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Conserved domains on  [gi|2217323603|ref|XP_047295542|]
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DNA-binding protein RFXANK isoform X1 [Homo sapiens]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-244 5.82e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 5.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 244
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-244 5.82e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 5.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 244
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-218 7.63e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 7.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 128 LIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERdVDINIYDwNGGTPLLYAVRGNHVKCVE 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2217323603 208 ALLARGADLTT 218
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-244 1.49e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 117 VNKPDERGFTPLIWASA--FGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI------------------VGLL 176
Cdd:PHA03100   99 VNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323603 177 LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVaLGYRKDGVSLLL 244
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-LNNNKEIFKLLL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 189-217 6.09e-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: 6.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217323603  189 NGGTPLLYAVRGNHVKCVEALLARGADLT 217
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 126-218 3.68e-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: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 126 TPLIWASAFGEIETVRFLLEW-GADPHILAKERESALSLASTGGYTDIVGLLLERDVD-IN------IYDwnGGTPLLYA 197
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtsdLYQ--GETALHIA 96

                          90       100
                  ....*....|....*....|.
gi 2217323603 198 VRGNHVKCVEALLARGADLTT 218
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVS 117
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-244 5.82e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 5.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 244
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-244 2.01e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 2.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  87 ATLDSLSIHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLAST 166
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323603 167 GGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGyRKDGVSLLL 244
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLL 206
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-248 8.41e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 8.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLLPRLE 248
Cdd:COG0666   203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-244 2.02e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  89 LDSLSIHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGG 168
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323603 169 YTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYrKDGVSLLL 244
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-218 7.63e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 7.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 128 LIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERdVDINIYDwNGGTPLLYAVRGNHVKCVE 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2217323603 208 ALLARGADLTT 218
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-227 5.59e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPM 227
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-244 1.49e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 117 VNKPDERGFTPLIWASA--FGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI------------------VGLL 176
Cdd:PHA03100   99 VNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323603 177 LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVaLGYRKDGVSLLL 244
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-LNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-244 8.81e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 8.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 161 LSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGAdlTTEADSGYTPMDLAVALGYRkDGV 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHL-EIV 77


                  ....
gi 2217323603 241 SLLL 244
Cdd:pfam12796  78 KLLL 81
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 117-244 1.10e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 117 VNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLY 196
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217323603 197 AVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVAlgYRKDGVSLLL 244
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-187 1.21e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEwgadpHILAKER---ESALSLASTGGYT 170
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-----HADVNLKdngRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 2217323603 171 DIVGLLLERDVDINIYD 187
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
104-244 1.08e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 104 DQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDI 183
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323603 184 NIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYrKDGVSLLL 244
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN-LEIVKLLL 140
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-246 2.20e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 173
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSG-YTPMDLAVAlGYRKDGVSLLLPR 246
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIE-NNKIDIVRLFIKR 224
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-244 3.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 3.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 136 EIETVRFLLEWGADPHILAKERESALSLASTGGYT-----DIVGLLLERDVDINIYDWNGGTPLLYAV--RGNHVKCVEA 208
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217323603 209 LLARGADLTTEADSGYTPMDLAVALGYRK-DGVSLLL 244
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlKILKLLI 163
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 136-259 1.79e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 136 EIETVRFLLEWGADPHILAKER-ESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGA 214
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217323603 215 DLTTEADSGYTPMDLAVALGYRKDGVSLLLPRLECYGVISAHCNF 259
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGL 270
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-246 2.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  93 SIHQLAAQGELdQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI 172
Cdd:PHA02876  148 LIKERIQQDEL-LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 173 VGLLLERDVDINIYD------------------WNGG-----------TPLLYAVRGNHV-KCVEALLARGADLTTEADS 222
Cdd:PHA02876  227 IKAIIDNRSNINKNDlsllkairnedletslllYDAGfsvnsiddcknTPLHHASQAPSLsRLVPKLLERGADVNAKNIK 306

                         170       180
                  ....*....|....*....|....
gi 2217323603 223 GYTPMDLAVALGYRKDGVSLLLPR 246
Cdd:PHA02876  307 GETPLYLMAKNGYDTENIRTLIML 330
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-185 3.33e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217323603 117 VNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINI 185
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-249 3.53e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  60 SPQAGSSLKHSTTLTNRQRGNEVSAlPATLDSLSIHQLAA-QGELDQLKEHLRK---GDNLVNKPDergftpliWASAFG 135
Cdd:PTZ00322    1 MSFLVCSVASSAFAAQLFFGTEGSR-KRRAKPISFERMAAiQEEIARIDTHLEAleaTENKDATPD--------HNLTTE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 136 EIetvrfllewgADP---HILAKEresALSLASTGgytDIVG--LLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL 210
Cdd:PTZ00322   72 EV----------IDPvvaHMLTVE---LCQLAASG---DAVGarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL 135

