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Conserved domains on  [gi|1370463973|ref|XP_024305151|]
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ankyrin repeat domain-containing protein 10 isoform X4 [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];
25-153 4.89e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-153 4.89e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-153 2.56e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  63 HWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIS 142
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1370463973 143 ALVANGAHVEL 153
Cdd:pfam12796  79 LLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-152 1.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  22 LRFPLHRACRDGDLATLCSLLQQTPHAhlasEDSFY--GWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIA 99
Cdd:PHA02875   68 IESELHDAVEEGDVKAVEELLDLGKFA----DDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370463973 100 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-149 3.93e-05

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: 42.31  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtPHAHLASEDSFyGWTPVHWAAHFGKLECLVQLVRAGATL-NVSTTR--YA-QTPAHIAA 100
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKC-PSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELvNEPMTSdlYQgETALHIAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463973 101 FGGHPQCLVWLIQAGANINKP-----------DCE---GETPIHKAARSGSLECISALVANGA 149
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 57-86 1.20e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370463973   57 YGWTPVHWAAHFGKLECLVQLVRAGATLNV 86
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-130 3.81e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  54 DSFY-GWTPVHWAAHFGKLECLVQLVRAGATLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90
                  ....*....|.
gi 1370463973 120 KPDCEGETPIH 130
Cdd:TIGR00870 203 TADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-153 4.89e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-153 7.78e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 7.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  57 YGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSG 136
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNA-RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          90
                  ....*....|....*..
gi 1370463973 137 SLECISALVANGAHVEL 153
Cdd:COG0666   165 NLEIVKLLLEAGADVNA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-149 1.53e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA--GADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGH 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGA 149
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-153 2.44e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEA--GADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGN 231

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:COG0666   232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-153 2.56e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  63 HWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIS 142
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1370463973 143 ALVANGAHVEL 153
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-153 2.54e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  19 LLSLRFPLHRACRDGDLATLCSLLQQTPHAHLASEDSfygwTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHI 98
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALG----ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370463973  99 AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:COG0666    94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA 148
Ank_2 pfam12796
Ankyrin repeats (3 copies);
26-122 8.44e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 8.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  26 LHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECLVQLVragATLNVSTTRYAQTPAHIAAFGGHP 105
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN---GRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1370463973 106 QCLVWLIQAGANINKPD 122
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-145 4.27e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370463973  94 TPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALV 145
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-152 1.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  22 LRFPLHRACRDGDLATLCSLLQQTPHAhlasEDSFY--GWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIA 99
Cdd:PHA02875   68 IESELHDAVEEGDVKAVEELLDLGKFA----DDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370463973 100 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-151 8.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  60 TPVHWAAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLE 139
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                          90
                  ....*....|..
gi 1370463973 140 CISALVANGAHV 151
Cdd:PHA02874  205 CIKLLIDHGNHI 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-132 1.03e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  26 LHRACRDGDLATLCSLLQQTPHAHLASEDSFYgwtPVHWAAHFGKLECLVQLVRAGATLNVSTTrYAQTPAHIAAFGGHP 105
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCY---PIHIAIKHNFFDIIKLLLEKGAYANVKDN-NGESPLHNAAEYGDY 203

                          90       100
                  ....*....|....*....|....*..
gi 1370463973 106 QCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:PHA02874  204 ACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-153 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  24 FPLHRACRDGDLATLCSLLQQTPHAHLaseDSFYGWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFgg 103
Cdd:PHA02874  159 YPIHIAIKHNFFDIIKLLLEKGAYANV---KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAII-- 232

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370463973 104 HPQCLVWLIQAGANINKPDCEGETPIHKAAR-SGSLECISALVANGAHVEL 153
Cdd:PHA02874  233 HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISI 283
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-151 3.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACR-DGDLATLCSLLQQTphAHLASEDsFYGWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIAAFGG 103
Cdd:PHA02876  344 PLHQASTlDRNKDIVITLLELG--ANVNARD-YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGT 419

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370463973 104 HPQCLV-WLIQAGANINKPDCEGETPIHKAARSG-SLECISALVANGAHV 151
Cdd:PHA02876  420 NPYMSVkTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-112 5.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370463973  58 GWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLI 112
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-152 5.96e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLC-SLLQQTPHAhlaSEDSFYGWTPVHWAAHFG-KLECLVQLVRAGATLNVSTTRYaQTPAHIAA-F 101
Cdd:PHA02876  276 PLHHASQAPSLSRLVpKLLERGADV---NAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLY-ITPLHQAStL 351

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370463973 102 GGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:PHA02876  352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-151 6.54e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  57 YGWTPVHWAAHFGKLECLVQ-LVRAGATLNVSTtRYAQTPAHI--AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAA 133
Cdd:PHA03095   82 CGFTPLHLYLYNATTLDVIKlLIKAGADVNAKD-KVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLL 160

                          90       100
                  ....*....|....*....|
gi 1370463973 134 RSG--SLECISALVANGAHV 151
Cdd:PHA03095  161 KSRnaNVELLRLLIDAGADV 180
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 26-149 8.54e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  26 LHRACRDGDLATLCSLLQQTPHA--HLASEDSFYGWTPVHWAAHFGKL---ECLVQLVRAGATLNVSTTRYAQTPAHIAA 100
Cdd:PHA02736   21 LHYLCRNGGVTDLLAFKNAISDEnrYLVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVFGNTPLHIAV 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370463973 101 FGGHPQCLVWLI-QAGANINKPDCEGETPIHKAARSGSLECISALVANGA 149
Cdd:PHA02736  101 YTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-129 5.08e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 5.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463973  58 GWTPVHWAAHFGKLECLV--QLVRAGATLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPI 129
Cdd:PHA03095  222 GNTPLHSMATGSSCKRSLvlPLLIAGISIN-ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 23-147 7.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 7.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  23 RFPLHRACRDGDLATLCSLLQQTphahlASED--SFYGWTPVHWAAHFGK-LECLVQLVRAGATLNVSTTRYAQTPAHIA 99
Cdd:PHA02878  202 NSPLHHAVKHYNKPIVHILLENG-----ASTDarDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILGLTALHSS 276

