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Conserved domains on  [gi|1698279859|ref|XP_003969291|]
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ankyrin repeat and MYND domain-containing protein 2-like isoform X3 [Takifugu rubripes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-129 7.81e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 7.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  16 LLQIIAAGDVqEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCnQHEFGYTALMFAALSGKTDI 95
Cdd:COG0666    91 LHAAARNGDL-EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGNLEI 168

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1698279859  96 TSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
zf-MYND pfam01753
MYND finger;
320-357 1.62e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.81  E-value: 1.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1698279859 320 CATCGERGA-DKKCSLCKLAKYCSLTCQKLHWFTHKKMC 357
Cdd:pfam01753   1 CAVCGKEALkLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
Ank_2 super family cl48147
Ankyrin repeats (3 copies);
84-190 1.33e-05

Ankyrin repeats (3 copies);


The actual alignment was detected with superfamily member pfam12796:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  84 LMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCVTV-INNFFSRARLEYYTrpqgletepklpprlag 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLlLEHADVNLKDNGRT----------------- 63

                          90       100
                  ....*....|....*....|....*...
gi 1698279859 163 PLHKIIMTTNLNPVKMVLLVKEHPMMID 190
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-129 7.81e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 7.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  16 LLQIIAAGDVqEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCnQHEFGYTALMFAALSGKTDI 95
Cdd:COG0666    91 LHAAARNGDL-EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGNLEI 168

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1698279859  96 TSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-110 6.60e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 6.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  17 LQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHgADVNCNQHefGYTALMFAALSGKTDIT 96
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1698279859  97 SMMLDAGAETDLVN 110
Cdd:pfam12796  78 KLLLEKGADINVKD 91
zf-MYND pfam01753
MYND finger;
320-357 1.62e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.81  E-value: 1.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1698279859 320 CATCGERGA-DKKCSLCKLAKYCSLTCQKLHWFTHKKMC 357
Cdd:pfam01753   1 CAVCGKEALkLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-112 1.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859   8 DVSASER--KLLQIIAAGDVQeAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQHEFGYTALM 85
Cdd:PHA02875  129 DIPNTDKfsPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207

                          90       100
                  ....*....|....*....|....*..
gi 1698279859  86 FAALSGKTDITSMMLDAGAETDLVNSV 112
Cdd:PHA02875  208 YAIENNKIDIVRLFIKRGADCNIMFMI 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-190 1.33e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  84 LMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCVTV-INNFFSRARLEYYTrpqgletepklpprlag 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLlLEHADVNLKDNGRT----------------- 63

                          90       100
                  ....*....|....*....|....*...
gi 1698279859 163 PLHKIIMTTNLNPVKMVLLVKEHPMMID 190
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 2.82e-05

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: 40.65  E-value: 2.82e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1698279859   45 YGMTPLMHAAYKGTADLCCLLLQHGADVNC 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 17-115 4.75e-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: 39.23  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  17 LQIIAAGDVQEAAELLASEDVR-VN---CLDEY-GMTPLMHAAYKGTADLCCLLLQHGADVN-------------CNQHE 78
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNepmTSDLYqGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNLIY 134

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1698279859  79 FGYTALMFAALSGKTDITSMMLDAGAETDLVNSVGRT 115
Cdd:cd22192   135 YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-129 7.81e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 7.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  16 LLQIIAAGDVqEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCnQHEFGYTALMFAALSGKTDI 95
Cdd:COG0666    91 LHAAARNGDL-EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGNLEI 168

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1698279859  96 TSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-129 2.95e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  16 LLQIIAAGDVqEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNcNQHEFGYTALMFAALSGKTDI 95
Cdd:COG0666   157 LHLAAANGNL-EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEI 234

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1698279859  96 TSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-110 6.60e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 6.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  17 LQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHgADVNCNQHefGYTALMFAALSGKTDIT 96
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1698279859  97 SMMLDAGAETDLVN 110
Cdd:pfam12796  78 KLLLEKGADINVKD 91
zf-MYND pfam01753
MYND finger;
320-357 1.62e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 52.81  E-value: 1.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1698279859 320 CATCGERGA-DKKCSLCKLAKYCSLTCQKLHWFTHKKMC 357
Cdd:pfam01753   1 CAVCGKEALkLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-129 2.59e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.96  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  16 LLQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQHEFGYTALMFAALSGKTDI 95
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1698279859  96 TSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-112 1.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859   8 DVSASER--KLLQIIAAGDVQeAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQHEFGYTALM 85
Cdd:PHA02875  129 DIPNTDKfsPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207

