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Conserved domains on  [gi|15239209|ref|NP_198432|]
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Ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12120816)

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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ank_2 pfam12796
Ankyrin repeats (3 copies);
126-213 1.04e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209   126 LHIAVAAKHEGFVRNLLGslESNDLALRNVDGNTALCFAAASGVVEIAKMLIEKNKdlPMIRGGGKTtPIHMAALFGHGE 205
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRT-ALHYAARSGHLE 75


                  ....*...
gi 15239209   206 MVKYLYKN 213
Cdd:pfam12796  76 IVKLLLEK 83
 
Name Accession Description Interval E-value
Ank_2 pfam12796
Ankyrin repeats (3 copies);
126-213 1.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209   126 LHIAVAAKHEGFVRNLLGslESNDLALRNVDGNTALCFAAASGVVEIAKMLIEKNKdlPMIRGGGKTtPIHMAALFGHGE 205
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRT-ALHYAARSGHLE 75


                  ....*...
gi 15239209   206 MVKYLYKN 213
Cdd:pfam12796  76 IVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-210 6.61e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 6.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  81 DDKLRAKGVQLYQAALKGDWKAANGIIIEQKYIIYQKiTSKSETVLHIAVAAKHEGFVRNLLgslESN-DLALRNVDGNT 159
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAK-DDGGNTLLHAAARNGDLEIVKLLL---EAGaDVNARDKDGET 122

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15239209 160 ALCFAAASGVVEIAKMLIEKNKDlPMIRGGGKTTPIHMAALFGHGEMVKYL 210
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLL 172
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 91-200 8.12e-04

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: 40.77  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  91 LYQAALKGDWKAANGIIIEQKYIIYQKITS---KSETVLHIAVAAKHEGFVRNLLGslesndlalRNVDGNTA------- 160
Cdd:cd22192  55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyQGETALHIAVVNQNLNLVRELIA---------RGADVVSPratgtff 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15239209 161 --------------LCFAAASGVVEIAKMLIEKNKDLPMIRGGGkTTPIHMAAL 200
Cdd:cd22192 126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-NTVLHILVL 178
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 123-213 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  123 ETVLHIAVAakhEGFVRNLLGSLESNDLA--LRNVDGNTALCFAAASGVVEIAKMLIEKNKDlPMIRGGGKTTPIHMAAL 200
Cdd:PHA02875  69 ESELHDAVE---EGDVKAVEELLDLGKFAddVFYKDGMTPLHLATILKKLDIMKLLIARGAD-PDIPNTDKFSPLHLAVM 144

                         90
                 ....*....|...
gi 15239209  201 FGHGEMVKYLYKN 213
Cdd:PHA02875 145 MGDIKGIELLIDH 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 156-183 5.09e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 5.09e-03
                           10        20
                   ....*....|....*....|....*...
gi 15239209    156 DGNTALCFAAASGVVEIAKMLIEKNKDL 183
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
Ank_2 pfam12796
Ankyrin repeats (3 copies);
126-213 1.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209   126 LHIAVAAKHEGFVRNLLGslESNDLALRNVDGNTALCFAAASGVVEIAKMLIEKNKdlPMIRGGGKTtPIHMAALFGHGE 205
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRT-ALHYAARSGHLE 75


                  ....*...
gi 15239209   206 MVKYLYKN 213
Cdd:pfam12796  76 IVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-210 6.61e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 6.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  81 DDKLRAKGVQLYQAALKGDWKAANGIIIEQKYIIYQKiTSKSETVLHIAVAAKHEGFVRNLLgslESN-DLALRNVDGNT 159
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAK-DDGGNTLLHAAARNGDLEIVKLLL---EAGaDVNARDKDGET 122

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15239209 160 ALCFAAASGVVEIAKMLIEKNKDlPMIRGGGKTTPIHMAALFGHGEMVKYL 210
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-210 5.63e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 5.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  91 LYQAALKGDWKAANgIIIEQKYIIYQKiTSKSETVLHIAVAAKHEGFVRNLLgslESN-DLALRNVDGNTALCFAAASGV 169
Cdd:COG0666 124 LHLAAYNGNLEIVK-LLLEAGADVNAQ-DNDGNTPLHLAAANGNLEIVKLLL---EAGaDVNARDNDGETPLHLAAENGH 198

