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Conserved domains on  [gi|14150169|ref|NP_115736|]
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acyl-CoA-binding domain-containing protein 6 [Homo sapiens]

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 1.71e-32

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 114.23  E-value: 1.71e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14150169    43 AELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-261 2.84e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666 128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90
                ....*....|....*.
gi 14150169 246 QSGADPTLRDQDGCLP 261
Cdd:COG0666 207 EAGADVNAKDNDGKTA 222
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
43-118 1.71e-32

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 114.23  E-value: 1.71e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14150169    43 AELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-261 2.84e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666 128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90
                ....*....|....*.
gi 14150169 246 QSGADPTLRDQDGCLP 261
Cdd:COG0666 207 EAGADVNAKDNDGKTA 222
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 42-121 7.96e-28

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: 102.40  E-value: 7.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  42 LAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKL 121
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
42-121 3.33e-22

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 87.98  E-value: 3.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  42 LAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKL 121
Cdd:COG4281   4 LQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNSL 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-255 2.39e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHrADINCQDNeGQTALHYASACEFLDIVELLL 245
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 14150169   246 QSGADPTLRD 255
Cdd:pfam12796  82 EKGADINVKD 91
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 42-125 3.68e-15

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 69.47  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   42 LAELFEKAAAHLQGLIQVA--SREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVK 119
Cdd:PTZ00458   1 MADLFEECVSFINSLPKTVnlSVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVT 80


                 ....*.
gi 14150169  120 KLDPGW 125
Cdd:PTZ00458  81 ELFPNW 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-261 1.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  176 KAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 14150169  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 7.10e-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: 50.01  E-value: 7.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 167 RENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRAD-----INCQDNEGQTALHYASACEFLDIV 241
Cdd:cd22192  26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                ....*....
gi 14150169 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 ...
 191-220 4.55e-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: 39.49  E-value: 4.55e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 14150169    191 EGRALLHWACDRGHKELVTVLLQHRADINC 220
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 162-250 1.51e-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: 40.06  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   162 IFDYCRENNIDHITKAIKSKNVDVnvkdEEGRALLHwACDRGHKELVTVLLQHRADINCQDN--------------EGQT 227
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelandqytseftPGIT 130

                          90       100
                  ....*....|....*....|...
gi 14150169   228 ALHYASACEFLDIVELLLQSGAD 250
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ACBP pfam00887
Acyl CoA binding protein;
43-118 1.71e-32

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 114.23  E-value: 1.71e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14150169    43 AELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVV 118
Cdd:pfam00887   1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-261 2.84e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666 128 AYNGNLE-IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90
                ....*....|....*.
gi 14150169 246 QSGADPTLRDQDGCLP 261
Cdd:COG0666 207 EAGADVNAKDNDGKTA 222
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 42-121 7.96e-28

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: 102.40  E-value: 7.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  42 LAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKL 121
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-261 9.57e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 9.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666  95 ARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        90
                ....*....|....*.
gi 14150169 246 QSGADPTLRDQDGCLP 261
Cdd:COG0666 174 EAGADVNARDNDGETP 189
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
42-121 3.33e-22

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 87.98  E-value: 3.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  42 LAELFEKAAAHLQGLIQVASREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKKL 121
Cdd:COG4281   4 LQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNSL 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-261 1.42e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 161 NIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDI 240
Cdd:COG0666  56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100
                ....*....|....*....|.
gi 14150169 241 VELLLQSGADPTLRDQDGCLP 261
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-255 2.39e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHrADINCQDNeGQTALHYASACEFLDIVELLL 245
Cdd:pfam12796   5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 14150169   246 QSGADPTLRD 255
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-258 4.44e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 4.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666 161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                        90
                ....*....|...
gi 14150169 246 QSGADPTLRDQDG 258
Cdd:COG0666 240 EAGADLNAKDKDG 252
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 42-125 3.68e-15

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 69.47  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   42 LAELFEKAAAHLQGLIQVA--SREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVK 119
Cdd:PTZ00458   1 MADLFEECVSFINSLPKTVnlSVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVT 80


