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Conserved domains on  [gi|256574784|ref|NP_001157912|]
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ankyrin repeat domain-containing protein 33B [Homo sapiens]

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];
89-250 8.61e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 8.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  89 LLRAACANNVGLLRTLVRRGVSVEEaqeTDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHA 168
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 169 IITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLMQRLLE 248
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243


                 ..
gi 256574784 249 RP 250
Cdd:COG0666  244 DL 245
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-250 8.61e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 8.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  89 LLRAACANNVGLLRTLVRRGVSVEEaqeTDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHA 168
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 169 IITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLMQRLLE 248
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243


                 ..
gi 256574784 249 RP 250
Cdd:COG0666  244 DL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-220 8.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 8.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  125 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHAIITNYLLNYFPGldleRRNAFGFTALMKAAMQGRTD 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 256574784  205 CIRALMLAGADVHARD 220
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-229 3.81e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  87 ATLLRAACANNVGLLRTLVRRGVSveeAQETDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAAQ 164
Cdd:PLN03192 527 SNLLTVASTGNAALLEELLKAKLD---PDIGDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 165 AGHAIITNYLLNYFP-----------------------------GLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGAD 215
Cdd:PLN03192 601 AKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                        170
                 ....*....|....
gi 256574784 216 VHARDPRRGMSPQE 229
Cdd:PLN03192 681 VDKANTDDDFSPTE 694
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-210 2.22e-05

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: 46.93  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  69 VESAESVPEGVPESV--PETA------TLLRAACAN-NVGLLRTLVRRGVSVEEAQETD---RNGRTGLivaCYHGfvDT 136
Cdd:cd22192   64 LEAAVVLMEAAPELVnePMTSdlyqgeTALHIAVVNqNLNLVRELIARGADVVSPRATGtffRPGPKNL---IYYG--EH 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 137 VVALAEC------------PHVDVNWQDSEGNTAL-ITAAQAGHAIIT---NYLLNYFPGLDLER----RNAFGFTALMK 196
Cdd:cd22192  139 PLSFAACvgneeivrllieHGADIRAQDSLGNTVLhILVLQPNKTFACqmyDLILSYDKEDDLQPldlvPNNQGLTPFKL 218

                        170
                 ....*....|....
gi 256574784 197 AAMQGRTDCIRALM 210
Cdd:cd22192  219 AAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 190-218 1.66e-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: 36.03  E-value: 1.66e-03
                           10        20
                   ....*....|....*....|....*....
gi 256574784   190 GFTALMKAAMQGRTDCIRALMLAGADVHA 218
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-250 8.61e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 8.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  89 LLRAACANNVGLLRTLVRRGVSVEEaqeTDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHA 168
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 169 IITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLMQRLLE 248
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243


                 ..
gi 256574784 249 RP 250
Cdd:COG0666  244 DL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-249 6.15e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 6.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  86 TATLLRAACANNVGLLRTLVRRGVSVeeaQETDRNGRTGLIVACYHGFVDTVVALAECPhVDVNWQDSEGNTALITAAQA 165
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADI---NAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 166 GHAIITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLmqr 245
Cdd:COG0666  131 GNLEIVKLLLEA--GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKL--- 204


                 ....
gi 256574784 246 LLER 249
Cdd:COG0666  205 LLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
88-249 5.42e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 5.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  88 TLLRAACANNVGLLRTLVRRGVSVEEaqeTDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGH 167
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNA---QDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 168 AIITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLMQRLL 247
Cdd:COG0666  199 LEIVKLLLEA--GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD-KDGLTALLLAAAAGAALIVKLLLLAL 275