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15239209 170 VEIAKMLIEKNKDlPMIRGGGKTTPIHMAALFGHGEMVKYL 210
Cdd:COG0666 199 LEIVKLLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-210 3.76e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15239209   157 GNTALCFAAASGVVEIAKMLIEKNKDLPMIRGGGkTTPIHMAALFGHGEMVKYL 210
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNG-ETALHFAASNGNVEVLKLL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
90-210 2.90e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 2.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  90 QLYQAALKGDWKAANGIIIEQKYIIYQKITSKSETVLHIAVAAKHEGFVRNLLGSLESNDLALRNVDGNTALCFAAASGV 169
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15239209 170 VEIAKMLIEKNKDlPMIRGGGKTTPIHMAALFGHGEMVKYL 210
Cdd:COG0666 100 LEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-233 1.17e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 1.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239209   161 LCFAAASGVVEIAKMLIEKNKDLPMIRGGGKTtPIHMAALFGHGEMVKYLYKNTRFREFNDEEFVnLFHAVIS 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT-ALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA-LHYAARS 71
Ank_2 pfam12796
Ankyrin repeats (3 copies);
91-183 1.73e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209    91 LYQAALKGDWKAANgIIIEQKYIIYQKiTSKSETVLHIAVAAKHEGFVRNLLGSLESNDlalrNVDGNTALCFAAASGVV 170
Cdd:pfam12796   1 LHLAAKNGNLELVK-LLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHL 74

                          90
                  ....*....|...
gi 15239209   171 EIAKMLIEKNKDL 183
Cdd:pfam12796  75 EIVKLLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-223 5.38e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.95  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  91 LYQAALKGDWKAANgIIIEQKYIIYQKiTSKSETVLHIAVAAKHEGFVRnLLgsLESN-DLALRNVDGNTALCFAAASGV 169
Cdd:COG0666 157 LHLAAANGNLEIVK-LLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LL--LEAGaDVNAKDNDGKTALDLAAENGN 231

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15239209 170 VEIAKMLIEKNKDLPMIRGGGKtTPIHMAALFGHGEMVKYLYKNTRFREFNDEE 223
Cdd:COG0666 232 LEIVKLLLEAGADLNAKDKDGL-TALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-177 8.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 8.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15239209   124 TVLHIAVAAKHEGFVRNLLGSleSNDLALRNVDGNTALCFAAASGVVEIAKMLI 177
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 91-200 8.12e-04

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: 40.77  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  91 LYQAALKGDWKAANGIIIEQKYIIYQKITS---KSETVLHIAVAAKHEGFVRNLLGslesndlalRNVDGNTA------- 160
Cdd:cd22192  55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyQGETALHIAVVNQNLNLVRELIA---------RGADVVSPratgtff 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15239209 161 --------------LCFAAASGVVEIAKMLIEKNKDLPMIRGGGkTTPIHMAAL 200
Cdd:cd22192 126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLG-NTVLHILVL 178
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 123-213 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239209  123 ETVLHIAVAakhEGFVRNLLGSLESNDLA--LRNVDGNTALCFAAASGVVEIAKMLIEKNKDlPMIRGGGKTTPIHMAAL 200
Cdd:PHA02875  69 ESELHDAVE---EGDVKAVEELLDLGKFAddVFYKDGMTPLHLATILKKLDIMKLLIARGAD-PDIPNTDKFSPLHLAVM 144

                         90
                 ....*....|...
gi 15239209  201 FGHGEMVKYLYKN 213
Cdd:PHA02875 145 MGDIKGIELLIDH 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
176-213 3.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 15239209   176 LIEKNKDLPMIRGGGKTTPIHMAALFGHGEMVKYLYKN 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY 38
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 156-183 5.09e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 5.09e-03
                           10        20
                   ....*....|....*....|....*...
gi 15239209    156 DGNTALCFAAASGVVEIAKMLIEKNKDL 183
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
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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