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Conserved domains on  [gi|2462577359|ref|XP_054199982|]
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ankyrin repeat domain-containing protein 53 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];
112-206 3.29e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90
                  ....*....|....*
gi 2462577359 192 pciyYLLEKGADLNA 206
Cdd:COG0666   204 ----LLLEAGADVNA 214
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-206 3.29e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90
                  ....*....|....*
gi 2462577359 192 pciyYLLEKGADLNA 206
Cdd:COG0666   204 ----LLLEAGADVNA 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-206 1.95e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 113 FAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeyKFPVDlLTNNSQTPLHLVIHRDNttvaLP 192
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVN-LKDNGRTALHYAARSGH----LE 75

                          90
                  ....*....|....
gi 2462577359 193 CIYYLLEKGADLNA 206
Cdd:pfam12796  76 IVKLLLEKGADINV 89
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 175-207 2.65e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462577359 175 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAF 207
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-206 3.29e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90
                  ....*....|....*
gi 2462577359 192 pciyYLLEKGADLNA 206
Cdd:COG0666   204 ----LLLEAGADVNA 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-206 1.95e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 113 FAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeyKFPVDlLTNNSQTPLHLVIHRDNttvaLP 192
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVN-LKDNGRTALHYAARSGH----LE 75

                          90
                  ....*....|....
gi 2462577359 193 CIYYLLEKGADLNA 206
Cdd:pfam12796  76 IVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-206 4.58e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90
                  ....*....|....*
gi 2462577359 192 pciyYLLEKGADLNA 206
Cdd:COG0666   138 ----LLLEAGADVNA 148
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-217 1.15e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.80  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          90       100
                  ....*....|....*....|....*.
gi 2462577359 192 pciyYLLEKGADLNAFLKDAMWKKDK 217
Cdd:COG0666   237 ----LLLEAGADLNAKDKDGLTALLL 258
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-198 1.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462577359 142 TAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNttvaLPCIYYLL 198
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGN----VEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-160 2.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 2.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462577359 112 LFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLV 160
Cdd:pfam13637   5 LHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 175-207 2.65e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462577359 175 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAF 207
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPAR 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-181 5.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 5.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462577359 136 TDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLV 181
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-206 8.93e-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: 33.42  E-value: 8.93e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462577359 175 QTPLHLVIHRDNttvALPCIYYLLEKGADLNA 206
Cdd:pfam00023   3 NTPLHLAAGRRG---NLEIVKLLLSKGADVNA 31
 
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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