                 ..
gi 256574784 248 ER 249
Cdd:COG0666  276 LL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-220 8.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 8.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  125 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHAIITNYLLNYFPGldleRRNAFGFTALMKAAMQGRTD 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 256574784  205 CIRALMLAGADVHARD 220
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
118-249 3.11e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.01  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 118 DRNGRTGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHAIITNYLLNYfpGLDLERRNAFGFTALMKA 197
Cdd:COG0666   50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLA 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 256574784 198 AMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLmqrLLER 249
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKL---LLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-187 2.85e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784   89 LLRAACANNVGLLRTLVRRGVsveEAQETDRNGRTGLIVACYHGFVDTVVALAECPHVDVnwqDSEGNTALITAAQAGHA 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*....
gi 256574784  169 IITNYLLNYfpGLDLERRN 187
Cdd:pfam12796  75 EIVKLLLEK--GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-249 6.09e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 6.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 137 VVALAECPHVDVNWQDSEGNTALITAAQAGHAIITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADV 216
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                         90       100       110
                 ....*....|....*....|....*....|...
gi 256574784 217 HARDpRRGMSPQEWATYTGRVDAVRLmqrLLER 249
Cdd:COG0666  114 NARD-KDGETPLHLAAYNGNLEIVKL---LLEA 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-229 3.81e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  87 ATLLRAACANNVGLLRTLVRRGVSveeAQETDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAAQ 164
Cdd:PLN03192 527 SNLLTVASTGNAALLEELLKAKLD---PDIGDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 165 AGHAIITNYLLNYFP-----------------------------GLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGAD 215
Cdd:PLN03192 601 AKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                        170
                 ....*....|....
gi 256574784 216 VHARDPRRGMSPQE 229
Cdd:PLN03192 681 VDKANTDDDFSPTE 694
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-194 1.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574784  140 LAECPHVDVNWQDSEGNTALITAAQAGHAIITNYLLNYfpGLDLERRNAFGFTAL 194
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-221 1.18e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  97 NVGLLRTLVRRGVSVeeaQETDRNGRTGLivacyHGFVDTVVALAEC------PHVDVNWQDSEGNTALITAAQAG---H 167
Cdd:PHA03095 166 NVELLRLLIDAGADV---YAVDDRFRSLL-----HHHLQSFKPRARIvrelirAGCDPAATDMLGNTPLHSMATGSsckR 237

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 256574784 168 AIITNYLLNyfpGLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDP 221
Cdd:PHA03095 238 SLVLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-210 2.22e-05

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: 46.93  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  69 VESAESVPEGVPESV--PETA------TLLRAACAN-NVGLLRTLVRRGVSVEEAQETD---RNGRTGLivaCYHGfvDT 136
Cdd:cd22192   64 LEAAVVLMEAAPELVnePMTSdlyqgeTALHIAVVNqNLNLVRELIARGADVVSPRATGtffRPGPKNL---IYYG--EH 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 137 VVALAEC------------PHVDVNWQDSEGNTAL-ITAAQAGHAIIT---NYLLNYFPGLDLER----RNAFGFTALMK 196
Cdd:cd22192  139 PLSFAACvgneeivrllieHGADIRAQDSLGNTVLhILVLQPNKTFACqmyDLILSYDKEDDLQPldlvPNNQGLTPFKL 218

                        170
                 ....*....|....
gi 256574784 197 AAMQGRTDCIRALM 210
Cdd:cd22192  219 AAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-243 2.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 2.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 256574784  192 TALMKAAMQGRTDCIRALMLAGADVHARDpRRGMSPQEWATYTGRVDAVRLM 243
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-175 3.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574784  121 GRTGLIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITAAQAGHAIITNYLL 175
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-209 5.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574784  155 GNTALITAAQAGHAIITNYLLNYfpGLDLERRNAFGFTALMKAAMQGRTDCIRAL 209
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-243 6.17e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 6.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 256574784  194 LMKAAMQGRTDCIRALMLAGADVHARDPrRGMSPQEWATYTGRVDAVRLM 243
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLL 49
Ank_5 pfam13857
Ankyrin repeats (many copies);
174-222 1.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 256574784  174 LLNYFPgLDLERRNAFGFTALMKAAMQGRTDCIRALMLAGADVHARDPR 222
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-223 2.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  88 TLLRAACANNVGLLRTLVRRGVSVEEAqetDRNGRTGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALIT--AAQA 165
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAP---ERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFN 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256574784 166 GHAIITNYLLNYfpGLDLERRNAFGFTALmkAAMQGRTDC----IRALMLAGADVHARDPRR 223
Cdd:PHA03095 130 INPKVIRLLLRK--GADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRF 187
Ank_4 pfam13637
Ankyrin repeats (many copies);
85-140 8.50e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 8.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 256574784   85 ETATLLRAACANNVGLLRTLVRRGVSVeeaQETDRNGRTGLIVACYHGFVDTVVAL 140
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADI---NAVDGNGETALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 190-218 1.66e-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: 36.03  E-value: 1.66e-03
                           10        20
                   ....*....|....*....|....*....
gi 256574784   190 GFTALMKAAMQGRTDCIRALMLAGADVHA 218
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 189-218 5.14e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 5.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 256574784  189 FGFTALMKAAMQGRTDCIRALMLAGADVHA 218
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-162 7.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 7.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 256574784  117 TDRNGRTGLIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITA 162
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 89-220 9.16e-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: 38.46  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784  89 LLRAACANNVGLLRTLVRrgVSVEEAQETDRNGRTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQ 164
Cdd:cd22192   21 LLLAAKENDVQAIKKLLK--CPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574784 165 AGHAIITNYLLNYfpGLDLE---------RRNA-----FGFTALMKAAMQGRTDCIRALMLAGADVHARD 220
Cdd:cd22192   99 NQNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
 
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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