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Conserved domains on  [gi|568909685|ref|XP_006529946|]
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acyl-CoA-binding domain-containing protein 6 isoform X1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-189 2.90e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568909685 153 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 189
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-189 2.90e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568909685 153 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 189
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-162 1.44e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685   73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYeAGINCQDNeGQTALHYAAACEFLDIVELLL 152
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 568909685  153 QSGADPTLRD 162
Cdd:pfam12796  82 EKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-168 4.32e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  83 KAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRD 162
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 568909685 163 QDGCLP 168
Cdd:PHA02874 188 NNGESP 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-157 1.65e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  74 RENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG-----INCQDNEGQTALHYAAACEFLDIV 148
Cdd:cd22192   26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                 ....*....
gi 568909685 149 ELLLQSGAD 157
Cdd:cd22192  106 RELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 131-160 1.07e-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: 37.95  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909685   131 EGQTALHYAAACEFLDIVELLLQSGADPTL 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-157 2.16e-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: 38.14  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685   59 EETIREEDKNIFDYCRENNIDHIAKAIK-SKAADVNMTDEEGR-ALLHWACDRGHKELVKVLLQYE------------AG 124
Cdd:TIGR00870  11 ESPLSDEEKAFLPAAERGDLASVYRDLEePKKLNINCPDRLGRsALFVAAIENENLELTELLLNLScrgavgdtllhaIS 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909685  125 INCQDN------------------------------EGQTALHYAAACEFLDIVELLLQSGAD 157
Cdd:TIGR00870  91 LEYVDAveaillhllaafrksgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-189 2.90e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568909685 153 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 189
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-168 1.09e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666   95 ARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         90
                 ....*....|....*.
gi 568909685 153 QSGADPTLRDQDGCLP 168
Cdd:COG0666  174 EAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-168 5.79e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 5.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  68 NIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDI 147
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100
                 ....*....|....*....|.
gi 568909685 148 VELLLQSGADPTLRDQDGCLP 168
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-162 1.44e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685   73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYeAGINCQDNeGQTALHYAAACEFLDIVELLL 152
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 568909685  153 QSGADPTLRD 162
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-165 1.30e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666  161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90
                 ....*....|...
gi 568909685 153 QSGADPTLRDQDG 165
Cdd:COG0666  240 EAGADLNAKDKDG 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-153 8.16e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 8.16e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568909685  103 LHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQ 153
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-152 6.79e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 6.79e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568909685   99 GRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-168 4.32e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  83 KAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRD 162
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 568909685 163 QDGCLP 168
Cdd:PHA02874 188 NNGESP 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-168 5.05e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 5.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  68 NIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDI 147
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100
                 ....*....|....*....|.
gi 568909685 148 VELLLQSGADPTLRDQDGCLP 168
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETP 123
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-165 2.86e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  73 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:COG0666  194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         90
                 ....*....|...
gi 568909685 153 QSGADPTLRDQDG 165
Cdd:COG0666  273 LALLLLAAALLDL 285
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-184 3.75e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 3.75e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909685 115 VKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRH 184
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELaeeNGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 80-187 4.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 4.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  80 HIAKAIKSKAADVNMTDEEGRALLHWACDRGHKEL------------------VKVLLQYEAGINCQDNEGQTALHYAAA 141
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVY 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568909685 142 CEFLDIVELLLQSGADPTLRDQDG--CLPEEVTGC-KAVSLLLQRHRAS 187
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGdtPLHIAILNNnKEIFKLLLNNGPS 250
Ank_5 pfam13857
Ankyrin repeats (many copies);
90-139 1.02e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 1.02e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568909685   90 ADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYA 139
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 82-152 1.68e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.68e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909685  82 AKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 152
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-157 2.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  76 NNIDHIaKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSG 155
Cdd:PHA03100 170 NAKNRV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248


                 ..
gi 568909685 156 AD 157
Cdd:PHA03100 249 PS 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 63-157 3.30e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  63 REEDKNIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAA- 141
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGy 244

