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Conserved domains on  [gi|281361020|ref|NP_728083|]
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Ankle2, isoform F [Drosophila melanogaster]

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
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
179-322 4.53e-07

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020  179 IEGGHIDRVKriiwenprFLISSGDTPTsLKEGCRYNAMHICAQVNKARIAQLLLK------TISDREFTQL-YVGKKGS 251
Cdd:COG0666    95 ARNGDLEIVK--------LLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEagadvnAQDNDGNTPLhLAAANGN 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361020  252 GKMCAALnislLDY--YLNMPDKGrGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANA 322
Cdd:COG0666   166 LEIVKLL----LEAgaDVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
179-322 4.53e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020  179 IEGGHIDRVKriiwenprFLISSGDTPTsLKEGCRYNAMHICAQVNKARIAQLLLK------TISDREFTQL-YVGKKGS 251
Cdd:COG0666    95 ARNGDLEIVK--------LLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEagadvnAQDNDGNTPLhLAAANGN 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361020  252 GKMCAALnislLDY--YLNMPDKGrGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANA 322
Cdd:COG0666   166 LEIVKLL----LEAgaDVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-297 1.40e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020   217 MHICAQVNKARIAQLLLKTISDREFTqlyvgkKGSGK---MCAALN-----ISLLDYYLNMPDKGRGETPLHFAAKNGHV 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ------DKNGRtalHLAAKNghleiVKLLLEHADVNLKDNGRTALHYAARSGHL 74


                   ....*....
gi 281361020   289 AMVEVLVSY 297
Cdd:pfam12796   75 EIVKLLLEK 83
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 274-297 2.21e-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: 36.41  E-value: 2.21e-03
                            10        20
                    ....*....|....*....|....
gi 281361020    274 RGETPLHFAAKNGHVAMVEVLVSY 297
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDK 24
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
179-322 4.53e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020  179 IEGGHIDRVKriiwenprFLISSGDTPTsLKEGCRYNAMHICAQVNKARIAQLLLK------TISDREFTQL-YVGKKGS 251
Cdd:COG0666    95 ARNGDLEIVK--------LLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEagadvnAQDNDGNTPLhLAAANGN 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361020  252 GKMCAALnislLDY--YLNMPDKGrGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANA 322
Cdd:COG0666   166 LEIVKLL----LEAgaDVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-297 1.40e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020   217 MHICAQVNKARIAQLLLKTISDREFTqlyvgkKGSGK---MCAALN-----ISLLDYYLNMPDKGRGETPLHFAAKNGHV 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ------DKNGRtalHLAAKNghleiVKLLLEHADVNLKDNGRTALHYAARSGHL 74


                   ....*....
gi 281361020   289 AMVEVLVSY 297
Cdd:pfam12796   75 EIVKLLLEK 83
Ank_5 pfam13857
Ankyrin repeats (many copies);
262-314 1.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281361020   262 LLDYY---LNMPDkGRGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEI 314
Cdd:pfam13857    1 LLEHGpidLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-295 1.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 281361020   259 NISLLDYYL------NMPDKGrGETPLHFAAKNGHVAMVEVLV 295
Cdd:pfam13637   13 HLELLRLLLekgadiNAVDGN-GETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
179-336 1.84e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.48  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020  179 IEGGHIDRVKriiwenprFLISSGDTPTsLKEGCRYNAMHICAQVNKARIAQLLLK------TISDREFTQLyvgkkgsg 252
Cdd:COG0666   128 AYNGNLEIVK--------LLLEAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEagadvnARDNDGETPL-------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361020  253 kMCAALNIS------LLDY--YLNMPDKgRGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANATH 324
Cdd:COG0666   191 -HLAAENGHleivklLLEAgaDVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                         170
                  ....*....|..
gi 281361020  325 VTIKKLELLLYD 336
Cdd:COG0666   269 KLLLLALLLLAA 280
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 274-297 2.21e-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: 36.41  E-value: 2.21e-03
                            10        20
                    ....*....|....*....|....
gi 281361020    274 RGETPLHFAAKNGHVAMVEVLVSY 297
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 274-298 3.13e-03

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: 36.08  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|....*
gi 281361020   274 RGETPLHFAAKNGHVAMVEVLVSYP 298
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENG 25
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 274-297 8.74e-03

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: 34.96  E-value: 8.74e-03
                           10        20
                   ....*....|....*....|....*
gi 281361020   274 RGETPLHFAA-KNGHVAMVEVLVSY 297
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSK 25
 
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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