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Conserved domains on  [gi|2217323609|ref|XP_047295545|]
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DNA-binding protein RFXANK isoform X2 [Homo sapiens]

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];
93-243 3.06e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 243
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-243 3.06e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 243
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-217 6.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 6.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 127 LIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERdVDINIYDwNGGTPLLYAVRGNHVKCVE 206
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2217323609 207 ALLARGADLTT 217
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-243 1.47e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 116 VNKPDERGFTPLIWASA--FGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI------------------VGLL 175
Cdd:PHA03100   99 VNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323609 176 LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVaLGYRKDGVSLLL 243
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-LNNNKEIFKLLL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 188-216 6.07e-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: 6.07e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217323609  188 NGGTPLLYAVRGNHVKCVEALLARGADLT 216
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 125-217 3.65e-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: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 125 TPLIWASAFGEIETVRFLLEW-GADPHILAKERESALSLASTGGYTDIVGLLLERDVD-IN------IYDwnGGTPLLYA 196
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtsdLYQ--GETALHIA 96

                          90       100
                  ....*....|....*....|.
gi 2217323609 197 VRGNHVKCVEALLARGADLTT 217
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVS 117
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-243 3.06e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 243
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-243 1.16e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  86 ATLDSLSIHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLAST 165
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323609 166 GGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGyRKDGVSLLL 243
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLL 206
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-247 4.93e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 4.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLLPRLE 247
Cdd:COG0666   203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
88-243 1.40e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  88 LDSLSIHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGG 167
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323609 168 YTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYrKDGVSLLL 243
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN-LEIVKLLL 173
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-217 6.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 6.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 127 LIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERdVDINIYDwNGGTPLLYAVRGNHVKCVE 206
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2217323609 207 ALLARGADLTT 217
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-226 3.75e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.01  E-value: 3.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPM 226
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-243 1.47e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 116 VNKPDERGFTPLIWASA--FGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI------------------VGLL 175
Cdd:PHA03100   99 VNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323609 176 LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVaLGYRKDGVSLLL 243
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-LNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
160-243 7.62e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 7.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 160 LSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGAdlTTEADSGYTPMDLAVALGYRkDGV 239
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHL-EIV 77


                  ....
gi 2217323609 240 SLLL 243
Cdd:pfam12796  78 KLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
93-186 1.08e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEwgadpHILAKER---ESALSLASTGGYT 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-----HADVNLKdngRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 2217323609 170 DIVGLLLERDVDINIYD 186
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-243 1.09e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 116 VNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLY 195
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217323609 196 AVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVAlgYRKDGVSLLL 243
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
103-243 8.27e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 8.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 103 DQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDI 182
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323609 183 NIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYrKDGVSLLL 243
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN-LEIVKLLL 140
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-245 2.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIV 172
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSG-YTPMDLAVAlGYRKDGVSLLLPR 245
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIE-NNKIDIVRLFIKR 224
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 135-243 3.48e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 135 EIETVRFLLEWGADPHILAKERESALSLASTGGYT-----DIVGLLLERDVDINIYDWNGGTPLLYAV--RGNHVKCVEA 207
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217323609 208 LLARGADLTTEADSGYTPMDLAVALGYRK-DGVSLLL 243
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlKILKLLI 163
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 59-248 1.14e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  59 SSPQGSSLKHSTTLTNRQRGNEVSAlPATLDSLSIHQLAA-QGELDQLKEHLRK---GDNLVNKPDergftpliWASAFG 134
Cdd:PTZ00322    1 MSFLVCSVASSAFAAQLFFGTEGSR-KRRAKPISFERMAAiQEEIARIDTHLEAleaTENKDATPD--------HNLTTE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 135 EIetvrfllewgADP---HILAKEresALSLASTGgytDIVG--LLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL 209
Cdd:PTZ00322   72 EV----------IDPvvaHMLTVE---LCQLAASG---DAVGarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL 135

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217323609 210 ARGADLTTEADSGYTPMDLAVALGYRkDGVSLLLPRLEC 248
Cdd:PTZ00322  136 EFGADPTLLDKDGKTPLELAEENGFR-EVVQLLSRHSQC 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 135-258 1.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 135 EIETVRFLLEWGADPHILAKER-ESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGA 213
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217323609 214 DLTTEADSGYTPMDLAVALGYRKDGVSLLLPRLECYGVISAHCNF 258
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGL 270
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-245 2.33e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  92 SIHQLAAQGELdQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDI 171
Cdd:PHA02876  148 LIKERIQQDEL-LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 172 VGLLLERDVDINIYD------------------WNGG-----------TPLLYAVRGNHV-KCVEALLARGADLTTEADS 221
Cdd:PHA02876  227 IKAIIDNRSNINKNDlsllkairnedletslllYDAGfsvnsiddcknTPLHHASQAPSLsRLVPKLLERGADVNAKNIK 306