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217323603 211 ARGADLTTEADSGYTPMDLAVALGYRkDGVSLLLPRLEC 249
Cdd:PTZ00322  136 EFGADPTLLDKDGKTPLELAEENGFR-EVVQLLSRHSQC 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-232 4.23e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 110 LRKGDNlVNKPDERGFTPL--IWASAFGEIETVRFLLEWGADP-----------HILA---KERES-------------- 159
Cdd:PHA03095  139 LRKGAD-VNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVyavddrfrsllHHHLqsfKPRARivreliragcdpaa 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 160 -------ALSLASTGGYTD--IVGLLLERDVDINIYDWNGGTPLLYA-VRGNHVKCVEaLLARGADLTTEADSGYTPMDL 229
Cdd:PHA03095  218 tdmlgntPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSL 296


                  ...
gi 2217323603 230 AVA 232
Cdd:PHA03095  297 MVR 299
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 136-234 6.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 136 EIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGAD 215
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90
                  ....*....|....*....
gi 2217323603 216 LTTEADSGYTPMDLAVALG 234
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYG 201
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-230 1.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323603 175 LLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLA 230
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 101-231 2.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 101 GELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLL---- 176
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidng 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217323603 177 -------------------LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAV 231
Cdd:PHA02874   92 vdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 78-235 3.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  78 RGNEVSALpatlDSLSIHQLAAQGELDQLKEH----LRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHIL 153
Cdd:PHA02876  330 LGADVNAA----DRLYITPLHQASTLDRNKDIvitlLELGAN-VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 154 AKERESAL--SLASTGGYTDiVGLLLERDVDINIYDWNGGTPLLYAVRGN-HVKCVEALLARGADLTTEADSGYTPmdLA 230
Cdd:PHA02876  405 SQKIGTALhfALCGTNPYMS-VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP--LL 481


                  ....*
gi 2217323603 231 VALGY 235
Cdd:PHA02876  482 IALEY 486
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-210 7.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323603 157 RESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL 210
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-231 8.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 8.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 117 VNKPDE-RGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLL 195
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217323603 196 YAV-RGNHVKCVEALLARGADLTTEAD-SGYTPMDLAV 231
Cdd:PHA02878  240 ISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI 277
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-230 8.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNLvNKPDERGFTPLIWASAFGEIETVRFLLEWGAdpHILAKERESALSLASTGGYTDIV 173
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHNRSA 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323603 174 GLLLERDVDINIYDWNGGTPLLYAVRGN-HVKCVEALLARGADLTTEADSGYTPMDLA 230
Cdd:PHA02874  238 IELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 103-228 1.10e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 103 LDQLKEHLRKGDNlVNKPDERGFTPL-IWASAFGE--IETVRFLLEWGADphILAKER--ESALSLASTGGYT-DIVGLL 176
Cdd:PHA03095   27 VEEVRRLLAAGAD-VNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGAD--VNAPERcgFTPLHLYLYNATTlDVIKLL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323603 177 LERDVDINIYDWNGGTPL-LYAVRGN-HVKCVEALLARGADLTTEADSGYTPMD 228
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 88-244 1.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  88 TLDSLSIHQLAAQGE-LDQLKEHLRKGDNlVNKPDergfTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLAS- 165
Cdd:PHA02876  208 ALDDLSVLECAVDSKnIDTIKAIIDNRSN-INKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASq 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 166 TGGYTDIVGLLLERDVDINIYDWNGGTPL-LYAVRGNHVKCVEALLARGADLTTeADSGY-TPMDLAVALGYRKDGVSLL 243
Cdd:PHA02876  283 APSLSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNA-ADRLYiTPLHQASTLDRNKDIVITL 361


                  .
gi 2217323603 244 L 244
Cdd:PHA02876  362 L 362
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 85-185 1.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  85 LPATLDSLSIHQLAAQGELDQLkEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERE-SALSL 163
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGI-ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCY 208