                         90
                 ....*....|....*.
gi 568909685 142 CEFLDIVELLLQSGAD 157
Cdd:PHA02878 245 CKDYDILKLLLEHGVD 260
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-183 8.76e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 8.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  76 NNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGH-----KELVKVLLQYEAGINCQDNEGQTALHYAAACEF--LDIV 148
Cdd:PHA03100  46 RNID-VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIV 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568909685 149 ELLLQSGADPTLRDQDG--CLPEEVTGC----KAVSLLLQR 183
Cdd:PHA03100 125 EYLLDNGANVNIKNSDGenLLHLYLESNkidlKILKLLIDK 165
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-157 9.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 9.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  75 ENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDR--GHKELVKVLLQYEAGINCQDNEGQTALHYAAACEF--LDIVEL 150
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKL 161


                 ....*..
gi 568909685 151 LLQSGAD 157
Cdd:PHA03100 162 LIDKGVD 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-157 1.65e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  74 RENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG-----INCQDNEGQTALHYAAACEFLDIV 148
Cdd:cd22192   26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                 ....*....
gi 568909685 149 ELLLQSGAD 157
Cdd:cd22192  106 RELIARGAD 114
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-180 2.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  65 EDKNIFDYCRENNID-HIAKAIKSKAADVNMTDEE-GRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAAC 142
Cdd:PHA02878 132 DLVYIDKKSKDDIIEaEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568909685 143 EFLDIVELLLQSGADPTLRDQDGCLPEE--VTGCKAVSLL 180
Cdd:PHA02878 212 YNKPIVHILLENGASTDARDKCGNTPLHisVGYCKDYDIL 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 65-168 3.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  65 EDKNIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEF 144
Cdd:PHA02874 123 ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         90       100
                 ....*....|....*....|....
gi 568909685 145 LDIVELLLQSGADPTLRDQDGCLP 168
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTP 226
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 131-162 1.91e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.91e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568909685  131 EGQTALHYAAACE-FLDIVELLLQSGADPTLRD 162
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 91-158 3.46e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 3.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  91 DVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQ--SGADP 158
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDP 619
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-168 6.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 6.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568909685 112 KELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 168
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-162 6.44e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  58 HEETIREEDknIFDY-CRENNID-HIAKAIKSKAADVNMTDEEGRALLHWACDRGH---KELVKVLLQYEAGINCQDNEG 132
Cdd:PHA03095   6 SVDIIMEAA--LYDYlLNASNVTvEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCG 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568909685 133 QTALH-YAAACEFLDIVELLLQSGADPTLRD 162
Cdd:PHA03095  84 FTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-183 7.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  77 NIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGA 156
Cdd:PHA02875 114 KLD-IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568909685 157 DPTLRDQDGCLpeeVTGCKA--------VSLLLQR 183
Cdd:PHA02875 193 NIDYFGKNGCV---AALCYAiennkidiVRLFIKR 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 81-154 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 1.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568909685  81 IAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQS 154
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-168 1.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568909685  125 INCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 168
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 81-168 2.45e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  81 IAKAIKSKAADVNMTDEEGRALLH-WACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLD--IVELLLQSGAD 157
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGAD 144

                         90
                 ....*....|.
gi 568909685 158 PTLRDQDGCLP 168
Cdd:PHA03095 145 VNALDLYGMTP 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 83-157 2.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 2.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568909685  83 KAIKSKAADVNMTDEEGRALLHWAC--DRgHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGAD 157
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStlDR-NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 74-165 8.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  74 RENNIDhIAKAIKSKAADVNMTDEEGRALLHWA----------------------CDRG---------HKELVKVLLQYE 122
Cdd:PHA02874 166 KHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAaeygdyacikllidhgnhimnkCKNGftplhnaiiHNRSAIELLINN 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568909685 123 AGINCQDNEGQTALHYA--AACEfLDIVELLLQSGADPTLRDQDG 165
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAinPPCD-IDIIDILLYHKADISIKDNKG 288
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 131-158 1.04e-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: 38.01  E-value: 1.04e-04
                          10        20
                  ....*....|....*....|....*...
gi 568909685  131 EGQTALHYAAACEFLDIVELLLQSGADP 158
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 131-160 1.07e-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: 37.95  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909685   131 EGQTALHYAAACEFLDIVELLLQSGADPTL 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-127 1.20e-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: 38.01  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 568909685   98 EGRALLHWACDRGHKELVKVLLQYEAGINC 127
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 69-184 1.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  69 IFDYCRENNidHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG--INCQDNEGQTALHYAA------ 140
Cdd:PHA03095 194 HLQSFKPRA--RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAvfnnpr 271