                          90       100
                  ....*....|....*....|....*..
gi 1698279859  86 FAALSGKTDITSMMLDAGAETDLVNSV 112
Cdd:PHA02875  208 YAIENNKIDIVRLFIKRGADCNIMFMI 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
31-87 1.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698279859  31 LLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQhEFGYTALMFA 87
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-111 8.13e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  30 ELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVN-CNqhEFGYTALMFAALSGKTDITSMMLDAGAETDL 108
Cdd:PHA03100  176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNlVN--KYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253


                  ...
gi 1698279859 109 VNS 111
Cdd:PHA03100  254 IIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-100 1.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1698279859  46 GMTPLMHAAYKGTADLCCLLLQHGADVNCnQHEFGYTALMFAALSGKTDITSMML 100
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-190 1.33e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  84 LMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCVTV-INNFFSRARLEYYTrpqgletepklpprlag 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLlLEHADVNLKDNGRT----------------- 63

                          90       100
                  ....*....|....*....|....*...
gi 1698279859 163 PLHKIIMTTNLNPVKMVLLVKEHPMMID 190
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 2.82e-05

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: 40.65  E-value: 2.82e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1698279859   45 YGMTPLMHAAYKGTADLCCLLLQHGADVNC 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-117 4.96e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.94  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  17 LQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQHEfGYTALMFAALSGKTDIT 96
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIV 268

                          90       100
                  ....*....|....*....|.
gi 1698279859  97 SMMLDAGAETDLVNSVGRTAA 117
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 39-116 6.43e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  39 VNCLDEYGMTPL---MHAAYKGTADLCCLLLQHGADVN----CnqhefGYTALMFAALSGKT-DITSMMLDAGAETDLVN 110
Cdd:PHA03095   40 VNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNaperC-----GFTPLHLYLYNATTlDVIKLLIKAGADVNAKD 114


                  ....*.
gi 1698279859 111 SVGRTA 116
Cdd:PHA03095  115 KVGRTP 120
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-101 8.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 8.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698279859  29 AELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVNCNQHEfGYTALMFAALSGKTDITSMMLD 101
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIID 232
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-74 2.62e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.62e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1698279859  45 YGMTPLMHAAYKGTADLCCLLLQHGADVNC 74
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-120 2.68e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698279859  65 LLQHGaDVNCN-QHEFGYTALMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMA 120
Cdd:pfam13857   1 LLEHG-PIDLNrLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-74 3.29e-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: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1698279859  45 YGMTPLMHAAYK-GTADLCCLLLQHGADVNC 74
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-138 4.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  13 ERKLLQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLLQHGADVN------------------- 73
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDipntdkfsplhlavmmgdi 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698279859  74 -----------CNQHE--FGYTALMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMAAFvgQHDCVTVINNFFSR 138
Cdd:PHA02875  149 kgiellidhkaCLDIEdcCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI--ENNKIDIVRLFIKR 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 23-128 6.22e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  23 GDVQEAAELLASEDVRVNCLDEYGMTPL-MHAAYKGTADLCCLLLQHGADVNcNQHEFGYTALMfAALSGK---TDITSM 98
Cdd:PHA03095   60 EKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN-AKDKVGRTPLH-VYLSGFninPKVIRL 137

                          90       100       110
                  ....*....|....*....|....*....|
gi 1698279859  99 MLDAGAETDLVNSVGRTAaqMAAFVGQHDC 128
Cdd:PHA03095  138 LLRKGADVNALDLYGMTP--LAVLLKSRNA 165
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-129 7.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 7.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1698279859  80 GYTALMFAALSGKTDITSMMLDAGAETDLVNSVGRTAAQMAAFVGQHDCV 129
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank_4 pfam13637
Ankyrin repeats (many copies);
13-66 1.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1698279859  13 ERKLLQIIAAGDVQEAAELLASEDVRVNCLDEYGMTPLMHAAYKGTADLCCLLL 66
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 17-115 4.75e-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: 39.23  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859  17 LQIIAAGDVQEAAELLASEDVR-VN---CLDEY-GMTPLMHAAYKGTADLCCLLLQHGADVN-------------CNQHE 78
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNepmTSDLYqGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNLIY 134

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1698279859  79 FGYTALMFAALSGKTDITSMMLDAGAETDLVNSVGRT 115
Cdd:cd22192   135 YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-121 7.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698279859   3 VPEKGDVSASERKLLQIIAAGDVqEAAELLASEDVRVNCLDEYGMTPLMHAAYKGT-ADLCCLLLQHGADVNCNQHEfGY 81
Cdd:PHA02876  231 IDNRSNINKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIK-GE 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1698279859  82 TALMFAALSG-KTDITSMMLDAGAETDLVNSVGRTAAQMAA 121
Cdd:PHA02876  309 TPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAS 349
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 64-115 8.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 8.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1698279859  64 LLLQHGADVNCNQHEFGYTALMFAALSGKTDITSMMLDAGAEtdlVNSVGRT 115
Cdd:PHA02878  152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGAN---VNIPDKT 200
 
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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