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Conserved domains on  [gi|351065608|emb|CCD61591|]
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Sex-determining protein fem-1 [Caenorhabditis elegans]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12150541)

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
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 40-76 4.70e-07

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.70e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 351065608  40 DCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-68 1.09e-04

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065608    9 RTVIYNAAAVGNLQRIKVFTINSrndrqwiIDCFNSDQDGRYPLVIAARNGHANVVEYLL 68
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKG-------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 40-76 4.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.70e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 351065608  40 DCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-77 7.37e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 7.37e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351065608    9 RTVIYNAAAVGNLQRIKVFtINSRNdrqwiidcFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLL-LEHAD--------VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-77 7.64e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 7.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351065608   9 RTVIYNAAAVGNLQRIKVF-----TINSRNDrqwiidcfnsdqDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLleagaDVNARDN------------DGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 47-76 4.95e-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: 37.18  E-value: 4.95e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 351065608    47 DGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-68 1.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065608    9 RTVIYNAAAVGNLQRIKVFTINSrndrqwiIDCFNSDQDGRYPLVIAARNGHANVVEYLL 68
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKG-------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 40-76 4.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.70e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 351065608  40 DCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-77 7.37e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 7.37e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351065608    9 RTVIYNAAAVGNLQRIKVFtINSRNdrqwiidcFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLL-LEHAD--------VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-77 7.64e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 7.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351065608   9 RTVIYNAAAVGNLQRIKVF-----TINSRNDrqwiidcfnsdqDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLleagaDVNARDN------------DGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-77 8.51e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.33  E-value: 8.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351065608   9 RTVIYNAAAVGNLQRIKVF-----TINSRNDrqwiidcfnsdqDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLleagaDVNAQDN------------DGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-77 3.37e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 3.37e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 351065608  45 DQDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:COG0666  117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-69 4.29e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 4.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 351065608   15 AAAVGNLQRIKVFTINSrndrqwiIDCFNSDQDGRYPLVIAARNGHANVVEYLLE 69
Cdd:pfam12796   4 AAKNGNLELVKLLLENG-------ADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
39-77 1.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 351065608   39 IDCFNSDQDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 47-76 2.94e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.94e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 351065608   47 DGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 47-77 4.89e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 4.89e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 351065608   47 DGRYPLVIAA-RNGHANVVEYLLEIGADPSVR 77
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 47-76 4.95e-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: 37.18  E-value: 4.95e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 351065608    47 DGRYPLVIAARNGHANVVEYLLEIGADPSV 76
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-68 1.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065608    9 RTVIYNAAAVGNLQRIKVFTINSrndrqwiIDCFNSDQDGRYPLVIAARNGHANVVEYLL 68
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKG-------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-77 7.02e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 37.24  E-value: 7.02e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 351065608  45 DQDGRYPLVIAARNGHANVVEYLLEIGADPSVR 77
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-89 4.01e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 33.55  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 351065608   52 LVIAARNGHANVVEYLLEIGADPsvrGVVEFDNENILF 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA---NLQDKNGRTALH 35
 
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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