHVAV----RMGHS-DCLEHLIECGAHINAQDKEGDTAL 134
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILsnikDYKHMlDIVKILIENGADINKKNSDGETPL 113
Ank_5 pfam13857
Ankyrin repeats (many copies);
19-68 1.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 1.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907070727  19 ADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPV 68
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-92 1.45e-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: 1.45e-03
                           10        20
                   ....*....|....*....|....*....
gi 1907070727   64 DRTPVFWACRGGHLDILKRLLNQGAQVNA 92
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
4-51 1.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907070727   4 KAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLL 51
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-154 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  66 TPVFWACRGGHLDILKRLL-NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAH-----INAQDKEGDTALHEAVR 139
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98

                          90
                  ....*....|....*
gi 1907070727 140 YGHHKATKLLLLYGA 154
Cdd:cd22192    99 NQNLNLVRELIARGA 113
PHA02917 PHA02917
ankyrin-like protein; Provisional
 112-177 1.88e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.44  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070727 112 CLEHLIEcgahINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGVKNVASQTPVQLARDWQRGI 177
Cdd:PHA02917  438 CLPYLKD----INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNI 499
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-104 2.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 2.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070727  50 LLAAG-AAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIWSTPLHVA 104
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 3-64 2.53e-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: 37.57  E-value: 2.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070727   3 LKAAAENQEALIDKYLaDGGDPnAHDKLHRtALHWACLKGHrqLVNKLLAAGAA-IEVRDLLD 64
Cdd:cd04170   202 LEAVAETDEELMEKYL-EEGEL-TEEELRA-GLRRALRAGL--IVPVFFGSALTgIGVRRLLD 259
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 79-143 3.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.41  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070727  79 ILKRLlnqgaQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHH 143
Cdd:PHA02989  243 ILKYI-----KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNI 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 18-124 3.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  18 LADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIEVRDLLDRTPVFWACRGGHLDILKRLLNQGAQVNAQDKIW 97
Cdd:PHA02875  122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

                          90       100
                  ....*....|....*....|....*...
gi 1907070727  98 S-TPLHVAVRMGHSDCLEHLIECGAHIN 124
Cdd:PHA02875  202 CvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 75-158 3.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070727  75 GHLDILKRLL-NQGAQVNAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYG 153
Cdd:PHA02874   12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91


                  ....*
gi 1907070727 154 AKLGV 158
Cdd:PHA02874   92 VDTSI 96
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-95 5.85e-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: 33.42  E-value: 5.85e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907070727  65 RTPVFWAC-RGGHLDILKRLLNQGAQVNAQDK 95
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 66-139 6.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 36.50  E-value: 6.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070727  66 TPVFWACRGGHLDILKRLLNQGAQVNA-QDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVR 139
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-59 7.76e-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: 32.94  E-value: 7.76e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907070727   32 RTALHWACLKGHRQLVNKLLAAGAAIEV 59
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-156 8.92e-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: 32.56  E-value: 8.92e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907070727  129 EGDTALHEAVRYGHHKATKLLLLYGAKL 156
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-92 9.12e-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: 32.61  E-value: 9.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907070727  65 RTPVFWACRGGHLDILKRLLNQGAQVNA 92
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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