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Conserved domains on  [gi|2217266915|ref|XP_047275162|]
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ankyrin repeat domain-containing protein 45 isoform X3 [Homo sapiens]

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];
58-182 4.22e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  58 PLLQPALTGDVEGLQKIFEDPENPH-----------------HEQAMQLLLE-------EDIVGRNLLYAACMAGQSDVI 113
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNardkdgetplhlaayngNLEIVKLLLEagadvnaQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217266915 114 RALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFL 182
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-182 4.22e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  58 PLLQPALTGDVEGLQKIFEDPENPH-----------------HEQAMQLLLE-------EDIVGRNLLYAACMAGQSDVI 113
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNardkdgetplhlaayngNLEIVKLLLEagadvnaQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217266915 114 RALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFL 182
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-160 3.38e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  83 HEQAMQLLLEE-------DIVGRNLLYAACMAGQSDVIRALAKYgVNLNEKTtRGYTLLHCAAAWGRLETLKALVELDVD 155
Cdd:pfam12796   9 NLELVKLLLENgadanlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86


                  ....*
gi 2217266915 156 IEALN 160
Cdd:pfam12796  87 INVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 90-162 1.48e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217266915  90 LLEEDIVGRNLLYAaCMAGQS---DVIRALAKYGVNLNEKTTRGYTLLHCAAAWGR--LETLKALVELDVDIEALNFR 162
Cdd:PHA03095  110 VNAKDKVGRTPLHV-YLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-158 3.91e-04

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: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217266915  129 RGYTLLHCAAAWGRLETLKALVELDVDIEA 158
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-182 4.22e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  58 PLLQPALTGDVEGLQKIFEDPENPH-----------------HEQAMQLLLE-------EDIVGRNLLYAACMAGQSDVI 113
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNardkdgetplhlaayngNLEIVKLLLEagadvnaQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217266915 114 RALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFL 182
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-182 2.83e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  97 GRNLLYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQT 176
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166


                  ....*.
gi 2217266915 177 ECVEFL 182
Cdd:COG0666   167 EIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-160 3.38e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  83 HEQAMQLLLEE-------DIVGRNLLYAACMAGQSDVIRALAKYgVNLNEKTtRGYTLLHCAAAWGRLETLKALVELDVD 155
Cdd:pfam12796   9 NLELVKLLLENgadanlqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86


                  ....*
gi 2217266915 156 IEALN 160
Cdd:pfam12796  87 INVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-182 2.62e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  83 HEQAMQLLLE-------EDIVGRNLLYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVD 155
Cdd:COG0666   165 NLEIVKLLLEagadvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          90       100
                  ....*....|....*....|....*..
gi 2217266915 156 IEALNFREERARDVAARYSQTECVEFL 182
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-182 5.54e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915 101 LYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVE-LDVDIEALNfreERARDVAARYSQTECV 179
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG---RTALHYAARSGHLEIV 77


                  ...
gi 2217266915 180 EFL 182
Cdd:pfam12796  78 KLL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-182 3.13e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  89 LLLEEDIVGRNLLYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARD 168
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                          90
                  ....*....|....
gi 2217266915 169 VAARYSQTECVEFL 182
Cdd:COG0666   126 LAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-150 8.11e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 8.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217266915  97 GRNLLYAACMAGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALV 150
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
130-182 1.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217266915 130 GYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFL 182
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 90-162 1.48e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217266915  90 LLEEDIVGRNLLYAaCMAGQS---DVIRALAKYGVNLNEKTTRGYTLLHCAAAWGR--LETLKALVELDVDIEALNFR 162
Cdd:PHA03095  110 VNAKDKVGRTPLHV-YLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDR 186
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 129-158 1.98e-04

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: 37.24  E-value: 1.98e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217266915 129 RGYTLLHCAAAWGRLETLKALVELDVDIEA 158
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-158 3.91e-04

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: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217266915  129 RGYTLLHCAAAWGRLETLKALVELDVDIEA 158
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-160 1.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 1.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217266915 111 DVIRALAKYGVNLNEKTTRGYTLLH--CAAAWGRLETLKALVELDVDIEALN 160
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALD 149
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 111-160 1.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217266915 111 DVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALN 160
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222
PHA02741 PHA02741
hypothetical protein; Provisional
 79-182 2.21e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266915  79 ENPHHEQAM-QLLLEEDIVGRNLLYAACMAGQSDVIRALAKYGVN------LNEKTTRGYTLLHCAA----AWGRLETLK 147
Cdd:PHA02741    2 ESPHFMTCLeEMIAEKNSEGENFFHEAARCGCFDIIARFTPFIRGdchaaaLNATDDAGQMCIHIAAekheAQLAAEIID 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217266915 148 ALVELDVDIEALNFRE-ERARDVAARYSQTECVEFL 182
Cdd:PHA02741   82 HLIELGADINAQEMLEgDTALHLAAHRRDHDLAEWL 117
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-158 2.34e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 2.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217266915 111 DVIRALAKYGVNLNEKTTRGYTLLHCAAAWG-RLETLKALVELDVDIEA 158
Cdd:PHA03095   64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNA 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 129-160 3.30e-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: 34.19  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217266915 129 RGYTLLHCAAA-WGRLETLKALVELDVDIEALN 160
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 107-182 3.94e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.57  E-value: 3.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217266915 107 AGQSDVIRALAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVAARYSQTECVEFL 182
Cdd:PTZ00322   92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
116-170 7.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.47  E-value: 7.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217266915 116 LAKYGVNLNEKTTRGYTLLHCAAAWGRLETLKALVELDVDIEALNFREERARDVA 170
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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