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Conserved domains on  [gi|1832932193|ref|XP_033390782|]
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uncharacterized protein K452DRAFT_314243, partial [Aplosporella prunicola CBS 121167]

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];
257-316 2.96e-14

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 2.96e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832932193 257 ALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
257-316 2.96e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 2.96e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832932193 257 ALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
Ank_2 pfam12796
Ankyrin repeats (3 copies);
257-316 6.88e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 6.88e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832932193 257 ALYYA-SFGGLDCsVENLLDKgADVNAQGGTFgNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:pfam12796  33 ALHLAaKNGHLEI-VKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 254-315 6.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 6.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832932193 254 LAPALYYASFG-GLDCSVENLLDKGADVNAQGGTFGNAL-YAASSEGHEKIVQMLLDKGADVNA 315
Cdd:PHA02876  408 IGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLhYACKKNCKLDVIEMLLDNGADVNA 471
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 289-315 1.71e-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: 38.34  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*..
gi 1832932193  289 NALYAASSEGHEKIVQMLLDKGADVNA 315
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 269-316 7.26e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 7.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832932193 269 SVENLLDKGADVN---AQGGTF----GNALYA-------ASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:cd22192   104 LVRELIARGADVVsprATGTFFrpgpKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQ 165
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
257-316 2.96e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 2.96e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832932193 257 ALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-316 1.25e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 1.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832932193 253 HLAPALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
257-316 1.28e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 1.28e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832932193 257 ALYYASFGG-LDCsVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666   156 PLHLAAANGnLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
Ank_2 pfam12796
Ankyrin repeats (3 copies);
257-316 6.88e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 6.88e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832932193 257 ALYYA-SFGGLDCsVENLLDKgADVNAQGGTFgNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:pfam12796  33 ALHLAaKNGHLEI-VKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
257-315 2.73e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 2.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1832932193 257 ALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNA 315
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
254-316 5.26e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.34  E-value: 5.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832932193 254 LAPALYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
Ank_2 pfam12796
Ankyrin repeats (3 copies);
258-316 2.27e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 2.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1832932193 258 LYYASFGGLDCSVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKgADVNAQ 316
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK 58
Ank_4 pfam13637
Ankyrin repeats (many copies);
253-307 2.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 2.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1832932193 253 HLAPALYYASFGGLDCsVENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLL 307
Cdd:pfam13637   1 ELTALHAAAASGHLEL-LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 292-316 3.91e-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: 39.97  E-value: 3.91e-05
                          10        20
                  ....*....|....*....|....*
gi 1832932193 292 YAASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:pfam00023   8 LAAGRRGNLEIVKLLLSKGADVNAR 32
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 254-315 6.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 6.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832932193 254 LAPALYYASFG-GLDCSVENLLDKGADVNAQGGTFGNAL-YAASSEGHEKIVQMLLDKGADVNA 315
Cdd:PHA02876  408 IGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLhYACKKNCKLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 270-315 9.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 9.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1832932193 270 VENLLDKGADVNAQGGTFGNALYAASSEGHE--KIVQMLLDKGADVNA 315
Cdd:PHA03100  124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 289-315 1.71e-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: 38.34  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*..
gi 1832932193  289 NALYAASSEGHEKIVQMLLDKGADVNA 315
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 273-315 2.87e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 2.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1832932193 273 LLDKGADVNAQGGTFGNAL--YAASSEGHEKIVQMLLDKGADVNA 315
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA 147
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 269-316 7.26e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 7.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832932193 269 SVENLLDKGADVN---AQGGTF----GNALYA-------ASSEGHEKIVQMLLDKGADVNAQ 316
Cdd:cd22192   104 LVRELIARGADVVsprATGTFFrpgpKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQ 165
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 271-314 2.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1832932193 271 ENLLDKGADVNAQGGTFGNALYAASSEGHEKIVQMLLDKGADVN 314
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
PHA03095 PHA03095
ankyrin-like protein; Provisional
 270-315 3.20e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 3.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1832932193 270 VENLLDKGADVNaQGGTFGN----ALYAASSEGHEKIVQMLLDKGADVNA 315
Cdd:PHA03095   30 VRRLLAAGADVN-FRGEYGKtplhLYLHYSSEKVKDIVRLLLEAGADVNA 78
 
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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