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Conserved domains on  [gi|2047259149|ref|NP_001178499|]
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ankyrin repeat domain-containing protein 13C [Rattus norvegicus]

Protein Classification

GPCR_chapero_1 domain-containing protein( domain architecture ID 12790908)

GPCR_chapero_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 258-531 2.77e-80

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


:

Pssm-ID: 463391  Cd Length: 298  Bit Score: 253.33  E-value: 2.77e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 258 RLDTTLIDFTDMKCQRGDLSFIFSGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 335
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 336 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGSLTEQNFEPVR-------- 407
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 408 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATVAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 483
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 484 FVQMKLPPGFPVKLDIPVFPTITATVTFQEFR-CDEFDG--------------------SIFAIPEDYK 531
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFEeLDPVEEfstpikspergspssceiddDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-198 2.64e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 2047259149 193 TALLRK 198
Cdd:COG0666   203 KLLLEA 208
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 258-531 2.77e-80

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 253.33  E-value: 2.77e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 258 RLDTTLIDFTDMKCQRGDLSFIFSGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 335
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 336 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGSLTEQNFEPVR-------- 407
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 408 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATVAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 483
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 484 FVQMKLPPGFPVKLDIPVFPTITATVTFQEFR-CDEFDG--------------------SIFAIPEDYK 531
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFEeLDPVEEfstpikspergspssceiddDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-198 2.64e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 2047259149 193 TALLRK 198
Cdd:COG0666   203 KLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-198 4.85e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 116 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 194
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 2047259149 195 LLRK 198
Cdd:pfam12796  80 LLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 114-197 2.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 189
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                  ....*...
gi 2047259149 190 QMITALLR 197
Cdd:PHA02875  149 KGIELLID 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 142-167 4.42e-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: 4.42e-05
                           10        20
                   ....*....|....*....|....*.
gi 2047259149  142 HGNTPLHLAVMLGNKECAHLLLAHNA 167
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 110-198 4.09e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 110 PSLYPVHECVFKGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLA 181
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALH 94

                          90
                  ....*....|....*..
gi 2047259149 182 EAISYGDRQMITALLRK 198
Cdd:cd22192    95 IAVVNQNLNLVRELIAR 111
 
Name Accession Description Interval E-value
GPCR_chapero_1 pfam11904
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
 258-531 2.77e-80

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


Pssm-ID: 463391  Cd Length: 298  Bit Score: 253.33  E-value: 2.77e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 258 RLDTTLIDFTDMKCQRGDLSFIFSGDAAPSESFVVLDNEQKVYQ--RIHHEESEMETEEEVDILMSSDIYSATLSTKSIS 335
Cdd:pfam11904   1 RADTTLLGFDGFKWQRGDQSFLFLGDGDSPGSLLELDHDEKEVQleGAGAEASEEEVEEEVAARLQTPIVRPGIDVTKIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 336 FTRAQTGWlFREDKTERVGNFLADFYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGSLTEQNFEPVR-------- 407
Cdd:pfam11904  81 FERNKSGW-RRQEKTEMVGGYKAKVYDASNVELSTKSRTEHLSEEEKAKLKSALEPPEGSRTPLQSFLGIAEeekgwfgk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 408 -RQSLTPPPQN--TITWEEYISAEngkaphlgRELvcKESKKTFKATVAMSQEFPLGIESLLNVLEVIA-PFKHFNKLRE 483
Cdd:pfam11904 160 tREESEAPPTNptALTPEEYFDPP--------KEE--SEKKKGFKATLWLSEDFPLSLEQLLPILDLLAnKVKHFRRLRE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 484 FVQMKLPPGFPVKLDIPVFPTITATVTFQEFR-CDEFDG--------------------SIFAIPEDYK 531
Cdd:pfam11904 230 FITLKLPPGFPVKIEIPVFPTVNARITFTKFEeLDPVEEfstpikspergspssceiddDPFEIPSGYT 298
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-198 2.64e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.53  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 2047259149 193 TALLRK 198
Cdd:COG0666   203 KLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-198 7.20e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169


