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Conserved domains on  [gi|224809389|ref|NP_082526|]
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acyl-CoA-binding domain-containing protein 6 isoform 1 [Mus musculus]

Protein Classification

acyl-CoA-binding domain-containing protein( domain architecture ID 12470595)

acyl-CoA-binding domain-containing protein (ACBP) with ankyrin repeats is mainly involved in acyl-CoA ester binding and trafficking in eukaryotic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
43-118 4.73e-31

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 110.76  E-value: 4.73e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809389   43 AELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-282 1.88e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 224809389 246 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 282
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
43-118 4.73e-31

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 110.76  E-value: 4.73e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809389   43 AELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-282 1.88e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 224809389 246 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 282
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 42-121 4.70e-27

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 100.48  E-value: 4.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  42 LAELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVKKL 121
Cdd:cd00435    1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-255 1.25e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYeAGINCQDNeGQTALHYAAACEFLDIVELLL 245
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 224809389  246 QSGADPTLRD 255
Cdd:pfam12796  82 EKGADINVKD 91
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
41-121 2.35e-21

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 85.67  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  41 SLAELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVKK 120
Cdd:COG4281    3 DLQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNS 82


                 .
gi 224809389 121 L 121
Cdd:COG4281   83 L 83
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 42-125 2.21e-14

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 67.15  E-value: 2.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  42 LAELFEKAAAHVQGLVQVA--SREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVK 119
Cdd:PTZ00458   1 MADLFEECVSFINSLPKTVnlSVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVT 80


                 ....*.
gi 224809389 120 KLDPGW 125
Cdd:PTZ00458  81 ELFPNW 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-261 1.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 176 KAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 224809389 256 QDGCLP 261
Cdd:PHA02874 188 NNGESP 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 167-250 6.31e-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: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 167 RENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG-----INCQDNEGQTALHYAAACEFLDIV 241
Cdd:cd22192   26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                 ....*....
gi 224809389 242 ELLLQSGAD 250
Cdd:cd22192  106 RELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 224-253 3.16e-05

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: 40.26  E-value: 3.16e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 224809389   224 EGQTALHYAAACEFLDIVELLLQSGADPTL 253
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
43-118 4.73e-31

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 110.76  E-value: 4.73e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809389   43 AELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-282 1.88e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666  128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 224809389 246 QSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRHRASKA 282
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLaaeNGNLEIVKLLLEAGADLN 246
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 42-121 4.70e-27

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 100.48  E-value: 4.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  42 LAELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVKKL 121
Cdd:cd00435    1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-261 8.24e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.81  E-value: 8.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666   95 ARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         90
                 ....*....|....*.
gi 224809389 246 QSGADPTLRDQDGCLP 261
Cdd:COG0666  174 EAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-255 1.25e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYeAGINCQDNeGQTALHYAAACEFLDIVELLL 245
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 224809389  246 QSGADPTLRD 255
Cdd:pfam12796  82 EKGADINVKD 91
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
41-121 2.35e-21

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 85.67  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  41 SLAELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVKK 120
Cdd:COG4281    3 DLQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNS 82


                 .
gi 224809389 121 L 121
Cdd:COG4281   83 L 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-261 5.74e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 5.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 161 NIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDI 240
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100
                 ....*....|....*....|.
gi 224809389 241 VELLLQSGADPTLRDQDGCLP 261
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTP 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-258 1.19e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666  161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90
                 ....*....|...
gi 224809389 246 QSGADPTLRDQDG 258
Cdd:COG0666  240 EAGADLNAKDKDG 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
196-246 2.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 2.05e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 224809389  196 LHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQ 246
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 42-125 2.21e-14

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 67.15  E-value: 2.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389  42 LAELFEKAAAHVQGLVQVA--SREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVK 119
Cdd:PTZ00458   1 MADLFEECVSFINSLPKTVnlSVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVT 80


