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Conserved domains on  [gi|530383069|ref|XP_005248741|]
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ankyrin repeat domain-containing protein 6 isoform X32 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13269884)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-202 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVA 180
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAEN 229

                         90       100
                 ....*....|....*....|..
gi 530383069 181 RKEEAREEFLSASPEPRAKDDR 202
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKD 251
PHA02874 super family cl31515
ankyrin repeat protein; Provisional
 32-168 2.89e-03

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02874:

Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGK------VRKDPRRSER---------- 95
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKtflhyaIKKGDLESIKmlfeygadvn 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383069  96 -EKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVS 168
Cdd:PHA02874 152 iEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-202 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVA 180
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAEN 229

                         90       100
                 ....*....|....*....|..
gi 530383069 181 RKEEAREEFLSASPEPRAKDDR 202
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 4.40e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 4.40e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383069  101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLIKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-173 6.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 6.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383069  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTP 173
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK----CGNTP 237
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-168 2.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGK------VRKDPRRSER---------- 95
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKtflhyaIKKGDLESIKmlfeygadvn 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383069  96 -EKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVS 168
Cdd:PHA02874 152 iEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 3.33e-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: 35.26  E-value: 3.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 530383069   132 DGNTALHEASWHGFSQSAKLLIKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-202 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVA 180
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAEN 229

                         90       100
                 ....*....|....*....|..
gi 530383069 181 RKEEAREEFLSASPEPRAKDDR 202
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-202 1.89e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTPSSEQ 177
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND----GETPLHLA 193

                         90       100
                 ....*....|....*....|....*
gi 530383069 178 AVARKEEAREEFLSASPEPRAKDDR 202
Cdd:COG0666  194 AENGHLEIVKLLLEAGADVNAKDND 218
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-173 3.77e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 3.77e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383069  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTP 173
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND----GNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 4.40e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 4.40e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383069  101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLIKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-188 1.61e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVSAGDTPSSEQAV 179
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265


                 ....*....
gi 530383069 180 ARKEEAREE 188
Cdd:COG0666  266 LIVKLLLLA 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 4.71e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.71e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530383069  102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-202 1.16e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTPSSE 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD----GETPLHL 126

                         90       100
                 ....*....|....*....|....*.
gi 530383069 177 QAVARKEEAREEFLSASPEPRAKDDR 202
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDND 152
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-165 2.45e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383069  104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaGANVLAKNKG 165
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG 61
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-164 9.67e-06

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: 42.66  E-value: 9.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530383069  132 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 164
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-173 6.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 6.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383069  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTP 173
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK----CGNTP 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 2.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530383069   86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-168 2.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGK------VRKDPRRSER---------- 95
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKtflhyaIKKGDLESIKmlfeygadvn 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383069  96 -EKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVS 168
Cdd:PHA02874 152 iEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 3.33e-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: 35.26  E-value: 3.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 530383069   132 DGNTALHEASWHGFSQSAKLLIKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-173 5.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLIKAGANVLAKNKgsvsAGDT 172
Cdd:PHA03095  44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDK----VGRT 119


                 .
gi 530383069 173 P 173
Cdd:PHA03095 120 P 120
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 119-194 7.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 7.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383069 119 LIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLSASP 194
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK----YGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 7.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530383069  121 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTP 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE----GLTA 52
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 111-247 7.63e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383069 111 GNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVlakNKGSVSAGDTPSSEQAVARKEEA--REE 188
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV---DKANTDDDFSPTELRELLQKRELghSIT 709

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530383069 189 FLSASPEPRAKDDRRRKSRPKVSAfsdpTPPADQQPGHQKNLHaHNHPKKRNRHRCSSP 247
Cdd:PLN03192 710 IVDSVPADEPDLGRDGGSRPGRLQ----GTSSDNQCRPRVSIY-KGHPLLRNERCCNEA 763
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-163 9.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 9.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383069  99 GDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSA-KLLIKAGANVLAKN 163
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKS 265
 
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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