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568909685 141 ACEFldivelLLQSGADPTLRDQDG--CLPEEVTGC--KAVSLLLQRH 184
Cdd:PHA03095 272 ACRR------LIALGADINAVSSDGntPLSLMVRNNngRAVRAALAKN 313
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-119 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568909685   69 IFDYCRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLL 119
Cdd:pfam13637   5 LHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 98-130 2.36e-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: 37.27  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568909685   98 EGRALLHWACDR-GHKELVKVLLQYEAGINCQDN 130
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 98-127 4.34e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 4.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909685    98 EGRALLHWACDRGHKELVKVLLQYEAGINC 127
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 113-168 6.38e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 6.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568909685 113 ELVKVLLQYEAGINCQDNEGQTALHYAAAC---EFLDIVELLLQSGADPTLRDQDGCLP 168
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTP 86
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 92-157 6.97e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.74  E-value: 6.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909685  92 VNMTDEEGRALLHWACDRGhkeLVKVLL--QYEAGincqDNEGQTALHYAAACEFLDIVELLLQSGAD 157
Cdd:cd22194  106 NENTKEIVRILLAFAEENG---ILDRFInaEYTEE----AYEGQTALNIAIERRQGDIVKLLIAKGAD 166
Ank_2 pfam12796
Ankyrin repeats (3 copies);
136-168 7.52e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.02  E-value: 7.52e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568909685  136 LHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 102-157 1.51e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909685 102 LLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGAD 157
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 68-157 1.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  68 NIFDYCRENNIDH--------IAKAIKSKAADVNMTDEEGRALLHWA-CDRGHKELVKVLLQYEAGINCQDNEGQTALHY 138
Cdd:PHA02876 369 NARDYCDKTPIHYaavrnnvvIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHY 448

                         90       100
                 ....*....|....*....|.
gi 568909685 139 AAA--CEfLDIVELLLQSGAD 157
Cdd:PHA02876 449 ACKknCK-LDVIEMLLDNGAD 468
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 98-165 1.98e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.20  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  98 EGRALLHWACDRGHKELVKVLLQYEAGINCQ----------DNE----GQTALHYAAACEFLDIVELLLQSGADP-TLRD 162
Cdd:cd22194  140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDiTSQD 219


                 ...
gi 568909685 163 QDG 165
Cdd:cd22194  220 SRG 222
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-157 2.16e-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: 38.14  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685   59 EETIREEDKNIFDYCRENNIDHIAKAIK-SKAADVNMTDEEGR-ALLHWACDRGHKELVKVLLQYE------------AG 124
Cdd:TIGR00870  11 ESPLSDEEKAFLPAAERGDLASVYRDLEePKKLNINCPDRLGRsALFVAAIENENLELTELLLNLScrgavgdtllhaIS 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909685  125 INCQDN------------------------------EGQTALHYAAACEFLDIVELLLQSGAD 157
Cdd:TIGR00870  91 LEYVDAveaillhllaafrksgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
PHA02741 PHA02741
hypothetical protein; Provisional
 87-171 6.03e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 35.79  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  87 SKAADVNMTDEEGRALLHWACDRGHK----ELVKVLLQYEAGINCQDN-EGQTALHYAAACEFLDIVELLL-QSGADPTL 160
Cdd:PHA02741  48 CHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHF 127

                         90
                 ....*....|.
gi 568909685 161 RDQDGCLPEEV 171
Cdd:PHA02741 128 CNADNKSPFEL 138
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 94-164 8.53e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 36.40  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909685  94 MTDE--EGRALLHWACDRGHKELVKVLLQYEAGINCQDNE-------------GQTALHYAAACEFLDIVELLLQSGADP 158
Cdd:cd21882   66 CTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145


                 ....*..
gi 568909685 159 -TLRDQD 164
Cdd:cd21882  146 aALEAQD 152
PHA02917 PHA02917
ankyrin-like protein; Provisional
 115-180 9.18e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 36.13  E-value: 9.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909685 115 VKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDG--CLPEEVTGCKAVSLL 180
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGytCIAIAINESRNIELL 502
 
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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