                 ....*.
gi 14150169  120 KLDPGW 125
Cdd:PTZ00458  81 ELFPNW 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-245 1.14e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.91  E-value: 1.14e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 14150169   192 GRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
196-246 2.67e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 2.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14150169   196 LHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQ 246
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-261 1.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  176 KAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 14150169  256 QDGCLP 261
Cdd:PHA02874 188 NNGESP 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-261 1.06e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 161 NIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDI 240
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                        90       100
                ....*....|....*....|.
gi 14150169 241 VELLLQSGADPTLRDQDGCLP 261
Cdd:COG0666 103 VKLLLEAGADVNARDKDGETP 123
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 208-278 3.74e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 3.74e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14150169  208 VTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLPEEV---TGCKTVSLVLQRHT 278
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELaeeNGFREVVQLLSRHS 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
166-258 4.96e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 4.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 166 CRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:COG0666 194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                        90
                ....*....|...
gi 14150169 246 QSGADPTLRDQDG 258
Cdd:COG0666 273 LALLLLAAALLDL 285
Ank_5 pfam13857
Ankyrin repeats (many copies);
178-232 7.18e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 7.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 14150169   178 IKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYA 232
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 170-250 8.58e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 8.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  170 NIDHITKaIK---SKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQ 246
Cdd:PHA03100 168 DINAKNR-VNyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                 ....
gi 14150169  247 SGAD 250
Cdd:PHA03100 247 NGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 165-258 1.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  165 YCRENNID-HITKAIKSKNVDVNVKDEegrallhwacdrghkelVTVLLQHRADINCQDNEGQTALHYASACEFLDIVEL 243
Cdd:PHA03100 148 YLESNKIDlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         90
                 ....*....|....*
gi 14150169  244 LLQSGADPTLRDQDG 258
Cdd:PHA03100 211 LLDLGANPNLVNKYG 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 184-245 4.90e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.90e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14150169  184 DVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLL 245
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 156-250 8.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  156 REEDKNIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASA- 234
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGy 244

                         90
                 ....*....|....*.
gi 14150169  235 CEFLDIVELLLQSGAD 250
Cdd:PHA02878 245 CKDYDILKLLLEHGVD 260
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 168-250 1.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  168 ENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDR--GHKELVTVLLQHRADINCQDNEGQTALHYA--SACEFLDIVEL 243
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKL 161


                 ....*..
gi 14150169  244 LLQSGAD 250
Cdd:PHA03100 162 LIDKGVD 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
211-261 2.44e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 14150169   211 LLQHR-ADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 167-250 7.10e-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: 50.01  E-value: 7.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169 167 RENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRAD-----INCQDNEGQTALHYASACEFLDIV 241
Cdd:cd22192  26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVVNQNLNLV 105


                ....*....
gi 14150169 242 ELLLQSGAD 250
Cdd:cd22192 106 RELIARGAD 114
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 169-258 8.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  169 NNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGH-----KELVTVLLQHRADINCQDNEGQTALHYASACEF--LDIV 241
Cdd:PHA03100  46 RNID-VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIV 124

                         90
                 ....*....|....*..
gi 14150169  242 ELLLQSGADPTLRDQDG 258
Cdd:PHA03100 125 EYLLDNGANVNIKNSDG 141
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 184-251 8.96e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 8.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  184 DVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQ--SGADP 251
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDP 619
PHA03095 PHA03095
ankyrin-like protein; Provisional
 181-255 1.74e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  181 KNVDVNVKDEEGRALLHwACDRG---HKELVTVLLQHRADINCQDNEGQTALH----YASACefLDIVELLLQSGADPTL 253
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYA 182