                 ....*.
gi 224809389 120 KLDPGW 125
Cdd:PTZ00458  81 ELFPNW 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-245 1.29e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 1.29e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 224809389  192 GRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-261 5.85e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 161 NIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDI 240
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100
                 ....*....|....*....|.
gi 224809389 241 VELLLQSGADPTLRDQDGCLP 261
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETP 123
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-261 1.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 176 KAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 224809389 256 QDGCLP 261
Cdd:PHA02874 188 NNGESP 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-258 2.67e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 2.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 166 CRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:COG0666  194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         90
                 ....*....|...
gi 224809389 246 QSGADPTLRDQDG 258
Cdd:COG0666  273 LALLLLAAALLDL 285
Ank_5 pfam13857
Ankyrin repeats (many copies);
183-232 2.92e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.66  E-value: 2.92e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 224809389  183 ADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYA 232
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 208-277 1.55e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809389 208 VKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLPEEV---TGCKAVSLLLQRH 277
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELaeeNGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 173-280 2.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 173 HIAKAIKSKAADVNMTDEEGRALLHWACDRGHKEL------------------VKVLLQYEAGINCQDNEGQTALHYAAA 234
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVY 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 224809389 235 CEFLDIVELLLQSGADPTLRDQDG--CLPEEVTGC-KAVSLLLQRHRAS 280
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGdtPLHIAILNNnKEIFKLLLNNGPS 250
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 156-250 6.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 6.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 156 REEDKNIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAA- 234
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGy 244

                         90
                 ....*....|....*.
gi 224809389 235 CEFLDIVELLLQSGAD 250
Cdd:PHA02878 245 CKDYDILKLLLEHGVD 260
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 175-245 6.37e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.37e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809389 175 AKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLL 245
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 169-250 1.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 169 NNIDHIaKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSG 248
Cdd:PHA03100 170 NAKNRV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248


                 ..
gi 224809389 249 AD 250
Cdd:PHA03100 249 PS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 169-276 3.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 169 NNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGH-----KELVKVLLQYEAGINCQDNEGQTALHYAAACEF--LDIV 241
Cdd:PHA03100  46 RNID-VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIV 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 224809389 242 ELLLQSGADPTLRDQDG--CLPEEVTGC----KAVSLLLQR 276
Cdd:PHA03100 125 EYLLDNGANVNIKNSDGenLLHLYLESNkidlKILKLLIDK 165
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 158-273 2.91e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 158 EDKNIFDYCRENNID-HIAKAIKSKAADVNMTDEE-GRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAAC 235
Cdd:PHA02878 132 DLVYIDKKSKDDIIEaEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 224809389 236 EFLDIVELLLQSGADPTLRDQDGCLPEE--VTGCKAVSLL 273
Cdd:PHA02878 212 YNKPIVHILLENGASTDARDKCGNTPLHisVGYCKDYDIL 251
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 168-250 3.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 168 ENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDR--GHKELVKVLLQYEAGINCQDNEGQTALHYAAACEF--LDIVEL 243
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKL 161


                 ....*..
gi 224809389 244 LLQSGAD 250
Cdd:PHA03100 162 LIDKGVD 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-255 3.45e-07

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: 45.74  E-value: 3.45e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 224809389  224 EGQTALHYAAACE-FLDIVELLLQSGADPTLRD 255
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 167-250 6.31e-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: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 167 RENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG-----INCQDNEGQTALHYAAACEFLDIV 241
Cdd:cd22192   26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                 ....*....
gi 224809389 242 ELLLQSGAD 250
Cdd:cd22192  106 RELIARGAD 114
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-261 9.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 9.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 158 EDKNIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEF 237
Cdd:PHA02874 123 ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         90       100
                 ....*....|....*....|....
gi 224809389 238 LDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTP 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-261 5.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 5.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 224809389  218 INCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 151-255 6.67e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 151 HEETIREEDknIFDY-CRENNID-HIAKAIKSKAADVNMTDEEGRALLHWACDRGH---KELVKVLLQYEAGINCQDNEG 225
Cdd:PHA03095   6 SVDIIMEAA--LYDYlLNASNVTvEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCG 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 224809389 226 QTALH-YAAACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA03095  84 FTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 184-251 1.18e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 184 DVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQ--SGADP 251
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDP 619
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 205-261 1.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 224809389 205 KELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 170-276 2.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 170 NIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGA 249
Cdd:PHA02875 114 KLD-IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 224809389 250 DPTLRDQDGCLpeeVTGCKA--------VSLLLQR 276
Cdd:PHA02875 193 NIDYFGKNGCV---AALCYAiennkidiVRLFIKR 224
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 224-253 3.16e-05

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: 40.26  E-value: 3.16e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 224809389   224 EGQTALHYAAACEFLDIVELLLQSGADPTL 253
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 174-261 3.24e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 174 IAKAIKSKAADVNMTDEEGRALLH-WACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLD--IVELLLQSGAD 250
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGAD 144