                         170       180
                  ....*....|....*....|....
gi 2217323609 222 GYTPMDLAVALGYRKDGVSLLLPR 245
Cdd:PHA02876  307 GETPLYLMAKNGYDTENIRTLIML 330
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-184 3.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217323609 116 VNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINI 184
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-231 4.18e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 109 LRKGDNlVNKPDERGFTPL--IWASAFGEIETVRFLLEWGADP-----------HILA---KERES-------------- 158
Cdd:PHA03095  139 LRKGAD-VNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVyavddrfrsllHHHLqsfKPRARivreliragcdpaa 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 159 -------ALSLASTGGYTD--IVGLLLERDVDINIYDWNGGTPLLYA-VRGNHVKCVEaLLARGADLTTEADSGYTPMDL 228
Cdd:PHA03095  218 tdmlgntPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR-LIALGADINAVSSDGNTPLSL 296


                  ...
gi 2217323609 229 AVA 231
Cdd:PHA03095  297 MVR 299
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 135-233 6.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 135 EIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGAD 214
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90
                  ....*....|....*....
gi 2217323609 215 LTTEADSGYTPMDLAVALG 233
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYG 201
Ank_5 pfam13857
Ankyrin repeats (many copies);
174-229 1.13e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323609 174 LLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLA 229
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 100-230 2.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 100 GELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLL---- 175
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidng 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217323609 176 -------------------LERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAV 230
Cdd:PHA02874   92 vdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-234 3.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  77 RGNEVSALpatlDSLSIHQLAAQGELDQLKEH----LRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHIL 152
Cdd:PHA02876  330 LGADVNAA----DRLYITPLHQASTLDRNKDIvitlLELGAN-VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 153 AKERESAL--SLASTGGYTDiVGLLLERDVDINIYDWNGGTPLLYAVRGN-HVKCVEALLARGADLTTEADSGYTPmdLA 229
Cdd:PHA02876  405 SQKIGTALhfALCGTNPYMS-VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP--LL 481


                  ....*
gi 2217323609 230 VALGY 234
Cdd:PHA02876  482 IALEY 486
Ank_4 pfam13637
Ankyrin repeats (many copies);
156-209 7.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323609 156 RESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL 209
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-230 8.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 8.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 116 VNKPDE-RGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLL 194
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2217323609 195 YAV-RGNHVKCVEALLARGADLTTEAD-SGYTPMDLAV 230
Cdd:PHA02878  240 ISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI 277
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 93-229 8.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 8.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNLvNKPDERGFTPLIWASAFGEIETVRFLLEWGAdpHILAKERESALSLASTGGYTDIV 172
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHNRSA 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217323609 173 GLLLERDVDINIYDWNGGTPLLYAVRGN-HVKCVEALLARGADLTTEADSGYTPMDLA 229
Cdd:PHA02874  238 IELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-227 1.09e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 102 LDQLKEHLRKGDNlVNKPDERGFTPL-IWASAFGE--IETVRFLLEWGADphILAKER--ESALSLASTGGYT-DIVGLL 175
Cdd:PHA03095   27 VEEVRRLLAAGAD-VNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGAD--VNAPERcgFTPLHLYLYNATTlDVIKLL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217323609 176 LERDVDINIYDWNGGTPL-LYAVRGN-HVKCVEALLARGADLTTEADSGYTPMD 227
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 87-243 1.82e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  87 TLDSLSIHQLAAQGE-LDQLKEHLRKGDNlVNKPDergfTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLAS- 164
Cdd:PHA02876  208 ALDDLSVLECAVDSKnIDTIKAIIDNRSN-INKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASq 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 165 TGGYTDIVGLLLERDVDINIYDWNGGTPL-LYAVRGNHVKCVEALLARGADLTTeADSGY-TPMDLAVALGYRKDGVSLL 242
Cdd:PHA02876  283 APSLSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNA-ADRLYiTPLHQASTLDRNKDIVITL 361


                  .
gi 2217323609 243 L 243
Cdd:PHA02876  362 L 362
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 84-184 1.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  84 LPATLDSLSIHQLAAQGELDQLkEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERE-SALSL 162
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGI-ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCY 208

                          90       100
                  ....*....|....*....|..
gi 2217323609 163 ASTGGYTDIVGLLLERDVDINI 184
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-215 2.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFG-EIETVRFLLEWGADPHILAKERESALSLAST-GGYTD 170
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKD 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217323609 171 IVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADL 215
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
Ank_5 pfam13857
Ankyrin repeats (many copies);
109-163 7.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217323609 109 LRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLA 163
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 96-243 2.58e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  96 LAAQGELDQLKEHLRKGDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLL 175
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVL 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 176 LERDVDINIYDWNGGTPL--------------LY-----------------AVRGNHVKCVEALLARGADLTTEADSGYT 224
Cdd:PLN03192  578 LKHACNVHIRDANGNTALwnaisakhhkifriLYhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657

