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Conserved domains on  [gi|2751354316|ref|WP_353278928|]
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MULTISPECIES: ankyrin repeat domain-containing protein [unclassified Wolbachia]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-154 1.97e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKK-----SRSDSSISekALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAADGGQLEV 105
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAgadvnAQDNDGNT--PLHLAAANGNLEIVKLLLEAGADVNArdndgETPLHLAAENGHLEI 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2751354316 106 VKLLLKRGANPYIRGWKEQTPRARAFKRSfyyrdkpYREIIDLLDQAEK 154
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENG-------NLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-154 1.97e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKK-----SRSDSSISekALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAADGGQLEV 105
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAgadvnAQDNDGNT--PLHLAAANGNLEIVKLLLEAGADVNArdndgETPLHLAAENGHLEI 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2751354316 106 VKLLLKRGANPYIRGWKEQTPRARAFKRSfyyrdkpYREIIDLLDQAEK 154
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENG-------NLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-119 1.04e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKKS---RSDSSISEKALYYVSEKGCLEIVTFLLDEgVDINISL----ALLGAADGGQLEVVKL 108
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGadaNLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDngrtALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 2751354316 109 LLKRGANPYIR 119
Cdd:pfam12796  80 LLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-134 1.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  41 KNCDLETVKSLV---KKSRSDSSISEKALYYVSEKGC--LEIVTFLLDEGVDINI---------------------SLAL 94
Cdd:PHA03100  117 KSNSYSIVEYLLdngANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsygvpinikdvygFTPL 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2751354316  95 LGAADGGQLEVVKLLLKRGANPYIRGWKEQTPRARAFKRS 134
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 39-149 8.49e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  39 AAKNCDLETVKSLVKKSRSD----SSISEKALYYVSEKGCLEIVTFLLDEGVD-INISL---------ALLGAADGGQLE 104
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDlfqrGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMtsdlyqgetALHIAVVNQNLN 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2751354316 105 VVKLLLKRGANPyirgwkeQTPRA--RAFKRS----FYYRDKP--------YREIIDLL 149
Cdd:cd22192   104 LVRELIARGADV-------VSPRAtgTFFRPGpknlIYYGEHPlsfaacvgNEEIVRLL 155
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-154 1.97e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKK-----SRSDSSISekALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAADGGQLEV 105
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAgadvnAQDNDGNT--PLHLAAANGNLEIVKLLLEAGADVNArdndgETPLHLAAENGHLEI 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2751354316 106 VKLLLKRGANPYIRGWKEQTPRARAFKRSfyyrdkpYREIIDLLDQAEK 154
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENG-------NLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-126 5.26e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  27 KAAEEYQKMLEVAAKNCDLETVKSLVKKSRSDSSISEK---ALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAA 98
Cdd:COG0666    49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGgntLLHAAARNGDLEIVKLLLEAGADVNArdkdgETPLHLAA 128

                          90       100
                  ....*....|....*....|....*...
gi 2751354316  99 DGGQLEVVKLLLKRGANPYIRGWKEQTP 126
Cdd:COG0666   129 YNGNLEIVKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-119 1.04e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKKS---RSDSSISEKALYYVSEKGCLEIVTFLLDEgVDINISL----ALLGAADGGQLEVVKL 108
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGadaNLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDngrtALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 2751354316 109 LLKRGANPYIR 119
Cdd:pfam12796  80 LLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-152 1.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  36 LEVAAKNCDLETVKSLVKK-----SRSDSSISekALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAADGGQLEV 105
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAgadvnARDNDGET--PLHLAAENGHLEIVKLLLEAGADVNAkdndgKTALDLAAENGNLEI 234

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2751354316 106 VKLLLKRGANPYIRGWKEQTPRARAFKRSFYYRDKPYREIIDLLDQA 152
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-134 1.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  41 KNCDLETVKSLV---KKSRSDSSISEKALYYVSEKGC--LEIVTFLLDEGVDINI---------------------SLAL 94
Cdd:PHA03100  117 KSNSYSIVEYLLdngANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAknrvnyllsygvpinikdvygFTPL 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2751354316  95 LGAADGGQLEVVKLLLKRGANPYIRGWKEQTPRARAFKRS 134
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 39-149 8.49e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  39 AAKNCDLETVKSLVKKSRSD----SSISEKALYYVSEKGCLEIVTFLLDEGVD-INISL---------ALLGAADGGQLE 104
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDlfqrGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMtsdlyqgetALHIAVVNQNLN 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2751354316 105 VVKLLLKRGANPyirgwkeQTPRA--RAFKRS----FYYRDKP--------YREIIDLL 149
Cdd:cd22192   104 LVRELIARGADV-------VSPRAtgTFFRPGpknlIYYGEHPlsfaacvgNEEIVRLL 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-110 2.05e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2751354316  65 ALYYVSEKGCLEIVTFLLDEGVDINIS-----LALLGAADGGQLEVVKLLL 110
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVdgngeTALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-136 9.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 35.32  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751354316  46 ETVKSLVK---KSRSDSSISEKALYYVSEKGCLEIVTFLLDEGVDINI-----SLALLGAADGGQLEVVKLLLKRGANPY 117
Cdd:PHA02874  105 DMIKTILDcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIeddngCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90
                  ....*....|....*....
gi 2751354316 118 IRGWKEQTPRARAFKRSFY 136
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDY 203
 
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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