                 ..
gi 14150169  254 RD 255
Cdd:PHA03095 183 VD 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-255 1.96e-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: 43.43  E-value: 1.96e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 14150169   224 EGQTALHYASACE-FLDIVELLLQSGADPTLRD 255
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-261 4.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  109 QAMQEYIAVVKKLDPGWNpqipEKKGKEA----NTGFGGPVISSLY-HEETIreEDKNIFDYCRENNID-HITKAIKSKN 182
Cdd:PHA02878  84 LGMKEMIRSINKCSVFYT----LVAIKDAfnnrNVEIFKIILTNRYkNIQTI--DLVYIDKKSKDDIIEaEITKLLLSYG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  183 VDVNVKDEE-GRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02878 158 ADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-223 5.90e-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: 42.28  E-value: 5.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 14150169   191 EGRALLHWACDR-GHKELVTVLLQHRADINCQDN 223
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-261 6.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  158 EDKNIFDYCRENNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEF 237
Cdd:PHA02874 123 ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         90       100
                 ....*....|....*....|....
gi 14150169  238 LDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 167-258 7.81e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 7.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  167 RENNIDhITKAIKSKNVDVNVKDEEGRALLHWA----------------------CDRGHKELVTVLLQHR--------- 215
Cdd:PHA02874 166 KHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAaeygdyacikllidhgnhimnkCKNGFTPLHNAIIHNRsaiellinn 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 14150169  216 ADINCQDNEGQTALHYA--SACEfLDIVELLLQSGADPTLRDQDG 258
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAinPPCD-IDIIDILLYHKADISIKDNKG 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 205-261 1.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14150169  205 KELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02874 104 KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 170-260 1.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  170 NIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGA 249
Cdd:PHA02875 114 KLD-IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                         90
                 ....*....|.
gi 14150169  250 DPTLRDQDGCL 260
Cdd:PHA02875 193 NIDYFGKNGCV 203
PHA03095 PHA03095
ankyrin-like protein; Provisional
 184-261 1.70e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  184 DVNVKDEEGRALLH-WACDRGHKELVTVLLQHRADINCQDNEGQTALH-YAS-ACEFLDIVELLLQSGADPTLRDQDGCL 260
Cdd:PHA03095  75 DVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMT 154


                 .
gi 14150169  261 P 261
Cdd:PHA03095 155 P 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 151-255 1.98e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  151 HEETIREEDknIFDY-CRENNID-HITKAIKSKNVDVNVKDEEGRALLHWACDRGH---KELVTVLLQHRADINCQDNEG 225
Cdd:PHA03095   6 SVDIIMEAA--LYDYlLNASNVTvEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCG 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 14150169  226 QTALH-YASACEFLDIVELLLQSGADPTLRD 255
Cdd:PHA03095  84 FTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114
PHA02798 PHA02798
ankyrin-like protein; Provisional
 161-250 2.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  161 NIFDYcreNNIDHITKAIKSKNVDVNVKDEEGRALLHWACDRGH---KELVTVLLQHRADINCQDNEGQTAL--HYASAC 235
Cdd:PHA02798  81 NIKDY---KHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLqvYLQSNH 157

                         90
                 ....*....|....*.
gi 14150169  236 EF-LDIVELLLQSGAD 250
Cdd:PHA02798 158 HIdIEIIKLLLEKGVD 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 174-247 2.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 2.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14150169  174 ITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQS 247
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-277 2.61e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  162 IFDYCRENNidHITKAIKSKNVDVNVKDEEGRALLHWA-----CDRGhkeLVTVLLQHRADINCQDNEGQTALHYAS--- 233
Cdd:PHA03095 194 HLQSFKPRA--RIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYAAvfn 268

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14150169  234 ---ACEFldivelLLQSGADPTLRDQDG--CLPEEVTGC--KTVSLVLQRH 277
Cdd:PHA03095 269 nprACRR------LIALGADINAVSSDGntPLSLMVRNNngRAVRAALAKN 313
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 191-220 4.55e-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: 39.49  E-value: 4.55e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 14150169    191 EGRALLHWACDRGHKELVTVLLQHRADINC 220
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 165-261 4.73e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  165 YCRENNIDH-ITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASAC--EFLDIV 241
Cdd:PHA02946  44 YCGIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTddEVIERI 123

                         90       100
                 ....*....|....*....|.
gi 14150169  242 ELLLQSGADPTLR-DQDGCLP 261
Cdd:PHA02946 124 NLLVQYGAKINNSvDEEGCGP 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-220 7.67e-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: 7.67e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 14150169   191 EGRALLHWACDRGHKELVTVLLQHRADINC 220
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 224-253 1.18e-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: 1.18e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 14150169    224 EGQTALHYASACEFLDIVELLLQSGADPTL 253
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-251 3.32e-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: 37.24  E-value: 3.32e-04
                          10        20
                  ....*....|....*....|....*...
gi 14150169   224 EGQTALHYASACEFLDIVELLLQSGADP 251
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 161-255 5.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  161 NIFDYCRENNIDHITKA---------IKSKNVDVNVKDEEGRALLHWACDRGH-KELVTVLLQHRADINCQDNEGQTALH 230
Cdd:PHA02876 267 NSIDDCKNTPLHHASQApslsrlvpkLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLH 346