                         170
                  ....*....|....*....
gi 2217323609 225 PMDLAVALGYrKDGVSLLL 243
Cdd:PLN03192  658 ALQVAMAEDH-VDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
142-196 5.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 5.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217323609 142 LLEWG-ADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYA 196
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
125-176 5.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 5.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217323609 125 TPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLL 176
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-221 1.33e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 116 VNKPDERGFTPLIWASAFGEIETVRFLLEWGAdphilakeresalslastggytdivglllerdvDINIYDWNGGTPLLY 195
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGA---------------------------------DINAVSSDGNTPLSL 296

                          90       100
                  ....*....|....*....|....*.
gi 2217323609 196 AVRGNHVKCVEALLARGADLTTEADS 221
Cdd:PHA03095  297 MVRNNNGRAVRAALAKNPSAETVAAT 322
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 122-151 5.38e-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: 5.38e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217323609 122 RGFTPLIWASA-FGEIETVRFLLEWGADPHI 151
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 188-216 6.07e-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: 6.07e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217323609  188 NGGTPLLYAVRGNHVKCVEALLARGADLT 216
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 104-223 6.22e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 104 QLKEHLRKGDNLvnKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILakERESALSLASTGGYTDIVGLLLERDVDIN 183
Cdd:PHA02791   13 QLKSFLSSKDAF--KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217323609 184 IYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGY 223
Cdd:PHA02791   89 QFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGW 128
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-143 6.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 6.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLL 143
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
189-243 9.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 9.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217323609 189 GGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGyRKDGVSLLL 243
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-215 9.94e-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: 9.94e-04
                          10        20
                  ....*....|....*....|....*...
gi 2217323609 188 NGGTPLLYAVRGNHVKCVEALLARGADL 215
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 188-215 1.80e-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: 1.80e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217323609 188 NGGTPLLYAV-RGNHVKCVEALLARGADL 215
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADV 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-198 1.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  85 PATLDSLSIHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPL-IWASAFGEIETVRFLLEWGADPHILAKERE-SALSL 162
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGlTALHS 275

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217323609 163 ASTGgyTDIVGLLLERDVDINIYDWNGGTPLLYAVR 198
Cdd:PHA02878  276 SIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 93-244 2.51e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.08  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609  93 IHQLAAQGELDQLKEHLRKGDNlVNKPDERGFTPLIWASAFGEIETVRFLLEWGA--DPHILAkereSALSLASTGGYTD 170
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHACN-VHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHAAG----DLLCTAAKRNDLT 636

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217323609 171 IVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLT-TEADSGYTPMDLAVALGYRKDGVSLLLP 244
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRELLQKRELGHSITIV 711
PHA03095 PHA03095
ankyrin-like protein; Provisional
 170-243 2.88e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217323609 170 DIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKC---VEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL 243
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLI 104
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 122-151 3.64e-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: 3.64e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217323609 122 RGFTPLIWASAFGEIETVRFLLEWGADPHI 151
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 125-217 3.65e-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: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 125 TPLIWASAFGEIETVRFLLEW-GADPHILAKERESALSLASTGGYTDIVGLLLERDVD-IN------IYDwnGGTPLLYA 196
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtsdLYQ--GETALHIA 96

                          90       100
                  ....*....|....*....|.
gi 2217323609 197 VRGNHVKCVEALLARGADLTT 217
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVS 117
PHA02917 PHA02917
ankyrin-like protein; Provisional
 181-248 3.76e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.83  E-value: 3.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217323609 181 DINIYDWNGGTPLLYAVRGNHVKCVEALLARGADLTTEADSGYTPMDLAVALGYRKDGVSLLL---PRLEC 248
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNIELLKMLLchkPTLDC 514
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 115-233 7.61e-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: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 115 LVNKPDE----RGFTPLIWASAFGEIETVRFLLEWGAD--------------PHILAKERESALSLASTGGYTDIVGLLL 176
Cdd:cd22192    77 LVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLI 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217323609 177 ERDVDINIYDWNGGTPL-LYAVRGNHVKCVEA---LLARGADLTTEA------DSGYTPMDLAVALG 233
Cdd:cd22192   157 EHGADIRAQDSLGNTVLhILVLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEG 223
PHA02798 PHA02798
ankyrin-like protein; Provisional
 170-277 7.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217323609 170 DIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL---ARGADLTTEADSGYTPMDLAVALGYRKD--GVSLLLP 244
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLE 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217323609 245 R-------LECYGVISAHCNFRLPVQQvIENHILKLFQSN 277
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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