                          90       100
                  ....*....|....*....|..
gi 2217323603 164 ASTGGYTDIVGLLLERDVDINI 185
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-216 2.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFG-EIETVRFLLEWGADPHILAKERESALSLAST-GGYTD 171
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKD 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217323603 172 IVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADL 216
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 7.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217323603 110 LRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLA 164
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 97-244 2.60e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  97 LAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLL 176
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVL 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 177 LERDVDINIYDWNGGTPL--------------LY-----------------AVRGNHVKCVEALLARGADLTTEADSGYT 225
Cdd:PLN03192  578 LKHACNVHIRDANGNTALwnaisakhhkifriLYhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657

                         170
                  ....*....|....*....
gi 2217323603 226 PMDLAVALGYrKDGVSLLL 244
Cdd:PLN03192  658 ALQVAMAEDH-VDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
143-197 5.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 5.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323603 143 LLEWG-ADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYA 197
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-177 6.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 6.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217323603 126 TPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLL 177
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 117-222 1.34e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 117 VNKPDERGFTPLIWASAFGEIETVRFLLEWGAdphilakeresalslastggytdivglllerdvDINIYDWNGGTPLLY 196
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGA---------------------------------DINAVSSDGNTPLSL 296

                          90       100
                  ....*....|....*....|....*.
gi 2217323603 197 AVRGNHVKCVEALLARGADLTTEADS 222
Cdd:PHA03095  297 MVRNNNGRAVRAALAKNPSAETVAAT 322
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 5.45e-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: 36.88  E-value: 5.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217323603 123 RGFTPLIWASA-FGEIETVRFLLEWGADPHI 152
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 189-217 6.09e-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: 6.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217323603  189 NGGTPLLYAVRGNHVKCVEALLARGADLT 217
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 105-224 6.26e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 105 QLKEHLRKGDNLvnKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILakERESALSLASTGGYTDIVGLLLERDVDIN 184
Cdd:PHA02791   13 QLKSFLSSKDAF--KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217323603 185 IYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGY 224
Cdd:PHA02791   89 QFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGW 128
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-144 6.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 6.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLL 144
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-244 9.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 9.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217323603 190 GGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGyRKDGVSLLL 244
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-216 1.01e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*...
gi 2217323603 189 NGGTPLLYAVRGNHVKCVEALLARGADL 216
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-216 1.88e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.88e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217323603 189 NGGTPLLYAV-RGNHVKCVEALLARGADL 216
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADV 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-199 1.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  86 PATLDSLSIHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPL-IWASAFGEIETVRFLLEWGADPHILAKERE-SALSL 163
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGlTALHS 275

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217323603 164 ASTGgyTDIVGLLLERDVDINIYDWNGGTPLLYAVR 199
Cdd:PHA02878  276 SIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 94-245 2.52e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603  94 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGA--DPHILAkereSALSLASTGGYTD 171
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHACN-VHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHAAG----DLLCTAAKRNDLT 636

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217323603 172 IVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLT-TEADSGYTPMDLAVALGYRKDGVSLLLP 245
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSITIV 711
PHA03095 PHA03095
ankyrin-like protein; Provisional
 171-244 2.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217323603 171 DIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKC---VEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 244
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLI 104
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 126-218 3.68e-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: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 126 TPLIWASAFGEIETVRFLLEW-GADPHILAKERESALSLASTGGYTDIVGLLLERDVD-IN------IYDwnGGTPLLYA 197
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtsdLYQ--GETALHIA 96

                          90       100
                  ....*....|....*....|.
gi 2217323603 198 VRGNHVKCVEALLARGADLTT 218
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVS 117
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 3.69e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 3.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217323603 123 RGFTPLIWASAFGEIETVRFLLEWGADPHI 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 182-249 3.75e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.83  E-value: 3.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323603 182 DINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL---PRLEC 249
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNIELLKMLLchkPTLDC 514
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 116-234 7.66e-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: 37.68  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 116 LVNKPDE----RGFTPLIWASAFGEIETVRFLLEWGAD--------------PHILAKERESALSLASTGGYTDIVGLLL 177
Cdd:cd22192    77 LVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLI 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217323603 178 ERDVDINIYDWNGGTPL-LYAVRGNHVKCVEA---LLARGADLTTEA------DSGYTPMDLAVALG 234
Cdd:cd22192   157 EHGADIRAQDSLGNTVLhILVLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEG 223
PHA02798 PHA02798
ankyrin-like protein; Provisional
 171-278 7.92e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323603 171 DIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL---ARGADLTTEADSGYTPMDLAVALGYRKD--GVSLLLP 245
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLE 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217323603 246 R-------LECYGVISAHCNFRLPVQQvIENHILKLFQSN 278
Cdd:PHA02798  170 KgvdinthNNKEKYDTLHCYFKYNIDR-IDADILKLFVDN 208
 
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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