                         90       100
                 ....*....|....*....|....*.
gi 14150169  231 YASACE-FLDIVELLLQSGADPTLRD 255
Cdd:PHA02876 347 QASTLDrNKDIVITLLELGANVNARD 372
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 182-262 6.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  182 NVDVNVKDEEGRALLHWA----CDrghKELVTVLLQHRADINCQDNEGQTALHyaSACEFLDIVELLLQSGADPTLRDQD 257
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADISIKDNKGENPID--TAFKYINKDPVIKDIIANAVLIKEA 318


                 ....*
gi 14150169  258 GCLPE 262
Cdd:PHA02874 319 DKLKD 323
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 195-250 1.09e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14150169  195 LLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGAD 250
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 144-261 1.15e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  144 PVISSLYHEETIREEDKNIFDYCRENN-IDHITKAIKS-----KNVDVNV-------------KDEEGRALLHWACDRGH 204
Cdd:PHA02716 250 PIMTYIINIDNINPEITNIYIESLDGNkVKNIPMILHSyitlaRNIDISVvysflqpgvklhyKDSAGRTCLHQYILRHN 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14150169  205 --KELVTVLLQHRADINCQDNEGQTALH-YASACEF-------------LDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA02716 330 isTDIIKLLHEYGNDLNEPDNIGNTVLHtYLSMLSVvnildpetdndirLDVIQCLISLGADITAVNCLGYTP 402
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 176-250 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 1.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14150169  176 KAIKSKNVDVNVKDEEGRALLHWAC--DRgHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDIVELLLQSGAD 250
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStlDR-NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-261 1.43e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.02  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 14150169   229 LHYASACEFLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 162-250 1.51e-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: 40.06  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169   162 IFDYCRENNIDHITKAIKSKNVDVnvkdEEGRALLHwACDRGHKELVTVLLQHRADINCQDN--------------EGQT 227
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelandqytseftPGIT 130

                          90       100
                  ....*....|....*....|...
gi 14150169   228 ALHYASACEFLDIVELLLQSGAD 250
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGAS 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-212 1.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14150169   162 IFDYCRENNIDhITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLL 212
Cdd:pfam13637   5 LHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-261 1.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  165 YCRENNID-HITKAIKSKNVDVNVKDEEGRALLHwACDRGHK---ELVTVLLQHRADINCQDNEGQTALHYasACEFL-- 238
Cdd:PHA03095 124 YLSGFNINpKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADVYAVDDRFRSLLHH--HLQSFkp 200

                         90       100
                 ....*....|....*....|....*
gi 14150169  239 --DIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA03095 201 raRIVRELIRAGCDPAATDMLGNTP 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 161-277 2.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14150169  161 NIFDYCRENNI-DHITKAIKSKNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEF-- 237
Cdd:PHA03100   3 SYIVLTKSRIIkVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnl 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 14150169  238 ---LDIVELLLQSGADPTLRDQDGCLP------EEVTGCKTVSLVLQRH 277
Cdd:PHA03100  83 tdvKEIVKLLLEYGANVNAPDNNGITPllyaisKKSNSYSIVEYLLDNG 131
PHA03095 PHA03095
ankyrin-like protein; Provisional
 206-261 2.70e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14150169  206 ELVTVLLQHRADINCQDNEGQTALHY--ASACE-FLDIVELLLQSGADPTLRDQDGCLP 261
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEkVKDIVRLLLEAGADVNAPERCGFTP 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 199-241 6.40e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 37.68  E-value: 6.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 14150169 199 ACdRGHKELVTVLLQHRADINCQDNEGQTALHY-------ASACEFLDIV 241
Cdd:cd22192 144 AC-VGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqpnkTFACQMYDLI 192
PHA02917 PHA02917
ankyrin-like protein; Provisional
 184-232 8.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 37.28  E-value: 8.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 14150169  184 DVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYA 232
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIA 492
 
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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