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370463973 100 AFGghPQCLVWLIQAGANINKPDCEGETPIHKAARSGS-LECISALVAN 147
Cdd:PHA02878  277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-152 8.50e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  57 YGWTPVHWAAHFGKLECL--VQ-LVRAGATLNVsTTRYAQTPAHI-AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:PHA03095   46 YGKTPLHLYLHYSSEKVKdiVRlLLEAGADVNA-PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVY 124

                          90       100
                  ....*....|....*....|..
gi 1370463973 133 ARSGSL--ECISALVANGAHVE 152
Cdd:PHA03095  125 LSGFNInpKVIRLLLRKGADVN 146
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-149 3.93e-05

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: 42.31  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQtPHAHLASEDSFyGWTPVHWAAHFGKLECLVQLVRAGATL-NVSTTR--YA-QTPAHIAA 100
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKC-PSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELvNEPMTSdlYQgETALHIAV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463973 101 FGGHPQCLVWLIQAGANINKP-----------DCE---GETPIHKAARSGSLECISALVANGA 149
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-132 4.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463973  77 LVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 65-136 5.16e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 5.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463973  65 AAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSG 136
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 77-152 5.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 5.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463973  77 LVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:PHA02878  153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 57-86 1.20e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370463973   57 YGWTPVHWAAHFGKLECLVQLVRAGATLNV 86
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-129 1.69e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECLVQLVRAGATLNVStTRYAQTPAHIAAFGGH 104
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDND---GKTALDLAAENGNLEIVKLLLEAGADLNAK-DKDGLTALLLAAAAGA 264

                          90       100
                  ....*....|....*....|....*
gi 1370463973 105 PQCLVWLIQAGANINKPDCEGETPI 129
Cdd:COG0666   265 ALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 91-152 2.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463973  91 YAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:PHA03100  191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 77-144 2.30e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463973  77 LVRAGATLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISAL 144
Cdd:PTZ00322  101 LLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-119 2.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 2.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463973  57 YGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:PHA03100  191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 77-151 3.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 3.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463973  77 LVRAGATLNVSTtRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHV 151
Cdd:PHA02874  110 ILDCGIDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-151 7.46e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 7.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463973  77 LVRAGATLNVsTTRYAQTPAHIAAFG--GHPQCLVWLIQAGANINKPDCEGETPIHKAARSGS--LECISALVANGAHV 151
Cdd:PHA03100   92 LLEYGANVNA-PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 49-134 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  49 HLASEDSFYgwTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETP 128
Cdd:PHA02884   63 FPLSENSKT--NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTP 140


                  ....*.
gi 1370463973 129 IHKAAR 134
Cdd:PHA02884  141 IELALM 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
25-74 1.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370463973  25 PLHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECL 74
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVL 50
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-120 1.46e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 1.46e-03
                           10        20
                   ....*....|....*....|....*..
gi 1370463973   94 TPAHIAAFGGHPQCLVWLIQAGANINK 120
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 111-154 3.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 36.57  E-value: 3.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370463973 111 LIQAGANINKPDCEGETPIHKAA--RSGSLECISALVANGAHVELH 154
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIK 137
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-151 3.26e-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: 36.91  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  60 TPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGAN-INKPDC----EGETPIHKAAR 134
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                          90
                  ....*....|....*..
gi 1370463973 135 SGSLECISALVANGAHV 151
Cdd:cd22192    99 NQNLNLVRELIARGADV 115
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-130 3.81e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  54 DSFY-GWTPVHWAAHFGKLECLVQLVRAGATLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90
                  ....*....|.
gi 1370463973 120 KPDCEGETPIH 130
Cdd:TIGR00870 203 TADSLGNTLLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 93-122 3.83e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.42  E-value: 3.83e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1370463973  93 QTPAHIAA-FGGHPQCLVWLIQAGANINKPD 122
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 124-151 4.79e-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: 33.00  E-value: 4.79e-03
                          10        20
                  ....*....|....*....|....*...
gi 1370463973 124 EGETPIHKAARSGSLECISALVANGAHV 151
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 54-130 5.26e-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: 36.14  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463973  54 DSFYGWTPVHWAAHFGKLECLVQLVRAGAtlNVSTTR---------------YAQTPAHIAAFGGHPQCLVWLIQAGANI 118
Cdd:cd22192    85 DLYQGETALHIAVVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADI 162

                          90
                  ....*....|..
gi 1370463973 119 NKPDCEGETPIH 130
Cdd:cd22192   163 RAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 124-153 5.29e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 32.94  E-value: 5.29e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370463973  124 EGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 111-153 6.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 35.81  E-value: 6.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370463973 111 LIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI 206
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 124-153 7.44e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 35.83  E-value: 7.44e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370463973 124 EGETPIHKAARSGSLECISALVANGAHVEL 153
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-151 7.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 35.81  E-value: 7.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463973  77 LVRAGATLNVSTTrYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHV 151
Cdd:PHA02876  164 LLEGGADVNAKDI-YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
 
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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