NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907111095|ref|XP_036015187|]
View 

photoreceptor ankyrin repeat protein isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-129 3.36e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLsccpfL----DVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQD 76
Cdd:COG0666   125 HLAAYNGNLEIVKLL-----LeagaDVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907111095  77 RSECVVALLMAGADLSSVDPvRGKTALEWAVLTDSFDTAQKIRQLLRRPQAEQ 129
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-129 3.36e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLsccpfL----DVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQD 76
Cdd:COG0666   125 HLAAYNGNLEIVKLL-----LeagaDVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907111095  77 RSECVVALLMAGADLSSVDPvRGKTALEWAVLTDSFDTAQKIRQLLRRPQAEQ 129
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-95 5.51e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 5.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLSCCPFlDVNQQDKDGNTALMLAAQAGHMSLVTLLLNYFAGldleRRDQRGLTALMKAAIQDRSEC 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1907111095  81 VVALLMAGADLSSVD 95
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-124 4.13e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  22 DVNQQDKDGNTAL--MLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALmkaAIQDRS-----ECVVALLMAGADLSSV 94
Cdd:PHA03095  109 DVNAKDKVGRTPLhvYLSGFNINPKVIRLLLR--KGADVNALDLYGMTPL---AVLLKSrnanvELLRLLIDAGADVYAV 183

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907111095  95 DpVRGKTALEwaVLTDSFDT-AQKIRQLLRR 124
Cdd:PHA03095  184 D-DRFRSLLH--HHLQSFKPrARIVRELIRA 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 29-58 1.57e-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: 1.57e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907111095   29 DGNTALMLAAQAGHMSLVTLLLNYFAGLDL 58
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-124 5.28e-03

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: 38.07  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  25 QQDKDGNTALMLAAQAGHMSLVTLLLNYfAGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSV----DPVRGK 100
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGE 90

                          90       100
                  ....*....|....*....|....
gi 1907111095 101 TALEWAVLTDSFDTaqkIRQLLRR 124
Cdd:cd22192    91 TALHIAVVNQNLNL---VRELIAR 111
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-129 3.36e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLsccpfL----DVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQD 76
Cdd:COG0666   125 HLAAYNGNLEIVKLL-----LeagaDVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907111095  77 RSECVVALLMAGADLSSVDPvRGKTALEWAVLTDSFDTAQKIRQLLRRPQAEQ 129
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 1.46e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLsccpfL----DVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQD 76
Cdd:COG0666    92 HAAARNGDLEIVKLL-----LeagaDVNARDKDGETPLHLAAYNGNLEIVKLLLE--AGADVNAQDNDGNTPLHLAAANG 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907111095  77 RSECVVALLMAGADLSSVDPvRGKTALEWAVLTDSFDTAQ 116
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-95 5.51e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 5.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLSCCPFlDVNQQDKDGNTALMLAAQAGHMSLVTLLLNYFAGldleRRDQRGLTALMKAAIQDRSEC 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1907111095  81 VVALLMAGADLSSVD 95
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-116 6.48e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 6.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095   1 MVACYHGFGSIVALLSCCPFLDVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQDRSEC 80
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907111095  81 VVALLMAGADLSSVDPvRGKTALEWAVLTDSFDTAQ 116
Cdd:COG0666   136 VKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-116 2.27e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  34 LMLAAQAGHMSLVTLLLNYfaGLDLERRDQRGLTALMKAAIQDRSECvVALLMAGADLSSVDpvRGKTALEWAVLTDSFD 113
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN--GADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD--NGRTALHYAARSGHLE 75


                  ...
gi 1907111095 114 TAQ 116
Cdd:pfam12796  76 IVK 78
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-116 1.03e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  11 IVALLSCCPFLDVNQQDKDGNTALMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGAD 90
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA--AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD 112

                          90       100
                  ....*....|....*....|....*.
gi 1907111095  91 LSSVDPvRGKTALEWAVLTDSFDTAQ 116
Cdd:COG0666   113 VNARDK-DGETPLHLAAYNGNLEIVK 137
Ank_5 pfam13857
Ankyrin repeats (many copies);
49-106 2.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111095  49 LLNYFaGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSVDPvRGKTALEWA 106
Cdd:pfam13857   1 LLEHG-PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
14-69 7.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111095  14 LLSCCPfLDVNQQDKDGNTALMLAAQAGHMSLVTLLLNYfaGLDLERRDQRGLTAL 69
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-124 4.13e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  22 DVNQQDKDGNTAL--MLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALmkaAIQDRS-----ECVVALLMAGADLSSV 94
Cdd:PHA03095  109 DVNAKDKVGRTPLhvYLSGFNINPKVIRLLLR--KGADVNALDLYGMTPL---AVLLKSrnanvELLRLLIDAGADVYAV 183

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907111095  95 DpVRGKTALEwaVLTDSFDT-AQKIRQLLRR 124
Cdd:PHA03095  184 D-DRFRSLLH--HHLQSFKPrARIVRELIRA 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
30-85 8.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 8.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111095  30 GNTALMLAAQAGHMSLVTLLLNYfaGLDLERRDQRGLTALMKAAIQDRSECVVALL 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-128 4.79e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  22 DVNQQDKDGNTALMLAAqAGHMSLVTLLLNYF-AGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSVDPvRGK 100
Cdd:PHA03095  214 DPAATDMLGNTPLHSMA-TGSSCKRSLVLPLLiAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGN 291

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907111095 101 TALEWAVL---TDSFDTAqkirqLLRRPQAE 128
Cdd:PHA03095  292 TPLSLMVRnnnGRAVRAA-----LAKNPSAE 317
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-50 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907111095   2 VACYHG-FGSIVALLscCPFLDVNQQDKDGNTALMLAAQAGHMSLVTLLL 50
Cdd:pfam13637   7 AAAASGhLELLRLLL--EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 22-86 1.14e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111095  22 DVNQQDKDGNTALMLAAQAGHMSLVTLLLNYfaGLDLERRDQRGLTALMKAAIQDRSEcVVALLM 86
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEF--GADPTLLDKDGKTPLELAEENGFRE-VVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 29-58 1.57e-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: 1.57e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907111095   29 DGNTALMLAAQAGHMSLVTLLLNYFAGLDL 58
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 29-62 2.75e-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: 34.57  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907111095  29 DGNTALMLAA-QAGHMSLVTLLLNYFAglDLERRD 62
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGA--DVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-124 5.28e-03

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: 38.07  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  25 QQDKDGNTALMLAAQAGHMSLVTLLLNYfAGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSV----DPVRGK 100
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGE 90

                          90       100
                  ....*....|....*....|....
gi 1907111095 101 TALEWAVLTDSFDTaqkIRQLLRR 124
Cdd:cd22192    91 TALHIAVVNQNLNL---VRELIAR 111
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 22-103 8.23e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111095  22 DVNQQDKDGNTA--LMLAAQAGHMSLVTLLLNyfAGLDLERRDQRGLTALMKAAIQDRSECVVALLMAGADLSSVDpVRG 99
Cdd:PLN03192  515 DNGGEHDDPNMAsnLLTVASTGNAALLEELLK--AKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD-ANG 591


                  ....
gi 1907111095 100 KTAL 103
Cdd:PLN03192  592 NTAL 595
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH