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Conserved domains on  [gi|1055568352|ref|WP_067210848|]
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MULTISPECIES: ankyrin repeat domain-containing protein [Sporosarcina]

Protein Classification

SUFU domain-containing protein( domain architecture ID 12122228)

SUFU domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SUFU pfam05076
Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila ...
 206-372 6.55e-40

Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila suppressor of fused, appears to have a conserved role in the repression of Hedgehog signaling. SUFU exerts its repressor role by physically interacting with GLI proteins in both the cytoplasm and the nucleus. SUFU has been found to be a tumour-suppressor gene that predisposes individuals to medulloblastoma by modulating the SHH signaling pathway. Genomic contextual analysis of bacterial SUFU versions revealed that they are immunity proteins against diverse nuclease toxins in polymorphic toxin systems.


:

Pssm-ID: 461543  Cd Length: 171  Bit Score: 139.37  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 206 VNVQVILPSKEHDYITLVTTGMSDVAMDDSEGSEEFK--YAELVLKLPAnspiSKEEMKNKDHYWPLKWLRMVAHIPHKY 283
Cdd:pfam05076   5 LDILSIPDTPEPGHWHYVTLGLSDLPMDEPEDLEEDSgpRAELTFRLPK----DEESLADEPPTWPLNLLQNLARYPFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 284 DGWLGEGVILPNGEPPmPFAATTALSCILVSES---EDMGSILDTENRIINFYTLLPIYEEEREIALHNGHDFLMGKFDE 360
Cdd:pfam05076  81 GTWLGPGHTIPNGGPI-PLAENTDLTGLLLVEPlddEELGALETPGGKKVNFLQLVPITEEELEYALEKGADALLELLLE 159

                         170
                  ....*....|..
gi 1055568352 361 FGISDVLDINRK 372
Cdd:pfam05076 160 EGPIDITDLNRK 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-181 4.92e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELI--GSDmelLNLVTTFG-TFLHVAATHGKLEIVKKLIELGADINRRGAIlGGGAINEAASDGHIEIV 89
Cdd:COG0666    94 AARNGDLEIVKLLLeaGAD---VNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  90 RYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLIENGIDIHVKytgeSMKNMGALAFAHERGQKVIADLLDPDKKEE 168
Cdd:COG0666   170 KLLLEAGADVNARDNDgETPLHLAAENGHLEIVKLLLEAGADVNAK----DNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                         170
                  ....*....|...
gi 1055568352 169 YKDTRQYETTEIL 181
Cdd:COG0666   246 NAKDKDGLTALLL 258
 
Name Accession Description Interval E-value
SUFU pfam05076
Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila ...
 206-372 6.55e-40

Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila suppressor of fused, appears to have a conserved role in the repression of Hedgehog signaling. SUFU exerts its repressor role by physically interacting with GLI proteins in both the cytoplasm and the nucleus. SUFU has been found to be a tumour-suppressor gene that predisposes individuals to medulloblastoma by modulating the SHH signaling pathway. Genomic contextual analysis of bacterial SUFU versions revealed that they are immunity proteins against diverse nuclease toxins in polymorphic toxin systems.


Pssm-ID: 461543  Cd Length: 171  Bit Score: 139.37  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 206 VNVQVILPSKEHDYITLVTTGMSDVAMDDSEGSEEFK--YAELVLKLPAnspiSKEEMKNKDHYWPLKWLRMVAHIPHKY 283
Cdd:pfam05076   5 LDILSIPDTPEPGHWHYVTLGLSDLPMDEPEDLEEDSgpRAELTFRLPK----DEESLADEPPTWPLNLLQNLARYPFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 284 DGWLGEGVILPNGEPPmPFAATTALSCILVSES---EDMGSILDTENRIINFYTLLPIYEEEREIALHNGHDFLMGKFDE 360
Cdd:pfam05076  81 GTWLGPGHTIPNGGPI-PLAENTDLTGLLLVEPlddEELGALETPGGKKVNFLQLVPITEEELEYALEKGADALLELLLE 159

                         170
                  ....*....|..
gi 1055568352 361 FGISDVLDINRK 372
Cdd:pfam05076 160 EGPIDITDLNRK 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-181 4.92e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELI--GSDmelLNLVTTFG-TFLHVAATHGKLEIVKKLIELGADINRRGAIlGGGAINEAASDGHIEIV 89
Cdd:COG0666    94 AARNGDLEIVKLLLeaGAD---VNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  90 RYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLIENGIDIHVKytgeSMKNMGALAFAHERGQKVIADLLDPDKKEE 168
Cdd:COG0666   170 KLLLEAGADVNARDNDgETPLHLAAENGHLEIVKLLLEAGADVNAK----DNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                         170
                  ....*....|...
gi 1055568352 169 YKDTRQYETTEIL 181
Cdd:COG0666   246 NAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-134 7.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  43 LHVAATHGKLEIVKKLIELGADINRRGAiLGGGAINEAASDGHIEIVRYLLSCgAELDVSEPERNPLFSAILGGHIDIVK 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1055568352 123 LLIENGIDIHVK 134
Cdd:pfam12796  79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-134 2.21e-07

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: 52.71  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELIGSDMELLNLVTTFG-TFLHVAATHGKLEIVKKLIElgadiNRRGAI---------LGGGAINEAAS 82
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLME-----AAPELVnepmtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055568352  83 DGHIEIVRYLLSCGAelDVSEPE-----------------RNPLFSAILGGHIDIVKLLIENGIDIHVK 134
Cdd:cd22192    99 NQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-134 2.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  41 TFLHVAATHGKLEIVKKLIELGADINRRGaILGGGAINEAASDGHIEIVRYLLSCGAELDVSEPERN-PLFSAILGGHID 119
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGEsPLHNAAEYGDYA 204

                          90
                  ....*....|....*
gi 1055568352 120 IVKLLIENGIDIHVK 134
Cdd:PHA02874  205 CIKLLIDHGNHIMNK 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-66 2.57e-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: 2.57e-04
                           10        20
                   ....*....|....*....|....*.
gi 1055568352   41 TFLHVAATHGKLEIVKKLIELGADIN 66
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
SUFU pfam05076
Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila ...
 206-372 6.55e-40

Suppressor of fused protein (SUFU); SUFU, encoding the human orthologue of Drosophila suppressor of fused, appears to have a conserved role in the repression of Hedgehog signaling. SUFU exerts its repressor role by physically interacting with GLI proteins in both the cytoplasm and the nucleus. SUFU has been found to be a tumour-suppressor gene that predisposes individuals to medulloblastoma by modulating the SHH signaling pathway. Genomic contextual analysis of bacterial SUFU versions revealed that they are immunity proteins against diverse nuclease toxins in polymorphic toxin systems.


Pssm-ID: 461543  Cd Length: 171  Bit Score: 139.37  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 206 VNVQVILPSKEHDYITLVTTGMSDVAMDDSEGSEEFK--YAELVLKLPAnspiSKEEMKNKDHYWPLKWLRMVAHIPHKY 283
Cdd:pfam05076   5 LDILSIPDTPEPGHWHYVTLGLSDLPMDEPEDLEEDSgpRAELTFRLPK----DEESLADEPPTWPLNLLQNLARYPFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352 284 DGWLGEGVILPNGEPPmPFAATTALSCILVSES---EDMGSILDTENRIINFYTLLPIYEEEREIALHNGHDFLMGKFDE 360
Cdd:pfam05076  81 GTWLGPGHTIPNGGPI-PLAENTDLTGLLLVEPlddEELGALETPGGKKVNFLQLVPITEEELEYALEKGADALLELLLE 159

                         170
                  ....*....|..
gi 1055568352 361 FGISDVLDINRK 372
Cdd:pfam05076 160 EGPIDITDLNRK 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-181 4.92e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELI--GSDmelLNLVTTFG-TFLHVAATHGKLEIVKKLIELGADINRRGAIlGGGAINEAASDGHIEIV 89
Cdd:COG0666    94 AARNGDLEIVKLLLeaGAD---VNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  90 RYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLIENGIDIHVKytgeSMKNMGALAFAHERGQKVIADLLDPDKKEE 168
Cdd:COG0666   170 KLLLEAGADVNARDNDgETPLHLAAENGHLEIVKLLLEAGADVNAK----DNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                         170
                  ....*....|...
gi 1055568352 169 YKDTRQYETTEIL 181
Cdd:COG0666   246 NAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-134 7.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 7.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  43 LHVAATHGKLEIVKKLIELGADINRRGAiLGGGAINEAASDGHIEIVRYLLSCgAELDVSEPERNPLFSAILGGHIDIVK 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1055568352 123 LLIENGIDIHVK 134
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-173 1.36e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.31  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELI--GSDmelLNLVTTFG-TFLHVAATHGKLEIVKKLIELGADINRRGAiLGGGAINEAASDGHIEIV 89
Cdd:COG0666   127 AAYNGNLEIVKLLLeaGAD---VNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  90 RYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLIENGIDIHVKYTGESMKNMGALAFAHERGQKVIADLLDPDKKEE 168
Cdd:COG0666   203 KLLLEAGADVNAKDNDgKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                  ....*
gi 1055568352 169 YKDTR 173
Cdd:COG0666   283 LDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-172 4.17e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 4.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352   3 IIQLAKEIRTAIKQNNVERVVELIGSDMELLNLVTTFGTFLHVAATHGKLEIVKKLIELGADINRRGAIlGGGAINEAAS 82
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAAR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  83 DGHIEIVRYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLIENGIDIHVKytgeSMKNMGALAFAHERGQKVIADLL 161
Cdd:COG0666    97 NGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQ----DNDGNTPLHLAAANGNLEIVKLL 172

                         170
                  ....*....|....*.
gi 1055568352 162 -----DPDKKEEYKDT 172
Cdd:COG0666   173 leagaDVNARDNDGET 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-101 7.86e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 7.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELIGSDMELlNLVTTFG-TFLHVAATHGKLEIVKKLIElGADINRRGAilGGGAINEAASDGHIEIVRY 91
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADA-NLQDKNGrTALHLAAKNGHLEIVKLLLE-HADVNLKDN--GRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1055568352  92 LLSCGAELDV 101
Cdd:pfam12796  80 LLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-93 5.40e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 5.40e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1055568352  41 TFLHVAATHGKLEIVKKLIELGADINRRGaILGGGAINEAASDGHIEIVRYLL 93
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-172 4.18e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  22 VVELIGSDMELLNLVTTFGTFLHVAATHGKLEIVKKLIELGADINRRGAILGGGAINEAASDGHIEIVRYLLSCGAELDV 101
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055568352 102 SEPERN-PLFSAILGGHIDIVKLLIENGIDIHVKYTgesmKNMGALAFAHERGQKVIADLL-----DPDKKEEYKDT 172
Cdd:COG0666    83 KDDGGNtLLHAAARNGDLEIVKLLLEAGADVNARDK----DGETPLHLAAYNGNLEIVKLLleagaDVNAQDNDGNT 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-134 2.21e-07

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: 52.71  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELIGSDMELLNLVTTFG-TFLHVAATHGKLEIVKKLIElgadiNRRGAI---------LGGGAINEAAS 82
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLME-----AAPELVnepmtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055568352  83 DGHIEIVRYLLSCGAelDVSEPE-----------------RNPLFSAILGGHIDIVKLLIENGIDIHVK 134
Cdd:cd22192    99 NQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-134 2.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  41 TFLHVAATHGKLEIVKKLIELGADINRRGaILGGGAINEAASDGHIEIVRYLLSCGAELDVSEPERN-PLFSAILGGHID 119
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGEsPLHNAAEYGDYA 204

                          90
                  ....*....|....*
gi 1055568352 120 IVKLLIENGIDIHVK 134
Cdd:PHA02874  205 CIKLLIDHGNHIMNK 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-131 8.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  15 KQNNVERVVELI--GSDMELLNlvTTFGTFLHVAAT--HGKLEIVKKLIELGADINRRGAI---------------LGGG 75
Cdd:PHA03100  117 KSNSYSIVEYLLdnGANVNIKN--SDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFT 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1055568352  76 AINEAASDGHIEIVRYLLSCGAEL-DVSEPERNPLFSAILGGHIDIVKLLIENGIDI 131
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-125 8.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 8.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1055568352  80 AASDGHIEIVRYLLSCGAELDVSEPE-RNPLFSAILGGHIDIVKLLI 125
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNgETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-68 5.46e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 5.46e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1055568352  13 AIKQNNVERVVELIgsDMELLNLVTTFGTFLHVAATHGKLEIVKKLIELGADINRR 68
Cdd:pfam12796  37 AAKNGHLEIVKLLL--EHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-158 5.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  53 EIVKKLIELGADINRRGAILGGGAINEAASDGHIEIVRYLLSCGAELDVSEPERN-PLFSAILGGHIDIVKLLIENGIDI 131
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNsPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1055568352 132 HVK---------YTGESMKNMGALAFAHERGQKVIA 158
Cdd:PHA02878  228 DARdkcgntplhISVGYCKDYDILKLLLEHGVDVNA 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-134 2.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  51 KLEIVKKLIELGADINRRGAI-------LGGGAINEAAsdghiEIVRYLLSCGAelDVSEPER---NPLFSAILGGH-ID 119
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYgktplhlYLHYSSEKVK-----DIVRLLLEAGA--DVNAPERcgfTPLHLYLYNATtLD 98

                          90
                  ....*....|....*
gi 1055568352 120 IVKLLIENGIDIHVK 134
Cdd:PHA03095   99 VIKLLIKAGADVNAK 113
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-134 1.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  18 NVERVVELI---GSDmelLNLVTTFG-TFLHVAATHG-KLEIVKKLIELGADINRRG--------AILGGGAINEaasdg 84
Cdd:PHA03095   61 KVKDIVRLLleaGAD---VNAPERCGfTPLHLYLYNAtTLDVIKLLIKAGADVNAKDkvgrtplhVYLSGFNINP----- 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055568352  85 hiEIVRYLLSCGAEL-DVSEPERNPLFsAILGGH---IDIVKLLIENGIDIHVK 134
Cdd:PHA03095  133 --KVIRLLLRKGADVnALDLYGMTPLA-VLLKSRnanVELLRLLIDAGADVYAV 183
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-66 2.57e-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: 2.57e-04
                           10        20
                   ....*....|....*....|....*.
gi 1055568352   41 TFLHVAATHGKLEIVKKLIELGADIN 66
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-126 4.21e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  24 ELIGSDMELLNLVTTFGTFLHVAATHG--KLEIVKKLIELGADINRRGAiLGGGAINEAASDGHIEIVRYLLSCGAELD- 100
Cdd:PHA03095  207 ELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINa 285

                          90       100
                  ....*....|....*....|....*.
gi 1055568352 101 VSEPERNPLFSAILGGHIDIVKLLIE 126
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRAVRAALA 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-133 5.26e-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: 37.18  E-value: 5.26e-04
                           10        20
                   ....*....|....*....|....*...
gi 1055568352  106 RNPLFSAILGGHIDIVKLLIENGIDIHV 133
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-66 6.61e-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: 36.85  E-value: 6.61e-04
                          10        20
                  ....*....|....*....|....*.
gi 1055568352  41 TFLHVAATHGKLEIVKKLIELGADIN 66
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-133 8.20e-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: 36.47  E-value: 8.20e-04
                          10        20
                  ....*....|....*....|....*...
gi 1055568352 106 RNPLFSAILGGHIDIVKLLIENGIDIHV 133
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 43-140 9.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  43 LHVAATHGKLEIVKKLIELGADINRRGAI---LGGGAINEAASDGH-IEIVRYLLSCGAelDVSEPERN---PLFSAILG 115
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNnstPLHYLSNIKYNLTDvKEIVKLLLEYGA--NVNAPDNNgitPLLYAISK 116

                          90       100
                  ....*....|....*....|....*...
gi 1055568352 116 --GHIDIVKLLIENGIDIHVK-YTGESM 140
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVNIKnSDGENL 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-68 1.57e-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: 35.73  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 1055568352  41 TFLHVAATH-GKLEIVKKLIELGADINRR 68
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 41-181 2.01e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  41 TFLHVAATHGKLEIVKKLIELGADINRRGaILGGGAINEAASDGHIEIVRYLLSCGAeldVSEPER--NPLFSAILGGHI 118
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRD-ANGNTALWNAISAKHHKIFRILYHFAS---ISDPHAagDLLCTAAKRNDL 635

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055568352 119 DIVKLLIENGIDIhvkyTGESMKNMGALAFAHERGQKVIADLL-----DPDKKEEYKDTRQYETTEIL 181
Cdd:PLN03192  636 TAMKELLKQGLNV----DSEDHQGATALQVAMAEDHVDMVRLLimngaDVDKANTDDDFSPTELRELL 699
PHA02798 PHA02798
ankyrin-like protein; Provisional
 51-133 2.41e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  51 KLEIVKKLIELGADINRRGA--------ILGGGAINeaasdgHIEIVRYLLSCGAELD-VSEPERNPLFSAILGGH---I 118
Cdd:PHA02798   88 MLDIVKILIENGADINKKNSdgetplycLLSNGYIN------NLEILLFMIENGADTTlLDKDGFTMLQVYLQSNHhidI 161

                          90
                  ....*....|....*
gi 1055568352 119 DIVKLLIENGIDIHV 133
Cdd:PHA02798  162 EIIKLLLEKGVDINT 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 79-133 2.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 2.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1055568352  79 EAASDGHIEIVRYLLSCGAELD-VSEPERNPLFSAILGGHIDIVKLLIENGIDIHV 133
Cdd:PHA02874   41 DAIRSGDAKIVELFIKHGADINhINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-136 4.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055568352  13 AIKQNNVERVVELI--GSDMELLNlvTTFGTFLHVAATHGKLEIVKKLIELGADINRRGAiLGGGAINEAASDGHIEIVR 90
Cdd:PHA02875  109 ATILKKLDIMKLLIarGADPDIPN--TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC-CGCTPLIIAMAKGDIAICK 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1055568352  91 YLLSCGAELDV--SEPERNPLFSAILGGHIDIVKLLIENGIDIHVKYT 136
Cdd:PHA02875  186 MLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-132 8.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 8.80e-03
                          10        20
                  ....*....|....*....|....*...
gi 1055568352 105 ERNPLFSAILGGHIDIVKLLIENGIDIH 132
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN 28
 
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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