                         90
                 ....*....|.
gi 224809389 251 PTLRDQDGCLP 261
Cdd:PHA03095 145 VNALDLYGMTP 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 174-247 3.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 3.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224809389 174 IAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQS 247
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-212 3.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 3.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 224809389  162 IFDYCRENNIDhIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLL 212
Cdd:pfam13637   5 LHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-251 5.02e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 5.02e-05
                          10        20
                  ....*....|....*....|....*...
gi 224809389  224 EGQTALHYAAACEFLDIVELLLQSGADP 251
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-223 5.04e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 5.04e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 224809389  191 EGRALLHWACDR-GHKELVKVLLQYEAGINCQDN 223
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 176-250 5.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 5.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809389 176 KAIKSKAADVNMTDEEGRALLHWAC--DRgHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGAD 250
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStlDR-NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-220 5.94e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 5.94e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 224809389  191 EGRALLHWACDRGHKELVKVLLQYEAGINC 220
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-277 1.23e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 162 IFDYCRENNidHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAG--INCQDNEGQTALHYAA------ 233
Cdd:PHA03095 194 HLQSFKPRA--RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAvfnnpr 271

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 224809389 234 ACEFldivelLLQSGADPTLRDQDG--CLPEEVTGC--KAVSLLLQRH 277
Cdd:PHA03095 272 ACRR------LIALGADINAVSSDGntPLSLMVRNNngRAVRAALAKN 313
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 191-220 1.34e-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: 38.34  E-value: 1.34e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 224809389   191 EGRALLHWACDRGHKELVKVLLQYEAGINC 220
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 167-258 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 167 RENNIDhIAKAIKSKAADVNMTDEEGRALLHWA----------------------CDRG---------HKELVKVLLQYE 215
Cdd:PHA02874 166 KHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAaeygdyacikllidhgnhimnkCKNGftplhnaiiHNRSAIELLINN 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 224809389 216 AGINCQDNEGQTALHYA--AACEfLDIVELLLQSGADPTLRDQDG 258
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAinPPCD-IDIIDILLYHKADISIKDNKG 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-261 2.99e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 2.99e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 224809389  229 LHYAAACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 206-261 8.55e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 8.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 224809389 206 ELVKVLLQYEAGINCQDNEGQTALHYAAAC---EFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTP 86
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 185-250 1.47e-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: 39.74  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809389 185 VNMTDEEGRALLHWACDRGhkeLVKVLL--QYEAGincqDNEGQTALHYAAACEFLDIVELLLQSGAD 250
Cdd:cd22194  106 NENTKEIVRILLAFAEENG---ILDRFInaEYTEE----AYEGQTALNIAIERRQGDIVKLLIAKGAD 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 161-250 3.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 161 NIFDYCRENNIDH--------IAKAIKSKAADVNMTDEEGRALLHWA-CDRGHKELVKVLLQYEAGINCQDNEGQTALHY 231
Cdd:PHA02876 369 NARDYCDKTPIHYaavrnnvvIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHY 448

                         90       100
                 ....*....|....*....|.
gi 224809389 232 AAA--CEfLDIVELLLQSGAD 250
Cdd:PHA02876 449 ACKknCK-LDVIEMLLDNGAD 468
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 191-258 3.89e-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: 38.59  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 191 EGRALLHWACDRGHKELVKVLLQYEAGINCQ----------DNE----GQTALHYAAACEFLDIVELLLQSGADP-TLRD 255
Cdd:cd22194  140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDiTSQD 219


                 ...
gi 224809389 256 QDG 258
Cdd:cd22194  220 SRG 222
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 195-250 3.95e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 3.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224809389 195 LLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGAD 250
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02741 PHA02741
hypothetical protein; Provisional
 180-264 4.40e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809389 180 SKAADVNMTDEEGRALLHWACDRGHK----ELVKVLLQYEAGINCQDN-EGQTALHYAAACEFLDIVELLL-QSGADPTL 253
Cdd:PHA02741  48 CHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHF 127

                         90
                 ....*....|.
gi 224809389 254 RDQDGCLPEEV 264
Cdd:PHA02741 128 CNADNKSPFEL 138
PHA02917 PHA02917
ankyrin-like protein; Provisional
 208-273 6.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 6.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809389 208 VKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDG--CLPEEVTGCKAVSLL 273
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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