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Conserved domains on  [gi|1039755815|ref|XP_017173362|]
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ankyrin repeat domain-containing protein 29 isoform X8 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-175 3.23e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  82 AAFWAAKRGNLALLKLLLNSGrVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQ 161
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVN-----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          90
                  ....*....|....
gi 1039755815 162 GHNDVVRFLFGFGA 175
Cdd:COG0666   164 GNLEIVKLLLEAGA 177
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-175 3.23e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  82 AAFWAAKRGNLALLKLLLNSGrVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQ 161
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVN-----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          90
                  ....*....|....
gi 1039755815 162 GHNDVVRFLFGFGA 175
Cdd:COG0666   164 GNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-170 1.01e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.01e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039755815 122 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 170
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-172 1.71e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755815 101 SGRVDVDCRDsvrrdTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 172
Cdd:PTZ00322  103 TGGADPNCRD-----YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 1.12e-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: 37.95  E-value: 1.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755815  117 HGTTLLMVASYAGHIDCVRELVLQGADINL 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-193 7.92e-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: 39.61  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGT------TALF--------FAAQQGHNDVVRFLFGFGASTECR--- 180
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIyygehplsFAACVGNEEIVRLLIEHGADIRAQdsl 168

                          90       100
                  ....*....|....*....|....*..
gi 1039755815 181 --------------TKVIQVYNTFMSS 193
Cdd:cd22192   169 gntvlhilvlqpnkTFACQMYDLILSY 195
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-175 3.23e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  82 AAFWAAKRGNLALLKLLLNSGrVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQ 161
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVN-----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          90
                  ....*....|....
gi 1039755815 162 GHNDVVRFLFGFGA 175
Cdd:COG0666   164 GNLEIVKLLLEAGA 177
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-175 7.41e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 7.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  76 ETPLanaaFWAAKRGNLALLKLLLNSGrVDVDCRDSvrrdtHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTAL 155
Cdd:COG0666   121 ETPL----HLAAYNGNLEIVKLLLEAG-ADVNAQDN-----DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                          90       100
                  ....*....|....*....|
gi 1039755815 156 FFAAQQGHNDVVRFLFGFGA 175
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-175 8.55e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  66 ADMCRMSFKKETPLanaaFWAAKRGNLALLKLLLNSGrVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADIN 145
Cdd:COG0666   144 ADVNAQDNDGNTPL----HLAAANGNLEIVKLLLEAG-ADVN-----ARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039755815 146 LQRESGTTALFFAAQQGHNDVVRFLFGFGA 175
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-170 1.01e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.01e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039755815 122 LMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 170
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-175 1.12e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  79 LANAAFWAAKRGNLALLKLLLNSGRVDVDcrdsvRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFA 158
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADIN-----AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90
                  ....*....|....*..
gi 1039755815 159 AQQGHNDVVRFLFGFGA 175
Cdd:COG0666   128 AYNGNLEIVKLLLEAGA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-176 5.45e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  84 FWAAKRGNLALLKLLLNSGrVDVDCRDSVrrdthGTTLLMVASYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGH 163
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKN-----GRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGH 73

                          90
                  ....*....|...
gi 1039755815 164 NDVVRFLFGFGAS 176
Cdd:pfam12796  74 LEIVKLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-170 1.10e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039755815 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 170
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
109-155 2.77e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039755815 109 RDSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTAL 155
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-147 3.45e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815  66 ADMCRMSFKKETPLanaaFWAAKRGNlallklllnsgrvdVDC------RDSVRRDTHGTTLLMVASYAGHIDCVRELVL 139
Cdd:pfam12796  21 ADANLQDKNGRTAL----HLAAKNGH--------------LEIvkllleHADVNLKDNGRTALHYAARSGHLEIVKLLLE 82


                  ....*...
gi 1039755815 140 QGADINLQ 147
Cdd:pfam12796  83 KGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-172 1.71e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755815 101 SGRVDVDCRDsvrrdTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 172
Cdd:PTZ00322  103 TGGADPNCRD-----YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 115-178 3.49e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 3.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039755815 115 DTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTE 178
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-179 6.76e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 6.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039755815 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEC 179
Cdd:PLN03192  622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-175 2.40e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 2.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039755815 110 DSVRRDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGA 175
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 1.12e-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: 37.95  E-value: 1.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039755815  117 HGTTLLMVASYAGHIDCVRELVLQGADINL 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 117-147 1.30e-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. 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: 38.04  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039755815 117 HGTTLLMVASY-AGHIDCVRELVLQGADINLQ 147
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-178 1.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815 104 VDVDCRDSVR-----------RDTHGTTLLMVASYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 172
Cdd:PHA03100  167 VDINAKNRVNyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....*.
gi 1039755815 173 FGASTE 178
Cdd:PHA03100  247 NGPSIK 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
142-182 4.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 4.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039755815 142 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTK 182
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-193 7.92e-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: 39.61  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039755815 118 GTTLLMVASYAGHIDCVRELVLQGADINLQRESGT------TALF--------FAAQQGHNDVVRFLFGFGASTECR--- 180
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIyygehplsFAACVGNEEIVRLLIEHGADIRAQdsl 168

                          90       100
                  ....*....|....*....|....*..
gi 1039755815 181 --------------TKVIQVYNTFMSS 193
Cdd:cd22192   169 gntvlhilvlqpnkTFACQMYDLILSY 195
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 86-144 3.66e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039755815  86 AAKRGNLALLKLLLNSGrVDVDCRDSvrrdtHGTTLLMVASYAGHIDCVRELVLQGADI 144
Cdd:PLN03192  629 AAKRNDLTAMKELLKQG-LNVDSEDH-----QGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-191 7.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 36.51  E-value: 7.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039755815 115 DTHGTTLLMVASYAGHIDCVRELVLQGADIN-LQRESGTTALFFAAQQGHNDVVRFLFGFGASTECRTKVIQVYNTFM 191
Cdd:PHA02875  165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
 
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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