                  ....*.
gi 2047259149 193 TALLRK 198
Cdd:COG0666   170 KLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-228 3.36e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 3.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2047259149 193 TALLRKLKQQSRESVGEKRPRLLKALKELGDFYLEL 228
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-198 4.05e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 4.05e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 130 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 198
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-198 4.85e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 116 HECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHnAPVKVKNaQGWSPLAEAISYGDRQMITA 194
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....
gi 2047259149 195 LLRK 198
Cdd:pfam12796  80 LLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-196 9.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 9.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2047259149 143 GNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 196
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-206 1.50e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 147 LHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRKLKQQSRES 206
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 114-197 2.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRT----HNIGQKDnhGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDR 189
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLgkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148


                  ....*...
gi 2047259149 190 QMITALLR 197
Cdd:PHA02875  149 KGIELLID 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
114-173 4.07e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 4.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRtHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKN 173
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 142-173 5.52e-06

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: 43.05  E-value: 5.52e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2047259149 142 HGNTPLHLAV-MLGNKECAHLLLAHNAPVKVKN 173
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-200 7.54e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.03  E-value: 7.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMI 192
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268


                  ....*...
gi 2047259149 193 TALLRKLK 200
Cdd:COG0666   269 KLLLLALL 276
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 145-196 1.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2047259149 145 TPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALL 196
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
135-183 2.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2047259149 135 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEA 183
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-196 2.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2047259149 139 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYgDRQMITALL 196
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-196 4.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 115 VHECVFKGDVRRLSSLIRTH-NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMIT 193
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGaDVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207


                  ...
gi 2047259149 194 ALL 196
Cdd:PHA02874  208 LLI 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 142-167 4.42e-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: 4.42e-05
                           10        20
                   ....*....|....*....|....*.
gi 2047259149  142 HGNTPLHLAVMLGNKECAHLLLAHNA 167
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-196 8.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 114 PVHECVFKGDVRRLSSLI-RTHNIGQKDNHGNTPLHLAVmLGNKECAHLLLaHNAPVKVKNAQGWSPLAEAISYG-DRQM 191
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIdHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDI 270


                  ....*
gi 2047259149 192 ITALL 196
Cdd:PHA02874  271 IDILL 275
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 142-169 1.42e-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: 39.16  E-value: 1.42e-04
                          10        20
                  ....*....|....*....|....*...
gi 2047259149 142 HGNTPLHLAVMLGNKECAHLLLAHNAPV 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 140-187 2.38e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 2.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2047259149 140 DNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYG 187
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-163 3.76e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2047259149 114 PVHECVFKGDVRRLSSLI-RTHNIGQKDNHGNTPLHLAVMLGNKECAHLLL 163
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 110-198 4.09e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 110 PSLYPVHECVFKGDVRRLSSLIRTH--NIGQKDNHGNTPLHLAVMLGNKECAhLLLAHNAPVKVKNA------QGWSPLA 181
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKKLLKCPscDLFQRGALGETALHVAALYDNLEAA-VVLMEAAPELVNEPmtsdlyQGETALH 94

                          90
                  ....*....|....*..
gi 2047259149 182 EAISYGDRQMITALLRK 198
Cdd:cd22192    95 IAVVNQNLNLVRELIAR 111
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 139-197 1.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 139 KDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 197
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-198 1.43e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259149 130 LIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 198
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-200 6.12e-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: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 118 CVFKGDVRRLssLIRTH-NIGQKDNHGNTPLHLAVMLGNKECA----HLLLAHNAPVK------VKNAQGWSPLAEAISY 186
Cdd:cd22192   145 CVGNEEIVRL--LIEHGaDIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKE 222

                          90
                  ....*....|....
gi 2047259149 187 GDRQMITALLRKLK 200
Cdd:cd22192   223 GNIVMFQHLVQKRR 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
 140-198 7.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 7.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259149 140 DNHGNTPLHLAVMLGNKE-CAHLLLAhNAPVKVKNAQGWSPLAEAISYGDRQMITALLRK 198
Cdd:PHA03095  254 NRYGQTPLHYAAVFNNPRaCRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 135-197 8.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 8.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047259149 135 NIGQKDNH-GNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 197
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 135-197 9.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 9.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047259149 135 NIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLR 197
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
 
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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