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Conserved domains on  [gi|985482212|ref|NP_001306229|]
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ankyrin repeat and SOCS box protein 8 isoform c [Homo sapiens]

Protein Classification

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];
37-77 6.44e-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: 44.94  E-value: 6.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 985482212  37 VEDLIRGGADVNCTHGTLK-PLHCACMVSDADCVELLLEKGA 77
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGA 177
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-77 6.44e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 6.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 985482212  37 VEDLIRGGADVNCTHGTLK-PLHCACMVSDADCVELLLEKGA 77
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGA 177
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
40-81 1.19e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 985482212  40 LIRGGADVNCT--HGTlKPLHCACMVSDADCVELLLEKGAEDSL 81
Cdd:PTZ00322 101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTL 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-75 2.71e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.25  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 985482212  28 AIRSFPHDNVEDLIRGGADVNCTHGT-LKPLHCACMVSDADCVELLLEK 75
Cdd:pfam12796  4 AAKNGNLELVKLLLENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
56-78 1.65e-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: 32.94  E-value: 1.65e-03
                          10        20
                  ....*....|....*....|...
gi 985482212   56 PLHCACMVSDADCVELLLEKGAE 78
Cdd:smart00248  5 PLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-77 6.44e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 6.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 985482212  37 VEDLIRGGADVNCTHGTLK-PLHCACMVSDADCVELLLEKGA 77
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGA 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-77 6.50e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 6.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 985482212  26 IAAIRSFPHDNVEDLIRGGADVN-CTHGTLKPLHCACMVSDADCVELLLEKGA 77
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-77 3.19e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 3.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 985482212  26 IAAIRSFPHDNVEDLIRGGADVNCT--HGTLkPLHCACMVSDADCVELLLEKGA 77
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARdnDGET-PLHLAAENGHLEIVKLLLEAGA 210
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
40-81 1.19e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 985482212  40 LIRGGADVNCT--HGTlKPLHCACMVSDADCVELLLEKGAEDSL 81
Cdd:PTZ00322 101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTL 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-75 2.71e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.25  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 985482212  28 AIRSFPHDNVEDLIRGGADVNCTHGT-LKPLHCACMVSDADCVELLLEK 75
Cdd:pfam12796  4 AAKNGNLELVKLLLENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH 52
Ank_2 pfam12796
Ankyrin repeats (3 copies);
26-78 4.37e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.48  E-value: 4.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 985482212  26 IAAIRSFPHDNVEDLIRGgADVNCTHGTLKPLHCACMVSDADCVELLLEKGAE 78
Cdd:pfam12796 35 HLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGAD 86
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
56-78 1.65e-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: 32.94  E-value: 1.65e-03
                          10        20
                  ....*....|....*....|...
gi 985482212   56 PLHCACMVSDADCVELLLEKGAE 78
Cdd:smart00248  5 PLHLAAENGNLEVVKLLLDKGAD 27
PHA02884 PHA02884
ankyrin repeat protein; Provisional
12-78 3.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 34.57  E-value: 3.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985482212  12 IQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLK--PLHCACMVSDADCVELLLEKGAE 78
Cdd:PHA02884  61 APFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKitPLYISVLHGCLKCLEILLSYGAD 129
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
56-77 6.15e-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: 31.49  E-value: 6.15e-03
                         10        20
                 ....*....|....*....|...
gi 985482212  56 PLHCAC-MVSDADCVELLLEKGA 77
Cdd:pfam00023  5 PLHLAAgRRGNLEIVKLLLSKGA 27
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-81 8.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 33.40  E-value: 8.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985482212  17 SLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTL-KPLHCACMVSDADCVELLLEKGAEDSL 81
Cdd:PHA02874  31 SVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIpHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
 
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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